Therapeutic polypeptides, nucleic acids encoding same, and methods of use

Abstract

Disclosed herein are nucleic acid sequences that encode novel polypeptides. Also disclosed are polypeptides encoded by these nucleic acid sequences, and antibodies that immunospecifically bind to the polypeptide, as well as derivatives, variants, mutants, or fragments of the novel polypeptide, polynucleotide, or antibody specific to the polypeptide. Vectors, host cells, antibodies and recombinant methods for producing the polypeptides and polynucleotides, as well as methods for using same are also included. The invention further discloses therapeutic, diagnostic and research methods for diagnosis, treatment, and prevention of disorders involving any one of these novel human nucleic acids and proteins.

Description

FIELD OF THE INVENTION

[0002] The present invention relates to novel polypeptides, and the nucleic acids encoding them, having properties related to stimulation of biochemical or physiological responses in a cell, a tissue, an organ or an organism. More particularly, the novel polypeptides are gene products of novel genes, or are specified biologically active fragments or derivatives thereof. Methods of use encompass diagnostic and prognostic assay procedures as well as methods of treating diverse pathological conditions.

BACKGROUND OF THE INVENTION

[0003] Eukaryotic cells are characterized by biochemical and physiological processes which under normal conditions are exquisitely balanced to achieve the preservation and propagation of the cells. When such cells are components of multicellular organisms such as vertebrates, or more particularly organisms such as mammals, the regulation of the biochemical and physiological processes involves intricate signaling pathways. Frequently, such signaling pathways involve extracellular signaling proteins, cellular receptors that bind the signaling proteins, and signal transducing components located within the cells.

[0004] Signaling proteins may be classified as endocrine effectors, paracrine effectors or autocrine effectors. Endocrine effectors are signaling molecules secreted by a given organ into the circulatory system, which are then transported to a distant target organ or tissue. The target cells include the receptors for the endocrine effector, and when the endocrine effector binds, a signaling cascade is induced. Paracrine effectors involve secreting cells and receptor cells in close proximity to each other, for example two different classes of cells in the same tissue or organ. One class of cells secretes the paracrine effector, which then reaches the second class of cells, for example by diffusion through the extracellular fluid. The second class of cells contains the receptors for the paracrine effector; binding of the effector results in induction of the signaling cascade that elicits the corresponding biochemical or physiological effect. Autocrine effectors are highly analogous to paracrine effectors, except that the same cell type that secretes the autocrine effector also contains the receptor. Thus the autocrine effector binds to receptors on the same cell, or on identical neighboring cells. The binding process then elicits the characteristic biochemical or physiological effect.

[0005] Signaling processes may elicit a variety of effects on cells and tissues including by way of nonlimiting example induction of cell or tissue proliferation, suppression of growth or proliferation, induction of differentiation or maturation of a cell or tissue, and suppression of differentiation or maturation of a cell or tissue.

[0006] Many pathological conditions involve dysregulation of expression of important effector proteins. In certain classes of pathologies the dysregulation is manifested as diminished or suppressed level of synthesis and secretion of protein effectors. In other classes of pathologies the dysregulation is manifested as increased or up-regulated level of synthesis and secretion of protein effectors. In a clinical setting a subject may be suspected of suffering from a condition brought on by altered or mis-regulated levels of a protein effector of interest. Therefore there is a need to assay for the level of the protein effector of interest in a biological sample from such a subject, and to compare the level with that characteristic of a nonpathological condition. There also is a need to provide the protein effector as a product of manufacture. Administration of the effector to a subject in need thereof is useful in treatment of the pathological condition. Accordingly, there is a need for a method of treatment of a pathological condition brought on by a diminished or suppressed levels of the protein effector of interest. In addition, there is a need for a method of treatment of a pathological condition brought on by a increased or up-regulated levels of the protein effector of interest.

[0007] Antibodies are multichain proteins that bind specifically to a given antigen, and bind poorly, or not at all, to substances deemed not to be cognate antigens. Antibodies are comprised of two short chains termed light chains and two long chains termed heavy chains. These chains are constituted of immunoglobulin domains, of which generally there are two classes: one variable domain per chain, one constant domain in light chains, and three or more constant domains in heavy chains. The antigen-specific portion of the immunoglobulin molecules resides in the variable domains; the variable domains of one light chain and one heavy chain associate with each other to generate the antigen-binding moiety. Antibodies that bind immunospecifically to a cognate or target antigen bind with high affinities. Accordingly, they are useful in assaying specifically for the presence of the antigen in a sample. In addition, they have the potential of inactivating the activity of the antigen.

[0008] Therefore there is a need to assay for the level of a protein effector of interest in a biological sample from such a subject, and to compare this level with that characteristic of a nonpathological condition. In particular, there is a need for such an assay based on the use of an antibody that binds immunospecifically to the antigen. There further is a need to inhibit the activity of the protein effector in cases where a pathological condition arises from elevated or excessive levels of the effector based on the use of an antibody that binds immunospecifically to the effector. Thus, there is a need for the antibody as a product of manufacture. There further is a need for a method of treatment of a pathological condition brought on by an elevated or excessive level of the protein effector of interest based on administering the antibody to the subject.

SUMMARY OF THE INVENTION

[0009] The invention is based in part upon the discovery of isolated polypeptides including amino acid sequences selected from mature forms of the amino acid sequences selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107. The novel nucleic acids and polypeptides are referred to herein as NOVX, or NOV1, NOV2, NOV3, etc., nucleic acids and polypeptides. These nucleic acids and polypeptides, as well as derivatives, homologs, analogs and fragments thereof, will hereinafter be collectively designated as “NOVX” nucleic acid or polypeptide sequences.

[0010] The invention also is based in part upon variants of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, wherein any amino acid in the mature form is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed. In another embodiment, the invention includes the amino acid sequences selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107. In another embodiment, the invention also comprises variants of the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 wherein any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed. The invention also involves fragments of any of the mature forms of the amino acid sequences selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, or any other amino acid sequence selected from this group. The invention also comprises fragments from these groups in which up to 15% of the residues are changed.

[0011] In another embodiment, the invention encompasses polypeptides that are naturally occurring allelic variants of the sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107. These allelic variants include amino acid sequences that are the translations of nucleic acid sequences differing by a single nucleotide from nucleic acid sequences selected from the group consisting of SEQ ID NOS: 2n−1, wherein n is an integer between 1 and 107. The variant polypeptide where any amino acid changed in the chosen sequence is changed to provide a conservative substitution.

[0012] In another embodiment, the invention comprises a pharmaceutical composition involving a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 and a pharmaceutically acceptable carrier. In another embodiment, the invention involves a kit, including, in one or more containers, this pharmaceutical composition.

[0013] In another embodiment, the invention includes the use of a therapeutic in the manufacture of a medicament for treating a syndrome associated with a human disease, the disease being selected from a pathology associated with a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 wherein said therapeutic is the polypeptide selected from this group.

[0014] In another embodiment, the invention comprises a method for determining the presence or amount of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 in a sample, the method involving providing the sample; introducing the sample to an antibody that binds immunospecifically to the polypeptide; and determining the presence or amount of antibody bound to the polypeptide, thereby determining the presence or amount of polypeptide in the sample.

[0015] In another embodiment, the invention includes a method for determining the presence of or predisposition to a disease associated with altered levels of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 in a first mammalian subject, the method involving measuring the level of expression of the polypeptide in a sample from the first mammalian subject; and comparing the amount of the polypeptide in this sample to the amount of the polypeptide present in a control sample from a second mammalian subject known not to have, or not to be predisposed to, the disease, wherein an alteration in the expression level of the polypeptide in the first subject as compared to the control sample indicates the presence of or predisposition to the disease.

[0016] In another embodiment, the invention involves a method of identifying an agent that binds to a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, the method including introducing the polypeptide to the agent; and determining whether the agent binds to the polypeptide. The agent could be a cellular receptor or a downstream effector.

[0017] In another embodiment, the invention involves a method for identifying a potential therapeutic agent for use in treatment of a pathology, wherein the pathology is related to aberrant expression or aberrant physiological interactions of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, the method including providing a cell expressing the polypeptide of the invention and having a property or function ascribable to the polypeptide; contacting the cell with a composition comprising a candidate substance; and determining whether the substance alters the property or function ascribable to the polypeptide; whereby, if an alteration observed in the presence of the substance is not observed when the cell is contacted with a composition devoid of the substance, the substance is identified as a potential therapeutic agent.

[0018] In another embodiment, the invention involves a method for screening for a modulator of activity or of latency or predisposition to a pathology associated with a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, the method including administering a test compound to a test animal at increased risk for a pathology associated with the polypeptide of the invention, wherein the test animal recombinantly expresses the polypeptide of the invention; measuring the activity of the polypeptide in the test animal after administering the test compound; and comparing the activity of the protein in the test animal with the activity of the polypeptide in a control animal not administered the polypeptide, wherein a change in the activity of the polypeptide in the test animal relative to the control animal indicates the test compound is a modulator of latency of, or predisposition to, a pathology associated with the polypeptide of the invention. The recombinant test animal could express a test protein transgene or express the transgene under the control of a promoter at an increased level relative to a wild-type test animal The promoter may or may not b the native gene promoter of the transgene.

[0019] In another embodiment, the invention involves a method for modulating the activity of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, the method including introducing a cell sample expressing the polypeptide with a compound that binds to the polypeptide in an amount sufficient to modulate the activity of the polypeptide.

[0020] In another embodiment, the invention involves a method of treating or preventing a pathology associated with a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, the method including administering the polypeptide to a subject in which such treatment or prevention is desired in an amount sufficient to treat or prevent the pathology in the subject. The subject could be human.

[0021] In another embodiment, the invention involves a method of treating a pathological state in a mammal, the method including administering to the mammal a polypeptide in an amount that is sufficient to alleviate the pathological state, wherein the polypeptide is a polypeptide having an amino acid sequence at least 95% identical to a polypeptide having the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 or a biologically active fragment thereof.

[0022] In another embodiment, the invention involves an isolated nucleic acid molecule comprising a nucleic acid sequence encoding a polypeptide having an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107; a variant of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 wherein any amino acid in the mature form of the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed; the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107; a variant of the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107, in which any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed; a nucleic acid fragment encoding at least a portion of a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 or any variant of the polypeptide wherein any amino acid of the chosen sequence is changed to a different amino acid, provided that no more than 10% of the amino acid residues in the sequence are so changed; and the complement of any of the nucleic acid molecules.

[0023] In another embodiment, the invention comprises an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107, wherein the nucleic acid molecule comprises the nucleotide sequence of a naturally occurring allelic nucleic acid variant.

[0024] In another embodiment, the invention involves an isolated nucleic acid molecule including a nucleic acid sequence encoding a polypeptide having an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107 that encodes a variant polypeptide, wherein the variant polypeptide has the polypeptide sequence of a naturally occurring polypeptide variant.

[0025] In another embodiment, the invention comprises an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107, wherein the nucleic acid molecule differs by a single nucleotide from a nucleic acid sequence selected from the group consisting of SEQ ID NOS: 2n-1, wherein n is an integer between 1 and 107.

[0026] In another embodiment, the invention includes an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107, wherein the nucleic acid molecule comprises a nucleotide sequence selected from the group consisting of the nucleotide sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107; a nucleotide sequence wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed; a nucleic acid fragment of the sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107; and a nucleic acid fragment wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed.

[0027] In another embodiment, the invention includes an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107, wherein the nucleic acid molecule hybridizes under stringent conditions to the nucleotide sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or a complement of the nucleotide sequence.

[0028] In another embodiment, the invention includes an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107, wherein the nucleic acid molecule has a nucleotide sequence in which any nucleotide specified in the coding sequence of the chosen nucleotide sequence is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides in the chosen coding sequence are so changed, an isolated second polynucleotide that is a complement of the first polynucleotide, or a fragment of any of them.

[0029] In another embodiment, the invention includes a vector involving the nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107. This vector can have a promoter operably linked to the nucleic acid molecule. This vector can be located within a cell.

[0030] In another embodiment, the invention involves a method for determining the presence or amount of a nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107 in a sample, the method including providing the sample; introducing the sample to a probe that binds to the nucleic acid molecule; and determining the presence or amount of the probe bound to the nucleic acid molecule, thereby determining the presence or amount of the nucleic acid molecule in the sample. The presence or amount of the nucleic acid molecule is used as a marker for cell or tissue type. The cell type can be cancerous.

[0031] In another embodiment, the invention involves a method for determining the presence of or predisposition for a disease associated with altered levels of a nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO:2n, wherein n is an integer between 1 and 107 in a first mammalian subject, the method including measuring the amount of the nucleic acid in a sample from the first mammalian subject; and comparing the amount of the nucleic acid in the sample of step (a) to the amount of the nucleic acid present in a control sample from a second mammalian subject known not to have or not be predisposed to, the disease; wherein an alteration in the level of the nucleic acid in the first subject as compared to the control sample indicates the presence of or predisposition to the disease.

[0032] The invention further provides an antibody that binds immunospecifically to a NOVX polypeptide. The NOVX antibody may be monoclonal, humanized, or a fully human antibody. Preferably, the antibody has a dissociation constant for the binding of the NOVX polypeptide to the antibody less than 1×10−9 M. More preferably, the NOVX antibody neutralizes the activity of the NOVX polypeptide.

[0033] In a further aspect, the invention provides for the use of a therapeutic in the manufacture of a medicament for treating a syndrome associated with a human disease, associated with a NOVX polypeptide. Preferably the therapeutic is a NOVX antibody.

[0034] In yet a further aspect, the invention provides a method of treating or preventing a NOVX-associated disorder, a method of treating a pathological state in a mammal, and a method of treating or preventing a pathology associated with a polypeptide by administering a NOVX antibody to a subject in an amount sufficient to treat or prevent the disorder.

[0035] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, suitable methods and materials are described below. All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety. In the case of conflict, the present specification, including definitions, will control. In addition, the materials, methods, and examples are illustrative only and are not intended to be limiting.

[0036] Other features and advantages of the invention will be apparent from the following detailed description and claims.

DETAILED DESCRIPTION OF THE INVENTION

[0037] The present invention provides novel nucleotides and polypeptides encoded thereby. Included in the invention are the novel nucleic acid sequences, their encoded polypeptides, antibodies, and other related compounds. The sequences are collectively referred to herein as “NOVX nucleic acids” or “NOVX polynucleotides” and the corresponding encoded polypeptides are referred to as “NOVX polypeptides” or “NOVX proteins.” Unless indicated otherwise, “NOVX” is meant to refer to any of the novel sequences disclosed herein. Table A provides a summary of the NOVX nucleic acids and their encoded polypeptides.

TABLE A
Sequences and Corresponding SEQ ID Numbers
		SEQ	SEQ
		ID NO	ID NO
NOVX	Internal	(nucleic	(amino
Assignment	Identification	acid)	acid	Homology
1a	CG105472-01	1	2	Novel KIAA0575/
				Greb1-like Proteins
				and Nucleic Acids
				Encoding Same
2a	CG106287-01	3	4	Integrin Alpha-11
2b	CG106287-02	5	6	Integrin Alpha-11
3a	CG106417-01	7	8	Fibrillin
3b	CG106417-03	9	10	Novel von Willebrand
				factor
3c	CG106417-04	11	12	Novel von Willebrand
				factor
3d	209749357	13	14	Fibrillin
3e	CG106417-02	15	16	Fibrillin
4a	CG108901-01	17	18	Cytokine Receptor
4b	CG108901-04	19	20	Cytokine Receptor
4c	CG108901-03	21	22	Cytokine Receptor
4d	CG108901-02	23	24	Cytokine Receptor
5a	CG112505-01	25	26	Laminin 5-Beta 3
5b	CG112505-02	27	28	Laminin 5-Beta 3
6a	CG121965-01	29	30	Fibulin 3
6b	CG121965-02	31	32	Fibulin 3
7a	CG126129-01	33	34	Epithelium
				differentiation factor
				(PEDF)
7b	CG126129-02	35	36	Epithelium
				differentiation factor
				(PEDF)
8a	CG142202-01	37	38	Cytokine Receptor
				CRL2 Precursor
8b	CG142202-03	39	40	Cytokine Receptor
				CRL2 Precursor
8c	CG142202-02	41	42	Cytokine Receptor
				CRL2 Precursor
9a	CG142621-01	43	44	Human GTP binding
				protein
10a	CG142761-01	45	46	Histocombatibility 13
11a	CG143926-01	47	48	HLA-B7 alpha chain
				precursor
12a	CG144193-01	49	50	Secreted
				phosphoprotein 24
12b	CG144193-02	51	52	Secreted
				phosphoprotein 24
13a	CG144545-01	53	54	Neuronal thread
				protein
14a	CG144884-01	55	56	B-Lymphocyte
				Activation Marker
				Blast-1 Precursor
14b	CG144884-02	57	58	B-Lymphocyte
				Activation Marker
				Blast-1 Precursor
15a	CG145122-01	59	60	MtN3/saliva Homolog
16a	CG145198-01	61	62	Secreted Protein
16b	278498076	63	64	Secreted Protein
16c	278498091	65	66	Secreted Protein
16d	CG145198-02	67	68	Secreted Protein
16e	CG145198-03	69	70	Secreted Protein
17a	CG145286-01	71	72	Tm6 protein
17b	CG145286-02	73	74	Tm6 protein
18a	CG145650-01	75	76	Lectin C-Type Domain
				Protein
18b	CG145650-02	77	78	Lectin C-Type Domain
				Protein
18c	CG145650-03	79	80	Lectin C-Type Domain
				Protein
19a	CG145836-01	81	82	STAR protein
19b	CG145836-02	83	84	STAR protein
20a	CG145978-01	85	86	DUF221 domain
				containing membrane
				protein
20b	CG145978-02	87	88	DUF221 domain
				containing membrane
				protein
21a	CG145997-01	89	90	Similar to Drosophila
				FRY gene protein
22a	CG146119-01	91	92	Papilin
23a	CG146202-01	93	94	Membrane-Associated
				Lectin Type-C
24a	CG146250-01	95	96	Membrane protein
				containing vwd
				domain
24b	CG146250-02	97	98	Membrane protein
				containing vwd
				domain
24c	CG146250-03	99	100	Membrane protein
				containing vwd
				domain
25a	CG146625-01	101	102	Type IIIa Membrane
				Protein
25b	CG146625-02	103	104	Type IIIa Membrane
				Protein
25c	CG146625-03	105	106	Type IIIa Membrane
				Protein
26a	CG147284-01	107	108	Cadherin 6
27a	CG147937-01	109	110	NK Cell Receptor
				CS-1
27b	CG147937-02	111	112	NK Cell Receptor
				CS-1
28a	CG148221-01	113	114	Claudin domain
				containing
				transmembrane protein
28b	CG148221-02	115	116	Claudin domain
				containing
				transmembrane protein
29a	CG148476-01	117	118	Membrane-bound
				protein PRO1383
30a	CG148818-01	119	120	Membrane protein
				KIAA0146
31a	CG149332-01	121	122	Interferon Induced
				Transmembrane
				Protein 3 (1-8U)
32a	CG149649-01	123	124	Type IIIA membrane
				protein
32b	CG149649-02	125	126	Type IIIA membrane
				protein
33a	CG149680-01	127	128	Pb39 (Prostate Cancer
				Overexpressed
				Gene 1)
33b	CG149680-02	129	130	Pb39 (Prostate Cancer
				Overexpressed
				Gene 1)
34a	CG149777-01	131	132	KIAA0575/Greb1
34b	CG149777-02	133	134	KIAA0575/Greb1
34c	257474374	135	136	Integrin Alpha-11
34d	257474386	137	138	Fibrillin
35a	CG150005-01	139	140	von Willebrand factor
36a	CG150189-01	141	142	von Willebrand factor
37a	CG150267-01	143	144	Fibrillin
38a	CG150362-01	145	146	Otoferlin
39a	CG150637-01	147	148	Cytokine Receptor
39b	CG150637-02	149	150	Cytokine Receptor
40a	CG150694-01	151	152	Cytokine Receptor
41a	CG151069-01	153	154	Bone marrow secreted
				protein
42a	CG151189-01	155	156	Human apoptosis
				protein (APOP-2)
43a	CG151801-01	157	158	Laminin 5-Beta 3
44a	CG165961-01	159	160	Fibulin 3
44b	CG165961-02	161	162	Fibulin 3
44c	CG165961-03	163	164	Fibulin 3
44d	CG165961-04	165	166	Epithelium
				differentiation
				factor (PEDF)
45a	CG171681-01	167	168	Cytokine Receptor
				CRL2 Precursor
45b	CG171681-02	169	170	Cytokine Receptor
				CRL2 Precursor
45c	CG171681-03	171	172	Cytokine Receptor
				CRL2 Precursor
46a	CG173318-01	173	174	Human metabolism
				protein 16
47a	CG51595-01	175	176	HLA-B7 alpha chain
				precursor
47b	CG51595-03	177	178	HLA-B7 alpha chain
				precursor
47c	CG51595-04	179	180	Secreted
				phosphoprotein 24
47d	CG51595-06	181	182	Secreted
				phosphoprotein 24
47e	CG51595-07	183	184	1700029J11RIK
				protein
47f	306395637	185	186	B-Lymphocyte
				Activation Marker
				Blast-1 Precursor
47g	CG51595-01	187	188	B-Lymphocyte
				Activation Marker
				Blast-1 Precursor
47h	283842727	189	190	MtN3/saliva Homolog
47i	283842704	191	192	MtN3/saliva Homolog
47j	CG51595-01	193	194	MtN3/saliva Homolog
47k	310658551	195	196	MtN3/saliva Homolog
47l	CG51595-02	197	198	MtN3/saliva Homolog
47m	CG51595-05	199	200	MtN3/saliva Homolog
48a	CG57209-01	201	202	Tm6 protein
48b	CG57209-03	203	204	Lectin C-Type Domain
				Protein
48c	CG57209-02	205	206	Lectin C-Type Domain
				Protein
48d	CG57209-04	207	208	Lectin C-Type Domain
				Protein
49a	CG57292-01	209	210	STAR protein
49b	CG57292-02	211	212	STAR protein
50a	CG97715-01	213	214	Transmembrane
				protein PT27

[0038] Table A indicates the homology of NOVX polypeptides to known protein families. Thus, the nucleic acids and polypeptides, antibodies and related compounds according to the invention corresponding to a NOVX as identified in column 1 of Table A will be useful in therapeutic and diagnostic applications implicated in, for example, pathologies and disorders associated with the known protein families identified in column 5 of Table A.

[0039] Pathologies, diseases, disorders and condition and the like that are associated with NOVX sequences include, but are not limited to: e.g., cardiomyopathy, atherosclerosis, hypertension, congenital heart defects, aortic stenosis, atrial septal defect (ASD), atrioventricular (A-V) canal defect, ductus arteriosus, pulmonary stenosis, subaortic stenosis, ventricular septal defect (VSD), valve diseases, tuberous sclerosis, scleroderma, obesity, metabolic disturbances associated with obesity, transplantation, adrenoleukodystrophy, congenital adrenal hyperplasia, prostate cancer, diabetes, metabolic disorders, neoplasm; adenocarcinoma, lymphoma, uterus cancer, fertility, hemophilia, hypercoagulation, idiopathic thrombocytopenic purpura, immunodeficiencies, graft versus host disease, AIDS, bronchial asthma, Crohn's disease; multiple sclerosis, treatment of Albright Hereditary Ostoeodystrophy, infectious disease, anorexia, cancer-associated cachexia, cancer, neurodegenerative disorders, Alzheimer's Disease, Parkinson's Disorder, immune disorders, hematopoietic disorders, and the various dyslipidemias, the metabolic syndrome X and wasting disorders associated with chronic diseases and various cancers, as well as conditions such as transplantation, neuroprotection, fertility, or regeneration (in vitro and in vivo).

[0040] NOVX nucleic acids and their encoded polypeptides are useful in a variety of applications and contexts. The various NOVX nucleic acids and polypeptides according to the invention are useful as novel members of the protein families according to the presence of domains and sequence relatedness to previously described proteins. Additionally, NOVX nucleic acids and polypeptides can also be used to identify proteins that are members of the family to which the NOVX polypeptides belong.

[0041] Consistent with other known members of the family of proteins, identified in column 5 of Table A, the NOVX polypeptides of the present invention show homology to, and contain domains that are characteristic of, other members of such protein families. Details of the sequence relatedness and domain analysis for each NOVX are presented in Example A.

[0042] The NOVX nucleic acids and polypeptides can also be used to screen for molecules, which inhibit or enhance NOVX activity or function. Specifically, the nucleic acids and polypeptides according to the invention may be used as targets for the identification of small molecules that modulate or inhibit diseases associated with the protein families listed in Table A.

[0043] The NOVX nucleic acids and polypeptides are also useful for detecting specific cell types. Details of the expression analysis for each NOVX are presented in Example C. Accordingly, the NOVX nucleic acids, polypeptides, antibodies and related compounds according to the invention will have diagnostic and therapeutic applications in the detection of a variety of diseases with differential expression in normal vs. diseased tissues, e.g. detection of a variety of cancers.

[0044] Additional utilities for NOVX nucleic acids and polypeptides according to the invention are disclosed herein.

[0045] NOVX Clones

[0046] NOVX nucleic acids and their encoded polypeptides are useful in a variety of applications and contexts. The various NOVX nucleic acids and polypeptides according to the invention are useful as novel members of the protein families according to the presence of domains and sequence relatedness to previously described proteins. Additionally, NOVX nucleic acids and polypeptides can also be used to identify proteins that are members of the family to which the NOVX polypeptides belong.

[0047] The NOVX genes and their corresponding encoded proteins are useful for preventing, treating or ameliorating medical conditions, e.g., by protein or gene therapy. Pathological conditions can be diagnosed by determining the amount of the new protein in a sample or by determining the presence of mutations in the new genes. Specific uses are described for each of the NOVX genes, based on the tissues in which they are most highly expressed. Uses include developing products for the diagnosis or treatment of a variety of diseases and disorders.

[0048] The NOVX nucleic acids and proteins of the invention are useful in potential diagnostic and therapeutic applications and as a research tool. These include serving as a specific or selective nucleic acid or protein diagnostic and/or prognostic marker, wherein the presence or amount of the nucleic acid or the protein are to be assessed, as well as potential therapeutic applications such as the following: (i) a protein therapeutic, (ii) a small molecule drug target, (iii) an antibody target (therapeutic, diagnostic, drug targeting/cytotoxic antibody), (iv) a nucleic acid useful in gene therapy (gene delivery/gene ablation), and (v) a composition promoting tissue regeneration in vitro and in vivo (vi) a biological defense weapon.

[0049] In one specific embodiment, the invention includes an isolated polypeptide comprising an amino acid sequence selected from the group consisting of: (a) a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107; (b) a variant of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107, wherein any amino acid in the mature form is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed; (c) an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107; (d) a variant of the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 wherein any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed; and (e) a fragment of any of (a) through (d).

[0050] In another specific embodiment, the invention includes an isolated nucleic acid molecule comprising a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence selected from the group consisting of: (a) a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 107; (b) a variant of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107 wherein any amino acid in the mature form of the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed; (c) the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107; (d) a variant of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107, in which any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed; (e) a nucleic acid fragment encoding at least a portion of a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 107 or any variant of said polypeptide wherein any amino acid of the chosen sequence is changed to a different amino acid, provided that no more than 10% of the amino acid residues in the sequence are so changed; and (f) the complement of any of said nucleic acid molecules.

[0051] In yet another specific embodiment, the invention includes an isolated nucleic acid molecule, wherein said nucleic acid. molecule comprises a nucleotide sequence selected from the group consisting of: (a) the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 107; (b) a nucleotide sequence wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 107 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed; (c) a nucleic acid fragment of the sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 107; and (d) a nucleic acid fragment wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 107 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed.

[0052] NOVX Nucleic Acids and Polypeptides

[0053] One aspect of the invention pertains to isolated nucleic acid molecules that encode NOVX polypeptides or biologically active portions thereof. Also included in the invention are nucleic acid fragments sufficient for use as hybridization probes to identify NOVX-encoding nucleic acids (e.g., NOVX mRNAs) and fragments for use as PCR primers for the amplification and/or mutation of NOVX nucleic acid molecules. As used herein, the term “nucleic acid molecule” is intended to include DNA molecules (e.g., cDNA or genomic DNA), RNA molecules (e.g., mRNA), analogs of the DNA or RNA generated using nucleotide analogs, and derivatives, fragments and homologs thereof. The nucleic acid molecule may be single-stranded or double-stranded, but preferably is comprised double-stranded DNA.

[0054] A NOVX nucleic acid can encode a mature NOVX polypeptide. As used herein, a “mature” form of a polypeptide or protein disclosed in the present invention is the product of a naturally occurring polypeptide or precursor form or proprotein. The naturally occurring polypeptide, precursor or proprotein includes, by way of nonlimiting example, the full-length gene product encoded by the corresponding gene. Alternatively, it may be defined as the polypeptide, precursor or proprotein encoded by an ORF described herein. The product “mature” form arises, by way of nonlimiting example, as a result of one or more naturally occurring processing steps that may take place within the cell (e.g., host cell) in which the gene product arises. Examples of such processing steps leading to a “mature” form of a polypeptide or protein include the cleavage of the N-terminal methionine residue encoded by the initiation codon of an ORF, or the proteolytic cleavage of a signal peptide or leader sequence. Thus a mature form arising from a precursor polypeptide or protein that has residues 1 to N, where residue 1 is the N-terminal methionine, would have residues 2 through N remaining after removal of the N-terminal methionine. Alternatively, a mature form arising from a precursor polypeptide or protein having residues 1 to N, in which an N-terminal signal sequence from residue 1 to residue M is cleaved, would have the residues from residue M+1 to residue N remaining. Further as used herein, a “mature” form of a polypeptide or protein may arise from a step of post-translational modification other than a proteolytic cleavage event. Such additional processes include, by way of non-limiting example, glycosylation, myristylation or phosphorylation. In general, a mature polypeptide or protein may result from the operation of only one of these processes, or a combination of any of them.

[0055] The term “probe”, as utilized herein, refers to nucleic acid sequences of variable length, preferably between at least about 10 nucleotides (nt), about 100 nt, or as manly as approximately, e.g., 6,000 nt, depending upon the specific use. Probes are used in the detection of identical, similar, or complementary nucleic acid sequences. Longer length probes are generally obtained from a natural or recombinant source, are highly specific, and much slower to hybridize than shorter-length oligomer probes. Probes may be single-stranded or double-stranded and designed to have specificity in PCR, membrane-based hybridization technologies, or ELISA-like technologies.

[0056] The term “isolated” nucleic acid molecule, as used herein, is a nucleic acid that is separated from other nucleic acid molecules which are present in the natural source of the nucleic acid. Preferably, an “isolated” nucleic acid is free of sequences which naturally flank the nucleic acid (i.e., sequences located at the 5′- and 3′-termini of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For example, in various embodiments, the isolated NOVX nucleic acid molecules can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb or 0.1 kb of nucleotide sequences which naturally flank the nucleic acid molecule in genomic DNA of the cell/tissue from which the nucleic acid is derived (e.g., brain, heart, liver, spleen, etc.). Moreover, an “isolated” nucleic acid molecule, such as a cDNA molecule, can be substantially free of other cellular material, or culture medium, or of chemical precursors or other chemicals.

[0057] A nucleic acid molecule of the invention, e.g., a nucleic acid molecule having the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or a complement of this nucleotide sequence, can be isolated using standard molecular biology techniques and the sequence information provided herein. Using all or a portion of the nucleic acid sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, as a hybridization probe, NOVX molecules can be isolated using standard hybridization and cloning techniques (e.g., as described in Sambrook, et al., (eds.), MOLECULAR CLONING: A LABORATORY MANUAL 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989; and Ausubel, et al., (eds.), CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, New York, N.Y., 1993.)

[0058] A nucleic acid of the invention can be amplified using cDNA, mRNA or alternatively, genomic DNA, as a template with appropriate oligonucleotide primers according to standard PCR amplification techniques. The nucleic acid so amplified can be cloned into an appropriate vector and characterized by DNA sequence analysis. Furthermore, oligonucleotides corresponding to NOVX nucleotide sequences can be prepared by standard synthetic techniques, e.g., using an automated DNA synthesizer.

[0059] As used herein, the term “oligonucleotide” refers to a series of linked nucleotide residues. A short oligonucleotide sequence may be based on, or designed from, a genomic or cDNA sequence and is used to amplify, confirm, or reveal the presence of an identical, similar or complementary DNA or RNA in a particular cell or tissue. Oligonucleotides comprise a nucleic acid sequence having about 10 nt, 50 nt, or 100 nt in length, preferably about 15 nt to 30 nt in length. In one embodiment of the invention, an oligonucleotide comprising a nucleic acid molecule less than 100 nt in length would further comprise at least 6 contiguous nucleotides of SEQ ID NO:2n−1, wherein ii is an integer between 1 and 107, or a complement thereof. Oligonucleotides may be chemically synthesized and may also be used as probes.

[0060] In another embodiment, an isolated nucleic acid molecule of the invention comprises a nucleic acid molecule that is a complement of the nucleotide sequence shown in SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or a portion of this nucleotide sequence (e.g., a fragment that can be used as a probe or primer or a fragment encoding a biologically-active portion of a NOVX polypeptide). A nucleic acid molecule that is complementary to the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, is one that is sufficiently complementary to the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, that it can hydrogen bond with few or no mismatches to the nucleotide sequence shown in SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, thereby forming a stable duplex.

[0061] As used herein, the term “complementary” refers to Watson-Crick or Hoogsteen base pairing between nucleotides units of a nucleic acid molecule, and the term “binding” means the physical or chemical interaction between two polypeptides or compounds or associated polypeptides or compounds or combinations thereof. Binding includes ionic, non-ionic, van der Waals, hydrophobic interactions, and the like. A physical interaction can be either direct or indirect. Indirect interactions may be through or due to the effects of another polypeptide or compound. Direct binding refers to interactions that do not take place through, or due to, the effect of another polypeptide or compound, but instead are without other substantial chemical intermediates.

[0062] A “fragment” provided herein is defined as a sequence of at least 6 (contiguous) nucleic acids or at least 4 (contiguous) amino acids, a length sufficient to allow for specific hybridization in the case of nucleic acids or for specific recognition of an epitope in the case of amino acids, and is at most some portion less than a full length sequence. Fragments may be derived from any contiguous portion of a nucleic acid or amino acid sequence of choice.

[0063] A full-length NOVX clone is identified as containing an ATG translation start codon and an in-frame stop codon. Any disclosed NOVX nucleotide sequence lacking an ATG start codon therefore encodes a truncated C-terminal fragment of the respective NOVX polypeptide, and requires that the corresponding full-length cDNA extend in the 5′ direction of the disclosed sequence. Any disclosed NOVX nucleotide sequence lacking an in-frame stop codon similarly encodes a truncated N-terminal fragment of the respective NOVX polypeptide, and requires that the corresponding full-length cDNA extend in the 3′ direction of the disclosed sequence.

[0064] A “derivative” is a nucleic acid sequence or amino acid sequence formed from the native compounds either directly, by modification or partial substitution. An “analog” is a nucleic acid sequence or amino acid sequence that has a structure similar to, but not identical to, the native compound, e.g. they differs from it in respect to certain components or side chains. Analogs may be synthetic or derived from a different evolutionary origin and may have a similar or opposite metabolic activity compared to wild type. A “homolog” is a nucleic acid sequence or amino acid sequence of a particular gene that is derived from different species.

[0065] Derivatives and analogs may be full length or other than full length. Derivatives or analogs of the nucleic acids or proteins of the invention include, but are not limited to, molecules comprising regions that are substantially homologous to the nucleic acids or proteins of the invention, in various embodiments, by at least about 70%, 80%, or 95% identity (with a preferred identity of 80-95%) over a nucleic acid or amino acid sequence of identical size or when compared to an aligned sequence in which the alignment is done by a computer homology program known in the art, or whose encoding nucleic acid is capable of hybridizing to the complement of a sequence encoding the proteins under stringent, moderately stringent, or low stringent conditions. See e.g. Ausubel, et al., CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, New York, N.Y., 1993, and below.

[0066] A “homologous nucleic acid sequence” or “homologous amino acid sequence,” or variations thereof, refer to sequences characterized by a homology at the nucleotide level or amino acid level as discussed above. Homologous nucleotide sequences include those sequences coding for isoforms of NOVX polypeptides. Isoforms can be expressed in different tissues of the same organism as a result of, for example, alternative splicing of RNA. Alternatively, isoforms can be encoded by different genes. In the invention, homologous nucleotide sequences include nucleotide sequences encoding for a NOVX polypeptide of species other than humans, including, but not limited to: vertebrates, and thus can include, e.g., frog, mouse, rat, rabbit, dog, cat cow, horse, and other organisms. Homologous nucleotide sequences also include, but are not limited to, naturally occurring allelic variations and mutations of the nucleotide sequences set forth herein. A homologous nucleotide sequence does not, however, include the exact nucleotide sequence encoding human NOVX protein. Homologous nucleic acid sequences include those nucleic acid sequences that encode conservative amino acid substitutions (see below) in SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, as well as a polypeptide possessing NOVX biological activity. Various biological activities of the NOVX proteins are described below.

[0067] A NOVX polypeptide is encoded by the open reading frame (“ORF”) of a NOVX nucleic acid. An ORF corresponds to a nucleotide sequence that could potentially be translated into a polypeptide. A stretch of nucleic acids comprising an ORF is uninterrupted by a stop codon. An ORF that represents the coding sequence for a full protein begins with an ATG “start” codon and terminates with one of the three “stop” codons, namely, TAA, TAG, or TGA. For the purposes of this invention, an ORF may be any part of a coding sequence, with or without a start codon, a stop codon, or both. For an ORF to be considered as a good candidate for coding for a bonafide cellular protein, a minimum size requirement is often set, e.g., a stretch of DNA that would encode a protein of 50 amino acids or more.

[0068] The nucleotide sequences determined from the cloning of the human NOVX genes allows for the generation of probes and primers designed for use in identifying and/or cloning NOVX homologues in other cell types, e.g. from other tissues, as well as NOVX homologues from other vertebrates. The probe/primer typically comprises substantially purified oligonucleotide. The oligonucleotide typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least about 12, 25, 50, 100, 150, 200, 250, 300, 350 or 400 consecutive sense strand nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107; or an anti-sense strand nucleotide sequence of SEQ ID NO:2n−1, wherein it is an integer between 1 and 107; or of a naturally occurring mutant of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107.

[0069] Probes based on the human NOVX nucleotide sequences can be used to detect transcripts or genomic sequences encoding the same or homologous proteins. In various embodiments, the probe has a detectable label attached, e.g. the label can be a radioisotope, a fluorescent compound, an enzyme, or an enzyme co-factor. Such probes can be used as a part of a diagnostic test kit for identifying cells or tissues which mis-express a NOVX protein, such as by measuring a level of a NOVX-encoding nucleic acid in a sample of cells from a subject e.g., detecting NOVX mRNA levels or determining whether a genomic NOVX gene has been mutated or deleted.

[0070] “A polypeptide having a biologically-active portion of a NOVX polypeptide” refers to polypeptides exhibiting activity similar, but not necessarily identical to, an activity of a polypeptide of the invention, including mature forms, as measured in a particular biological assay, with or without dose dependency. A nucleic acid fragment encoding a “biologically-active portion of NOVX” can be prepared by isolating a portion of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, that encodes a polypeptide having a NOVX biological activity (the biological activities of the NOVX proteins are described below), expressing the encoded portion of NOVX protein (e.g., by recombinant expression in vitro) and assessing the activity of the encoded portion of NOVX.

[0071] NOVX Nucleic Acid and Polypeptide Variants

[0072] The invention further encompasses nucleic acid molecules that differ from the nucleotide sequences of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, due to degeneracy of the genetic code and thus encode the same NOVX proteins as that encoded by the nucleotide sequences of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107. In another embodiment, an isolated nucleic acid molecule of the invention has a nucleotide sequence encoding a protein having an amino acid sequence of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

[0073] In addition to the human NOVX nucleotide sequences of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, it will be appreciated by those skilled in the art that DNA sequence polymorphisms that lead to changes in the amino acid sequences of the NOVX polypeptides may exist within a population (e.g., the human population). Such genetic polymorphism in the NOVX genes may exist among individuals within a population due to natural allelic variation. As used herein, the terms “gene” and “recombinant gene” refer to nucleic acid molecules comprising an open reading frame (ORF) encoding a NOVX protein, preferably a vertebrate NOVX protein. Such natural allelic variations can typically result in 1-5% variance in the nucleotide sequence of the NOVX genes. Any and all such nucleotide variations and resulting amino acid polymorphisms in the NOVX polypeptides, which are the result of natural allelic variation and that do not alter the functional activity of the NOVX polypeptides, are intended to be within the scope of the invention.

[0074] Moreover, nucleic acid molecules encoding NOVX proteins from other species, and thus that have a nucleotide sequence that differs from a human SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, are intended to be within the scope of the invention. Nucleic acid molecules corresponding to natural allelic variants and homologues of the NOVX cDNAs of the invention can be isolated based on their homology to the human NOVX nucleic acids disclosed herein using the human cDNAs, or a portion thereof, as a hybridization probe according to standard hybridization techniques under stringent hybridization conditions.

[0075] Accordingly, in another embodiment, an isolated nucleic acid molecule of the invention is at least 6 nucleotides in length and hybridizes under stringent conditions to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107. In another embodiment, the nucleic acid is at least 10, 25, 50, 100, 250, 500, 750, 1000, 1500, or 2000 or more nucleotides in length. In yet another embodiment, an isolated nucleic acid molecule of the invention hybridizes to the coding region. As used herein, the term “hybridizes under stringent conditions” is intended to describe conditions for hybridization and washing under which nucleotide sequences at least about 65% homologous to each other typically remain hybridized to each other.

[0076] Homologs (i.e., nucleic acids encoding NOVX proteins derived from species other than human) or other related sequences (e.g., paralogs) can be obtained by low, moderate or high stringency hybridization with all or a portion of the particular human sequence as a probe using methods well known in the art for nucleic acid hybridization and cloning.

[0077] As used herein, the phrase “stringent hybridization conditions” refers to conditions under which a probe, primer or oligonucleotide will hybridize to its target sequence, but to no other sequences. Stringent conditions are sequence-dependent and will be different in different circumstances. Longer sequences hybridize specifically at higher temperatures than shorter sequences. Generally, stringent conditions are selected to be about 5° C. lower than the thermal melting point (Tm) for the specific sequence at a defined ionic strength and pH. The Tm is the temperature (under defined ionic strength, pH and nucleic acid concentration) at which 50% of the probes complementary to the target sequence hybridize to the target sequence at equilibrium. Since the target sequences are generally present at excess, at Tm, 50% of the probes are occupied at equilibrium. Typically, stringent conditions will be those in which the salt concentration is less than about 1.0 M sodium ion, typically about 0.01 to 1.0 M sodium ion (or other salts) at pH 7.0 to 8.3 and the temperature is at least about 30° C. for short probes, primers or oligonucleotides (e.g., 10 nt to 50 nt) and at least about 60° C. for longer probes, primers and oligonucleotides. Stringent conditions may also be achieved with the addition of destabilizing agents, such as formamide.

[0078] Stringent conditions are known to those skilled in the art and can be found in Ausubel, et al., (eds.), CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, N.Y. (1989), 6.3.1-6.3.6. Preferably, the conditions are such that sequences at least about 65%, 70%, 75%, 85%, 90%, 95%, 98%, or 99% homologous to each other typically remain hybridized to each other. A non-limiting example of stringent hybridization conditions are hybridization in a high salt buffer comprising 6×SSC, 50 mM Tris-HCl (pH 7.5), 1 mM EDTA, 0.02% PVP, 0.02% Ficoll, 0.02% BSA, and 500 mg/ml denatured salmon sperm DNA at 65° C., followed by one or more washes in 0.2×SSC, 0.01% BSA at 50° C. An isolated nucleic acid molecule of the invention that hybridizes under stringent conditions to a sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, corresponds to a naturally-occurring nucleic acid molecule. As used herein, a “naturally-occurring” nucleic acid molecule refers to an RNA or DNA molecule having a nucleotide sequence that occurs in nature (e.g., encodes a natural protein).

[0079] In a second embodiment, a nucleic acid sequence that is hybridizable to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or fragments, analogs or derivatives thereof, under conditions of moderate stringency is provided. A non-limiting example of moderate stringency hybridization conditions are hybridization in 6×SSC, 5×Reinhardt's solution, 0.5% SDS and 100 mg/ml denatured salmon sperm DNA at 55° C., followed by one or more washes in 1×SSC, 0.1% SDS at 37° C. Other conditions of moderate stringency that may be used are well-known within the art. See, e.g., Ausubel, et al. (eds.), 1993, CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, NY, and Krieger, 1990; GENE TRANSFER AND EXPRESSION, A LABORATORY MANUAL, Stockton Press, NY.

[0080] In a third embodiment, a nucleic acid that is hybridizable to the nucleic acid molecule comprising the nucleotide sequences of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or fragments, analogs or derivatives thereof, under conditions of low stringency, is provided. A non-limiting example of low stringency hybridization conditions are hybridization in 35% formamide, 5×SSC, 50 mM Tris-HCl (pH 7.5), 5 mM EDTA, 0.02% PVP, 0.02% Ficoll, 0.2% BSA, 100 mg/ml denatured salmon sperm DNA, 10% (wt/vol) dextran sulfate at 40° C., followed by one or more washes in 2×SSC, 25 mM Tris-HCl (pH 7.4), 5 mM EDTA, and 0.1% SDS at 50° C. Other conditions of low stringency that may be used are well known in the art (e.g., as employed for cross-species hybridizations). See, e.g., Ausubel, et al. (eds.), 1993, CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, NY, and Kriegler, 1990, GENE TRANSFER AND EXPRESSION, A LABORATORY MANUAL, Stockton Press, NY; Shilo and Weinberg, 1981. Proc Natl Acad Sci USA 78: 6789-6792.

[0081] Conservative Mutations

[0082] In addition to naturally-occurring allelic variants of NOVX sequences that may exist in the population, the skilled artisan will further appreciate that changes can be introduced by mutation into the nucleotide sequences of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, thereby leading to changes in the amino acid sequences of the encoded NOVX protein, without altering the functional ability of that NOVX protein. For example, nucleotide substitutions leading to amino acid substitutions at “non-essential” amino acid residues can be made in the sequence of SEQ ID NO:2n, wherein n is an integer between 1 and 107. A “non-essential” amino acid residue is a residue that can be altered from the wild-type sequences of the NOVX proteins without altering their biological activity, whereas an “essential” amino acid residue is required for such biological activity. For example, amino acid residues that are conserved among the NOVX proteins of the invention are predicted to be particularly non-amenable to alteration. Amino acids for which conservative substitutions can be made are well-known within the art.

[0083] Another aspect of the invention pertains to nucleic acid molecules encoding NOVX proteins that contain changes in amino acid residues that are not essential for activity. Such NOVX proteins differ in amino acid sequence from SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, yet retain biological activity. In one embodiment, the isolated nucleic acid molecule comprises a nucleotide sequence encoding a protein, wherein the protein comprises an amino acid sequence at least about 40% homologous to the amino acid sequences of SEQ ID NO:2n, wherein n is an integer between 1 and 107. Preferably, the protein encoded by the nucleic acid molecule is at least about 60% homologous to SEQ ID NO:2n, wherein n is an integer between 1 and 107; more preferably at least about 70% homologous to SEQ ID NO:2n, wherein n is an integer between 1 and 107; still more preferably at least about 80% homologous to SEQ ID NO:2n, wherein n is an integer between 1 and 107; even more preferably at least about 90% homologous to SEQ ID NO:2n, wherein n is an integer between 1 and 107; and most preferably at least about 95% homologous to SEQ ID NO:2n, wherein n is an integer between 1 and 107.

[0084] An isolated nucleic acid molecule encoding a NOVX protein homologous to the protein of SEQ ID NO:2n, wherein n is an integer between 1 and 107, can be created by introducing one or more nucleotide substitutions, additions or deletions into the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, such that one or more amino acid substitutions, additions or deletions are introduced into the encoded protein.

[0085] Mutations can be introduced any one of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, by standard techniques, such as site-directed mutagenesis and PCR-mediated mutagenesis. Preferably, conservative amino acid substitutions are made at one or more predicted, non-essential amino acid residues. A “conservative amino acid substitution” is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined within the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). Thus, a predicted non-essential amino acid residue in the NOVX protein is replaced with another amino acid residue from the same side chain family. Alternatively, in another embodiment, mutations can be introduced randomly along all or part of a NOVX coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for NOVX biological activity to identify mutants that retain activity. Following mutagenesis of a nucleic acid of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, the encoded protein can be expressed by any recombinant technology known in the art and the activity of the protein can be determined.

[0086] The relatedness of amino acid families may also be determined based on side chain interactions. Substituted amino acids may be fully conserved “strong” residues or fully conserved “weak” residues. The “strong” group of conserved amino acid residues may be any one of the following groups: STA, NEQK, NHQK, NDEQ, QHRK, MILV, MILF, HY, FYW, wherein the single letter amino acid codes are grouped by those amino acids that may be substituted for each other. Likewise, the “weak” group of conserved residues may be any one of the following: CSA, ATV, SAG, STNK, STPA, SGND, SNDEQK, NDEQHK, NEQHRK, HFY, wherein the letters within each group represent the single letter amino acid code.

[0087] In one embodiment, a mutant NOVX protein can be assayed for (i) the ability to form protein:protein interactions with other NOVX proteins, other cell-surface proteins, or biologically-active portions thereof, (ii) complex formation between a mutant NOVX protein and a NOVX ligand; or (iii) the ability of a mutant NOVX protein to bind to an intracellular target protein or biologically-active portion thereof; (e.g. avidin proteins).

[0088] In yet another embodiment, a mutant NOVX protein can be assayed for the ability to regulate a specific biological function (e.g., regulation of insulin release).

[0089] Interfering RNA

[0090] In one aspect of the invention, NOVX gene expression can be attenuated by RNA interference. One approach well-known in the art is short interfering RNA (siRNA) mediated gene silencing where expression products of a NOVX gene are targeted by specific double stranded NOVX derived siRNA nucleotide sequences that are complementary to at least a 19-25 nt long segment of the NOVX gene transcript, including the 5′ untranslated (UT) region, the ORF, or the 3′ UT region. See, e.g., PCT applications WO00/44895, WO99/32619, WO01/75164, WO01/92513, WO 01/29058, WO01/89304, WO02/16620, and WO02/29858, each incorporated by reference herein in their entirety. Targeted genes can be a NOVX gene, or an upstream or downstream modulator of the NOVX gene. Nonlimiting examples of upstream or downstream modulators of a NOVX gene include, e.g., a transcription factor that binds the NOVX gene promoter, a kinase or phosphatase that interacts with a NOVX polypeptide, and polypeptides involved in a NOVX regulatory pathway.

[0091] According to the methods of the present invention, NOVX gene expression is silenced using short interfering RNA. A NOVX polynucleotide according to the invention includes a siRNA polynucleotide. Such a NOVX siRNA can be obtained using a NOVX polynucleotide sequence, for example, by processing the NOVX ribopolynucleotide sequence in a cell-free system, such as but not limited to a Drosophila extract, or by transcription of recombinant double stranded NOVX RNA or by chemical synthesis of nucleotide sequences homologous to a NOVX sequence. See, e.g., Tuschl, Zamore, Lehmann, Bartel and Sharp (1999), Genes & Dev. 13: 3191-3197, incorporated herein by reference in its entirety. When synthesized, a typical 0.2 micromolar-scale RNA synthesis provides about 1 milligram of siRNA, which is sufficient for 1000 transfection experiments using a 24-well tissue culture plate format.

[0092] The most efficient silencing is generally observed with siRNA duplexes composed of a 21-nt sense strand and a 21-nt antisense strand, paired in a manner to have a 2-nt 3′ overhang. The sequence of the 2-nt 3′ overhang makes an additional small contribution to the specificity of siRNA target recognition. The contribution to specificity is localized to the unpaired nucleotide adjacent to the first paired bases. In one embodiment, the nucleotides in the 3′ overhang are ribonucleotides. In an alternative embodiment, the nucleotides in the 3′ overhang are deoxyribonucleotides. Using 2′-deoxyribonucleotides in the 3′ overhangs is as efficient as using ribonucleotides, but deoxyribonucleotides are often cheaper to synthesize and are most likely more nuclease resistant.

[0093] A contemplated recombinant expression vector of the invention comprises a NOVX DNA molecule cloned into an expression vector comprising operatively-linked regulatory sequences flanking the NOVX sequence in a manner that allows for expression (by transcription of the DNA molecule) of both strands. An RNA molecule that is antisense to NOVX mRNA is transcribed by a first promoter (e.g., a promoter sequence 3′ of the cloned DNA) and an RNA molecule that is the sense strand for the NOVX mRNA is transcribed by a second promoter (e.g., a promoter sequence 5′ of the cloned DNA). The sense and antisense strands may hybridize in vivo to generate siRNA constructs for silencing of the NOVX gene. Alternatively, two constructs can be utilized to create the sense and anti-sense strands of a siRNA construct. Finally, cloned DNA can encode a construct having secondary structure, wherein a single transcript has both the sense and complementary antisense sequences from the target gene or genes. In an example of this embodiment, a hairpin RNAi product is homologous to all or a portion of the target gene. In another example, a hairpin RNAi product is a siRNA. The regulatory sequences flanking the NOVX sequence may be identical or may be different, such that their expression may be modulated independently, or in a temporal or spatial manner.

[0094] In a specific embodiment, siRNAs are transcribed intracellularly by cloning the NOVX gene templates into a vector containing, e.g., a RNA pol III transcription unit from the smaller nuclear RNA (snRNA) U6 or the human RNase P RNA HI. One example of a vector system is the GeneSuppressorm RNA Interference kit (commercially available from Imgenex). The U6 and H1 promoters are members of the type III class of Pol HII promoters. The +1 nucleotide of the U6-like promoters is always guanosine, whereas the +1 for H1 promoters is adenosine. The termination signal for these promoters is defined by five consecutive thymidines. The transcript is typically cleaved after the second uridine. Cleavage at this position generates a 3′ UU overhang in the expressed siRNA, which is similar to the 3′ overhangs of synthetic siRNAs. Any sequence less than 400 nucleotides in length can be transcribed by these promoter, therefore they are ideally suited for the expression of around 21-nucleotide siRNAs in, e.g., an approximately 50-nucleotide RNA stem-loop transcript.

[0095] A siRNA vector appears to have an advantage over synthetic siRNAs where long term knock-down of expression is desired. Cells transfected with a siRNA expression vector would experience steady, long-term mRNA inhibition. In contrast, cells transfected with exogenous synthetic siRNAs typically recover from mRNA suppression within seven days or ten rounds of cell division. The long-term gene silencing ability of siRNA expression vectors may provide for applications in gene therapy.

[0096] In general, siRNAs are chopped from longer dsRNA by an ATP-dependent ribonuclease called DICER. DICER is a member of the RNase III family of double-stranded RNA-specific endonucleases. The siRNAs assemble with cellular proteins into an endonuclease complex. In vitro studies in Drosophila suggest that the siRNAs/protein complex (siRNP) is then transferred to a second enzyme complex, called an RNA-induced silencing complex (RISC), which contains an endoribonuclease that is distinct from DICER. RISC uses the sequence encoded by the antisense siRNA strand to find and destroy mRNAs of complementary sequence. The siRNA thus acts as a guide, restricting the ribonuclease to cleave only mRNAs complementary to one of the two siRNA strands.

[0097] A NOVX mRNA region to be targeted by siRNA is generally selected from a desired NOVX sequence beginning 50 to 100 nt downstream of the start codon. Alternatively, 5′ or 3′ UTRs and regions nearby the start codon can be used but are generally avoided, as these may be richer in regulatory protein binding sites. UTR-binding proteins and/or translation initiation complexes may interfere with binding of the siRNP or RISC endonuclease complex. An initial BLAST homology search for the selected siRNA sequence is done against an available nucleotide sequence library to ensure that only one gene is targeted. Specificity of target recognition by siRNA duplexes indicate that a single point mutation located in the paired region of an siRNA duplex is sufficient to abolish target mRNA degradation. See, Elbashir et al. 2001 EMBO J. 20(23):6877-88. Hence, consideration should be taken to accommodate SNPs, polymorphisms, allelic variants or species-specific variations when targeting a desired gene.

[0098] In one embodiment, a complete NOVX siRNA experiment includes the proper negative control. A negative control siRNA generally has the same nucleotide composition as the NOVX siRNA but lack significant sequence homology to the genome. Typically, one would scramble the nucleotide sequence of the NOVX siRNA and do a homology search to make sure it lacks homology to any other gene.

[0099] Two independent NOVX siRNA duplexes can be used to knock-down a target NOVX gene. This helps to control for specificity of the silencing effect. In addition, expression of two independent genes can be simultaneously knocked down by using equal concentrations of different NOVX siRNA duplexes, e.g., a NOVX siRNA and an siRNA for a regulator of a NOVX gene or polypeptide. Availability of siRNA-associating proteins is believed to be more limiting than target mRNA accessibility.

[0100] A targeted NOVX region is typically a sequence of two adenines (AA) and two thymidines (TT) divided by a spacer region of nineteen (N19) residues (e.g., AA(N19)TT). A desirable spacer region has a G/C-content of approximately 30% to 70%, and more preferably of about 50%. If the sequence AA(N19)TT is not present in the target sequence, an alternative target region would be AA(N21). The sequence of the NOVX sense siRNA corresponds to (N19)TT or N21, respectively. In the latter case, conversion of the 3′ end of the sense siRNA to TT can be performed if such a sequence does not naturally occur in the NOVX polynucleotide. The rationale for this sequence conversion is to generate a symmetric duplex with respect to the sequence composition of the sense and antisense 3′ overhangs. Symmetric 3′ overhangs may help to ensure that the siRNPs are formed with approximately equal ratios of sense and antisense target RNA-cleaving siRNPs. See, e.g., Elbashir, Lendeckel and Tuschl (2001). Genes & Dev. 15: 188-200, incorporated by reference herein in its entirely. The modification of the overhang of the sense sequence of the siRNA duplex is not expected to affect targeted mRNA recognition, as the antisense siRNA strand guides target recognition.

[0101] Alternatively, if the NOVX target mRNA does not contain a suitable AA(N21) sequence, one may search for the sequence NA(N21). Further, the sequence of the sense strand and antisense strand may still be synthesized as 5′ (N19)TT, as it is believed that the sequence of the 3′-most nucleotide of the antisense siRNA does not contribute to specificity. Unlike antisense or ribozyme technology, the secondary structure of the target mRNA does not appear to have a strong effect on silencing. See, Harborth, et al. (2001) J. Cell Science 114: 4557-4565, incorporated by reference in its entirety.

[0102] Transfection of NOVX siRNA duplexes can be achieved using standard nucleic acid transfection methods, for example, OLIGOFECTAMINE Reagent (commercially available from Invitrogen). An assay for NOVX gene silencing is generally performed approximately 2 days after transfection. No NOVX gene silencing has been observed in the absence of transfection reagent, allowing for a comparative analysis of the wild-type and silenced NOVX phenotypes. In a specific embodiment, for one well of a 24-well plate, approximately 0.84 μg of the siRNA duplex is generally sufficient. Cells are typically seeded the previous day, and are transfected at about 50% confluence. The choice of cell culture media and conditions are routine to those of skill in the art, and will vary with the choice of cell type. The efficiency of transfection may depend on the cell type, but also on the passage number and the confluency of the cells. The time and the manner of formation of siRNA-liposome complexes (e.g. inversion versus vortexing) are also critical. Low transfection efficiencies are the most frequent cause of unsuccessful NOVX silencing. The efficiency of transfection needs to be carefully examined for each new cell line to be used. Preferred cell are derived from a mammal, more preferably from a rodent such as a rat or mouse, and most preferably from a human. Where used for therapeutic treatment, the cells are preferentially autologous, although non-autologous cell sources are also contemplated as within the scope of the present invention.

[0103] For a control experiment, transfection of 0.84 μg single-stranded sense NOVX siRNA will have no effect on NOVX silencing, and 0.84 μg antisense siRNA has a weak silencing effect when compared to 0.84 μg of duplex siRNAs. Control experiments again allow for a comparative analysis of the wild-type and silenced NOVX phenotypes. To control for transfection efficiency, targeting of common proteins is typically performed, for example targeting of lamin A/C or transfection of a CMV-driven EGFP-expression plasmid (e.g. commercially available from Clontech). In the above example, a determination of the fraction of lamin A/C knockdown in cells is determined the next day by such techniques as immunofluorescence, Western blot, Northern blot or other similar assays for protein expression or gene expression. Lamin A/C monoclonal antibodies may be obtained from Santa Cruz Biotechnology.

[0104] Depending on the abundance and the half life (or turnover) of the targeted NOVX polynucleotide in a cell, a knock-down phenotype may become apparent after 1 to 3 days, or even later. In cases where no NOVX knock-down phenotype is observed, depletion of the NOVX polynucleotide may be observed by immunofluorescence or Western blotting. If the NOVX polynucleotide is still abundant after 3 days, cells need to be split and transferred to a fresh 24-well plate for re-transfection. If no knock-down of the targeted protein is observed, it may be desirable to analyze whether the target mRNA (NOVX or a NOVX upstream or downstream gene) was effectively destroyed by the transfected siRNA duplex. Two days after transfection, total RNA is prepared, reverse transcribed using a target-specific primer, and PCR-amplified with a primer pair covering at least one exon-exon junction in order to control for amplification of pre-mRNAs. RT/PCR of a non-targeted mRNA is also needed as control. Effective depletion of the mRNA yet undetectable reduction of target protein may indicate that a large reservoir of stable NOVX protein may exist in the cell. Multiple transfection in sufficiently long intervals may be necessary until the target protein is finally depleted to a point where a phenotype may become apparent. If multiple transfection steps are required, cells are split 2 to 3 days after transfection. The cells may be transfected immediately after splitting.

[0105] An inventive therapeutic method of the invention contemplates administering a NOVX siRNA construct as therapy to compensate for increased or aberrant NOVX expression or activity. The NOVX ribopolynucleotide is obtained and processed into siRNA fragments, or a NOVX siRNA is synthesized, as described above. The NOVX siRNA is administered to cells or tissues using known nucleic acid transfection techniques, as described above. A NOVX siRNA specific for a NOVX gene will decrease or knockdown NOVX transcription products, which will lead to reduced NOVX polypeptide production, resulting in reduced NOVX polypeptide activity in the cells or tissues.

[0106] The present invention also encompasses a method of treating a disease or condition associated with the presence of a NOVX protein in an individual comprising administering to the individual an RNAi construct that targets the mRNA of the protein (the mRNA that encodes the protein) for degradation. A specific RNAi construct includes a siRNA or a double stranded gene transcript that is processed into siRNAs. Upon treatment, the target protein is not produced or is not produced to the extent it would be in the absence of the treatment.

[0107] Where the NOVX gene function is not correlated with a known phenotype, a control sample of cells or tissues from healthy individuals provides a reference standard for determining NOVX expression levels. Expression levels are detected using the assays described, e.g., RT-PCR, Northern blotting, Western blotting, ELISA, and the like. A subject sample of cells or tissues is taken from a mammal, preferably a human subject, suffering from a disease state. The NOVX ribopolynucleotide is used to produce siRNA constructs, that are specific for the NOVX gene product. These cells or tissues are treated by administering NOVX siRNA's to the cells or tissues by methods described for the transfection of nucleic acids into a cell or tissue, and a change in NOVX polypeptide or polynucleotide expression is observed in the subject sample relative to the control sample, using the assays described. This NOVX gene knockdown approach provides a rapid method for determination of a NOVX minus (NOVX−) phenotype in the treated subject sample. The NOVX− phenotype observed in the treated subject sample thus serves as a marker for monitoring the course of a disease state during treatment.

[0108] In specific embodiments, a NOVX siRNA is used in therapy. Methods for the generation and use of a NOVX siRNA are known to those skilled in the art. Example techniques are provided below.

[0109] Production of RNAs

[0110] Sense RNA (ssRNA) and antisense RNA (asRNA) of NOVX are produced using known methods such as transcription in RNA expression vectors. In the initial experiments, the sense and antisense RNA are about 500 bases in length each. The produced ssRNA and asRNA (0.5 μM) in 10 mM Tris-HCl (pH 7.5) with 20 mM NaCl were heated to 950 C for 1 min then cooled and annealed at room temperature for 12 to 16 h. The RNAs are precipitated and resuspended in lysis buffer (below). To monitor annealing, RNAs are electrophoresed in a 2% agarose gel in TBE buffer and stained with ethidium bromide. See, e.g., Sambrook et al., Molecular Cloning. Cold Spring Harbor Laboratory Press, Plainview, N.Y. (1989).

[0111] Lysate Preparation

[0112] Untreated rabbit reticulocyte lysate (Ambion) are assembled according to the manufacturer's directions. dsRNA is incubated in the lysate at 30° C. for 10 min prior to the addition of mRNAs. Then NOVX mRNAs are added and the incubation continued for an additional 60 min. The molar ratio of double stranded RNA and mRNA is about 200:1. The NOVX mRNA is radiolabeled (using known techniques) and its stability is monitored by gel electrophoresis.

[0113] In a parallel experiment made with the same conditions, the double stranded RNA is internally radiolabeled with a 32P-ATP. Reactions are stopped by the addition of 2×proteinase K buffer and deproteinized as described previously (Tuschl et al., Genes Dev., 13:3191-3197 (1999)). Products are analyzed by electrophoresis in 15% or 18% polyacrylamide sequencing gels using appropriate RNA standards. By monitoring the gels for radioactivity, the natural production of 10 to 25 nt RNAs from the double stranded RNA can be determined.

[0114] The band of double stranded RNA, about 21-23 bps, is eluded. The efficacy of these 21-23 mers for suppressing NOVX transcription is assayed in vitro using the same rabbit reticulocyte assay described above using 50 nanomolar of double stranded 21-23 mer for each assay. The sequence of these 21-23 mers is then determined using standard nucleic acid sequencing techniques.

[0115] RNA Preparation

[0116] 21 nt RNAs, based on the sequence determined above, are chemically synthesized using Expedite RNA phosphoramidites and thymidine phosphoramidite (Proligo, Germany). Synthetic oligonucleotides are deprotected and gel-purified (Elbashir, Lendeckel, & Tuschl, Genes & Dev. 15, 188-200 (2001)), followed by Sep-Pak C18 cartridge (Waters, Milford, Mass., USA) purification (Tuschl, et al., Biochemistry, 32:11658-11668 (1993)).

[0117] These RNAs (20 μM) single strands are incubated in annealing buffer (100 mM potassium acetate, 30 mM HEPES-KOH at pH 7.4, 2 mM magnesium acetate) for 1 min at 90° C. followed by 1 h at 370 C.

[0118] Cell Culture

[0119] A cell culture known in the art to regularly express NOVX is propagated using standard conditions. 24 hours before transfection, at approx. 80% confluency, the cells are trypsinized and diluted 1:5 with fresh medium without antibiotics (1-3×105 cells/ml) and transferred to 24-well plates (500 ml/well). Transfection is performed using a commercially available lipofection kit and NOVX expression is monitored using standard techniques with positive and negative control. A positive control is cells that naturally express NOVX while a negative control is cells that do not express NOVX. Base-paired 21 and 22 nt siRNAs with overhanging 3′ ends mediate efficient sequence-specific mRNA degradation in lysates and in cell culture. Different concentrations of siRNAs are used. An efficient concentration for suppression in vitro in mammalian culture is between 25 nM to 100 nM final concentration. This indicates that siRNAs are effective at concentrations that are several orders of magnitude below the concentrations applied in conventional antisense or ribozyme gene targeting experiments.

[0120] The above method provides a way both for the deduction of NOVX siRNA sequence and the use of such siRNA for in vitro suppression. In vivo suppression may be performed using the same siRNA using well known in vivo transfection or gene therapy transfection techniques.

[0121] Antisense Nucleic Acids

[0122] Another aspect of the invention pertains to isolated antisense nucleic acid molecules that are hybridizable to or complementary to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or fragments, analogs or derivatives thereof. An “antisense” nucleic acid comprises a nucleotide sequence that is complementary to a “sense” nucleic acid encoding a protein (e.g., complementary to the coding strand of a double-stranded cDNA molecule or complementary to an mRNA sequence). In specific aspects, antisense nucleic acid molecules are provided that comprise a sequence complementary to at least about 10, 25, 50, 100, 250 or 500 nucleotides or an entire NOVX coding strand, or to only a portion thereof. Nucleic acid molecules encoding fragments, homologs, derivatives and analogs of a NOVX protein of SEQ ID NO:2n, wherein n is an integer between 1 and 107, or antisense nucleic acids complementary to a NOVX nucleic acid sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, are additionally provided.

[0123] In one embodiment, an antisense nucleic acid molecule is antisense to a “coding region” of the coding strand of a nucleotide sequence encoding a NOVX protein. The term “coding region” refers to the region of the nucleotide sequence comprising codons which are translated into amino acid residues., In another embodiment, the antisense nucleic acid molecule is antisense to a “noncoding region” of the coding strand of a nucleotide sequence encoding the NOVX protein. The term “noncoding region” refers to 5′ and 3′ sequences which flank the coding region that are not translated into amino acids (i.e., also referred to as 5′ and 3′ untranslated regions).

[0124] Given the coding strand sequences encoding the NOVX protein disclosed herein, antisense nucleic acids of the invention can be designed according to the rules of Watson and Crick or Hoogsteen base pairing. The antisense nucleic acid molecule can be complementary to the entire coding region of NOVX mRNA, but more preferably is an oligonucleotide that is antisense to only a portion of the coding or noncoding region of NOVX mRNA. For example, the antisense oligonucleotide can be complementary to the region surrounding the translation start site of NOVX mRNA. An antisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50 nucleotides in length. An antisense nucleic acid of the invention can be constructed using chemical synthesis or enzymatic ligation reactions using procedures known in the art. For example, an antisense nucleic acid (e.g., an antisense oligonucleotide) can be chemically synthesized using naturally-occurring nucleotides or variously modified nucleotides designed to increase the biological stability of the molecules or to increase the physical stability of the duplex formed between the antisense and sense nucleic acids (e.g., phosphorothioate derivatives and acridine substituted nucleotides can be used).

[0125] Examples of modified nucleotides that can be used to generate the antisense nucleic acid include: 5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xanthine, 4-acetylcytosine, 5-carboxymethylaminomethyl-2-thiouridine, 5-(carboxyhydroxylmethyl) uracil, 5-carboxymethyl aminomethyluracil, dihydrouracil, beta-D-galactosylqueosine, inosine, N6-isopentenyladenine, 1-methylguanine, 1-methylinosine, 2,2-dimethylguanine, 2-methyladenine, 2-methylguanine, 5-methoxyuracil, 3-methylcytosine, 5-methylcytosine, N6-adenine, 7-methylguanine, 5-methylaminomethyluracil, 5-methoxyaminomethyl-2-thiouracil, 2-thiouracil, 4-thiouracil, beta-D-mannosylqueosine, 5′-methoxycarboxymethyluracil, 2-methylthio-N-6-isopentenyladenine, uracil-5-oxyacetic acid (v), wybutoxosine, pseudouracil, queosine, 2-thiocytosine, 5-methyl-2-thiouracil, 5-methyluracil, uracil-5-oxyacetic acid methylester, uracil-5-oxyacetic acid (v), 5-methyl-2-thiouracil, 3-(3-amino-3-N-2-carboxypropyl) uracil, (acp3)w, and 2,6-diaminopurine. Alternatively, the antisense nucleic acid can be produced biologically using an expression vector into which a nucleic acid has been subcloned in an antisense orientation (i.e., RNA transcribed from the inserted nucleic acid will be of an antisense orientation to a target nucleic acid of interest, described further in the following subsection).

[0126] The antisense nucleic acid molecules of the invention are typically administered to a subject or generated in situ such that they hybridize with or bind to cellular mRNA and/or genomic DNA encoding a NOVX protein to thereby inhibit expression of the protein (e.g., by inhibiting transcription and/or translation). The hybridization can be by conventional nucleotide complementarity to form a stable duplex, or, for example, in the case of an antisense nucleic acid molecule that binds to DNA duplexes, through specific interactions in the major groove of the double helix. An example of a route of administration of antisense nucleic acid molecules of the invention includes direct injection at a tissue site. Alternatively, antisense nucleic acid molecules can be modified to target selected cells and then administered systemically. For example, for systemic administration, antisense molecules can be modified such that they specifically bind to receptors or antigens expressed on a selected cell surface (e.g., by linking the antisense nucleic acid molecules to peptides or antibodies that bind to cell surface receptors or antigens). The antisense nucleic acid molecules can also be delivered to cells using the vectors described herein. To achieve sufficient nucleic acid molecules, vector constructs in which the antisense nucleic acid molecule is placed under the control of a strong pol 11 or pol III promoter are preferred.

[0127] In yet another embodiment, the antisense nucleic acid molecule of the invention is an α-anomeric nucleic acid molecule. An u.-anomeric nucleic acid molecule forms specific double-stranded hybrids with complementary RNA in which, contrary to the usual P-units, the strands run parallel to each other. See, e.g., Gaultier, et al., 1987. Nucl. Acids Res. 15: 6625-6641. The antisense nucleic acid molecule can also comprise a 2′-o-methylribonucleotide (See, e.g., Inoue, et al. 1987. Nucl. Acids Res. 15: 6131-6148) or a chimeric RNA-DNA analogue (See, e.g., Inoue, et al., 1987. FEBS Lett. 215: 327-330.

[0128] Ribozymes and PNA Moieties

[0129] Nucleic acid modifications include, by way of non-limiting example, modified bases, and nucleic acids whose sugar phosphate backbones are modified or derivatized. These modifications are carried out at least in part to enhance the chemical stability of the modified nucleic acid, such that they may be used, for example, as antisense binding nucleic acids in therapeutic applications in a subject.

[0130] In one embodiment, an antisense nucleic acid of the invention is a ribozyme. Ribozymes are catalytic RNA molecules with ribonuclease activity that are capable of cleaving a single-stranded nucleic acid, such as an mRNA, to which they have a complementary region. Thus, ribozymes (e.g., hammerhead ribozymes as described in Haselhoff and Gerlach 1988. Nature 334: 585-591) can be used to catalytically cleave NOVX mRNA transcripts to thereby inhibit translation of NOVX mRNA. A ribozyme having specificity for a NOVX-encoding nucleic acid can be designed based upon the nucleotide sequence of a NOVX cDNA disclosed herein (i.e., SEQ ID NO:2n−1, wherein n is an integer between 1 and 107). For example, a derivative of a Tetrahymena L-19 IVS RNA can be constructed in which the nucleotide sequence of the active site is complementary to the nucleotide sequence to be cleaved in a NOVX-encoding mRNA. See, e.g., U.S. Pat. No. 4,987,071 to Cech, et al. and U.S. Pat. No. 5,116,742 to Cech, et al. NOVX mRNA can also be used to select a catalytic RNA having a specific ribonuclease activity from a pool of RNA molecules. See, e.g., Bartel et al., (1993) Science 261:1411-1418.

[0131] Alternatively, NOVX gene expression can be inhibited by targeting nucleotide sequences complementary to the regulatory region of the NOVX nucleic acid (e.g., the NOVX promoter and/or enhancers) to form triple helical structures that prevent transcription of the NOVX gene in target cells. See, e.g., Helene, 1991. Anticancer Drug Des. 6: 569-84; Helene, et al. 1992. Ann. N.Y. Acad. Sci. 660: 27-36; Maher, 1992. Bioassays 14: 807-15.

[0132] In various embodiments, the NOVX nucleic acids can be modified at the base moiety, sugar moiety or phosphate backbone to improve, e.g., the stability, hybridization, or solubility of the molecule. For example, the deoxyribose phosphate backbone of the nucleic acids can be modified to generate peptide nucleic acids. See, e.g., Hyrup, et al., 1996. Bioorg Med Chem 4: 5-23. As used herein, the terms “peptide nucleic acids” or “PNAs” refer to nucleic acid mimics (e.g., DNA mimics) in which the deoxyribose phosphate backbone is replaced by a pseudopeptide backbone and only the four natural nucleotide bases are retained. The neutral backbone of PNAs has been shown to allow for specific hybridization to DNA and RNA under conditions of low ionic strength. The synthesis of PNA oligomer can be performed using standard solid phase peptide synthesis protocols as described in Hyrup, et al., 1996. supra; Perry-O'Keefe, et al., 1996. Proc. Natl. Acad. Sci. USA 93: 14670-14675.

[0133] PNAs of NOVX can be used in therapeutic and diagnostic applications. For example, PNAs can be used as antisense or antigene agents for sequence-specific modulation of gene expression by, e.g., inducing transcription or translation arrest or inhibiting replication. PNAs of NOVX can also be used, for example, in the analysis of single base pair mutations in a gene (e.g., PNA directed PCR clamping; as artificial restriction enzymes when used in combination with other enzymes, e.g., S1 nucleases (See, Hyrup, et al., 1996.supra); or as probes or primers for DNA sequence and hybridization (See, Hyrup, et al., 1996, supra; Perry-O'Keefe, et al., 1996. supra).

[0134] In another embodiment, PNAs of NOVX can be modified, e.g., to enhance their stability or cellular uptake, by attaching lipophilic or other helper groups to PNA, by the formation of PNA-DNA chimeras, or by the use of liposomes or other techniques of drug delivery known in the art. For example, PNA-DNA chimeras of NOVX can be generated that may combine the advantageous properties of PNA and DNA. Such chimeras allow DNA recognition enzymes (e.g., RNase H and DNA polymerases) to interact with the DNA portion while the PNA portion would provide high binding affinity and specificity. PNA-DNA chimeras can be linked using linkers of appropriate lengths selected in terms of base stacking, number of bonds between the nucleotide bases, and orientation (see, Hyrup, et al., 1996. supra). The synthesis of PNA-DNA chimeras can be performed as described in Hyrup, et al., 1996. supra and Finn, et al., 1996. Nucl Acids Res 24: 3357-3363. For example, a DNA chain can be synthesized on a solid support using standard phosphoramidite coupling chemistry, and modified nucleoside analogs, e.g., 5′-(4-methoxytrityl)amino-5′-deoxy-thymidine phosphoramidite, can be used between the PNA and the 5′ end of DNA. See, e.g., Mag, et al., 1989. Nucl Acid Res 17: 5973-5988. PNA monomers are then coupled in a stepwise manner to produce a chimeric molecule with a 5′ PNA segment and a 3′ DNA segment. See, e.g., Finn, et al., 1996. supra. Alternatively, chimeric molecules can be synthesized with a 5′ DNA segment and a 3′ PNA segment. See, e.g., Petersen, et al., 1975. Bioorg. Med. Chem. Lett. 5: 1119-11124.

[0135] In other embodiments, the oligonucleotide may include other appended groups such as peptides (e.g., for targeting host cell receptors in vivo), or agents facilitating transport across the cell membrane (see, e.g., Letsinger, et al., 1989. Proc. Natl. Acad. Sci. U.S.A. 86: 6553-6556; Lemaitre, et al., 1987. Proc. Natl. Acad. Sci. 84: 648-652; PCT Publication No. WO88/09810) or the blood-brain barrier (see, e.g., PCT Publication No. WO 89/10134). In addition, oligonucleotides can be modified with hybridization triggered cleavage agents (see, e.g., Krol, et al., 1988. BioTechniques 6:958-976) or intercalating agents (see, e.g., Zon, 1988. Pharm. Res. 5: 539-549). To this end, the oligonucleotide may be conjugated to another molecule, e.g., a peptide, a hybridization triggered cross-linking agent, a transport agent, a hybridization-triggered cleavage agent, and the like.

[0136] NOVX Polypeptides

[0137] A polypeptide according to the invention includes a polypeptide including the amino acid sequence of NOVX polypeptides whose sequences are provided in any one of SEQ ID NO:2n, wherein n is an integer between 1 and 107. The invention also includes a mutant or variant protein any of whose residues may be changed from the corresponding residues shown in any one of SEQ ID NO:2n, wherein n is an integer between 1 and 107, while still encoding a protein that maintains its NOVX activities and physiological functions, or a functional fragment thereof.

[0138] In general, a NOVX variant that preserves NOVX-like function includes any variant in which residues at a particular position in the sequence have been substituted by other amino acids, and further include the possibility of inserting an additional residue or residues between two residues of the parent protein as well as the possibility of deleting one or more residues from the parent sequence. Any amino acid substitution, insertion, or deletion is encompassed by the invention. In favorable circumstances, the substitution is a conservative substitution as defined above.

[0139] One aspect of the invention pertains to isolated NOVX proteins, and biologically-active portions thereof, or derivatives, fragments, analogs or homologs thereof. Also provided are polypeptide fragments suitable for use as immunogens to raise anti-NOVX antibodies. In one embodiment, native NOVX proteins can be isolated from cells or tissue sources by an appropriate purification scheme using standard protein purification techniques. In another embodiment, NOVX proteins are produced by recombinant DNA techniques. Alternative to recombinant expression, a NOVX protein or polypeptide can be synthesized chemically using standard peptide synthesis techniques.

[0140] An “isolated” or “purified” polypeptide or protein or biologically-active portion thereof is substantially free of cellular material or other contaminating proteins from the cell or tissue source from which the NOVX protein is derived, or substantially free from chemical precursors or other chemicals when chemically synthesized. The language “substantially free of cellular material” includes preparations of NOVX proteins in which the protein is separated from cellular components of the cells from which it is isolated or recombinantly-produced. In one embodiment, the language “substantially free of cellular material” includes preparations of NOVX proteins having less than about 30% (by dry weight) of non-NOVX proteins (also referred to herein as a “contaminating protein”), more preferably less than about 20% of non-NOVX proteins, still more preferably less than about 10% of non-NOVX proteins, and most preferably less than about 5% of non-NOVX proteins. When the NOVX protein or biologically-active portion thereof is recombinantly-produced, it is also preferably substantially free of culture medium, i.e., culture medium represents less than about 20%, more preferably less than about 10%, and most preferably less than about 5% of the volume of the NOVX protein preparation.

[0141] The language “substantially free of chemical precursors or other chemicals” includes preparations of NOVX proteins in which the protein is separated from chemical precursors or other chemicals that are involved in the synthesis of the protein. In one embodiment, the language “substantially free of chemical precursors or other chemicals” includes preparations of NOVX proteins having less than about 30% (by dry weight) of chemical precursors or non-NOVX chemicals, more preferably less than about 20% chemical precursors or non-NOVX chemicals, still more preferably less than about 10% chemical precursors or non-NOVX chemicals, and most preferably less than about 5% chemical precursors or non-NOVX chemicals.

[0142] Biologically-active portions of NOVX proteins include peptides comprising amino acid sequences sufficiently homologous to or derived from the amino acid sequences of the NOVX proteins (e.g., the amino acid sequence of SEQ ID NO:2n, wherein n is an integer between 1 and 107) that include fewer amino acids than the full-length NOVX proteins, and exhibit at least one activity of a NOVX protein. Typically, biologically-active portions comprise a domain or motif with at least one activity of the NOVX protein. A biologically-active portion of a NOVX protein can be a polypeptide which is, for example, 10, 25, 50, 100 or more amino acid residues in length.

[0143] Moreover, other biologically-active portions, in which other regions of the protein are deleted, can be prepared by recombinant techniques and evaluated for one or more of the functional activities of a native NOVX protein.

[0144] In an embodiment, the NOVX protein has an amino acid sequence of SEQ If) NO:2n, wherein n is an integer between 1 and 107. In other embodiments, the NOVX protein is substantially homologous to SEQ ID NO:2n, wherein n is an integer between 1 and 107, and retains the functional activity of the protein of SEQ ID NO:2n, wherein n is an integer between 1 and 107, yet differs in amino acid sequence due to natural allelic variation or mutagenesis, as described in detail, below. Accordingly, in another embodiment, the NOVX protein is a protein that comprises an amino acid sequence at least about 45% homologous to the amino acid sequence of SEQ ID NO:2n, wherein n is an integer between 1 and 107, and retains the functional activity of the NOVX proteins of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

[0145] Determining Homology Between Two or More Sequences

[0146] To determine the percent homology of two amino acid sequences or of two nucleic acids, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the sequence of a first amino acid or nucleic acid sequence for optimal alignment with a second amino or nucleic acid sequence). The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are homologous at that position (i.e., as used herein amino acid or nucleic acid “homology” is equivalent to amino acid or nucleic acid “identity”).

[0147] The nucleic acid sequence homology may be determined as the degree of identity between two sequences. The homology may be determined using computer programs known in the art, such as GAP software provided in the GCG program package. See, Needleman and Wunsch, 1970. J Mol Biol 48: 443-453. Using GCG GAP software with the following settings for nucleic acid sequence comparison: GAP creation penalty of 5.0 and GAP extension penalty of 0.3, the coding region of the analogous nucleic acid sequences referred to above exhibits a degree of identity preferably of at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99%, with the CDS (encoding) part of the DNA sequence of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107.

[0148] The term “sequence identity” refers to the degree to which two polynucleotide or polypeptide sequences are identical on a residue-by-residue basis over a particular region of comparison. The term “percentage of sequence identity” is calculated by comparing two, optimally aligned sequences over that region of comparison, determining the number of positions at which the identical nucleic acid base (e.g., A, T, C, G, U, or I, in the case of nucleic acids) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the region of comparison (i.e., the window size), and multiplying the result by 100 to yield the percentage of sequence identity. The term “substantial identity” as used herein denotes a characteristic of a polynucleotide sequence, wherein the polynucleotide comprises a sequence that has at least 80 percent sequence identity, preferably at least 85 percent identity and often 90 to 95 percent sequence identity, more usually at least 99 percent sequence identity as compared to a reference sequence over a comparison region.

[0149] Chimeric and Fusion Proteins

[0150] The invention also provides NOVX chimeric or fusion proteins. As used herein, a NOVX “chimeric protein” or “fusion protein” comprises a NOVX polypeptide operatively-linked to a non-NOVX polypeptide. An “NOVX polypeptide” refers to a polypeptide having an amino acid sequence corresponding to a NOVX protein of SEQ ID NO:2n, wherein n is an integer between 1 and 107, whereas a “non-NOVX polypeptide” refers to a polypeptide having an amino acid sequence corresponding to a protein that is not substantially homologous to the NOVX protein, e.g., a protein that is different from the NOVX protein and that is derived from the same or a different organism. Within a NOVX fusion protein the NOVX polypeptide can correspond to all or a portion of a NOVX protein. In one embodiment, a NOVX fusion protein comprises at least one biologically-active portion of a NOVX protein. In another embodiment, a NOVX fusion protein comprises at least two biologically-active portions of a NOVX protein. In yet another embodiment, a NOVX fusion protein comprises at least three biologically-active portions of a NOVX protein. Within the fusion protein, the term “operatively-linked” is intended to indicate that the NOVX polypeptide and the non-NOVX polypeptide are fused in-frame with one another. The non-NOVX polypeptide can be fused to the N-terminus or C-terminus of the NOVX polypeptide.

[0151] In one embodiment, the fusion protein is a GST-NOVX fusion protein in which the NOVX sequences are fused to the C-terminus of the GST (glutathione S-transferase) sequences. Such fusion proteins can facilitate the purification of recombinant NOVX polypeptides.

[0152] In another embodiment, the fusion protein is a NOVX protein containing a heterologous signal sequence at its N-terminus. In certain host cells (e.g., mammalian host cells), expression and/or secretion of NOVX can be increased through use of a heterologous signal sequence.

[0153] In yet another embodiment, the fusion protein is a NOVX-immunoglobulin fusion protein in which the NOVX sequences are fused to sequences derived from a member of the immunoglobulin protein family. The NOVX-immunoglobulin fusion proteins of the invention can be incorporated into pharmaceutical compositions and administered to a subject to inhibit an interaction between a NOVX ligand and a NOVX protein on the surface of a cell, to thereby suppress NOVX-mediated signal transduction in vivo. The NOVX-immunoglobulin fusion proteins can be used to affect the bioavailability of a NOVX cognate ligand. Inhibition of the NOVX ligand/NOVX interaction may be useful therapeutically for both the treatment of proliferative and differentiative disorders, as well as modulating (e.g. promoting or inhibiting) cell survival. Moreover, the NOVX-immunoglobulin fusion proteins of the invention can be used as immunogens to produce anti-NOVX antibodies in a subject, to purify NOVX ligands, and in screening assays to identify molecules that inhibit the interaction of NOVX with a NOVX ligand.

[0154] A NOVX chimeric or fusion protein of the invention can be produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different polypeptide sequences are ligated together in-frame in accordance with conventional techniques, e.g., by employing blunt-ended or stagger-ended termini for ligation, restriction enzyme digestion to provide for appropriate termini, filling-in of cohesive ends as appropriate, alkaline phosphatase treatment to avoid undesirable joining, and enzymatic ligation. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers that give rise to complementary overhangs between two consecutive gene fragments that can subsequently be annealed and reamplified to generate a chimeric gene sequence (see, e.g., Ausubel, et al. (eds.) CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). A NOVX-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the NOVX protein.

[0155] NOVX Agonists and Antagonists

[0156] The invention also pertains to variants of the NOVX proteins that function as either NOVX agonists (i.e., mimetics) or as NOVX antagonists. Variants of the NOVX protein can be generated by mutagenesis (e.g., discrete point mutation or truncation of the NOVX protein). An agonist of the NOVX protein can retain substantially the same, or a subset of, the biological activities of the naturally occurring form of the NOVX protein. An antagonist of the NOVX protein can inhibit one or more of the activities of the naturally occurring form of the NOVX protein by, for example, competitively binding to a downstream or upstream member of a cellular signaling cascade which includes the NOVX protein. Thus, specific biological effects can be elicited by treatment with a variant of limited function. In one embodiment, treatment of a subject with a variant having a subset of the biological activities of the naturally occurring form of the protein has fewer side effects in a subject relative to treatment with the naturally occurring form of the NOVX proteins.

[0157] Variants of the NOVX proteins that function as either NOVX agonists (i.e., mimetics) or as NOVX antagonists can be identified by screening combinatorial libraries of mutants (e.g., truncation mutants) of the NOVX proteins for NOVX protein agonist or antagonist activity. In one embodiment, a variegated library of NOVX variants is generated by combinatorial mutagenesis at the nucleic acid level and is encoded by a variegated gene library. A variegated library of NOVX variants can be produced by, for example, enzymatically ligating a mixture of synthetic oligonucleotides into gene sequences such that a degenerate set of potential NOVX sequences is expressible as individual polypeptides, or alternatively, as a set of larger fusion proteins (e.g., for phage display) containing the set of NOVX sequences therein. There are a variety of methods which can be used to produce libraries of potential NOVX variants from a degenerate oligonucleotide sequence. Chemical synthesis of a degenerate gene sequence can be performed in an automatic DNA synthesizer, and the synthetic gene then ligated into an appropriate expression vector. Use of a degenerate set of genes allows for the provision, in one mixture, of all of the sequences encoding the desired set of potential NOVX sequences. Methods for synthesizing degenerate oligonucleotides are well-known within the art. See, e.g., Narang, 1983. Tetrahedron 39: 3; Itakura, et al., 1984. Annu. Rev. Biochem. 53: 323; Itakura, et al., 1984. Science 198: 1056; Ike, et al., 1983. Nucl. Acids Res. 11: 477.

[0158] Polypeptide Libraries

[0159] In addition, libraries of fragments of the NOVX protein coding sequences can be used to generate a variegated population of NOVX fragments for screening and subsequent selection of variants of a NOVX protein. In one embodiment, a library of coding sequence fragments can be generated by treating a double stranded PCR fragment of a NOVX coding sequence with a nuclease under conditions wherein nicking occurs only about once per molecule, denaturing the double stranded DNA, renaturing the DNA to form double-stranded DNA that can include sense/antisense pairs from different nicked products, removing single stranded portions from reformed duplexes by treatment with S1 nuclease, and ligating the resulting fragment library into an expression vector. By this method, expression libraries can be derived which encodes N-terminal and internal fragments of various sizes of the NOVX proteins.

[0160] Various techniques are known in the art for screening gene products of combinatorial libraries made by point mutations or truncation, and for screening cDNA libraries for gene products having a selected property. Such techniques are adaptable for rapid screening of the gene libraries generated by the combinatorial mutagenesis of NOVX proteins. The most widely used techniques, which are amenable to high throughput analysis, for screening large gene libraries typically include cloning the gene library into replicable expression vectors, transforming appropriate cells with the resulting library of vectors, and expressing the combinatorial genes under conditions in which detection of a desired activity facilitates isolation of the vector encoding the gene whose product was detected. Recursive ensemble mutagenesis (REM), a new technique that enhances the frequency of functional mutants in the libraries, can be used in combination with the screening assays to identify NOVX variants. See, e.g., Arkin and Yourvan, 1992. Proc. Natl. Acad. Sci. USA 89: 7811-7815; Delgrave, et al., 1993. Protein Engineering 6:327-331.

[0161] Anti-NOVX Antibodies

[0162] Included in the invention are antibodies to NOVX proteins, or fragments of NOVX proteins. The term “antibody” as used herein refers to immunoglobulin molecules and immunologically active portions of Immunoglobulin (Ig) molecules, i.e., molecules that contain an antigen binding site that specifically binds (immunoreacts with) an antigen. Such antibodies include, but are not limited to, polyclonal, monoclonal, chimeric, single chain, Fab, Fab, and F(ab′)2 fragments, and an Fab expression library. In general, antibody molecules obtained from humans relates to any of the classes IgG, IgM, IgA, IgE and IgD, which differ from one another by the nature of the heavy chain present in the molecule. Certain classes have subclasses as well, such as IgG1, IgG2, and others. Furthermore, in humans, the light chain may be a kappa chain or a lambda chain. Reference herein to antibodies includes a reference to all such classes, subclasses and types of human antibody species.

[0163] An isolated protein of the invention intended to serve as an antigen, or a portion or fragment thereof, can be used as an immunogen to generate antibodies that immunospecifically bind the antigen, using standard techniques for polyclonal and monoclonal antibody preparation. The full-length protein can be used or, alternatively, the invention provides antigenic peptide fragments of the antigen for use as immunogens. An antigenic peptide fragment comprises at least 6 amino acid residues of the amino acid sequence of the full length protein, such as an amino acid sequence of SEQ ID NO:2n, wherein n is an integer between 1 and 107, and encompasses an epitope thereof such that an antibody raised against the peptide forms a specific immune complex with the full length protein or with any fragment that contains the epitope. Preferably, the antigenic peptide comprises at least 10 amino acid residues, or at least 15 amino acid residues, or at least 20 amino acid residues, or at least 30 amino acid residues. Preferred epitopes encompassed by the antigenic peptide are regions of the protein that are located on its surface; commonly these are hydrophilic regions.

[0164] In certain embodiments of the invention, at least one epitope encompassed by the antigenic peptide is a region of NOVX that is located on the surface of the protein, e.g., a hydrophilic region. A hydrophobicity analysis of the human NOVX protein sequence will indicate which regions of a NOVX polypeptide are particularly hydrophilic and, therefore, are likely to encode surface residues useful for targeting antibody production. As a means for targeting antibody production, hydropathy plots showing regions of hydrophilicity and hydrophobicity may be generated by any method well known in the art, including, for example, the Kyte Doolittle or the Hopp Woods methods, either with or without Fourier transformation. See, e.g., Hopp and Woods, 1981, Proc. Nat. Acad. Sci. USA 78: 3824-3828; Kyte and Doolittle 1982, J. Mol. Biol. 157: 105-142, each incorporated herein by reference in their entirety. Antibodies that are specific for one or more domains within an antigenic protein, or derivatives, fragments, analogs or homologs thereof, are also provided herein.

[0165] The term “epitope” includes any protein determinant capable of specific binding to an immunoglobulin or T-cell receptor. Epitopic determinants usually consist of chemically active surface groupings of molecules such as amino acids or sugar side chains and usually have specific three dimensional structural characteristics, as well as specific charge characteristics. A NOVX polypeptide or a fragment thereof comprises at least one antigenic epitope. An anti-NOVX antibody of the present invention is said to specifically bind to antigen NOVX when the equilibrium binding constant (KD) is ≦1 μM, preferably ≦100 nM, more preferably ≦10 nM, and most preferably ≦100 μM to about 1 μM, as measured by assays such as radioligand binding assays or similar assays known to those skilled in the art.

[0166] A protein of the invention, or a derivative, fragment, analog, homolog or ortholog thereof, may be utilized as an immunogen in the generation of antibodies that immunospecifically bind these protein components.

[0167] Various procedures known within the art may be used for the production of polyclonal or monoclonal antibodies directed against a protein of the invention, or against derivatives, fragments, analogs homologs or orthologs thereof (see, for example, Antibodies: A Laboratory Manual, Harlow E, and Lane D, 1988, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., incorporated herein by reference). Some of these antibodies are discussed below.

[0168] Polyclonal Antibodies

[0169] For the production of polyclonal antibodies, various suitable host animals (e.g., rabbit, goat, mouse or other mammal) may be immunized by one or more injections with the native protein, a synthetic variant thereof, or a derivative of the foregoing. An appropriate immunogenic preparation can contain, for example, the naturally occurring immunogenic protein, a chemically synthesized polypeptide representing the immunogenic protein, or a recombinantly expressed immunogenic protein. Furthermore, the protein may be conjugated to a second protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic proteins include but are not limited to keyhole limpet hemocyanin, serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. The preparation can further include an adjuvant. Various adjuvants used to increase the immunological response include, but are not limited to, Freund's (complete and incomplete), mineral gels (e.g., aluminum hydroxide), surface active substances (e.g., lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, dinitrophenol, etc.), adjuvants usable in humans such as Bacille Calmette-Guerin and Corynebacterium parvum, or similar immunostimulatory agents. Additional examples of adjuvants which can be employed include MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate).

[0170] The polyclonal antibody molecules directed against the immunogenic protein can be isolated from the mammal (e.g., from the blood) and further purified by well known techniques, such as affinity chromatography using protein A or protein G, which provide primarily the IgG fraction of immune serum. Subsequently, or alternatively, the specific antigen which is the target of the immunoglobulin sought, or an epitope thereof, may be immobilized on a column to purify the immune specific antibody by immunoaffinity chromatography. Purification of immunoglobulins is discussed, for example, by D. Wilkinson (The Scientist, published by The Scientist, Inc., Philadelphia Pa., Vol. 14, No. 8 (Apr. 17, 2000), pp. 25-28).

[0171] Monoclonal Antibodies

[0172] The term “monoclonal antibody” (MAb) or “monoclonal antibody composition”, as used herein, refers to a population of antibody molecules that contain only one molecular species of antibody molecule consisting of a unique light chain gene product and a unique heavy chain gene product. In particular, the complementarity determining regions (CDRs) of the monoclonal antibody are identical in all the molecules of the population. MAbs thus contain an antigen binding site capable of immunoreacting with a particular epitope of the antigen characterized by a unique binding affinity for it.

[0173] Monoclonal antibodies can be prepared using hybridoma methods, such as those described by Kohler and Milstein, Nature, 256:495 (1975). In a hybridoma method, a mouse, hamster, or other appropriate host animal, is typically immunized with an immunizing agent to elicit lymphocytes that produce or are capable of producing antibodies that will specifically bind to the immunizing agent. Alternatively, the lymphocytes can be immunized in vitro.

[0174] The immunizing agent will typically include the protein antigen, a fragment thereof or a fusion protein thereof. Generally, either peripheral blood lymphocytes are used if cells of human origin are desired, or spleen cells or lymph node cells are used if non-human mammalian sources are desired. The lymphocytes are then fused with an immortalized cell line using a suitable fusing agent, such as polyethylene glycol, to form a hybridoma cell (Goding, Monoclonal Antibodies: Principles and Practice, Academic Press, (1986) pp. 59-103). Immortalized cell lines are usually transformed mammalian cells, particularly myeloma cells of rodent, bovine and human origin. Usually, rat or mouse myeloma cell lines are employed. The hybridoma cells can be cultured in a suitable culture medium that preferably contains one or more substances that inhibit the growth or survival of the unfused, immortalized cells. For example, if the parental cells lack the enzyme hypoxanthine guanine phosphoribosyl transferase (HGPRT or HPRT), the culture medium for the hybridomas typically will include hypoxanthine, aminopterin, and thymidine (“HAT medium”), which substances prevent the growth of HGPRT-deficient cells.

[0175] Preferred immortalized cell lines are those that fuse efficiently, support stable high level expression of antibody by the selected antibody-producing cells, and are sensitive to a medium such as HAT medium. More preferred immortalized cell lines are murine myeloma lines, which can be obtained, for instance, from the Salk Institute Cell Distribution Center, San Diego, Calif. and the American Type Culture Collection, Manassas, Va. Human myeloma and mouse-human heteromyeloma cell lines also have been described for the production of human monoclonal antibodies (Kozbor, J. Immunol., 133:3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, Marcel Dekker, Inc., New York, (1987) pp. 51-63).

[0176] The culture medium in which the hybridoma cells are cultured can then be assayed for the presence of monoclonal antibodies directed against the antigen. Preferably, the binding specificity of monoclonal antibodies produced by the hybridoma cells is determined by immunoprecipitation or by an in vitro binding assay, such as radioimmunoassay (RIA) or enzyme-linked immunoabsorbent assay (ELISA). Such techniques and assays are known in the art. The binding affinity of the monoclonal antibody can, for example, be determined by the Scatchard analysis of Munson and Pollard, Anal. Biochem., 107:220 (1980). It is an objective, especially important in therapeutic applications of monoclonal antibodies, to identify antibodies having a high degree of specificity and a high binding affinity for the target antigen.

[0177] After the desired hybridoma cells are identified, the clones can be subcloned by limiting dilution procedures and grown by standard methods (Goding, 1986). Suitable culture media for this purpose include, for example, Dulbecco's Modified Eagle's Medium and RPMI-1640 medium. Alternatively, the hybridoma cells can be grown in vivo as ascites in a mammal.

[0178] The monoclonal antibodies secreted by the subclones can be isolated or purified from the culture medium or ascites fluid by conventional immunoglobulin purification procedures such as, for example, protein A-Sepharose, hydroxylapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography.

[0179] The monoclonal antibodies can also be made by recombinant DNA methods, such as those described in U.S. Pat. No. 4,816,567. DNA encoding the monoclonal antibodies of the invention can be readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of murine antibodies). The hybridoma cells of the invention serve as a preferred source of such DNA. Once isolated, the DNA can be placed into expression vectors, which are then transfected into host cells such as simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, to obtain the synthesis of monoclonal antibodies in the recombinant host cells. The DNA also can be modified, for example, by substituting the coding sequence for human heavy and light chain constant domains in place of the homologous murine sequences (U.S. Pat. No. 4,816,567; Morrison, Nature 368, 812-13 (1994)) or by covalently joining to the immunoglobulin coding sequence all or part of the coding sequence for a non-immunoglobulin polypeptide. Such a non-immunoglobulin polypeptide can be substituted for the constant domains of an antibody of the invention, or can be substituted for the variable domains of one antigen-combining site of an antibody of the invention to create a chimeric bivalent antibody.

[0180] Humanized Antibodies

[0181] The antibodies directed against the protein antigens of the invention can further comprise humanized antibodies or human antibodies. These antibodies are suitable for administration to humans without engendering an immune response by the human against the administered immunoglobulin. Humanized forms of antibodies are chimeric immunoglobulins, immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab′, F(ab′)2 or other antigen-binding subsequences of antibodies) that are principally comprised of the sequence of a human immunoglobulin, and contain minimal sequence derived from a non-human immunoglobulin. Humanization can be performed following the method of Winter and co-workers (Jones et al., Nature, 321:522-525 (1986); Riechmann et al., Nature, 332:323-327 (1988); Verhoeyen et al., Science, 239:1534-1536 (1988)), by substituting rodent CDRs or CDR sequences for the corresponding sequences of a human antibody. (See also U.S. Pat. No. 5,225,539.) In some instances, Fv framework residues of the human immunoglobulin are replaced by corresponding non-human residues. Humanized antibodies can also comprise residues which are found neither in the recipient antibody nor in the imported CDR or framework sequences. In general, the humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the CDR regions correspond to those of a non-human immunoglobulin and all or substantially all of the framework regions are those of a human immunoglobulin consensus sequence. The humanized antibody optimally also will comprise at least a portion of an immunoglobulin constant region (Fe), typically that of a human immunoglobulin (Jones et al., 1986; Riechmann et al., 1988; and Presta, Curr. Op. Struct. Biol., 2:593-596 (1992)).

[0182] Human Antibodies

[0183] Fully human antibodies essentially relate to antibody molecules in which the entire sequence of both the light chain and the heavy chain, including the CDRs, arise from human genes. Such antibodies are termed “human antibodies”, or “fully human antibodies” herein. Human monoclonal antibodies can be prepared by the trioma technique; the human B-cell hybridoma technique (see Kozbor, et al., 1983 Immunol Today 4: 72) and the EBV hybridoma technique to produce human monoclonal antibodies (see Cole, et al., 1985 In: MONOCLONAL ANTIBODIES AND CANCER THERAPY, Alan R. Liss, Inc., pp. 77-96). Human monoclonal antibodies may be utilized in the practice of the present invention and may be produced by using human hybridomas (see Cote, et al., 1983. Proc Natl Acad Sci USA 80: 2026-2030) or by transforming human B-cells with Epstein Barr Virus in vitro (see Cole, et al., 1985 In: MONOCLONAL ANTIBODIES AND CANCER THERAPY, Alan R. Liss, Inc., pp. 77-96).

[0184] In addition, human antibodies can also be produced using additional techniques, including phage display libraries (Hoogenboom and Winter, J. Mol. Biol., 227:381 (1991); Marks et al., J. Mol. Biol., 222:581 (1991)). Similarly, human antibodies can be made by introducing human immunoglobulin loci into transgenic animals, e.g., mice in which the endogenous immunoglobulin genes have been partially or completely inactivated. Upon challenge, human antibody production is observed, which closely resembles that seen in humans in all respects, including gene rearrangement, assembly, and antibody repertoire. This approach is described, for example, in U.S. Pat. Nos. 5,545,807; 5,545,806; 5,569,825; 5,625,126; 5,633,425; 5,661,016, and in Marks et al. (Bio/Technology 10, 779-783 (1992)); Lonberg et al. (Nature 368 856-859 (1994)); Morrison (Nature 368, 812-13 (1994)); Fishwild et al,(Nature Biotechnology 14, 845-51 (1996)); Neuberger (Nature Biotechnology 14, 826 (1996)); and Lonberg and Huszar (Intern. Rev. Immunol. 13 65-93 (1995)).

[0185] Human antibodies may additionally be produced using transgenic nonhuman animals which are modified so as to produce fully human antibodies rather than the animal's endogenous antibodies in response to challenge by an antigen. (See PCT publication WO94/02602). The endogenous genes encoding the heavy and light immunoglobulin chains in the nonhuman host have been incapacitated, and active loci encoding human heavy and light chain immunoglobulins are inserted into the host's genome. The human genes are incorporated, for example, using yeast artificial chromosomes containing the requisite human DNA segments. An animal which provides all the desired modifications is then obtained as progeny by crossbreeding intermediate transgenic animals containing fewer than the full complement of the modifications. The preferred embodiment of such a nonhuman animal is a mouse, and is termed the Xenomouse™ as disclosed in PCT publications WO 96/33735 and WO 96/34096. This animal produces B cells which secrete fully human immunoglobulins. The antibodies can be obtained directly from the animal after immunization with an immunogen of interest, as, for example, a preparation of a polyclonal antibody, or alternatively from immortalized B cells derived from the animal, such as hybridomas producing monoclonal antibodies. Additionally, the genes encoding the immunoglobulins with human variable regions can be recovered and expressed to obtain the antibodies directly, or can be further modified to obtain analogs of antibodies such as, for example, single chain Fv molecules.

[0186] An example of a method of producing a nonhuman host, exemplified as a mouse, lacking expression of an endogenous immunoglobulin heavy chain is disclosed in U.S. Pat. No. 5,939,598. It can be obtained by a method including deleting the J segment genes from at least one endogenous heavy chain locus in an embryonic stem cell to prevent rearrangement of the locus and to prevent formation of a transcript of a rearranged immunoglobulin heavy chain locus, the deletion being effected by a targeting vector containing a gene encoding a selectable marker; and producing from the embryonic stem cell a transgenic mouse whose somatic and germ cells contain the gene encoding the, selectable marker.

[0187] A method for producing an antibody of interest, such as a human antibody, is disclosed in U.S. Pat. No. 5,916,771. It includes introducing an expression vector that contains a nucleotide sequence encoding a heavy chain into one mammalian host cell in culture, introducing an expression vector containing a nucleotide sequence encoding a light chain into another mammalian host cell, and fusing the two cells to form a hybrid cell. The hybrid cell expresses an antibody containing the heavy chain and the light chain.

[0188] In a further improvement on this procedure, a method for identifying a clinically relevant epitope on an immunogen, and a correlative method for selecting an antibody that binds immunospecifically to the relevant epitope with high affinity, are disclosed in PCT publication WO 99/53049.

[0189] Fab Fragments and Single Chain Antibodies

[0190] According to the invention, techniques can be adapted for the production of single-chain antibodies specific to an antigenic protein of the invention (see e.g., U.S. Pat. No. 4,946,778). In addition, methods can be adapted for the construction of Fab expression libraries (see e.g., Huse, et al., 1989 Science 246: 1275-1281) to allow rapid and effective identification of monoclonal Fab fragments with the desired specificity for a protein or derivatives, fragments, analogs or homologs thereof. Antibody fragments that contain the idiotypes to a protein antigen may be produced by techniques known in the art including, but not limited to: (i) an F(ab′)2 fragment produced by pepsin digestion of an antibody molecule; (ii) an Fab fragment generated by reducing the disulfide bridges of an F(ab′)2 fragment; (iii) an Fab fragment generated by the treatment of the antibody molecule with papain and a reducing agent and (iv) Fv fragments.

[0191] Bispecific Antibodies

[0192] Bispecific antibodies are monoclonal, preferably human or humanized, antibodies that have binding specificities for at least two different antigens. In the present case, one of the binding specificities is for an antigenic protein of the invention. The second binding target is any other antigen, and advantageously is a cell-surface protein or receptor or receptor subunit.

[0193] Methods for making bispecific antibodies are known in the art. Traditionally, the recombinant production of bispecific antibodies is based on the co-expression of two immunoglobulin heavy-chain/light-chain pairs, where the two heavy chains have different specificities (Milstein and Cuello, Nature, 305:537-539 (1983)). Because of the random assortment of immunoglobulin heavy and light chains, these hybridomas (quadromas) produce a potential mixture of ten different antibody molecules, of which only one has the correct bispecific structure. The purification of the correct molecule is usually accomplished by affinity chromatography steps. Similar procedures are disclosed in WO 93/08829, published May 13, 1993, and in Traunecker et al., EMBO J., 10:3655-3659 (1991).

[0194] Antibody variable domains with the desired binding specificities (antibody-antigen combining sites) can be fused to immunoglobulin constant domain sequences. The fusion preferably is with an immunoglobulin heavy-chain constant domain, comprising at least part of the hinge, CH2, and CH3 regions. It is preferred to have the first heavy-chain constant region (CHI) containing the site necessary for light-chain binding present in at least one of the fusions. DNAs encoding the immunoglobulin heavy-chain fusions and, if desired, the immunoglobulin light chain, are inserted into separate expression vectors, and are co-transfected into a suitable host organism. For further details of generating bispecific antibodies see, for example, Suresh et al., Methods in Enzymology, 121:210 (1986).

[0195] According to another approach described in WO 96/27011, the interface between a pair of antibody molecules can be engineered to maximize the percentage of heterodimers which are recovered from recombinant cell culture. The preferred interface comprises at least a part of the CH3 region of an antibody constant domain. In this method, one or more small amino acid side chains from the interface of the first antibody molecule are replaced with larger side chains (e.g. tyrosine or tryptophan). Compensatory “cavities” of identical or similar size to the large side chain(s) are created on the interface of the second antibody molecule by replacing large amino acid side chains with smaller ones (e.g. alanine or threonine). This provides a mechanism for increasing the yield of the heterodimer over other unwanted end-products such as homodimers.

[0196] Bispecific antibodies can be prepared as full length antibodies or antibody fragments (e.g. F(ab′)2 bispecific antibodies). Techniques for generating bispecific antibodies from antibody fragments have been described in the literature. For example, bispecific antibodies can be prepared using chemical linkage. Brennan et al., Science 229:81 (1985) describe a procedure wherein intact antibodies are proteolytically cleaved to generate F(ab′)2 fragments. These fragments are reduced in the presence of the dithiol complexing agent sodium arsenite to stabilize vicinal dithiols and prevent intermolecular disulfide formation. The Fab′ fragments generated are then converted to thionitrobenzoate (TNB) derivatives. One of the Fab′-TNB derivatives is then reconverted to the Fab′-thiol by reduction with mercaptoethylamine and is mixed with an equimolar amount of the other Fab′-TNB derivative to form the bispecific antibody. The bispecific antibodies produced can be used as agents for the selective immobilization of enzymes.

[0197] Additionally, Fab′ fragments can be directly recovered from E. coli and chemically coupled to form bispecific antibodies. Shalaby et al., J. Exp. Med. 175:217-225 (1992) describe the production of a fully humanized bispecific antibody F(ab′)2 molecule. Each Fab′ fragment was separately secreted from E. coli and subjected to directed chemical coupling in vitro to form the bispecific antibody. The bispecific antibody thus formed was able to bind to cells overexpressing the ErbB2 receptor and normal human T cells, as well as trigger the lytic activity of human cytotoxic lymphocytes against human breast tumor targets.

[0198] Various techniques for making and isolating bispecific antibody fragments directly from recombinant cell culture have also been described. For example, bispecific antibodies have been produced using leucine zippers. Kostelny et al., J. Immunol. 148(5):1547-1553 (1992). The leucine zipper peptides from the Fos and Jun proteins were linked to the Fab′ portions of two different antibodies by gene fusion. The antibody homodimers were reduced at the hinge region to form monomers and then re-oxidized to form the antibody heterodimers. This method can also be utilized for the production of antibody homodimers. The “diabody” technology described by Hollinger et al., Proc. Natl. Acad. Sci. USA 90:6444-6448 (1993) has provided an alternative mechanism for making bispecific antibody fragments. The fragments comprise a heavy-chain variable domain (VH) connected to a light-chain variable domain (VL) by a linker which is too short to allow pairing between the two domains on the same chain. Accordingly, the VH and VL domains of one fragment are forced to pair with the complementary VL and VH domains of another fragment, thereby forming two antigen-binding sites. Another strategy for making bispecific antibody fragments by the use of single-chain Fv (sFv) dimers has also been reported. See, Gruber et al., J. Immunol. 152:5368 (1994).

[0199] Antibodies with more than two valencies are contemplated. For example, trispecific antibodies can be prepared. Tutt et al., J. Immunol. 147:60 (1991).

[0200] Exemplary bispecific antibodies can bind to two different epitopes, at least one of which originates in the protein antigen of the invention. Alternatively, an anti-antigenic arm of an immunoglobulin molecule can be combined with an arm which binds to a, triggering molecule on a leukocyte such as a T-cell receptor molecule (e.g. CD2, CD3, CD28, or B7), or Fc receptors for IgG (FcγR), such as FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD16) so as to focus cellular defense mechanisms to the cell expressing the particular antigen. Bispecific antibodies can also be used to direct cytotoxic agents to cells which express a particular antigen. These antibodies possess an antigen-binding arm and an arm which binds a cytotoxic agent or a radionuclide chelator, such as EOTUBE, DPTA, DOTA, or TETA. Another bispecific antibody of interest binds the protein antigen described herein and further binds tissue factor (TF).

[0201] Heteroconjugate Antibodies

[0202] Heteroconjugate antibodies are also within the scope of the present invention. Heteroconjugate antibodies are composed of two covalently joined antibodies. Such antibodies have, for example, been proposed to target immune system cells to unwanted cells (U.S. Pat. No. 4,676,980), and for treatment of HIV infection (WO 91/00360; WO 92/200373; EP 03089). It is contemplated that the antibodies can be prepared in vitro using known methods in synthetic protein chemistry, including those involving crosslinking agents. For example, immunotoxins can be constructed using a disulfide exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4-mercaptobutyrimidate and those disclosed, for example, in U.S. Pat. No. 4,676,980.

[0203] Effector Function Engineering

[0204] It can be desirable to modify the antibody of the invention with respect to effector function, so as to enhance, e.g., the effectiveness of the antibody in treating cancer. For example, cysteine residue(s) can be introduced into the Fc region, thereby allowing interchain disulfide bond formation in this region. The homodimeric antibody thus generated can have improved internalization capability and/or increased complement-mediated cell killing and antibody-dependent cellular cytotoxicity (ADCC). See Caron et al., J. Exp Med., 176: 1191-1195 (1992) and Shopes, J. Immunol., 148: 2918-2922 (1992). Homodimeric antibodies with enhanced anti-tumor activity can also be prepared using heterobifunctional cross-linkers as described in Wolff et al. Cancer Research, 53: 2560-2565 (1993). Alternatively, an antibody can be engineered that has dual Fc regions and can thereby have enhanced complement lysis and ADCC capabilities. See Stevenson et al., Anti-Cancer Drug Design, 3: 219-230 (1989).

[0205] Immunoconjugates

[0206] The invention also pertains to immunoconjugates comprising an antibody conjugated to a cytotoxic agent such as a chemotherapeutic agent, toxin (e.g., an enzymatically active toxin of bacterial, fungal, plant, or animal origin, or fragments thereof), or a radioactive isotope (i.e., a radioconjugate).

[0207] Chemotherapeutic agents useful in the generation of such immunoconjugates have been described above. Enzymatically active toxins and fragments thereof that can be used include diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. A variety of radionuclides are available for the production of radioconjugated antibodies. Examples include 212Bi, 131In, 90Y, and 186Re.

[0208] Conjugates of the antibody and cytotoxic agent are made using a variety of bifunctional protein-coupling agents such as N-succinimidyl-3-(2-pyridyldithiol) propionate (SPDP), iminothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCL), active esters (such as disuccinimidyl suberate), aldehydes (such as glutareldehyde), bis-azido compounds (such as bis (p-azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), dilsocyanates (such as tolyene 2,6-diusocyanate), and bis-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). For example, a ricin immunotoxin can be prepared as described in Vitetta et al., Science, 238: 1098 (1987). Carbon-14-labeled 1-isothiocyanatobenzyl-3-methyldiethylene triaminepentaacetic acid (MX-DTPA) is an exemplary chelating agent for conjugation of radionucleotide to the antibody. See WO94/11026.

[0209] In another embodiment, the antibody can be conjugated to a “receptor” (such streptavidin) for utilization in tumor pretargeting wherein the antibody-receptor conjugate is administered to the patient, followed by removal of unbound conjugate from the circulation using a clearing agent and then administration of a “ligand” (e.g., avidin) that is in turn conjugated to a cytotoxic agent.

[0210] Immunoliposomes

[0211] The antibodies disclosed herein can also be formulated as immunoliposomes. Liposomes containing the antibody are prepared by methods known in the art, such as described in Epstein et al., Proc. Natl. Acad. Sci. USA, 82: 3688 (1985); Hwang et al., Proc. Natl. Acad. Sci. USA, 77: 4030 (1980); and U.S. Pat. Nos. 4,485,045 and 4,544,545. Liposomes with enhanced circulation time are disclosed in U.S. Pat. No. 5,013,556.

[0212] Particularly useful liposomes can be generated by the reverse-phase evaporation method with a lipid composition comprising phosphatidylcholine, cholesterol, and PEG-derivatized phosphatidylethanolamine (PEG-PE). Liposomes are extruded through filters of defined pore size to yield liposomes with the desired diameter. Fab′ fragments of the antibody of the present invention can be conjugated to the liposomes as described in Martin et al., J. Biol. Chem., 257: 286-288 (1982) via a disulfide-interchange reaction. A chemotherapeutic agent (such as Doxorubicin) is optionally contained within the liposome. See Gabizon et al., J. National Cancer Inst., 81(19): 1484 (1989).

[0213] Diagnostic Applications of Antibodies Directed Against the Proteins of the Invention

[0214] In one embodiment, methods for the screening of antibodies that possess the desired specificity include, but are not limited to, enzyme linked immunosorbent assay (ELISA) and other immunologically mediated techniques known within the art. In a specific embodiment, selection of antibodies that are specific to a particular domain of an NOVX protein is facilitated by generation of hybridomas that bind to the fragment of an NOVX protein possessing such a domain. Thus, antibodies that are specific for a desired domain within an NOVX protein, or derivatives, fragments, analogs or homologs thereof, are also provided herein.

[0215] Antibodies directed against a NOVX protein of the invention may be used in methods known within the art relating to the localization and/or quantitation of a NOVX protein (e.g., for use in measuring levels of the NOVX protein within appropriate physiological samples, for use in diagnostic methods, for use in imaging the protein, and the like). In a given embodiment, antibodies specific to a NOVX protein, or derivative, fragment, analog or homolog thereof, that contain the antibody derived antigen binding domain, are utilized as pharmacologically active compounds (referred to hereinafter as “Therapeutics”).

[0216] An antibody specific for a NOVX protein of the invention (e.g., a monoclonal antibody or a polyclonal antibody) can be used to isolate a NOVX polypeptide by standard techniques, such as immunoaffinity, chromatography or immunoprecipitation. An antibody to a NOVX polypeptide can facilitate the purification of a natural NOVX antigen from cells, or of a recombinantly produced NOVX antigen expressed in host cells. Moreover, such an anti-NOVX antibody can be used to detect the antigenic NOVX protein (e.g., in a cellular lysate or cell supernatant) in order to evaluate the abundance and pattern of expression of the antigenic NOVX protein. Antibodies directed against a NOVX protein can be used diagnostically to monitor protein levels in tissue as part of a clinical testing procedure, e.g., to, for example, determine the efficacy of a given treatment regimen. Detection can be facilitated by coupling (i.e., physically linking) the antibody to a detectable substance. Examples of detectable substances include various enzymes, prosthetic groups, fluorescent materials, luminescent materials, bioluminescent materials, and radioactive materials. Examples of suitable enzymes include horseradish peroxidase, alkaline phosphatase, O-galactosidase, or acetylcholinesterase; examples of suitable prosthetic group complexes include streptavidin/biotin and avidin/biotin; examples of suitable fluorescent materials include umbelliferone, fluorescein, fluorescein isothiocyanate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride or phycoerythrin; an example of a luminescent material includes luminol; examples of bioluminescent materials include luciferase, luciferin, and aequorin, and examples of suitable radioactive material include 125I, 131I, 35S or 3H.

[0217] Antibody Therapeutics

[0218] Antibodies of the invention, including polyclonal, monoclonal, humanized and fully human antibodies, may used as therapeutic agents. Such agents will generally be employed to treat or prevent a disease or pathology in a subject. An antibody preparation, preferably one having high specificity and high affinity for its target antigen, is administered to the subject and will generally have an effect due to its binding with the target. Such an effect may be one of two kinds, depending on the specific nature of the interaction between the given antibody molecule and the target antigen in question. In the first instance, administration of the antibody may abrogate or inhibit the binding of the target with an endogenous ligand to which it naturally binds. In this case, the antibody binds to the target and masks a binding site of the naturally occurring ligand, wherein the ligand serves as an effector molecule. Thus the receptor mediates a signal transduction pathway for which ligand is responsible.

[0219] Alternatively, the effect may be one in which the antibody elicits a physiological result by virtue of binding to an effector binding site on the target molecule. (In this case the target, a receptor having an endogenous ligand which may be absent or defective in the disease or pathology, binds the antibody as a surrogate effector ligand, initiating a receptor-based signal transduction event by the receptor.

[0220] A therapeutically effective amount of an antibody of the invention relates generally to the amount needed to achieve a therapeutic objective. As noted above, this may be a binding interaction between the antibody and its target antigen that, in certain cases, interferes with the functioning of the target, and in other cases, promotes a physiological response. The amount required to be administered will furthermore depend on the binding affinity of the antibody for its specific antigen, and will also depend on the rate at which an administered antibody is depleted from the free volume other subject to which it is administered. Common ranges for therapeutically effective dosing of an antibody or antibody fragment of the invention may be, by way of nonlimiting example, from about 0.1 mg/kg body weight to about 50 mg/kg body weight. Common dosing frequencies may range, for example, from twice daily to once a week.

[0221] Pharmaceutical Compositions of Antibodies

[0222] Antibodies specifically binding a protein of the invention, as well as other molecules identified by the screening assays disclosed herein, can be administered for the treatment of various disorders in the form of pharmaceutical compositions. Principles and considerations involved in preparing such compositions, as well as guidance in the choice of components are provided, for example, in Remington: The Science And Practice Of Pharmacy 19th ed. (Alfonso R. Gennaro, et al., editors) Mack Pub. Co., Easton, Pa.: 1995; Drug Absorption Enhancement: Concepts, Possibilities, Limitations, And Trends, Harwood Academic Publishers, Langhorne, Pa., 1994; and Peptide And Protein Drug Delivery (Advances In Parenteral Sciences, Vol. 4), 1991, M. Dekker, New York.

[0223] If the antigenic protein is intracellular and whole antibodies are used as inhibitors, internalizing antibodies are preferred. However, liposomes can also be used to deliver the antibody, or an antibody fragment, into cells. Where antibody fragments are used, the smallest inhibitory fragment that specifically binds to the binding domain of the target protein is preferred. For example, based upon the variable-region sequences of an antibody, peptide molecules can be designed that retain the ability to bind the target protein sequence. Such peptides can be synthesized chemically and/or produced by recombinant DNA technology. See, e.g., Marasco et al., Proc. Natl. Acad. Sci. USA, 90: 7889-7893 (1993). The formulation herein can also contain more than one active compound as necessary for the particular indication being treated, preferably those with complementary activities that do not adversely affect each other. Alternatively, or in addition, the composition can comprise an agent that enhances its function, such as, for example, a cytotoxic agent, cytokine, chemotherapeutic agent, or growth-inhibitory agent. Such molecules are suitably present in combination in amounts that are effective for the purpose intended.

[0224] The active ingredients can also be entrapped in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatin-microcapsules and poly-(methylmethacrylate) microcapsules, respectively, in colloidal drug delivery systems (for example, liposomes, albumin microspheres, microemulsions, nano-particles, and nanocapsules) or in macroemulsions.

[0225] The formulations to be used for in vivo administration must be sterile. This is readily accomplished by filtration through sterile filtration membranes.

[0226] Sustained-release preparations can be prepared. Suitable examples of sustained-release preparations include semipermeable matrices of solid hydrophobic polymers containing the antibody, which matrices are in the form of shaped articles, e.g., films, or microcapsules. Examples of sustained-release matrices include polyesters, hydrogels (for example, poly(2-hydroxyethyl-methacrylate), or poly(vinylalcohol)), polylactides (U.S. Pat. No. 3,773,919), copolymers of L-glutamic acid and γ ethyl-L-glutamate, non-degradable ethylene-vinyl acetate, degradable lactic acid-glycolic acid copolymers such as the LUPRON DEPOT™ (injectable microspheres composed of lactic acid-glycolic acid copolymer and leuprolide acetate), and poly-D-(−)-3-hydroxybutyric acid. While polymers such as ethylene-vinyl acetate and lactic acid-glycolic acid enable release of molecules for over 100 days, certain hydrogels release proteins for shorter time periods.

[0227] ELISA Assay

[0228] An agent for detecting an analyte protein is an antibody capable of binding to an analyte protein, preferably an antibody with a detectable label. Antibodies can be polyclonal, or more preferably, monoclonal. An intact antibody, or a fragment thereof (e.g., Fab or F(ab)2) can be used. The term “labeled”, with regard to the probe or antibody, is intended to encompass direct labeling of the probe or antibody by coupling (i.e., physically linking) a detectable substance to the probe or antibody, as well as indirect labeling of the probe or antibody by reactivity with another reagent that is directly labeled. Examples of indirect labeling include detection of a primary antibody using a fluorescently-labeled secondary antibody and end-labeling of a DNA probe with biotin such that it can be detected with fluorescently-labeled streptavidin. The term “biological sample” is intended to include tissues, cells and biological fluids isolated from a subject, as well as tissues, cells and fluids present within a subject. Included within the usage of the term “biological sample”, therefore, is blood and a fraction or component of blood including blood serum, blood plasma, or lymph. That is, the detection method of the invention can be used to detect an analyte mRNA, protein, or genomic DNA in a biological sample in vitro as well as in vivo. For example, in vitro techniques for detection of an analyte mRNA include Northern hybridizations and in situ hybridizations. In vitro techniques for detection of an analyte protein include enzyme linked immunosorbent assays (ELISAs), Western blots, immunoprecipitations, and immunofluorescence. In vitro techniques for detection of an analyte genomic DNA include Southern hybridizations. Procedures for conducting immunoassays are described, for example in “ELISA: Theory and Practice: Methods in Molecular Biology”, Vol. 42, J. R. Crowther (Ed.) Human Press, Totowa, N.J., 1995; “Immunoassay”, E. Diamandis and T. Christopoulus, Academic Press, Inc., San Diego, Calif., 1996; and “Practice and Thory of Enzyme Immunoassays”, P. Tijssen, Elsevier Science Publishers, Amsterdam, 1985. Furthermore, in vivo techniques for detection of an analyte protein include introducing into a subject a labeled anti-an analyte protein antibody. For example, the antibody can be labeled with a radioactive marker whose presence and location in a subject can be detected by standard imaging techniques.

[0229] NOVX Recombinant Expression Vectors and Host Cells

[0230] Another aspect of the invention pertains to vectors, preferably expression vectors, containing a nucleic acid encoding a NOVX protein, or derivatives, fragments, analogs or homologs thereof. As used herein, the term “vector” refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a “plasmid”, which refers to a circular double stranded DNA loop into which additional DNA segments can be ligated. Another type of vector is a viral vector, wherein additional DNA segments can be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) are integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively-linked. Such vectors are referred to herein as “expression vectors”. In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids. In the present specification, “plasmid” and “vector” can be used interchangeably as the plasmid is the most commonly used form of vector. However, the invention is intended to include such other forms of expression vectors, such as viral vectors (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses), which serve equivalent functions.

[0231] The recombinant expression vectors of the invention comprise a nucleic acid of the invention in a form suitable for expression of the nucleic acid in a host cell, which means that the recombinant expression vectors include one or more regulatory sequences, selected on the basis of the host cells to be used for expression, that is operatively-linked to the nucleic acid sequence to be expressed. Within a recombinant expression vector, “operably-linked” is intended to mean that the nucleotide sequence of interest is linked to the regulatory sequence(s) in a manner that allows for expression of the nucleotide sequence (e.g., in an in vitro transcription/translation system or in a host cell when the vector is introduced into the host cell).

[0232] The term “regulatory sequence” is intended to includes promoters, enhancers and other expression control elements (e.g., polyadenylation signals). Such regulatory sequences are described, for example, in Goeddel, GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990). Regulatory sequences include those that direct constitutive expression of a nucleotide sequence in many types of host cell and those that direct expression of the nucleotide sequence only in certain host cells (e.g., tissue-specific regulatory sequences). It will be appreciated by those skilled in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expression of protein desired, etc. The expression vectors of the invention can be introduced into host cells to thereby produce proteins or peptides, including fusion proteins or peptides, encoded by nucleic acids as described herein (e.g., NOVX proteins, mutant forms of NOVX proteins, fusion proteins, etc.).

[0233] The recombinant expression vectors of the invention can be designed for expression of NOVX proteins in prokaryotic or eukaryotic cells. For example, NOVX proteins can be expressed in bacterial cells such as Escherichia coli, insect cells (using baculovirus expression vectors) yeast cells or mammalian cells. Suitable host cells are discussed further in Goeddel, GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990). Alternatively, the recombinant expression vector can be transcribed and translated in vitro, for example using T7 promoter regulatory sequences and T7 polymerase.

[0234] Expression of proteins in prokaryotes is most often carried out in Escherichia coli with vectors containing constitutive or inducible promoters directing the expression of either fusion or non-fusion proteins. Fusion vectors add a number of amino acids to a protein encoded therein, usually to the amino terminus of the recombinant protein. Such fusion vectors typically serve three purposes: (i) to increase expression of recombinant protein; (ii) to increase the solubility of the recombinant protein; and (iii) to aid in the purification of the recombinant protein by acting as a ligand in affinity purification. Often, in fusion expression vectors, a proteolytic cleavage site is introduced at the junction of the fusion moiety and the recombinant protein to enable separation of the recombinant protein from the fusion moiety subsequent to purification of the fusion protein. Such enzymes, and their cognate recognition sequences, include Factor Xa, thrombin and enterokinase. Typical fusion expression vectors include pGEX (Pharmacia Biotech Inc; Smith and Johnson, 1988. Gene 67: 31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) that fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to the target recombinant protein.

[0235] Examples of suitable inducible non-fusion E. coli expression vectors include pTrc (Amrann et al., (1988) Gene 69:301-315) and pET 11d (Studier et al., GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990) 60-89).

[0236] One strategy to maximize recombinant protein expression in E. coli is to express the protein in a host bacteria with an impaired capacity to proteolytically cleave the recombinant protein. See, e.g., Gottesman, GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990) 119-128. Another strategy is to alter the nucleic acid sequence of the nucleic acid to be inserted into an expression vector so that the individual codons for each amino acid are those preferentially utilized in E. coli (see, e.g., Wada, et al., 1992. Nucl. Acids Res. 20: 2111-2118). Such alteration of nucleic acid sequences of the invention can be carried out by standard DNA synthesis techniques.

[0237] In another embodiment, the NOVX expression vector is a yeast expression vector. Examples of vectors for expression in yeast Saccharomyces cerivisae include pYepSec1 (Baldari, et al., 1987. EMBO J. 6: 229-234), pMFa (Kurjan and Herskowitz, 1982. Cell 30: 933-943), pJRY88 (Schultz et al., 1987. Gene 54: 113-123), pYES2 (Invitrogen Corporation, San Diego, Calif.), and picZ (InVitrogen Corp, San Diego, Calif.).

[0238] Alternatively, NOVX can be expressed in insect cells using baculovirus expression vectors. Baculovirus vectors available for expression of proteins in cultured insect cells (e.g., SF9 cells) include the pAc series (Smith, et al., 1983. Mol. Cell. Biol. 3: 2156-2165) and the pVL series (Lucklow and Summers, 1989. Virology 170: 31-39).

[0239] In yet another embodiment, a nucleic acid of the invention is expressed in mammalian cells using a mammalian expression vector. Examples of mammalian expression vectors include pCDM8 (Seed, 1987. Nature 329: 840) and pMT2PC (Kaufman, et al., 1987. EMBO J. 6: 187-195). When used in mammalian cells, the expression vector's control functions are often provided by viral regulatory elements. For example, commonly used promoters are derived from polyoma, adenovirus 2, cytomegalovirus, and simian virus 40. For other suitable expression systems for both prokaryotic and eukaryotic cells see, e.g., Chapters 16 and 17 of Sambrook, et al., MOLECULAR CLONING: A LABORATORY MANUAL. 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989.

[0240] In another embodiment, the recombinant mammalian expression vector is capable of directing expression of the nucleic acid preferentially in a particular cell type (e.g., tissue-specific regulatory elements are used to express the nucleic acid). Tissue-specific regulatory elements are known in the art. Non-limiting examples of suitable tissue-specific promoters include the albumin promoter (liver-specific; Pinkert, et al., 1987. Genes Dev. 1: 268-277), lymphoid-specific promoters (Calame and Eaton, 1988. Adv. Immunol. 43: 235-275), in particular promoters of T cell receptors (Winoto and Baltimore, 1989. EMBO J. 8: 729-733) and immunoglobulins (Banerji, et al., 1983. Cell 33: 729-740; Queen and Baltimore, 1983. Cell 33: 741-748), neuron-specific promoters (e.g., the neurofilament promoter; Byrne and Ruddle, 1989. Proc. Natl. Acad. Sci. USA 86: 5473-5477), pancreas-specific promoters (Edlund, et al., 1985. Science 230: 912-916), and mammary gland-specific promoters (e.g., milk whey promoter; U.S. Pat. No. 4,873,316 and European Application Publication No. 264,166). Developmentally-regulated promoters are also encompassed, e.g., the murine hox promoters (Kessel and Gruss, 1990. Science 249: 374-379) and the α-fetoprotein promoter (Campes and Tilghman, 1989. Genes Dev. 3: 537-546).

[0241] The invention further provides a recombinant expression vector comprising a DNA molecule of the invention cloned into the expression vector in an antisense orientation. That is, the DNA molecule is operatively-linked to a regulatory sequence in a manner that allows for expression (by transcription of the DNA molecule) of an RNA molecule that is antisense to NOVX mRNA. Regulatory sequences operatively linked to a nucleic acid cloned in the antisense orientation can be chosen that direct the continuous expression of the antisense RNA molecule in a variety of cell types, for instance viral promoters and/or enhancers, or regulatory sequences can be chosen that direct constitutive, tissue specific or cell type specific expression of antisense RNA. The antisense expression vector can be in the form of a recombinant plasmid, phagemid or attenuated virus in which antisense nucleic acids are produced under the control of a high efficiency regulatory region, the activity of which can be determined by the cell type into which the vector is introduced. For a discussion of the regulation of gene expression using antisense genes see, e.g., Weintraub, et al., “Antisense RNA as a molecular tool for genetic analysis,” Reviews-Trends in Genetics, Vol. 1(1) 1986.

[0242] Another aspect of the invention pertains to host cells into which a recombinant expression vector of the invention has been introduced. The terms “host cell” and “recombinant host cell” are used interchangeably herein. It is understood that such terms refer not only to the particular subject cell but also to the progeny or potential progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.

[0243] A host cell can be any prokaryotic or eukaryotic cell. For example, NOVX protein can be expressed in bacterial cells such as E. coli, insect cells, yeast or mammalian cells (such as Chinese hamster ovary cells (CHO) or COS cells). Other suitable host cells are known to those skilled in the art.

[0244] Vector DNA can be introduced into prokaryotic or eukaryotic cells via conventional transformation or transfection techniques. As used herein, the terms “transformation” and “transfection” are intended to refer to a variety of art-recognized techniques for introducing foreign nucleic acid (e.g., DNA) into a host cell, including calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, lipofection, or electroporation. Suitable methods for transforming or transfecting host cells can be found in Sambrook, et al. (MOLECULAR CLONING: A LABORATORY MANUAL. 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989), and other laboratory manuals.

[0245] For stable transfection of mammalian cells, it is known that, depending upon the expression vector and transfection technique used, only a small fraction of cells may integrate the foreign DNA into their genome. In order to identify and select these integrants, a gene that encodes a selectable marker (e.g., resistance to antibiotics) is generally introduced into the host cells along with the gene of interest. Various selectable markers include those that confer resistance to drugs, such as G418, hygromycin and methotrexate. Nucleic acid encoding a selectable marker can be introduced into a host cell on the same vector as that encoding NOVX or can be introduced on a separate vector. Cells stably transfected with the introduced nucleic acid can be identified by drug selection (e.g., cells that have incorporated the selectable marker gene will survive, while the other cells die).

[0246] A host cell of the invention, such as a prokaryotic or eukaryotic host cell in culture, can be used to produce (i.e., express) NOVX protein. Accordingly, the invention further provides methods for producing NOVX protein using the host cells of the invention. In one embodiment, the method comprises culturing the host cell of invention (into which a recombinant expression vector encoding NOVX protein has been introduced) in a suitable medium such that NOVX protein is produced. In another embodiment, the method further comprises isolating NOVX protein from the medium or the host cell.

[0247] Transgenic NOVX Animals

[0248] The host cells of the invention can also be used to produce non-human transgenic animals. For example, in one embodiment, a host cell of the invention is a fertilized oocyte or an embryonic stem cell into which NOVX protein-coding sequences have been introduced. Such host cells can then be used to create non-human transgenic animals in which exogenous NOVX sequences have been introduced into their genome or homologous recombinant animals in which endogenous NOVX sequences have been altered. Such animals are useful for studying the function and/or activity of NOVX protein and for identifying and/or evaluating modulators of NOVX protein activity. As used herein, a “transgenic animal” is a non-human animal, preferably a mammal, more preferably a rodent such as a rat or mouse, in which one or more of the cells of the animal includes a transgene. Other examples of transgenic animals include non-human primates, sheep, dogs, cows, goats, chickens, amphibians, etc. A transgene is exogenous DNA that is integrated into the genome of a cell from which a transgenic animal develops and that remains in the genome of the mature animal, thereby directing the expression of an encoded gene product in one or more cell types or tissues of the transgenic animal. As used herein, a “homologous recombinant animal” is a non-human animal, preferably a mammal, more preferably a mouse, in which an endogenous NOVX gene has been altered by homologous recombination between the endogenous gene and an exogenous DNA molecule introduced into a cell of the animal, e.g., an embryonic cell of the animal, prior to development of the animal.

[0249] A transgenic animal of the invention can be created by introducing NOVX-encoding nucleic acid into the male pronuclei of a fertilized oocyte (e.g., by microinjection, retroviral infection) and allowing the oocyte to develop in a pseudopregnant female foster animal. The human NOVX cDNA sequences, i.e., any one of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, can be introduced as a transgene into the genome of a non-human animal. Alternatively, a non-human homologue of the human NOVX gene, such as a mouse NOVX gene, can be isolated based on hybridization to the human NOVX cDNA (described further supra) and used as a transgene. Intronic sequences and polyadenylation signals can also be included in the transgene to increase the efficiency of expression of the transgene. A tissue-specific regulatory sequence(s) can be operably-linked to the NOVX transgene to direct expression of NOVX protein to particular cells. Methods for generating transgenic animals via embryo manipulation and microinjection, particularly animals such as mice, have become conventional in the art and are described, for example, in U.S. Pat. Nos. 4,736,866; 4,870,009; and 4,873,191; and Hogan, 1986. In: MANIPULATING THE MOUSE EMBRYO, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. Similar methods are used for production of other transgenic animals. A transgenic founder animal can be identified based upon the presence of the NOVX transgene in its genome and/or expression of NOVX mRNA in tissues or cells of the animals. A transgenic founder animal can then be used to breed additional animals carrying the transgene. Moreover, transgenic animals carrying a transgene-encoding NOVX protein can further be bred to other transgenic animals carrying other transgenes.

[0250] To create a homologous recombinant animal, a vector is prepared which contains at least a portion of a NOVX gene into which a deletion, addition or substitution has been introduced to thereby alter, e.g., functionally disrupt, the NOVX gene. The NOVX gene can be a human gene (e.g., the cDNA of any one of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107), but more preferably, is a non-human homologue of a human NOVX gene. For example, a mouse homologue of human NOVX gene of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, can be used to construct a homologous recombination vector suitable for altering an endogenous NOVX gene in the mouse genome. In one embodiment, the vector is designed such that, upon homologous recombination, the endogenous NOVX gene is functionally disrupted (i.e., no longer encodes a functional protein; also referred to as a “knock out” vector).

[0251] Alternatively, the vector can be designed such that, upon homologous recombination, the endogenous NOVX gene is mutated or otherwise altered but still encodes functional protein (e.g., the upstream regulatory region can be altered to thereby alter the expression of the endogenous NOVX protein). In the homologous recombination vector, the altered portion of the NOVX gene is flanked at its 5′- and 3′-termini by additional nucleic acid of the NOVX gene to allow for homologous recombination to occur between the exogenous NOVX gene carried by the vector and an endogenous NOVX gene in an embryonic stem cell. The additional flanking NOVX nucleic acid is of sufficient length for successful homologous recombination with the endogenous gene. Typically, several kilobases of flanking DNA (both at the 5′- and 3′-termini) are included in the vector. See, e.g., Thomas, et al., 1987. Cell 51: 503 for a description of homologous recombination vectors. The vector is ten introduced into an embryonic stem cell line (e.g., by electroporation) and cells in which the introduced NOVX gene has homologously-recombined with the endogenous NOVX gene are selected. See, e.g., Li, et al., 1992. Cell 69: 915.

[0252] The selected cells are then injected into a blastocyst of an animal (e.g., a mouse) to form aggregation chimeras. See, e.g., Bradley, 1987. In: TERATOCARCINOMAS AND EMBRYONIC STEM CELLS: A PRACTICAL APPROACH, Robertson, ed. IRL, Oxford, pp. 113-152. A chimeric embryo can then be implanted into a suitable pseudopregnant female foster animal and the embryo brought to term. Progeny harboring the homologously-recombined DNA in their germ cells can be used to breed animals in which all cells of the animal contain the homologously-recombined DNA by germline transmission of the transgene. Methods for constructing homologous recombination vectors and; homologous recombinant animals are described further in Bradley, 1991. Curr. Opin. Biotechnol. 2: 823-829; PCT International Publication Nos.: WO 90/11354; WO 91/01140; WO 92/0968; and WO 93/04169.

[0253] In another embodiment, transgenic non-humans animals can be produced that contain selected systems that allow for regulated expression of the transgene. One example of such a system is the cre/loxP recombinase system of bacteriophage P1. For a description of the cre/loxP recombinase system, See, e.g., Lakso, et al., 1992. Proc. Natl. Acad. Sci. USA 89: 6232-6236. Another example of a recombinase system is the FLP recombinase system of Saccharomyces cerevisiae. See, O'Gorman, et al., 1991. Science 251:1351-1355. If a cre/loxP recombinase system is used to regulate expression of the transgene, animals containing transgenes encoding both the Cre recombinase and a selected protein are required. Such animals can be provided through the construction of “double” transgenic animals, e.g., by mating two transgenic animals, one containing a transgene encoding a selected protein and the other containing a transgene encoding a recombinase.

[0254] Clones of the non-human transgenic animals described herein can also be produced according to the methods described in Wilmut, et al., 1997. Nature 385: 810-813. In brief, a cell (e.g., a somatic cell) from the transgenic animal can be isolated and induced to exit the growth cycle and enter G0 phase. The quiescent cell can then be fused, e.g., through the use of electrical pulses, to an enucleated oocyte from an animal of the same species from which the quiescent cell is isolated. The reconstructed oocyte is then cultured such that it develops to morula or blastocyte and then transferred to pseudopregnant female foster animal. The offspring borne of this female foster animal will be a clone of the animal from which the cell (e.g., the somatic cell) is isolated.

[0255] Pharmaceutical Compositions

[0256] The NOVX nucleic acid molecules, NOVX proteins, and anti-NOVX antibodies (also referred to herein as “active compounds”) of the invention, and derivatives, fragments, analogs and homologs thereof, can be incorporated into pharmaceutical compositions suitable for administration. Such compositions typically comprise the nucleic acid molecule, protein, or antibody and a pharmaceutically acceptable carrier. As used herein, “pharmaceutically acceptable carrier” is intended to include any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like, compatible with pharmaceutical administration. Suitable carriers are described in the most recent edition of Remington's Pharmaceutical Sciences, a standard reference text in the field, which is incorporated herein by reference. Preferred examples of such carriers or diluents include, but are not limited to, water, saline, finger's solutions, dextrose solution, and 5% human serum albumin. Liposomes and non-aqueous vehicles such as fixed oils may also be used. The use of such media and agents for pharmaceutically active substances is well known in the art. Except insofar as any conventional media or agent is incompatible with the active compound, use thereof in the compositions is contemplated. Supplementary active compounds can also be incorporated into the compositions.

[0257] A pharmaceutical composition of the invention is formulated to be compatible with its intended route of administration. Examples of routes of administration include parenteral, e.g., intravenous, intradermal, subcutaneous, oral (e.g., inhalation), transdermal (i.e., topical), transmucosal, and rectal administration. Solutions or suspensions used for parenteral, intradermal, or subcutaneous application can include the following components: a sterile diluent such as water for injection, saline solution, fixed oils, polyethylene glycols, glycerine, propylene glycol or other synthetic solvents; antibacterial agents such as benzyl alcohol or methyl parabens; antioxidants such as ascorbic acid or sodium bisulfite; chelating agents such as ethylenediaminetetraacetic acid (EDTA); buffers such as acetates, citrates or phosphates, and agents for the adjustment of tonicity such as sodium chloride or dextrose. The pH can be adjusted with acids or bases, such as hydrochloric acid or sodium hydroxide. The parenteral preparation can be enclosed in ampoules, disposable syringes or multiple dose vials made of glass or plastic.

[0258] Pharmaceutical compositions suitable for injectable use include sterile aqueous solutions (where water soluble) or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersion. For intravenous administration, suitable carriers include physiological saline, bacteriostatic water, Cremophor EL™ (BASF, Parsippany, N.J.) or phosphate buffered saline (PBS). In all cases, the composition must be sterile and should be fluid to the extent that easy syringeability exists. It must be stable under the conditions of manufacture and storage and must be preserved against the contaminating action of microorganisms such as bacteria and fungi. The carner can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), and suitable mixtures thereof. The proper fluidity can be maintained, for example, by the use of a coating such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of surfactants. Prevention of the action of microorganisms can be achieved by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, ascorbic acid, thimerosal, and the like. In many cases, it will be preferable to include isotonic agents, for example, sugars, polyalcohols such as manitol, sorbitol, sodium chloride in the composition. Prolonged absorption of the injectable compositions can be brought about by including in the composition an agent which delays absorption, for example, aluminum monostearate and gelatin.

[0259] Sterile injectable solutions can be prepared by incorporating the active compound (e.g., a NOVX protein or anti-NOVX antibody) in the required amount in an appropriate solvent with one or a combination of ingredients enumerated above, as required, followed by filtered sterilization. Generally, dispersions are prepared by incorporating the active compound into a sterile vehicle that contains a basic dispersion medium and the required other ingredients from those enumerated above. In the case of sterile powders for the preparation of sterile injectable solutions, methods of preparation are vacuum drying and freeze-drying that yields a powder of the active ingredient plus any additional desired ingredient from a previously sterile-filtered solution thereof.

[0260] Oral compositions generally include an inert diluent or an edible carrier. They can be enclosed in gelatin capsules or compressed into tablets. For the purpose of oral therapeutic administration, the active compound can be incorporated with excipients and used in the form of tablets, troches, or capsules. Oral compositions can also be prepared using a fluid carrier for use as a mouthwash, wherein the compound in the fluid carrier is applied orally and swished and expectorated or swallowed. Pharmaceutically compatible binding agents, and/or adjuvant materials can be included as part of the composition. The tablets, pills, capsules, troches and the like can contain any of the following ingredients, or compounds of a similar nature: a binder such as microcrystalline cellulose, gum tragacanth or gelatin; an excipient such as starch or lactose, a disintegrating agent such as alginic acid, Primogel, or corn starch; a lubricant such as magnesium stearate or Sterotes; a glidant such as colloidal silicon dioxide; a sweetening agent such as sucrose or saccharin; or a flavoring agent such as peppermint, methyl salicylate, or orange flavoring.

[0261] For administration by inhalation, the compounds are delivered in the form of an aerosol spray from pressured container or dispenser which contains a suitable propellant, e.g., a gas such as carbon dioxide, or a nebulizer.

[0262] Systemic administration can also be by transmucosal or transdermal means. For transmucosal or transdermal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are generally known in the art, and include, for example, for transmucosal administration, detergents, bile salts, and fusidic acid derivatives. Transmucosal administration can be accomplished through the use of nasal sprays or suppositories. For transdermal administration, the active compounds are formulated into ointments, salves, gels, or creams as generally known in the art.

[0263] The compounds can also be prepared in the form of suppositories (e.g., with conventional suppository bases such as cocoa butter and other glycerides) or retention enemas for rectal delivery.

[0264] In one embodiment, the active compounds are prepared with carriers that will protect the compound against rapid elimination from the body, such as a controlled release formulation, including implants and microencapsulated delivery systems. Biodegradable, biocompatible polymers can be used, such as ethylene vinyl acetate, polyanhydrides, polyglycolic acid, collagen, polyorthoesters, and polylactic acid. Methods for preparation of such formulations will be apparent to those skilled in the art. The materials can also be obtained commercially from Alza Corporation and Nova Pharmaceuticals, Inc. Liposomal suspensions (including liposomes targeted to infected cells with monoclonal antibodies to viral antigens) can also be used as pharmaceutically acceptable carriers. These can be prepared according to methods known to those skilled in the art, for example, as described in U.S. Pat. No. 4,522,811.

[0265] It is especially advantageous to formulate oral or parenteral compositions in dosage unit form for ease of administration and uniformity of dosage. Dosage unit form as used herein refers to physically discrete units suited as unitary dosages for the subject to be treated; each unit containing a predetermined quantity of active compound calculated to produce the desired therapeutic effect in association with the required pharmaceutical carrier. The specification for the dosage unit forms of the invention are dictated by and directly dependent on the unique characteristics of the active compound and the particular therapeutic effect to be achieved, and the limitations inherent in the art of compounding such an active compound for the treatment of individuals.

[0266] The nucleic acid molecules of the invention can be inserted into vectors and used as gene therapy vectors. Gene therapy vectors can be delivered to a subject by, for example, intravenous injection, local administration (see, e.g., U.S. Pat. No. 5,328,470) or by stereotactic injection (see, e.g., Chen, et al., 1994. Proc. Natl. Acad. Sci. USA 91: 3054-3057). The pharmaceutical preparation of the gene therapy vector can include the gene therapy vector in an acceptable diluent, or can comprise a slow release matrix in which the gene delivery vehicle is imbedded. Alternatively, where the complete gene delivery vector can be produced intact from recombinant cells, e.g., retroviral vectors, the pharmaceutical preparation can include one or more cells that produce the gene delivery system.

[0267] The pharmaceutical compositions can be included in a container, pack, or dispenser together with instructions for administration.

[0268] Screening and Detection Methods

[0269] The isolated nucleic acid molecules of the invention can be used to express NOVX protein (e.g., via a recombinant expression vector in a host cell in gene therapy applications), to detect NOVX mRNA (e.g., in a biological sample) or a genetic lesion in a NOVX gene, and to modulate NOVX activity, as described further, below. In addition, the NOVX proteins can be used to screen drugs or compounds that modulate the NOVX protein activity or expression as well as to treat disorders characterized by insufficient or excessive production of NOVX protein or production of NOVX protein forms that have decreased or aberrant activity compared to NOVX wild-type protein (e.g.; diabetes (regulates insulin release); obesity (binds and transport lipids); metabolic disturbances associated with obesity, the metabolic syndrome X as well as anorexia and wasting disorders associated with chronic diseases and various cancers, and infectious disease(possesses anti-microbial activity) and the various dyslipidemias. In addition, the anti-NOVX antibodies of the invention can be used to detect and isolate NOVX proteins and modulate NOVX activity. In yet a further aspect, the invention can be used in methods to influence appetite, absorption of nutrients and the disposition of metabolic substrates in both a positive and negative fashion.

[0270] The invention further pertains to novel agents identified by the screening assays described herein and uses thereof for treatments as described, supra.

[0271] Screening Assays

[0272] The invention provides a method (also referred to herein as a “screening assay”) for identifying modulators, i.e., candidate or test compounds or agents (e.g., peptides, peptidomimetics, small molecules or other drugs) that bind to NOVX proteins or have a stimulatory or inhibitory effect on, e.g., NOVX protein expression or NOVX protein activity. The invention also includes compounds identified in the screening assays described herein.

[0273] In one embodiment, the invention provides assays for screening candidate or test compounds which bind to or modulate the activity of the membrane-bound form of a NOVX protein or polypeptide or biologically-active portion thereof. The test compounds of the invention can be obtained using any of the numerous approaches in combinatorial library methods known in the art, including: biological libraries; spatially addressable parallel solid phase or solution phase libraries; synthetic library methods requiring deconvolution; the “one-bead one-compound” library method; and synthetic library methods using affinity chromatography selection. The biological library approach is limited to peptide libraries, while the other four approaches are applicable to peptide, non-peptide oligomer or small molecule libraries of compounds. See, e.g., Lam, 1997. Anticancer Drug Design 12: 145.

[0274] A “small molecule” as used herein, is meant to refer to a composition that has a molecular weight of less than about 5 kD and most preferably less than about 4 kD. Small molecules can be, e.g., nucleic acids, peptides, polypeptides, peptidomimetics, carbohydrates, lipids or other organic or inorganic molecules. Libraries of chemical and/or biological mixtures, such as fungal, bacterial, or algal extracts, are known in the art and can be screened with any of the assays of the invention.

[0275] Examples of methods for the synthesis of molecular libraries can be found in the art, for example in: DeWitt, et al., 1993. Proc. Natl. Acad. Sci. U.S.A. 90: 6909; Erb, et al., 1994. Proc. Natl. Acad. Sci. U.S.A. 91: 11422; Zuckermann, et al., 1994. J. Med. Chem. 37: 2678; Cho, et al., 1993. Science 261: 1303; Carrell, et al., 1994. Angew. Chern. Int. Ed. Engl. 33: 2059; Carell, et al., 1994. Angew. Chem. Int. Ed. Engl. 33: 2061; and Gallop, et al., 1994. J. Med. Chem. 37: 1233.

[0276] Libraries of compounds may be presented in solution (e.g., Houghten, 1992. Biotechniques 13: 412-421), or on beads (Lam, 1991. Nature 354: 82-84), on chips (Fodor, 1993. Nature 364: 555-556), bacteria (Ladner, U.S. Pat. No. 5,223,409), spores (Ladner, U.S. Pat. No. 5,233,409), plasmids (Cull, et al., 1992. Proc. Natl. Acad. Sci. USA 89: 1865-1869) or on phage (Scott and Smith, 1990. Science 249: 386-390; Devlin, 1990. Science 249: 404-406; Cwirla, et al., 1990. Proc. Natl. Acad. Sci. U.S.A. 87: 6378-6382; Felici, 1991. J. Mol. Biol. 222: 301-310; Ladner, U.S. Pat. No. 5,233,409.).

[0277] In one embodiment, an assay is a cell-based assay in which a cell which expresses a membrane-bound form of NOVX protein, or a biologically-active portion thereof, on the cell surface is contacted with a test compound and the ability of the test compound to bind to a NOVX protein determined. The cell, for example, can of mammalian origin or a yeast cell. Determining the ability of the test compound to bind to the NOVX protein can be accomplished, for example, by coupling the test compound with a radioisotope or enzymatic label such that binding of the test compound to the NOVX protein or biologically-active portion thereof can be determined by detecting the labeled compound in a complex. For example, test compounds can be labeled with 125I, 35S, 14C, or 3H, either directly or indirectly, and the radioisotope detected by direct counting of radioemission or by scintillation counting. Alternatively, test compounds can be enzymatically-labeled with, for example, horseradish peroxidase, alkaline phosphatase, or luciferase, and the enzymatic label detected by determination of conversion of an appropriate substrate to product. In one embodiment, the assay comprises contacting a cell which expresses a membrane-bound form of NOVX protein, or a biologically-active portion thereof, on the cell surface with a known compound which binds NOVX to form an assay mixture, contacting the assay mixture with a test compound, and determining the ability of the test compound to interact with a NOVX protein, wherein determining the ability of the test compound to interact with a NOVX protein comprises determining the ability of the test compound to preferentially bind to NOVX protein or a biologically-active portion thereof as compared to the known compound.

[0278] In another embodiment, an assay is a cell-based assay comprising contacting a cell expressing a membrane-bound form of NOVX protein, or a biologically-active portion thereof, on the cell surface with a test compound and determining the ability of the test compound to modulate (e.g., stimulate or inhibit) the activity of the NOVX protein or biologically-active portion thereof. Determining the ability of the test compound to modulate the activity of NOVX or a biologically-active portion thereof can be accomplished, for example, by determining the ability of the NOVX protein to bind to or interact with a NOVX target molecule. As used herein, a “target molecule” is a molecule with which a NOVX protein binds or interacts in nature, for example, a molecule on the surface of a cell which expresses a NOVX interacting protein, a molecule on the surface of a second cell, a molecule in the extracellular milieu, a molecule associated with the internal surface of a cell membrane or a cytoplasmic molecule. A NOVX target molecule can be a non-NOVX molecule or a NOVX protein or polypeptide of the invention. In one embodiment, a NOVX target molecule is a component of a signal transduction pathway that facilitates transduction of an extracellular signal (e.g. a signal generated by binding of a compound to a membrane-bound NOVX molecule) through the cell membrane and into the cell. The target, for example, can be a second intercellular protein that has catalytic activity or a protein that facilitates the association of downstream signaling molecules with NOVX.

[0279] Determining the ability of the NOVX protein to bind to or interact with a NOVX target molecule can be accomplished by one of the methods described above for determining direct binding. In one embodiment, determining the ability of the NOVX protein to bind to or interact with a NOVX target molecule can be accomplished by determining the activity of the target molecule. For example, the activity of the target molecule can be determined by detecting induction of a cellular second messenger of the target (i.e. intracellular Ca2+, diacylglycerol, IP3, etc.), detecting catalytic/enzymatic activity of the target an appropriate substrate, detecting the induction of a reporter gene (comprising a NOVX-responsive regulatory element operatively linked to a nucleic acid encoding a detectable marker, e.g., luciferase), or detecting a cellular response, for example, cell survival, cellular differentiation, or cell proliferation.

[0280] In yet another embodiment, an assay of the invention is a cell-free assay comprising contacting a NOVX protein or biologically-active portion thereof with a test compound and determining the ability of the test compound to bind to the NOVX protein or biologically-active portion thereof. Binding of the test compound to the NOVX protein can be determined either directly or indirectly as described above. In one such embodiment, the assay comprises contacting the NOVX protein or biologically-active portion thereof with a known compound which binds NOVX to form an assay mixture, contacting the assay mixture with a test compound, and determining the ability of the test compound to interact with a NOVX protein, wherein determining the ability of the test compound to interact with a NOVX protein comprises determining the ability of the test compound to preferentially bind to NOVX or biologically-active portion thereof as compared to the known compound.

[0281] In still another embodiment, an assay is a cell-free assay comprising contacting NOVX protein or biologically-active portion thereof with a test compound and determining the ability of the test compound to modulate (e.g. stimulate or inhibit) the activity of the NOVX protein or biologically-active portion thereof. Determining the ability of the test compound to modulate the activity of NOVX can be accomplished, for example, by determining the ability of the NOVX protein to bind to a NOVX target molecule by one of the methods described above for determining direct binding. In an alternative embodiment, determining the ability of the test compound to modulate the activity of NOVX protein can be accomplished by determining the ability of the NOVX protein further modulate a NOVX target molecule. For example, the catalytic/enzymatic activity of the target molecule on an appropriate substrate can be determined as described, supra.

[0282] In yet another embodiment, the cell-free assay comprises contacting the NOVX protein or biologically-active portion thereof with a known compound which binds NOVX protein to form an assay mixture, contacting the assay mixture with a test compound, and determining the ability of the test compound to interact with a NOVX protein, wherein determining the ability of the test compound to interact with a NOVX protein comprises determining the ability of the NOVX protein to preferentially bind to or modulate the activity of a NOVX target molecule.

[0283] The cell-free assays of the invention are amenable to use of both the soluble form or the membrane-bound form of NOVX protein. In the case of cell-free assays comprising the membrane-bound form of NOVX protein, it may be desirable to utilize a solubilizing agent such that the membrane-bound form of NOVX protein is maintained in solution. Examples of such solubilizing agents include non-ionic detergents such as n-octylglucoside, n-dodecylglucoside, n-dodecylmaltoside, octanoyl-N-methylglucamide, decanoyl-N-methylglucamide, Triton® X-100, Triton® X-114, Thesit®, Isotridecypoly(ethylene glycol ether)n, N-dodecyl-N,N-dimethyl-3-ammonio-1-propane sulfonate, 3-(3-cholamidopropyl) dimethylamminiol-1-propane sulfonate (CHAPS), or 3-(3-cholamidopropyl)dimethylamminiol-2-hydroxy-1-propane sulfonate (CHAPSO).

[0284] In more than one embodiment of the above assay methods of the invention, it may be desirable to immobilize either NOVX protein or its target molecule to facilitate separation of complexed from uncomplexed forms of one or both of the proteins, as well as to accommodate automation of the assay. Binding of a test compound to NOVX protein, or interaction of NOVX protein with a target molecule in the presence and absence of a candidate compound, can be accomplished in any vessel suitable for containing the reactants. Examples of such vessels include microtiter plates, test tubes, and micro-centrifuge tubes. In one embodiment, a fusion protein can be provided that adds a domain that allows one or both of the proteins to be bound to a matrix. For example, GST-NOVX fusion proteins or GST-target fusion proteins can be adsorbed onto glutathione sepharose beads (Sigma Chemical, St. Louis, Mo.) or glutathione derivatized microtiter plates, that are then combined with the test compound or the test compound and either the non-adsorbed target protein or NOVX protein, and the mixture is incubated under conditions conducive to complex formation (e.g., at physiological conditions for salt and pH). Following incubation, the beads or microtiter plate wells are washed to remove any unbound components, the matrix immobilized in the case of beads, complex determined either directly or indirectly, for example, as described, supra. Alternatively, the complexes can be dissociated from the matrix, and the level of NOVX protein binding or activity determined using standard techniques.

[0285] Other techniques for immobilizing proteins on matrices can also be used in the screening assays of the invention. For example, either the NOVX protein or its target molecule can be immobilized utilizing conjugation of biotin and streptavidin. Biotinylated NOVX protein or target molecules can be prepared from biotin-NHS (N-hydroxy-succinimide) using techniques well-known within the art (e.g., biotinylation kit, Pierce Chemicals, Rockford, Ill.), and immobilized in the wells of streptavidin-coated 96 well plates (Pierce Chemical). Alternatively, antibodies reactive with NOVX protein or target molecules, but which do not interfere with binding of the NOVX protein to its target molecule, can be derivatized to the wells of the plate, and unbound target or NOVX protein trapped in the wells by antibody conjugation. Methods for detecting such complexes, in addition to those described above for the GST-immobilized complexes, include immunodetection of complexes using antibodies reactive with the NOVX protein or target molecule, as well as enzyme-linked assays that rely on detecting an enzymatic activity associated with the NOVX protein or target molecule.

[0286] In another embodiment, modulators of NOVX protein expression are identified in a method wherein a cell is contacted with a candidate compound and the expression of NOVX mRNA or protein in the cell is determined. The level of expression of NOVX mRNA or protein in the presence of the candidate compound is compared to the level of expression of NOVX mRNA or protein in the absence of the candidate compound. The candidate compound can then be identified as a modulator of NOVX mRNA or protein expression based upon this comparison. For example, when expression of NOVX mRNA or protein is greater (i.e., statistically significantly greater) in the presence of the candidate compound than in its absence, the candidate compound is identified as a stimulator of NOVX mRNA or protein expression. Alternatively, when expression of NOVX mRNA or protein is less (statistically significantly less) in the presence of the candidate compound than in its absence, the candidate compound is identified as an inhibitor of NOVX mRNA or protein expression. The level of NOVX mRNA or protein expression in the cells can be determined by methods described herein for detecting NOVX mRNA or protein.

[0287] In yet another aspect of the invention, the NOVX proteins can be used as “bait proteins” in a two-hybrid assay or three hybrid assay (see, e.g., U.S. Pat. No. 5,283,317; Zervos, et al., 1993. Cell 72: 223-232; Madura, et al., 1993. J. Biol. Chem. 268: 12046-12054; Bartel, et al., 1993. Biotechniques 14: 920-924; Iwabuchi, et al., 1993. Oncogene 8: 1693-1696; and Brent WO 94/10300), to identify other proteins that bind to or interact with NOVX (“NOVX-binding proteins” or “NOVX-bp”) and modulate NOVX activity. Such NOVX-binding proteins are also involved in the propagation of signals by the NOVX proteins as, for example, upstream or downstream elements of the NOVX pathway.

[0288] The two-hybrid system is based on the modular nature of most transcription factors, which consist of separable DNA-binding and activation domains. Briefly, the assay utilizes two different DNA constructs. In one construct, the gene that codes for NOVX is fused to a gene encoding the DNA binding domain of a known transcription factor (e.g., GAL-4). In the other construct, a DNA sequence, from a library of DNA sequences, that encodes an unidentified protein (“prey” or “sample”) is fused to a gene that codes for the activation domain of the known transcription factor. If the “bait” and the “prey” proteins are able to interact, in vivo, forming a NOVX-dependent complex, the DNA-binding and activation domains of the transcription factor are brought into close proximity. This proximity allows transcription of a reporter gene (e.g., LacZ) that is operably linked to a transcriptional regulatory site responsive to the transcription factor. Expression of the reporter gene can be detected and cell colonies containing the functional transcription factor can be isolated and used to obtain the cloned gene that encodes the protein which interacts with NOVX.

[0289] The invention further pertains to novel agents identified by the aforementioned screening assays and uses thereof for treatments as described herein.

[0290] Detection Assays

[0291] Portions or fragments of the cDNA sequences identified herein (and the corresponding complete gene sequences) can be used in numerous ways as polynucleotide reagents. By way of example, and not of limitation, these sequences can be used to: (i) map their respective genes on a chromosome; and, thus, locate gene regions associated with genetic disease; (ii) identify an individual from a minute biological sample (tissue typing); and (iii) aid in forensic identification of a biological sample. Some of these applications are described in the subsections, below.

[0292] Chromosome Mapping

[0293] Once the sequence (or a portion of the sequence) of a gene has been isolated, this sequence can be used to map the location of the gene on a chromosome. This process is called chromosome mapping. Accordingly, portions or fragments of the NOVX sequences of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or fragments or derivatives thereof, can be used to map the location of the NOVX genes, respectively, on a chromosome. The mapping of the NOVX sequences to chromosomes is an important first step in correlating these sequences with genes associated with disease.

[0294] Briefly, NOVX genes can be mapped to chromosomes by preparing PCR primers (preferably 15-25 bp in length) from the NOVX sequences. Computer analysis of the NOVX, sequences can be used to rapidly select primers that do not span more than one exon in the genomic DNA, thus complicating the amplification process. These primers can then be used for PCR screening of somatic cell hybrids containing individual human chromosomes. Only those hybrids containing the human gene corresponding to the NOVX sequences will yield an amplified fragment.

[0295] Somatic cell hybrids are prepared by fusing somatic cells from different mammals (e.g., human and mouse cells). As hybrids of human and mouse cells grow and divide, they gradually lose human chromosomes in random order, but retain the mouse chromosomes. By using media in which mouse cells cannot grow, because they lack a particular enzyme, but in which human cells can, the one human chromosome that contains the gene encoding the needed enzyme will be retained. By using various media, panels of hybrid cell lines can be established. Each cell line in a panel contains either a single human chromosome or a small number of human chromosomes, and a full set of mouse chromosomes, allowing easy mapping of individual genes to specific human chromosomes. See, e.g., D'Eustachio, et al., 1983. Science 220: 919-924. Somatic cell hybrids containing only fragments of human chromosomes can also be produced by using human chromosomes with translocations and deletions.

[0296] PCR mapping of somatic cell hybrids is a rapid procedure for assigning a particular sequence to a particular chromosome. Three or more sequences can be assigned per day using a single thermal cycler. Using the NOVX sequences to design oligonucleotide primers, sub-localization can be achieved with panels of fragments from specific chromosomes.

[0297] Fluorescence in situ hybridization (FISH) of a DNA sequence to a metaphase chromosomal spread can further be used to provide a precise chromosomal location in one step. Chromosome spreads can be made using cells whose division has been blocked in metaphase by a chemical like colcemid that disrupts the mitotic spindle. The chromosomes can be treated briefly with trypsin, and then stained with Giemsa. A pattern of light and dark bands develops on each chromosome, so that the chromosomes can be identified individually. The FISH technique can be used with a DNA sequence as short as 500 or 600 bases. However, clones larger than 1,000 bases have a higher likelihood of binding to a unique chromosomal location with sufficient signal intensity for simple detection. Preferably 1,000 bases, and more preferably 2,000 bases, will suffice to get good results at a reasonable amount of time. For a review of this technique, see, Verma, et al., HUMAN CHROMOSOMES: A MANUAL OF BASIC TECHNIQUES (Pergamon Press, New York 1988).

[0298] Reagents for chromosome mapping can be used individually to mark a single chromosome or a single site on that chromosome, or panels of reagents can be used for marking multiple sites and/or multiple chromosomes. Reagents corresponding to noncoding regions of the genes actually are preferred for mapping purposes. Coding sequences are more likely to be conserved within gene families, thus increasing the chance of cross hybridizations during chromosomal mapping.

[0299] Once a sequence has been mapped to a precise chromosomal location, the physical position of the sequence on the chromosome can be correlated with genetic map data. Such data are found, e.g., in McKusick, MENDELIAN INHERITANCE IN MAN, available on-line through Johns Hopkins University Welch Medical Library). The relationship between genes and disease, mapped to the same chromosomal region, can then be identified through linkage analysis (co-inheritance of physically adjacent genes), described in, e.g., Egeland, et al., 1987. Nature, 325: 783-787.

[0300] Moreover, differences in the DNA sequences between individuals affected and unaffected with a disease associated with the NOVX gene, can be determined. If a mutation is observed in some or all of the affected individuals but not in any unaffected individuals, then the mutation is likely to be the causative agent of the particular disease. Comparison of affected and unaffected individuals generally involves first looking for structural alterations in the chromosomes, such as deletions or translocations that are visible from chromosome spreads or detectable using PCR based on that DNA sequence. Ultimately, complete sequencing of genes from several individuals can be performed to confirm the presence of a mutation and to distinguish mutations from polymorphisms.

[0301] Tissue Typing

[0302] The NOVX sequences of the invention can also be used to identify individuals from minute biological samples. In this technique, an individual's genomic DNA is digested with one or more restriction enzymes, and probed on a Southern blot to yield unique bands for identification. The sequences of the invention are useful as additional DNA markers for RFLP (“restriction fragment length polymorphisms,” described in U.S. Pat. No. 5,272,057).

[0303] Furthermore, the sequences of the invention can be used to provide an alternative technique that determines the actual base-by-base DNA sequence of selected portions of an individual's genome. Thus, the NOVX sequences described herein can be used to prepare two PCR primers from the 5′- and 3′-termini of the sequences. These primers can then be used to amplify an individual's DNA and subsequently sequence it.

[0304] Panels of corresponding DNA sequences from individuals, prepared in this manner, can provide unique individual identifications, as each individual will have a unique set of such DNA sequences due to allelic differences. The sequences of the invention can be used to obtain such identification sequences from individuals and from tissue. The NOVX sequences of the invention uniquely represent portions of the human genome. Allelic variation occurs to some degree in the coding regions of these sequences, and to a greater degree in the noncoding regions. It is estimated that allelic variation between individual humans occurs with a frequency of about once per each 500 bases. Much of the allelic variation is due to single nucleotide polymorphisms (SNPs), which include restriction fragment length polymorphisms (RFLPs).

[0305] Each of the sequences described herein can, to some degree, be used as a standard against which DNA from an individual can be compared for identification purposes. Because greater numbers of polymorphisms occur in the noncoding regions, fewer sequences are necessary to differentiate individuals. The noncoding sequences can comfortably provide positive individual identification with a panel of perhaps 10 to 1,000 primers that each yield a noncoding amplified sequence of 100 bases. If coding sequences, such as those of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, are used, a more appropriate number of primers for positive individual identification would be 500-2,000.

[0306] Predictive Medicine

[0307] The invention also pertains to the field of predictive medicine in which diagnostic assays, prognostic assays, pharmacogenomics, and monitoring clinical trials are used for prognostic (predictive) purposes to thereby treat an individual prophylactically. Accordingly, one aspect of the invention relates to diagnostic assays for determining NOVX protein and/or nucleic acid expression as well as NOVX activity, in the context of a biological sample (e.g., blood, serum, cells, tissue) to thereby determine whether an individual is afflicted with a disease or disorder, or is at risk of developing a disorder, associated with aberrant NOVX expression or activity. The disorders include metabolic disorders, diabetes, obesity, infectious disease, anorexia, cancer-associated cachexia, cancer, neurodegenerative disorders, Alzheimer's Disease, Parkinson's Disorder, immune disorders, and hematopoietic disorders, and the various dyslipidemias, metabolic disturbances associated with obesity, the metabolic syndrome X and wasting disorders associated with chronic diseases and various cancers. The invention also provides for prognostic (or predictive) assays for determining whether an individual is at risk of developing a disorder associated with NOVX protein, nucleic acid expression or activity. For example, mutations in a NOVX gene can be assayed in a biological sample. Such assays can be used for prognostic or predictive purpose to thereby prophylactically treat an individual prior to the onset of a disorder characterized by or associated with NOVX protein, nucleic acid expression, or biological activity.

[0308] Another aspect of the invention provides methods for determining NOVX protein, nucleic acid expression or activity in an individual to thereby select appropriate therapeutic or prophylactic agents for that individual (referred to herein as “pharmacogenomics”). Pharmacogenomics allows for the selection of agents (e.g., drugs) for therapeutic or prophylactic treatment of an individual based on the genotype of the individual (e.g., the genotype of the individual examined to determine the ability of the individual to respond to a particular agent.)

[0309] Yet another aspect of the invention pertains to monitoring the influence of agents (e.g., drugs, compounds) on the expression or activity of NOVX in clinical trials.

[0310] These and other agents are described in further detail in the following sections.

[0311] Diagnostic Assays

[0312] An exemplary method for detecting the presence or absence of NOVX in a biological sample involves obtaining a biological sample from a test subject and contacting the biological sample with a compound or an agent capable of detecting NOVX protein or nucleic acid (e.g., mRNA, genomic DNA) that encodes NOVX protein such that the presence of NOVX is detected in the biological sample. An agent for detecting NOVX mRNA or genomic DNA is a labeled nucleic acid probe capable of hybridizing to NOVX mRNA or genomic DNA. The nucleic acid probe can be, for example, a full-length NOVX nucleic acid, such as the nucleic acid of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107, or a portion thereof, such as an oligonucleotide of at least 15, 30, 50, 100, 250 or 500 nucleotides in length and sufficient to specifically hybridize under stringent conditions to NOVX mRNA or genomic DNA. Other suitable probes for use in the diagnostic assays of the invention are described herein.

[0313] An agent for detecting NOVX protein is an antibody capable of binding to NOVX protein, preferably an antibody with a detectable label. Antibodies can be polyclonal, or more preferably, monoclonal. An intact antibody, or a fragment thereof (e.g., Fab or F(ab′)2) can be used. The term “labeled”, with regard to the probe or antibody, is intended to encompass direct labeling of the probe or antibody by coupling (i.e., physically linking) a detectable substance to the probe or antibody, as well as indirect labeling of the probe or antibody by reactivity with another reagent that is directly labeled. Examples of indirect labeling include detection of a primary antibody using a fluorescently-labeled secondary antibody and end-labeling of a DNA probe with biotin such that it can be detected with fluorescently-labeled streptavidin. The term “biological sample” is intended to include tissues, cells and biological fluids isolated from a subject, as well as tissues, cells and fluids present within a subject. That is, the detection method of the invention can be used to detect NOVX mRNA, protein, or genomic DNA in a biological sample in vitro as well as in vivo. For example, in vitro techniques for detection of NOVX mRNA include Northern hybridizations and in situ hybridizations. In vitro techniques for detection of NOVX protein include enzyme linked immunosorbent assays (ELISAs), Western blots, immunoprecipitations, and immunofluorescence. In vitro techniques for detection of NOVX genomic DNA include Southern hybridizations. Furthermore, in vivo techniques for detection of NOVX protein include introducing into a subject a labeled anti-NOVX antibody. For example, the antibody can be labeled with a radioactive marker whose presence and location in a subject can be detected by standard imaging techniques.

[0314] In one embodiment, the biological sample contains protein molecules from the test subject. Alternatively, the biological sample can contain mRNA molecules from the test subject or genomic DNA molecules from the test subject. A preferred biological sample is a peripheral blood leukocyte sample isolated by conventional means from a subject.

[0315] In another embodiment, the methods further involve obtaining a control biological sample from a control subject, contacting the control sample with a compound or agent capable of detecting NOVX protein, mRNA, or genomic DNA, such that the presence of NOVX protein, mRNA or genomic DNA is detected in the biological sample, and comparing the presence of NOVX protein, mRNA or genomic DNA in the control sample with the presence of NOVX protein, mRNA or genomic DNA in the test sample.

[0316] The invention also encompasses kits for detecting the presence of NOVX in a biological sample. For example, the kit can comprise: a labeled compound or agent capable of detecting NOVX protein or mRNA in a biological sample; means for determining the amount of NOVX in the sample; and means for comparing the amount of NOVX in the sample with a standard. The compound or agent can be packaged in a suitable container. The kit can further comprise instructions for using the kit to detect NOVX protein or nucleic acid.

[0317] Prognostic Assays

[0318] The diagnostic methods described herein can furthermore be utilized to identify subjects having or at risk of developing a disease or disorder associated with aberrant NOVX expression or activity. For example, the assays described herein, such as the preceding diagnostic assays or the following assays, can be utilized to identify a subject having or at risk of developing a disorder associated with NOVX protein, nucleic acid expression or activity. Alternatively, the prognostic assays can be utilized to identify a subject having or at risk for developing a disease or disorder. Thus, the invention provides a method for identifying a disease or disorder associated with aberrant NOVX expression or activity in which a test sample is obtained from a subject and NOVX protein or nucleic acid (e.g., mRNA, genomic DNA) is detected, wherein the presence of NOVX protein or nucleic acid is diagnostic for a subject having or at risk of developing a disease or disorder associated with aberrant NOVX expression or activity. As used herein, a “test sample” refers to a biological sample obtained from a subject of interest. For example, a test sample can be a biological fluid (e.g., serum), cell sample, or tissue.

[0319] Furthermore, the prognostic assays described herein can be used to determine whether a subject can be administered an agent (e.g., an agonist, antagonist, peptidomimetic, protein, peptide, nucleic acid, small molecule, or other drug candidate) to treat a disease or disorder associated with aberrant NOVX expression or activity. For example, such methods can be used to determine whether a subject can be effectively treated with an agent for a disorder. Thus, the invention provides methods for determining whether a subject can be effectively treated with an agent for a disorder associated with aberrant NOVX expression or activity in which a test sample is obtained and NOVX protein or nucleic acid is detected (e.g., wherein the presence of NOVX protein or nucleic acid is diagnostic for a subject that can be administered the agent to treat a disorder associated with aberrant NOVX expression or activity).

[0320] The methods of the invention can also be used to detect genetic lesions in a NOVX gene, thereby determining if a subject with the lesioned gene is at risk for a disorder characterized by aberrant cell proliferation and/or differentiation. In various embodiments, the methods include detecting, in a sample of cells from the subject, the presence or absence of a genetic lesion characterized by at least one of an alteration affecting the integrity of a gene encoding a NOVX-protein, or the misexpression of the NOVX gene. For example, such genetic lesions can be detected by ascertaining the existence of at least one of: (i) a deletion of one or more nucleotides from a NOVX gene; (ii) an addition of one or more nucleotides to a NOVX gene; (iii) a substitution of one or more nucleotides of a NOVX gene, (iv) a chromosomal rearrangement of a NOVX gene; (v) an alteration in the level of a messenger RNA transcript of a NOVX gene, (vi) aberrant modification of a NOVX gene, such as of the methylation pattern of the genomic DNA, (vii) the presence of a non-wild-type splicing pattern of a messenger RNA transcript of a NOVX gene, (viii) a non-wild-type level of a NOVX protein, (ix) allelic loss of a NOVX gene, and (x) inappropriate post-translational modification of a NOVX protein. As described herein, there are a large number of assay techniques known in the art which can be used for detecting lesions in a NOVX gene. A preferred biological sample is a peripheral blood leukocyte sample isolated by conventional means from a subject. However, any biological sample containing nucleated cells may be used, including, for example, buccal mucosal cells.

[0321] In certain embodiments, detection of the lesion involves the use of a probe/primer in a polymerase chain reaction (PCR) (see, e.g., U.S. Pat. Nos. 4,683,195 and 4,683,202), such as anchor PCR or RACE PCR, or, alternatively, in a ligation chain reaction (LCR) (see, e.g., Landegran, et al., 1988. Science 241: 1077-1080; and Nakazawa, et al., 1994. Proc. Natl. Acad. Sci. USA 91: 360-364), the latter of which can be particularly useful for detecting point mutations in the NOVX-gene (see, Abravaya, et al., 1995. Nucl. Acids Res. 23: 675-682). This method can include the steps of collecting a sample of cells from a patient, isolating nucleic acid (e.g., genomic, mRNA or both) from the cells of the sample, contacting the nucleic acid sample with one or more primers that specifically hybridize to a NOVX gene under conditions such that hybridization and amplification of the NOVX gene (if present) occurs, and detecting the presence or absence of an amplification product, or detecting the size of the amplification product and comparing the length to a control sample. It is anticipated that PCR and/or LCR may be desirable to use as a preliminary amplification step in conjunction with any of the techniques used for detecting mutations described herein.

[0322] Alternative amplification methods include: self sustained sequence replication (see, Guatelli, et al., 1990. Proc. Natl. Acad. Sci. USA 87: 1874-1878), transcriptional amplification system (see, Kwoh, et al., 1989. Proc. Natl. Acad. Sci. USA 86: 1173-1177); Qβ Replicase (see, Lizardi, et al, 1988. BioTechinology 6: 1197), or any other nucleic acid amplification method, followed by the detection of the amplified molecules using techniques well known to those of skill in the art. These detection schemes are especially useful for the detection of nucleic acid molecules if such molecules are present in very low numbers.

[0323] In an alternative embodiment, mutations in a NOVX gene from a sample cell can be identified by alterations in restriction enzyme cleavage patterns. For example, sample and control DNA is isolated, amplified (optionally), digested with one or more restriction endonucleases, and fragment length sizes are determined by gel electrophoresis and compared. Differences in fragment length sizes between sample and control DNA indicates mutations in the sample DNA. Moreover, the use of sequence specific ribozymes (see, e.g., U.S. Pat. No. 5,493,531) can be used to score for the presence of specific mutations by development or loss of a ribozyme cleavage site.

[0324] In other embodiments, genetic mutations in NOVX can be identified by hybridizing a sample and control nucleic acids, e.g., DNA or RNA, to high-density arrays containing hundreds or thousands of oligonucleotides probes. See, e.g., Cronin, et al., 1996. Human Mutation 7: 244-255; Kozal, et al., 1996. Nat. Med. 2: 753-759. For example, genetic mutations in NOVX can be identified in two dimensional arrays containing light-generated DNA probes as described in Cronin, et al., supra. Briefly, a first hybridization array of probes can be used to scan through long stretches of DNA in a sample and control to identify base changes between the sequences by making linear arrays of sequential overlapping probes. This step allows the identification of point mutations. This is followed by a second hybridization array that allows the characterization of specific mutations by using smaller, specialized probe arrays complementary to all variants or mutations detected. Each mutation array is composed of parallel probe sets, one complementary to the wild-type gene and the other complementary to the mutant gene.

[0325] In yet another embodiment, any of a variety of sequencing reactions known in the art can be used to directly sequence the NOVX gene and detect mutations by comparing the sequence of the sample NOVX with the corresponding wild-type (control) sequence. Examples of sequencing reactions include those based on techniques developed by Maxim and Gilbert, 1977. Proc. Natl. Acad. Sci. USA 74: 560 or Sanger, 1977. Proc. Natl. Acad. Sci. USA 74: 5463. It is also contemplated that any of a variety of automated sequencing procedures can be utilized when performing the diagnostic assays (see, e.g., Naeve, et al., 1995. Biotechniques 19: 448), including sequencing by mass spectrometry (see, e.g., PCT International Publication No. WO 94/16101; Cohen, et al., 1996. Adv. Chromatography 36: 127-162; and Griffin, et al., 1993. Appl. Biochem. Biotechnol. 38: 147-159).

[0326] Other methods for detecting mutations in the NOVX gene include methods in which protection from cleavage agents is used to detect mismatched bases in RNA/RNA or RNA/DNA heteroduplexes. See, e.g., Myers, et al., 1985. Science 230: 1242. In general, the art technique of “mismatch cleavage” starts by providing heteroduplexes of formed by hybridizing (labeled) RNA or DNA containing the wild-type NOVX sequence with potentially mutant RNA or DNA obtained from a tissue sample. The double-stranded duplexes are treated with an agent that cleaves single-stranded regions of the duplex such as which will exist due to basepair mismatches between the control and sample strands. For instance, RNA/DNA duplexes can be treated with RNase and DNA/DNA hybrids treated with S1 nuclease to enzymatically digesting the mismatched regions. In other embodiments, either DNA/DNA or RNA/DNA duplexes can be treated with hydroxylamine or osmium tetroxide and with piperidine in order to digest mismatched regions. After digestion of the mismatched regions, the resulting material is then separated by size on denaturing polyacrylamide gels to determine the site of mutation. See, e.g., Cotton, et al., 1988. Proc. Natl. Acad. Sci. USA 85: 4397; Saleeba, et al., 1992. Methods Enzymol. 217: 286-295. In an embodiment, the control DNA or RNA can be labeled for detection.

[0327] In still another embodiment, the mismatch cleavage reaction employs one or more proteins that recognize mismatched base pairs in double-stranded DNA (so called “DNA mismatch repair” enzymes) in defined systems for detecting and mapping point mutations in NOVX cDNAs obtained from samples of cells. For example, the mutY enzyme of E. coli cleaves A at G/A mismatches and the thymidine DNA glycosylase from HeLa cells cleaves T at G/T mismatches. See, e.g., Hsu, et al., 1994. Carcinogenesis 15: 1657-1662. According to an exemplary embodiment, a probe based on a NOVX sequence, e.g., a wild-type NOVX sequence, is hybridized to a cDNA or other DNA product from a test cell(s). The duplex is treated with a DNA mismatch repair enzyme, and the cleavage products, if any, can be detected from electrophoresis protocols or the like. See, e.g., U.S. Pat. No. 5,459,039.

[0328] In other embodiments, alterations in electrophoretic mobility will be used to identify mutations in NOVX genes. For example, single strand conformation polymorphism (SSCP) may be used to detect differences in electrophoretic mobility between mutant and wild type nucleic acids. See, e.g., Orita, et al., 1989. Proc. Natl. Acad. Sci. USA: 86: 2766; Cotton, 1993. Mutat. Res. 285:125-144; Hayashi, 1992. Genet. Anal. Tech. Appi. 9: 73-79. Single-stranded DNA fragments of sample and control NOVX nucleic acids will be denatured and allowed to renature. The secondary structure of single-stranded nucleic acids varies according to sequence, the resulting alteration in electrophoretic mobility enables the detection of even a single base change. The DNA fragments may be labeled or detected with labeled probes. The sensitivity of the assay may be enhanced by using RNA (rather than DNA), in which the secondary structure is more sensitive to a change in sequence. In one embodiment, the subject method utilizes heteroduplex analysis to separate double stranded heteroduplex molecules on the basis of changes in electrophoretic mobility. See, e.g., Keen, et al., 1991. Trends Genet. 7: 5.

[0329] In yet another embodiment, the movement of mutant or wild-type fragments in polyacrylamide gels containing a gradient of denaturant is assayed using denaturing gradient gel electrophoresis (DGGE). See, e.g., Myers, et al., 1985. Nature 313: 495. When DGGE is used as the method of analysis, DNA will be modified to insure that it does not completely denature, for example by adding a GC clamp of approximately 40 bp of high-melting GC-rich DNA by PCR. In a further embodiment, a temperature gradient is used in place of a denaturing gradient to identify differences in the mobility of control and sample DNA. See, e.g., Rosenbaum and Reissner, 1987. Biophys. Chem. 265:12753.

[0330] Examples of other techniques for detecting point mutations include, but are not limited to, selective oligonucleotide hybridization, selective amplification, or selective primer extension. For example, oligonucleotide primers may be prepared in which the known mutation is placed centrally and then hybridized to target DNA under conditions that permit hybridization only if a perfect match is found. See, e.g., Saiki, et al., 1986. Nature 324:163; Saiki, et al., 1989. Proc. Natl. Acad. Sci. USA 86: 6230. Such allele specific oligonucleotides are hybridized to PCR amplified target DNA or a number of different mutations when the oligonucleotides are attached to the hybridizing membrane and hybridized with labeled target DNA.

[0331] Alternatively, allele specific amplification technology that depends on selective PCR amplification may be used in conjunction with the instant invention. Oligonucleotides used as primers for specific amplification may carry the mutation of interest in the center of the molecule (so that amplification depends on differential hybridization; see, e.g., Gibbs, et al., 1989. Nucl. Acids Res. 17: 2437-2448) or at the extreme 3′-terminus of one primer where, under appropriate conditions, mismatch can prevent, or reduce polymerase extension (see, e.g., Prossner, 1993. Tibtech. 11: 238). In addition it may be desirable to introduce a novel restriction site in the region of the mutation to create cleavage-based detection. See, e.g., Gasparini, et al., 1992. Mol. Cell Probes 6: 1. It is anticipated that in certain embodiments amplification may also be performed using Taq ligase for amplification. See, e.g., Barany, 1991. Proc. Natl. Acad. Sci. USA 88: 189. In such cases, ligation will occur only if there is a perfect match at the 3′-terminus of the 5′ sequence, making it possible to detect the presence of a known mutation at a specific site by looking for the presence or absence of amplification.

[0332] The methods described herein may be performed, for example, by utilizing pre-packaged diagnostic kits comprising at least one probe nucleic acid or antibody reagent described herein, which may be conveniently used, e.g., in clinical settings to diagnose patients exhibiting symptoms or family history of a disease or illness involving a NOVX gene.

[0333] Furthermore, any cell type or tissue, preferably peripheral blood leukocytes, in which NOVX is expressed may be utilized in the prognostic assays described herein. However, any biological sample containing nucleated cells may be used, including, for example, buccal mucosal cells.

[0334] Pharmacogenomics

[0335] Agents, or modulators that have a stimulatory or inhibitory effect on NOVX activity (e.g., NOVX gene expression), as identified by a screening assay described herein can be administered to individuals to treat (prophylactically or therapeutically) disorders. The disorders include but are not limited to, e.g., those diseases, disorders and conditions listed above, and more particularly include those diseases, disorders, or conditions associated with homologs of a NOVX protein, such as those summarized in Table A.

[0336] In conjunction with such treatment, the pharmacogenomics (i.e., the study of the relationship between an individual's genotype and that individual's response to a foreign compound or drug) of the individual may be considered. Differences in metabolism of therapeutics can lead to severe toxicity or therapeutic failure by altering the relation between dose and blood concentration of the pharmacologically active drug. Thus, the pharmacogenomics of the individual permits the selection of effective agents (e.g., drugs) for prophylactic or therapeutic treatments based on a consideration of the individual's genotype. Such pharmacogenomics can further be used to determine appropriate dosages and therapeutic regimens. Accordingly, the activity of NOVX protein, expression of NOVX nucleic acid, or mutation content of NOVX genes in an individual can be determined to thereby select appropriate agent(s) for therapeutic or prophylactic treatment of the individual.

[0337] Pharmacogenomics deals with clinically significant hereditary variations in the response to drugs due to altered drug disposition and abnormal action in affected persons. See e.g., Eichelbaum, 1996. Clin. Exp. Pharmacol. Physiol., 23: 983-985; Linder, 1997. Clin. Chem., 43: 254-266. In general, two types of pharmacogenetic conditions can be differentiated. Genetic conditions transmitted as a single factor altering the way drugs act on the body (altered drug action) or genetic conditions transmitted as single factors altering the way the body acts on drugs (altered drug metabolism). These pharmacogenetic conditions can occur either as rare defects or as polymorphisms. For example, glucose-6-phosphate dehydrogenase (G6PD) deficiency is a common inherited enzymopathy in which the main clinical complication is hemolysis after ingestion of oxidant drugs (anti-malarials, sulfonamides, analgesics, nitrofurans) and consumption of fava beans.

[0338] As an illustrative embodiment, the activity of drug metabolizing enzymes is a major determinant of both the intensity and duration of drug action. The discovery of genetic polymorphisms of drug metabolizing enzymes (e.g., N-acetyltransferase 2 (NAT 2) and cytochrome pregnancy zone protein precursor enzymes CYP2D6 and CYP2C19) has provided an explanation as to why some patients do not obtain the expected drug effects or show exaggerated drug response and serious toxicity after taking the standard and safe dose of a drug. These polymorphisms are expressed in two phenotypes in the population, the extensive metabolizer (EM) and poor metabolizer (PM). The prevalence of PM is different among different populations. For example, the gene coding for CYP2D6 is highly polymorphic and several mutations have been identified in PM, which all lead to the absence of functional CYP2D6. Poor metabolizers of CYP2D6 and CYP2C19 quite frequently experience exaggerated drug response and side effects when they receive standard doses. If a metabolite is the active therapeutic moiety, PM show no therapeutic response, as demonstrated for the analgesic effect of codeine mediated by its CYP2D6-formed metabolite morphine. At the other extreme are the so called ultra-rapid metabolizers who do not respond to standard doses. Recently, the molecular basis of ultra-rapid metabolism has been identified to be due to CYP2D6 gene amplification.

[0339] Thus, the activity of NOVX protein, expression of NOVX nucleic acid, or mutation content of NOVX genes in an individual can be determined to thereby select appropriate agent(s) for therapeutic or prophylactic treatment of the individual. In addition, pharmacogenetic studies can be used to apply genotyping of polymorphic alleles encoding drug-metabolizing enzymes to the identification of an individual's drug responsiveness phenotype. This knowledge, when applied to dosing or drug selection, can avoid adverse reactions or therapeutic failure and thus enhance therapeutic or prophylactic efficiency when treating a subject with a NOVX modulator, such as a modulator identified by one of the exemplary screening assays described herein.

[0340] Monitoring of Effects During Clinical Trials

[0341] Monitoring the influence of agents (e.g., drugs, compounds) on the expression or activity of NOVX (e.g., the ability to modulate aberrant cell proliferation and/or differentiation) can be applied not only in basic drug screening, but also in clinical trials. For example, the effectiveness of an agent determined by a screening assay as described herein to increase NOVX gene expression, protein levels, or upregulate NOVX activity, can be monitored in clinical trails of subjects exhibiting decreased NOVX gene expression, protein levels, or downregulated NOVX activity. Alternatively, the effectiveness of an agent determined by a screening assay to decrease NOVX gene expression, protein levels, or downregulate NOVX activity, can be monitored in clinical trails of subjects exhibiting increased NOVX gene expression, protein levels, or upregulated NOVX activity. In such clinical trials, the expression or activity of NOVX and, preferably, other genes that have been implicated in, for example, a cellular proliferation or immune disorder can be used as a “read out” or markers of the immune responsiveness of a particular cell.

[0342] By way of example, and not of limitation, genes, including NOVX, that are modulated in cells by treatment with an agent (e.g., compound, drug or small molecule) that modulates NOVX activity (e.g., identified in a screening assay as described herein) can be identified. Thus, to study the effect of agents on cellular proliferation disorders, for example, in a clinical trial, cells can be isolated and RNA prepared and analyzed for the levels of expression of NOVX and other genes implicated in the disorder. The levels of gene expression (i.e., a gene expression pattern) can be quantified by Northern blot analysis or RT-PCR, as described herein, or alternatively by measuring the amount of protein produced, by one of the methods as described herein, or by measuring the levels of activity of NOVX or other genes. In this manner, the gene expression pattern can serve as a marker, indicative of the physiological response of the cells to the agent. Accordingly, this response state may be determined before, and at various points during, treatment of the individual with the agent.

[0343] In one embodiment, the invention provides a method for monitoring the effectiveness of treatment of a subject with an agent (e.g., an agonist, antagonist, protein, peptide, peptidomimetic, nucleic acid, small molecule, or other drug candidate identified by the screening assays described herein) comprising the steps of (i) obtaining a pre-administration sample from a subject prior to administration of the agent; (ii) detecting the level of expression of a NOVX protein, mRNA, or genomic DNA in the preadministration sample; (iii) obtaining one or more post-administration samples from the subject; (iv) detecting the level of expression or activity of the NOVX protein, mRNA, or genomic DNA in the post-administration samples; (v) comparing the level of expression or activity of the NOVX protein, mRNA, or genomic DNA in the pre-administration sample with the NOVX protein, mRNA, or genomic DNA in the post administration sample or samples; and (vi) altering the administration of the agent to the subject accordingly. For example, increased administration of the agent may be desirable to increase the expression or activity of NOVX to higher levels than detected, i.e., to increase the effectiveness of the agent. Alternatively, decreased administration of the agent may be desirable to decrease expression or activity of NOVX to lower levels than detected, i.e., to decrease the effectiveness of the agent.

[0344] Methods of Treatment

[0345] The invention provides for both prophylactic and therapeutic methods of treating a subject at risk of (or susceptible to) a disorder or having a disorder associated with aberrant NOVX expression or activity. The disorders include but are not limited to, e.g., those diseases, disorders and conditions listed above, and more particularly include those diseases, disorders, or conditions associated with homologs of a NOVX protein, such as those summarized in Table A.

[0346] These methods of treatment will be discussed more fully, below.

[0347] Diseases and Disorders

[0348] Diseases and disorders that are characterized by increased (relative to a subject not suffering from the disease or disorder) levels or biological activity may be treated with Therapeutics that antagonize (i.e., reduce or inhibit) activity. Therapeutics that antagonize activity may be administered in a therapeutic or prophylactic manner. Therapeutics that may be utilized include, but are not limited to: (i) an aforementioned peptide, or analogs, derivatives, fragments or homologs thereof; (ii) antibodies to an aforementioned peptide; (iii) nucleic acids encoding an aforementioned peptide; (iv) administration of antisense nucleic acid and nucleic acids that are “dysfunctional” (i.e., due to a heterologous insertion within the coding sequences of coding sequences to an aforementioned peptide) that are utilized to “knockout” endogenous function of an aforementioned peptide by homologous recombination (see, e.g., Capecchi, 1989. Science 244: 1288-1292); or (v) modulators (i.e., inhibitors, agonists and antagonists, including additional peptide mimetic of the invention or antibodies specific to a peptide of the invention) that alter the interaction between an aforementioned peptide and its binding partner.

[0349] Diseases and disorders that are characterized by decreased (relative to a subject not suffering from the disease or disorder) levels or biological activity may be treated with Therapeutics that increase (i.e., are agonists to) activity. Therapeutics that upregulate activity may be administered in a therapeutic or prophylactic manner. Therapeutics that may be utilized include, but are not limited to, an aforementioned peptide, or analogs, derivatives, fragments or homologs thereof; or an agonist that increases bioavailability.

[0350] Increased or decreased levels can be readily detected by quantifying peptide and/or RNA, by obtaining a patient tissue sample (e.g., from biopsy tissue) and assaying it in vitro for RNA or peptide levels, structure and/or activity of the expressed peptides (or mRNAs of an aforementioned peptide). Methods that are well-known within the art include, but are not limited to, immunoassays (e.g., by Western blot analysis, immunoprecipitation followed by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis, immunocytochemistry, etc.) and/or hybridization assays to detect expression of mRNAs (e.g., Northern assays, dot blots, in situ hybridization, and the like).

[0351] Prophylactic Methods

[0352] In one aspect, the invention provides a method for preventing, in a subject, a disease or condition associated with an aberrant NOVX expression or activity, by administering to the subject an agent that modulates NOVX expression or at least one NOVX activity. Subjects at risk for a disease that is caused or contributed to by aberrant NOVX expression or activity can be identified by, for example, any or a combination of diagnostic or prognostic assays as described herein. Administration of a prophylactic agent can occur prior to the manifestation of symptoms characteristic of the NOVX aberrancy, such that a disease or disorder is prevented or, alternatively, delayed in its progression. Depending upon the type of NOVX aberrancy, for example, a NOVX agonist or NOVX antagonist agent can be used for treating the subject. The appropriate agent can be determined based on screening assays described herein. The prophylactic methods of the invention are further discussed in the following subsections.

[0353] Therapeutic Methods

[0354] Another aspect of the invention pertains to methods of modulating NOVX expression or activity for therapeutic purposes. The modulatory method of the invention involves contacting a cell with an agent that modulates one or more of the activities of NOVX protein activity associated with the cell. An agent that modulates NOVX protein activity can be an agent as described herein, such as a nucleic acid or a protein, a naturally-occurring cognate ligand of a NOVX protein, a peptide, a NOVX peptidomimetic, or other small molecule. In one embodiment, the agent stimulates one or more NOVX protein activity. Examples of such stimulatory agents include active NOVX protein and a nucleic acid molecule encoding NOVX that has been introduced into the cell. In another embodiment, the agent inhibits one or more NOVX protein activity. Examples of such inhibitory agents include antisense NOVX nucleic acid molecules and anti-NOVX antibodies. These modulatory methods can be performed in vitro (e.g., by culturing the cell with the agent) or, alternatively, in vivo (e.g., by administering the agent to a subject). As such, the invention provides methods of treating an individual afflicted with a disease or disorder characterized by aberrant expression or activity of a NOVX protein or nucleic acid molecule. In one embodiment, the method involves administering an agent (e.g., an agent identified by a screening assay described herein), or combination of agents that modulates (e.g., up-regulates or down-regulates) NOVX expression or activity. In another embodiment, the method involves administering a NOVX protein or nucleic acid molecule as therapy to compensate for reduced or aberrant NOVX expression or activity.

[0355] Stimulation of NOVX activity is desirable in situations in which NOVX is abnormally downregulated and/or in which increased NOVX activity is likely to have a beneficial effect. One example of such a situation is where a subject has a disorder characterized by aberrant cell proliferation and/or differentiation (e.g., cancer or immune associated disorders). Another example of such a situation is where the subject has a gestational disease (e.g., preclampsia).

[0356] Determination of the Biological Effect of the Therapeutic

[0357] In various embodiments of the invention, suitable in vitro or in vivo assays are performed to determine the effect of a specific Therapeutic and whether its administration is indicated for treatment of the affected tissue.

[0358] In various specific embodiments, in vitro assays may be performed with representative cells of the type(s) involved in the patient's disorder, to determine if a given Therapeutic exerts the desired effect upon the cell type(s). Compounds for use in therapy may be tested in suitable animal model systems including, but not limited to rats, mice, chicken, cows, monkeys, rabbits, and the like, prior to testing in human subjects. Similarly, for in vivo testing, any of the animal model system known in the art may be used prior to administration to human subjects.

[0359] Prophylactic and Therapeutic Uses of the Compositions of the Invention

[0360] The NOVX nucleic acids and proteins of the invention are useful in potential prophylactic and therapeutic applications implicated in a variety of disorders. The disorders include but are not limited to, e.g., those diseases, disorders and conditions listed above, and more particularly include those diseases, disorders, or conditions associated with homologs of a NOVX protein, such as those summarized in Table A.

[0361] As an example, a cDNA encoding the NOVX protein of the invention may be useful in gene therapy, and the protein may be useful when administered to a subject in need thereof. By way of non-limiting example, the compositions of the invention will have efficacy for treatment of patients suffering from diseases, disorders, conditions and the like, including but not limited to those listed herein.

[0362] Both the novel nucleic acid encoding the NOVX protein, and the NOVX protein of the invention, or fragments thereof, may also be useful in diagnostic applications, wherein the presence or amount of the nucleic acid or the protein are to be assessed. A further use could be as an anti-bacterial molecule (i.e., some peptides have been found to possess anti-bacterial properties). These materials are further useful in the generation of antibodies, which immunospecifically-bind to the novel substances of the invention for use in therapeutic or diagnostic methods.

[0363] The invention will be further described in the following examples, which do not limit the scope of the invention described in the claims.

EXAMPLES

Example A

Polynucleotide and Polypeptide Sequences, and Homology Data

Example 1

[0364] The NOV1 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 1A.

TABLE 1A
NOV1 Sequence Analysis
             SEQ ID NO: 1              8482 bp
NOV 1a,      AAATAAAGTTTTTTCAATGGAAGGCTTGCAGCTCTTGAGGACCTGCCAAATGGAAGAAGGACAGAGAC
CG105472-01
DNA Sequence CTGGAGCCCTATGGAAAGTTCTGACACCATGTGTGGAAGGACATGGCTTTTAACACGTGTGGTGACTG
             GAGTAGCTGCAGCTGAGGACAGCCACCCTTTCTTCGTCTCTGCTGAGCGAAGGCTACACGGCCCTTCC
             TCCTTGCAGCTGTTTCACCTTCTACCTTGCGTGGAGCCAGGCTTTTGCACCGAATCTGAGATGCCATT
             TTAAACAGAAGACTCCATCCTCTTGAAGATGGGAAATTCTTACGCTGGACAGCTGAAGACGACACGCT
             TTGAAGAGGTCTTGCACAATTCCATCGAGGCATCCCTGCGGTCCAACAACCTGGTGCCCAGGCCCATC
             TTTTCCCAGCTGTACCTGGAAGCTGAGCAGCAGCTTGCCGCTCTAGAAGGTGGTAGCCGAGTGGACAA
             TGAGGAAGAGGAAGAAGAGGGAGAAGGAGGGCTGGAAACAAATGGCCCCCCAAACCCTTTCCAGCTGC
             ACCCTCTGCCTGAAGGATGCTGTACCACAGACGGTTTTTGCCAGGCCGGGAAGGACCTGCGCCTTGTC
             TCCATTTCCAACGAGCCCATGGATGTCCCTGCGGGCTTTCTCCTCGTGGGGGTCAAGTCCCCCAGCCT
             GCCGGACCATCTCCTGGTGTGCGCCGTTGACAAGAGGTTCTTGCCAGATGACAATGGCCACAATGCTC
             TTCTTGGTTTCTCTGGGAATTGTGTTGGCTGTGGAAAGAAAGGCTTCTGTTACTTCACGGAATTCTCC
             AATCATATAAATCTGAAACTGACCACTCAACCCAAGAAGCAGAAACACTTGAAGTATTACCTGGTCCG
             TAATGCACAAGGGACTCTAACCAAAGGACCTTTAATCTGTTGGAAAGGCTCAGAGTTTAGAAGCCGGC
             AGATCCCCGCCAGTACTTGTTCCAGTTCCCTCTTCCCAGCCCTGGAGAGCACGGCTGCCTTCCCCAGC
             GAGCCCGTTCCTGGGACGAACCCCAGCATCCTGATGGGAGCTCAGCAGGCAGGTCCAGCTTCTGATCA
             CCCCTCACTAAACGCAGCAATGGGTCCGGCTGTTTTCAACGGCAAAGATTCCCCGAAGTGCCAACAAC
             TGGCAAAGAATAACCTGTTGGCCCTGCCGCGACCATCGGCTTTAGGTATCTTGTCAAACTCCGGGCCC
             CCCAAAAAACGCCACAAAGGGTGGTCTCCAGAATCTCCATCAGCTCCAGATGGTGGCTGCCCCCAAGG
             TGGTGGGAACAGAGCTAAGTATGAGAGCGCAGGCATGTCCTGCGTGCCGCAGGTTGGCTTGGTGGGAC
             CAGCTTCAGTCACCTTTCCAGTGGTGGCCTCTGGAGAACCAGTGTCTGTTCCTGACAACTTGCTGAAA
             ATATGCAAGGCCAAGCCAGTGATATTTAAAGGCGATGGGAACTTCCCTTACCTCTGTGGGAACCTGAA
             TGACGTCGTGGTCAGCCCCCTCTTGTACACGTGCTACCAGAATTCCCAGTCTGTCTCACGGGCATACG
             AGCAGTACGGCGCCTCTGCCATCCAGCCCATCTCCGAGGAGATGCAGCTCCTGCTTACCGTCTACTAC
             CTGGTCCAGCTGGCCGCGGACCAGGTGCCCTTGATGGAGGACCTGGAGCAGATCTTCCTGCGCTCTTG
             GCGCGAGTCGCACCTGACCGAGATCCGGCAGTACCAGCAGGCGCCGCCGCAGCCCTTCCCGCCCGCGC
             CCAGCGCCGCGGCACCCGTGACCTCCGCGCAGCTGCCCTGGCTGGCCAGCCTGGCCGCCAGCTCCTGC
             AACGACAGCGTGCACGTCATCGAGTGTGCTTACTCCCTGGCCGAGGGCCTCTCCGAGATGTTCCGGCT
             GTTGGTCGAGGGCAAGCTTGCCAAGACCAACTACGTGGTCATCATCTGCGCCTGCCGCAGCGCGGCCA
             TCGACTCCTGCATCGCCGTCACCGGTAAATACCAAGCCCGGATTCTTTCCGAGAGCCTTCTCACTCCT
             GCGGAGTACCAGAAGGAAGTCAATTACGAGCTGGTTACGGGGAAGGTAGACTCGCTGGGGGCCTTCTT
             TAGCACCCTCTGTCCAGAGGGTGACATTGACATTTTGCTGGACAAATTTCACCAGGAAAATCAAGGCC
             ATATTTCTTCCTCACTCGCTGCCTCTTCTGTCACTAAAGCAGCATCCCTGGATGTCAGTGGGACACCG
             GTGTGCACAAGTTACAATCTGGAGCCACACAGCATCCGGCCCTTCCAGCTGGCAGTAGCGCAGAAGCT
             CCTCTCCCATGTGTGTTCCATTGCGGATTCCAGCACCCAAAATCTGGACCTGGGATCCTTTGAGAAGG
             TGGACTTTCTCATTTGCATTCCCCCCTCAGAAGTGACCTACCAGCAGACTCTGCTCCATGTGTGGCAT
             TCAGGTGTTTTGCTGGAGCTTGGTCTGAAGAAAGAGCACATGACGAAGCAGAGGGTGGAACAGTATGT
             TCTGAAGCTAGACACGGAGGCACAGACAAAATTTAAGGCTTTTCTGCAAAACTCCTTCCAGAACCCGC
             ATACACTTTTTGTCCTAATCCATGACCATGCGCACTGGGATCTTGTGAGTAGCACTGTTCATAACCTC
             TATTCTCAAAGTGACCCGTCGGTGGGATTGGTGGACCGATTGCTCAACTGCAGGGAGGTGAAGGAGGC
             CCCCAACATTGTGACACTTCACGTGACCTCCTTCCCGTATGCACTGCAGACACAGCACACCCTCATCA
             GCCCCTACAACGAGATCCACTGGCCTGCCTCCTGCAGTAATGGAGTGGACTTATATCATGAAAATAAG
             AAGTACTTCGGGCTGTCGGAGTTTATTGAATCCACCCTTTCAGGACACAGCCTCCCCTTGCTCAGATA
             CGATAGCTCCTTTGAGGCCATGGTCACTGCATTAGGAAAAAGGTTCCCCCGCCTGCACAGCGCGGTGA
             TCAGGACCTTTGTTCTCGTGCAGCACTACGCGGCCGCCCTGATGGCCGTAAGCGGCCTCCCGCAGATG
             AAGAACTACACGTCGGTGGAGACGCTGGAGATCACGCAGAACCTCCTCAACTCCCCGAAGCAGTGCCC
             CTGCGGCCACGGGCTCATGGTCCTGCTGCGGGTGCCCTGTTCGCCCCTGGCGGTGGTGGCCTATGAGC
             GGCTGGCCCACGTGCGGGCCCGGCTGGCGCTGGAGGAGCACTTTGAGATCATCCTGGGCAGTCCCAGC
             TCAGGCGTCACCGTGGGGAAGCACTTCGTAAAGCAGCTCAGGGTATGGCAGAAAATTGAGGATGTGGA
             GTGGAGACCCCAGACTTACTTGGAGCTGGAGGGTCTGCCTTGCATCCTGATCTTCAGTGGGATGGACC
             CGCATGGGGAGTCCTTGCCGAGGTCTTTGAGGTACTGTGACCTGCGATTGATAAACTCCTCCTGCTTG
             GTGAGAACAGCCTTGGAGCAGGAGCTGGGCCTGGCTGCCTACTTTGTGAGCAACGAGGTTCCCTTGGA
             GAAGGGGGCTAGGAACGAGGCCTTGGAGAGTGATGCTGAGAAGCTGAGCAGCACAGACAACGAGGATG
             AGGAGCTGGGGACAGAAGGCTCTACCTCGGAGAAGAGAAGCCCCATGAAAAGGGAGAGGTCCCGCTCC
             CACGACTCAGCATCCTCATCCCTCTCCTCCAAGGCTTCCGGTTCCGCGCTCGGTGGCGAGTCCTCGGC
             TCAGCCCACAGCACTCCCCCAGGGAGAGCATGCCAGGTCGCCCCAGCCCCGTGGCCCCGCAGAGGAGG
             GCAGAGCCCCTGGTGAGAAACAGAGGCCCCGGGCAAGTCAGGGGCCACCCTCGGCCATCAGCAGGCAC
             AGTCCCGGGCCGACGCCCCAGCCCGACTGTAGCCTCAGGACCGGCCAGAGGAGCGTCCAGGTGTCGGT
             CACCTCGTCGTGCTCCCAGCTGTCCTCCTCCTCGGGCTCATCCTCCTCATCCGTGGCGCCCGCTGCCG
             GCACGTGGGTCCTGCAGGCCTCCCAGTGCTCCTTGACCAAGGCCTGCCGCCAGCCACCCATTGTCTTC
             TTGCCCAAGCTCGTGTACGACATGGTTGTGTCCACTGACAGCAGTGGCCTGCCCAAGGCCGCCTCCCT
             CCTGCCCTCCCCCTCGGTCATGTGGGCCAGCTCTTTCCGCCCCCTGCTCAGCAAGACCATGACATCCA
             CCGAGCAGTCCCTCTACTACCGGCAGTGGACGGTGCCCCGGCCCAGCCACATGGACTACGGCAACCGG
             GCCGAGGGCCGCGTGGACGGCTTCCACCCCCGCAGGCTGCTGCTCAGCGGCCCCCCTCAGATCGGGAA
             GACAGGTGCCTACCTGCAGTTCCTCAGTGTCCTGTCCAGGATGCTTGTTCGGCTCACAGAAGTGGATG
             TCTATGACGAGGAGGAGATCAATATCAACCTGAGAGAAGAATCTGACTGGCATTATCTCCAGCTTAGC
             GACCCCTGGCCAGACCTGGAGCTGTTCAAGAAGTTGCCCTTTGACTACATCATTCACGACCCGAAGTA
             TGAAGATGCCAGCCTGATTTGTTCGCACTATCAGGGTATAAAGAGTGAAGACAGAGGGATGTCCCGGA
             AGCCGGAGGACCTTTATGTGCGGCGTCAGACGGCACGGATGAGACTGTCCAAGTACGCAGCGTACAAC
             ACTTACCACCACTGTGAGCAGTGCCACCAGTACATGGGCTTCCACCCCCGCTACCAGCTGTATGAGTC
             CACCCTGCACGCCTTTGCCTTCTCTTACTCCATGCTAGGAGAGGAGATCCAGCTGCACTTCATCATCC
             CCAAGTCCAAGGAGCACCACTTTGTCTTCAGCCAACCTGGAGGCCAGCTGGAGAGCATGCGACTACCC
             CTCGTGACAGACAAGAGCCATGAATATATAAAAAGTCCGACATTCACTCCAACCACCGGCCGTCACGA
             ACATGGGCTCTTTAATCTGTACCACGCAATGGACGGTGCCAGCCATTTGCACGTGCTGGTTGTCAAGG
             AATACGAGATGGCAATTTATAAGAAATATTGGCCCAACCACATCATGCTGGTGCTCCCCAGTATCTTC
             AACAGTGCTGGAGTTGGTGCTGCTCATTTCCTCATCAAGGAGCTGTCCTACCATAACCTGGAGCTCGA
             GCGGAACCGGCAGGAGGAGCTGGGAATCAAGCCGCAGGACATCTGGCCTTTCATTGTGATCTCTGATG
             ACTCCTGCGTGATGTGGAACGTGGTGGATGTCAACTCTGCTGGGGAGAGAAGCAGGGAGTTCTCCTGG
             TCGGAAAGGAACGTGTCTTTGAAGCACATCATGCAGCACATCGAGGCGGCCCCCGACATCATGCACTA
             CGCCCTGCTGGGCCTGCGGAAGTGGTCCAGCAAGACCCGGGCCAGCGAGGTGCAAGAGCCCTTCTCCC
             GCTGCCACGTGCACAACTTCATCATCCTGAACGTGGACCTGACCCAGAACGTGCAGTACAACCAGAAC
             CGGTTCCTGTGTGACGATGTAGACTTCAACCTGCGGGTGCACAGCGCCGGCCTCCTGCTCTGCCGGTT
             CAACCGCTTCAGCGTGATGAAGAAGCAGATCGTGGTGGGCGGCCACAGGTCCTTCCACATCACATCCA
             AGGTGTCTGATAACTCTGCCGCGGTCGTGCCGGCCCAGTACATCTGTGCCCCGGACAGCAAGCACACG
             TTCCTCGCAGCGCCCGCCCAGCTCCTGCTGGAGAAGTTCCTGCAGCACCACAGCCACCTCTTCTTCCC
             GCTGTCCCTGAAGAACCATGACCACCCAGTGCTGTCTGTCGACTGTTACCTGAACCTGGGATCTCAGA
             TTTCTGTTTGCTATGTGAGCTCCAGGCCCCACTCTTTAAACATCAGCTGCTCGGACTTGCTGTTCAGT
             GGGCTGCTGCTGTACCTCTGTGACTCTTTTGTGGGAGCTAGCTTTTTGAAAAAGTTTCATTTTCTGAA
             AGGTGCGACGTTGTGTGTCATCTGTCAGGACCGGAGCTCACTGCGCCAGACGGTCGTCCGCCTGGAGC
             TCGAGGACGAGTGGCAGTTCCGGCTGCGCGATGAGTTCCAGACCGCCAATGCCAGGGAAGACCGGCCG
             CTCTTTTTTCTGACGGGACGACACATCTGAGGAAGACAGCGGCGAGTTTTCTGAAGAGATGAGTGCTC
             AGAGCCCTCATGCTGTTGAGGCTAAAGGGAGGCCTGGAACGGTGGGGCGTTTGACTGGAATGGACCCC
             AGGGACTGTCCAGGTGCAGCCCCTCCTAGTACACATGGGCCCCCGAGGCCGTGGTCCTGGGAGCCAGG
             AAGACTCCGCAGTGGGTGAGAATGAAAACTTGAGACTCCCAAGTTCTGGGCCAGCCCATTGCTCTGGG
             CTGTTTTAAAGCCCATTTCACGAGGAACAAAGATTTACTTCCTGTCCTGCCATTCGTGTGCTTCCATG
             GACAAACCTGATTTTTTTCTCTTAGTTCTAAAGAATCTTGGGTTATTTTGTAGCGGTGCCAGTATTTC
             AGTAGATGGGATTTCAGCCAAGTAGGTTCCCCTGTAACCTCCTACAAAGCAATATTCCAAAGGAACAT
             TTTAACTGTAAAGGCTGGAGACAAGAAAAAATAAGTAGATCGTTTTAATAACAATTATTTAATTGCCT
             ATAAGTTTGCTGTTTCAGAGGCTAGCCCAAAGGCATCAAATTTAATAAAGTTAAACAAATTGATTTAC
             TTCAGAGCAAATATGATCCTATTAAAATAATATAGGGTAAATACCCTACCTCTTAGAAAGGGCAAAAA
             TGCAAAGAAGCTTTCTTTAAAACTAAAAGGGTTTTTTGGGGGGGGAGTTGGCGGGGAGGAAATAAGGC
             TAACAGAGGTTGACCTAAAATTAGCCTTACAAAGGAGAAAGGACCACATTGCTTACTTGAAACAGACA
             ATGAAAACAACCAAAGTGATATATAAAATAGTTGATGAGAACTAGACTTATGACTGTAGTTTACTAGA
             GTTTAGTTTTCAGTTGCTGAAGTAGCTCATTTTCTCTTACTAATGTTTGGTTCCTCAGGGAAGAATCT
             CACTTGACTAGAGAGGAGGTGGGAACAGAAGAGAGAAGGAGGCAGGGAGATGTATTTCTTAGGGCTCA
             CCCCTTCACAGACTGACAGAATGGTTTTGTTTTGTTTTGTTTTGTTTTGTTTTGTTTTTGAGATGGAC
             TCTAGCTCTGTCACCCAGGCTGGAGTGCAGTGGTGCGATCTCGGCTCACTGCAAGCTCCGCCTCCCGG
             GTTCTCACCATTCTCCTGCCTCAGCCTCCCGAGTAGCTGGGACTACAGGCGCCCACCACCACGCCCGG
             CTAATTTTTTGTATTTTTTAGTAGAGACGGGGTTTCACCATGTTAGCCAGGATGGTCTCGATCTCCTG
             ACCTCGTGATCCGCCCGCCTCGGCCTCCCAAAGTGCTGGGATTACAGGCGTGAGCCACCGTGCCTGCC
             CCAGAATGGTTTTTAAAGCCACAGTTGAGAGGCCACCCATTGCCCGGCGCCTGGACAGTGATCATCTT
             GTTCATCTTGTTCAGTCCTTTCTTGTGTGATTGGAATTATTCATCCCCTTTGAAAGATGAGAAGGTTG
             AGATGCAAAGAGTCTACCTTTCCAAGTTCTCACTGCTGGAAAGAGCTAGAAGCACAGTTCAAAGTTCT
             GGCTTCTGGACTCTGCAGTCCAGGTCTCCCTTCTCCCACTTGCCTACCCTCAATGCCACACTGTTTTT
             GAAGTGGCCCATAACTTGAAGGAAAAGTTTAAAGACAGTTCAATTTAATCATCAGAATGCATTCTTTT
             TTTTTTCGGAGACGGAGTTTCACTCTTGCTGCCCAGGCTGGAGTGCAATGGTGCAATGATCTCGGCTC
             ACTGCAACCTCTGCCTCCTGGGTTCAAGTGATTCTCCAGCCTCAGCCTCCCGAGTAGCTGGGATTATG
             GGCGCCCACCACCATGCCCAGCTAATTTTTGTATTTTTTTTTTTTAGTAGAGATGGGGTTTCGCCAGG
             TTGGCCAGGCTGGTCTTGTGAACTCCTGGCCTCAGGTGATCTGCCCACCTCATCCTCCAAAAGTGCTG
             GGATTACAGGCATGAGCCACTGCGCCTGGCCTCAGAATGCATTCTTACACATCTATCCTAGACATTTA
             TAAGCACTCTAATGGATAACAATCCAAGAATAAATGATTGTAAAAGATGATGCCGAAGAGTTGATGTC
             AATCTTTTTTTCCTAAGAAAAAAAGTCCGCGAGTATTAAATATTTAGATCAATGTTTATAAAATGATT
             ACTTTGTATATCTCATTATTCCTATTTTGGAATAAAAACTGACCTTCTTTAATCATATACTTGTCTTT
             TGTAAATAGCAGCTTTTGTGTCATTCTCCCCACTTTATTAGTTAATTTAAATTGGAAAAAACCCTCAA
             ACTAATATTCTTGTCTGTTCCAGTCTTATAAATAAAACTTATAATGCATG
             ORF Start: ATG at 301     ORF Stop: TGA at 6148
             SEQ ID NO: 2              1949 aa   MW at 216410.6kD
NOV 1a,      MGNSYAGQLKTTRFEEVLHNSIEASLRSNNLVPRPIFSQLYLEAEQQLAALEGGSRVDNEEEEEEGEG
CG105472-01
Protein      GLETNGPPNPFQLHPLPEGCCTTDGFCQAGKDLRLVSISNEPMDVPAGFLLVGVKSPSLPDHLLVCAV
Sequence
             DKRFLPDDNGHNALLGFSGNCVGCGKKGFCYFTEFSNHINLKLTTQPKKQKHLKYYLVRNAQGTLTKG
             PLICWKGSEFRSRQIPASTCSSSLFPALESTAAFPSEPVPGTNPSILMGAQQAGPASDHPSLNAAMGP
             AVFNGKDSPKCQQLAKNNLLALPRPSALGILSNSGPPKKRHKGWSPESPSAPDGGCPQGGGNRAKYES
             AGMSCVPQVGLVGPASVTFPVVASGEPVSVPDNLLKICKAKPVIFKGDGNFPYLCGNLNDVVVSPLLY
             TCYQNSQSVSRAYEQYGASAIQPISEEMQLLLTVYYLVQLAADQVPLMEDLEQIFLRSWRESHLTEIR
             QYQQAPPQPFPPAPSAAAPVTSAQLPWLASLAASSCNDSVHVIECAYSLAEGLSEMFRLLVEGKLAKT
             NYVVIICACRSAAIDSCIAVTGKYQARILSESLLTPAEYQKEVNYELVTGKVDSLGAFFSTLCPEGDI
             DILLDKFHQENQGHISSSLAASSVTKAASLDVSGTPVCTSYNLEPHSIRPFQLAVAQKLLSHVCSIAD
             SSTQNLDLGSFEKVDFLICIPPSEVTYQQTLLHVWHSGVLLELGLKKEHMTKQRVEQYVLKLDTEAQT
             KFKAFLQNSFQNPHTLFVLIHDHAHWDLVSSTVHNLYSQSDPSVGLVDRLLNCREVKEAPNIVTLHVT
             SFPYALQTQHTLISPYNEIHWPASCSNGVDLYHENKKYFGLSEFIESTLSGHSLPLLRYDSSFEAMVT
             ALGKRFPRLHSAVIRTFVLVQHYAAALMAVSGLPQMKNYTSVETLEITQNLLNSPKQCPCGHGLMVLL
             RVPCSPLAVVAYERLAHVRARLALEEHFEIILGSPSSGVTVGKHFVKQLRVWQKIEDVEWRPQTYLEL
             EGLPCILIFSGMDPHGESLPRSLRYCDLRLINSSCLVRTALEQELGLAAYFVSNEVPLEKGARNEALE
             SDAEKLSSTDNEDEELGTEGSTSEKRSPMKRERSRSHDSASSSLSSKASGSALGGESSAQPTALPQGE
             HARSPQPRGPAEEGRAPGEKQRPRASQGPPSAISRHSPGPTPQPDCSLRTGQRSVQVSVTSSCSQLSS
             SSGSSSSSVAPAAGTWVLQASQCSLTKACRQPPIVFLPKLVYDMVVSTDSSGLPKAASLLPSPSVMWA
             SSFRPLLSKTMTSTEQSLYYRQWTVPRPSHMDYGNRAEGRVDGFHPRRLLLSGPPQIGKTGAYLQFLS
             VLSRMLVRLTEVDVYDEEEININLREESDWHYLQLSDPWPDLELFKKLPFDYIIHDPKYEDASLICSH
             YQGIKSEDRGMSRKPEDLYVRRQTARMRLSKYAAYNTYHHCEQCHQYMGFHPRYQLYESTLHAFAFSY
             SMLGEEIQLHFIIPKSKEHHFVFSQPGGQLESMRLPLVTDKSHEYIKSPTFTPTTGRHEHGLFNLYHA
             MDGASHLHVLVVKEYEMAIYKKYWPNHIMLVLPSIFNSAGVGAAHFLIKELSYHNLELERNRQEELGI
             KPQDIWPFIVISDDSCVMWNVVDVNSAGERSREFSWSERNVSLKHIMQHIEAAPDIMHYALLGLRKWS
             SKTRASEVQEPFSRCHVHNFIILNVDLTQNVQYNQNRFLCDDVDFNLRVHSAGLLLCRFNRFSVMKKQ
             IVVGGHRSFHITSKVSDNSAAVVPAQYICAPDSKHTFLAAPAQLLLEKFLQHHSHLFFPLSLKNHDHP
             VLSVDCYLNLGSQISVCYVSSRPHSLNISCSDLLFSGLLLYLCDSFVGASFLKKFHFLKGATLCVICQ
             DRSSLRQTVVRLELEDEWQFRLRDEFQTANAREDRPLFFLTGRHI

[0365] Further analysis of the NOV1a protein yielded the following properties shown in Table 1B.

TABLE 1B
Protein Sequence Properties NOV1a
PSort     0.6400 probability located in plasma membrane; 0.4000
analysis: probability located in Golgi body; 0.3000 probability
          located in endoplasmic reticulum (membrane); 0.3000
          probability located in microbody (peroxisome)
SignalP   No Known Signal Sequence Predicted
analysis:

[0366] A search of the NOV1a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 1C.

TABLE 1C
Geneseq Results for NOV1a
			Identities/
		NOV1a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABG61876	Prostate cancer-	1003 . . . 1949	946/947	0.0
	associated protein		(99%)
	#77—Mammalia,	1 . . . 947	947/947
	947 aa.		(99%)
	[WO200230268-
	A2, 18 APR.
	2002]
AAB95517	Human protein	775 . . . 1606	399/835	0.0
	sequence SEQ ID		(47%)
	NO: 18089—	59 . . . 854	534/835
	Homo sapiens,		(63%)
	875 aa.
	[EP1074617-A2,
	7 FEB. 2001]
AAO04442	Human poly-	1190 . . . 1301	110/112	5e−56
	peptide SEQ ID		(98%)
	NO 18334—	1 . . . 112	110/112
	Homo sapiens,		(98%)
	112 aa.
	[WO200164835-
	A2, 7 SEP. 2001]
ABG00933	Novel human	109 . . . 258	101/150	9e−51
	diagnostic protein		(67%)
	#924—Homo	2 . . . 145	115/150
	sapiens, 172 aa.		(76%)
	[WO200175067-
	A2, 11 OCT.
	2001]
ABG07439	Novel human	1223 . . . 1348	61/128	5e−24
	diagnostic protein		(47%)
	#7430—Homo	4 . . . 131	75/128
	sapiens, 175 aa.		(57%)
	[WO200175067-
	A2, 11 OCT.
	2001]

[0367] In a BLAST search of public sequence datbases, the NOV1a protein was found to have homology to the proteins shown in the BLASTP data in Table 1D.

TABLE 1D
Public BLASTP Results for NOV1a
			Identities/
		NOV1a	Similarities
Protein		Residues/	for the
Accession	Protein/	Match	Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9JLG7	Kiaa0575—Mus	1 . . . 1949	1729/1957	0.0
	musculus (Mouse),		(88%)
	1954 aa.	1 . . . 1954	1818/1957
			(92%)
Q9H2Q8	GREB1a—Homo	1 . . . 1001	999/1001	0.0
	sapiens (Human),		(99%)
	1001 aa (fragment).	1 . . . 1001	999/1001
			(99%)
O60321	KIAA0575	1003 . . . 1949	946/947	0.0
	protein—Homo		(99%)
	sapiens (Human),	1 . . . 947	947/947
	947 aa.		(99%)
Q9CYA3	8 days embryo	1439 . . . 1949	471/511	0.0
	cDNA, RIKEN full-		(92%)
	length enriched	1 . . .511	492/511
	library, clone:		(96%)
	5730583K22, full
	insert sequence—
	Mus musculus
	(Mouse), 511 aa.
Q9H2Q7	GREB1b—Homo	1 . . . 449	448/449	0.0
	sapiens (Human),		(99%)
	457 aa.	1 . . . 449	448/449
			(99%)

[0368] PFam analysis predicts that the NOV1a protein contains the domains shown in the Table 1E.

TABLE 1E
Domain Analysis of NOV1a
	Pfam	NOV1a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value
	zf-C4	1898 . . . 1908	5/11 (45%)	0.6
			10/11 (91%)

Example 2

[0369] The NOV2 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 2A.

TABLE 2A
NOV2 Sequence Analysis
             SEQ ID NO: 3              4995 bp
NOV2a,       GCCGCGCCGAGGAGGCTGCCGCTCTGGCTTGCCGCCCCCCGCCGCCGCTGCACACCGGACCCAGCCGC
CG106287-01
DNA Sequence CGTGCCGCGGGCCATGGACCTGCCCAGGGGCCTGGTGGTGGCCTGGGCGCTCAGCCTGTGGCCAGGGT
             TCACGGACACCTTCAACATGGACACCAGGAAGCCCCGGGTCATCCCTGGCTCCAGGACCGCCTTCTTT
             GGCTACACAGTGCAGCAGCACGACATCAGTGGCAATAAGTGGCTGGTCGTGGGCGCCCCACTGGAAAC
             CAATGGCTACCAGAAGACGGGAGACGTGTACAAGTGTCCAGTGATCCACGGGAACTGCACCAAACTCA
             ACCTGGGAAGGGTCACCCTGTCCAACGTGTCCGAGCGGAAAGACAACATGCGCCTCGGCCTTAGTCTC
             GCCACCAACCCCAAGGACAACAGCTTCCTGGCCTGCAGCCCCCTCTGGTCTCATGAGTGTGGGAGCTC
             CTACTACACCACAGGGATGTGTTCAAGAGTCAACTCCAACTTCAGGTTCTCCAAGACCGTGGCCCCAG
             CTCTCCAAAGGTGCCAGACCTACATGGACATCGTCATTGTCCTGGATGGCTCCAACAGCATCTACCCC
             TGGGTGGAGGTTCAGCACTTCCTCATCAACATCCTGAAAAAGTTTTACATTGGCCCAGGGCAGATCCA
             GGTTGGAGTTGTGCAGTATGGCGAAGATGTGGTGCATGAGTTTCACCTCAATGACTACAGGTCTGTAA
             AAGATGTGGTGGAAGCTGCCAGCCACATTGAGCAGAGAGGAGGAACAGAGACCCGGACGGCATTTGGC
             ATTGAATTTGCACGCTCAGAGGCTTTCCAGAAGGGTGGAAGGAAAGGAGCCAAGAAGGTGATGATTGT
             CATCACAGATGGGGAGTCCCACGACAGCCCAGACCTGGAGAAGGTGATCCAGCAAAGCGAAAGAGACA
             ACGTAACAAGATATGCGGTGGCCGTCCTGGGCTACTACAACCGCAGGGGGATCAATCCAGAAACTTTT
             CTAAATGAAATCAAATACATCGCCAGTGACCCTGATGACAAGCACTTCTTCAATGTCACTGATGAGGC
             TGCCTTGAAGGACATTGTCGATGCCCTGGGGGACAGAATCTTCAGCCTGGAAGGCACCAACAAGAACG
             AGACCTCCTTTGGGCTGGAGATGTCACAGACGGGCTTTTCCTCGCACGTGGTGGAGGATGGGGTTCTG
             CTGGGAGCCGTCGGTGCCTATGACTGGAATGGAGCTGTGCTAAAGGAGACGAGTGCCGGGAAGGTCAT
             TCCTCTCCGCGAGTCCTACCTGAAAGAGTTCCCCGAGGAGCTCAAGAACCATGGTGCATACCTGGGGT
             ACACAGTCACATCGGTCGTGTCCTCCAGGCAGGGGCGAGTGTACGTGGCCGGAGCCCCCCGGTTCAAC
             CACACGGGCAAGGTCATCCTGTTCACCATGCACAACAACCGGAGCCTCACCATCCACCAGGCTATGCG
             GGGCCAGCAGATAGGCTCTTACTTTGGGAGTGAAATCACCTCGGTGGACATCGACGGCGACGGCGTGA
             CTGATGTCCTGCTGGTGGGCGCACCCATGTACTTCAACGAGGGCCGTGAGCGAGGCAAGGTGTACGTC
             TATGAGCTGAGACAGAACCGGTTTGTTTATAACGGAACGCTAAAGGATTCACACAGTTACCAGAATGC
             CCGATTTGGGTCCTCCATTGCCTCAGTTCGAGACCTCAACCAGGATTCCTACAATGACGTGGTGGTGG
             GAGCCCCCCTGGAGGACAACCACGCAGGAGCCATCTACATCTTCCACGGCTTCCGAGGCAGCATCCTG
             AAGACACCTAAGCAGAGAATCACAGCCTCAGAGCTGGCTACCGGCCTCCAGTATTTTGGCTGCAGCAT
             CCACGGGCAATTGGACCTCAATGAGGATGGGCTCATCGACCTGGCAGTGGGAGCCCTTGGCAACGCTG
             TGATTCTGTGGTCCCGCCCAGTGGTTCAGATCAATGCCAGCCTCCACTTTGAGCCATCCAAGATCAAC
             ATCTTCCACAGAGACTGCAAGCGCAGTGGCAGGGATGCCACCTGCCTGGCCGCCTTCCTCTGCTTCAC
             GCCCATCTTCCTGGCACCCCATTTCCAAACAACAACTGTTGGCATCAGATACAACGCCACCATGGATG
             AGAGGCGGTATACACCGAGGGCCCACCTGGACGAGGGCGGGGACCGATTCACCAACAGAGCCGTACTG
             CTCTCCTCCGGCCAGGAGCTCTGTGAGCGGATCAACTTCCATGTCCTGGACACTGCTGACTACGTGAA
             GCCAGTGACCTTCTCAGTCGAGTATTCCCTGGAGGACCCTGACCATGGCCCCATGCTGGACGACGGCT
             GGCCCACCACTCTCAGAGTCTCGGTGCCCTTCTGGAACGGCTGCAATGAGGATGAGCACTGTGTCCCT
             GACCTTGTGTTGGATGCCCGGAGTGACCTGCCCACGGCCATGGAGTACTGCCAGAGGGTGCTGAGGAA
             GCCTGCGCAGGACTGCTCCGCATACACGCTGTCCTTCGACACCACAGTCTTCATCATAGAGAGCACAC
             GCCAGCGAGTGGCGGTGGAGGCCACACTGGAGAACAGGGGCGAGAACGCCTACAGCACGGTCCTAAAT
             ATCTCGCAGTCAGCAAACCTGCAGTTTGCCAGCTTGATCCAGAAGGAGGACTCAGACGGTAGCATTGA
             GTGTGTGAACGAGGAGAGGAGGCTCCAGAAGCAAGTCTGCAACGTCAGCTATCCCTTCTTCCGGGCCA
             AGGCCAAGGTGGCTTTCCGTCTTGATTTTGAGTTCAGCAAATCCATCTTCCTACACCACCTGGAGATC
             GAGCTCGCTGCAGGCAGTGACAGTAATGAGCGGGACAGCACCAAGGAAGACAACGTGGCCCCCTTACG
             CTTCCACCTCAAATACGAGGCTGACGTCCTCTTCACCAGGAGCAGCAGCCTGAGCCACTACGAGGTCA
             AGCTCAACAGCTCGCTGGAGAGATACGATGGTATCGGGCCTCCCTTCAGCTGCATCTTCAGGATCCAG
             AACTTGGGCTTGTTCCCCATCCACGGGATTATGATGAAGATCACCATTCCCATCGCCACCAGGAGCGG
             CAACCGCCTACTGAAGCTGAGGGACTTCCTCACGGACGAGGTAGCGAACACGTCCTGTAACATCTGGG
             GCAATAGCACTGAGTACCGGCCCACCCCAGTGGAGGAAGACTTGCGTCGTGCTCCACAGCTGAATCAC
             AGCAACTCTGATGTCGTCTCCATCAACTGCAATATACGGCTGGTCCCCAACCAGGAAATCAATTTCCA
             TCTACTGGGGAACCTGTGGTTGAGGTCCCTAAAAGCACTCAAGTACAAATCCATGAAAATCATGGTCA
             ACGCAGCCTTGCAGAGGCAGTTCCACAGCCCCTTCATCTTCCGTGAGGAGGATCCCAGCCGCCAGATC
             GTGTTTGAGATCTCCAAGCAAGAGGACTGGCAGGTCCCCATCTGGATCATTGTAGGCAGCACCCTGGG
             GGGCCTCCTACTGCTGGCCCTGCTGGTCCTGGCACTGTGGAAGCTCGGCTTCTTTAGAAGTGCCAGGC
             GCAGGAGGGAGCCTGGTCTGGACCCCACCCCCAAAGTGCTGGAGTGAGGCTCCAGAGGAGACTTTGAG
             TTGATGGGGGCCAGGACACCAGTCCAGGTAGTGTTGAGACCCAGGCCTGTGGCCCCACCGAGCTGGAG
             CGGAGAGGAAGCCAGCTGGCTTTGCACTTGACCTCATCTCCCGAGCAATGGCGCCTGCTCCCTCCAGA
             ATGGAACTCAAGCTGGTTTTAAGTGGAACTGCCCTACTGGGAGACTGGGACACCTTTAACACAGACCC
             CTAGGGATTTAAAGGGACACCCCTACACACACCCAGGCCCACGCCAAGGCCTCCCTCAGGCTCTGTGG
             AGGGCATTTGCTGCCCCAGCTACTAAGGTGCTAGGAATTCGTAATCATCCCCATCCTCCAGAGAAACC
             CAGGGAGGAAGACTGTAAATACGAACCCAATCTGCACACTCCAGGCCTCTAGTTCCAGAAGGATCCAA
             GACAAAACAGATCTGAATTCTGCCCTTTTCTCTCACCCATCCCACCCCTCCATTGGCTCCCAAGTCAC
             ACCCACTCCCTTCCCCATAGATAGGCCCCTGGGGCTCCCGAAGAATGAACCCAAGAGCAAGGGCTTGA
             TGGTGACAGCTGCAAGCCAGGGATGAAGAAAGACTCTGAGATGTGGAGACTGATGGCCAGGCAAGTGG
             GACCAGGATACTGGACGCTGTCCTGAGATGAGAGGTAGCCGGGCTCTGCACCCACGTGCATTCACATT
             GACCGCAACTCACACATTCCCCCACCAGCTGCAGCCCCTTGCTCTCAGCTGCCAACCCTCCCGGGTCA
             CTTTTGTTCCCAGGTACCTCATGGGAAGCATGTGGATGACACAATCCCTGGGGCTGTGCATTCCCACG
             TCTTCTTGCTGCAGCCTGCCCCTAGACATGGACGCACCGGCCTGGCTGCAGCTGGGCAGCAGGGGTAG
             GGGTAGGGAGCCTCCCCTCCCTGTATCACCCCCTCCCTACACACACACACACACACACACACACACAC
             TGCCTCCCATCCTTCCCTCATGCCCGCCAGTGCACAGGGAAGGGCTTGGCCAGCGCTGTTGAGGGGTC
             CCCTCTGGAATGCACTGAATAAAGCACGTGCAAGGACTCCCGGAGCCTGTGCAGCCTTGGTGGCAAAT
             ATCTCATCTGCCGGCCCCCAGGACAAGTGGTATGACCAGTGATAATGCCCCAAGGACAAGGGGCGTGC
             CTGGCGCCCAGTGGAGTAATTTATGCCTTAGTCTTGTTTTGAGGTAGAAATGCAAGGGGGACACATGA
             AAGGCATCAGTCCCCCTGTGCATAGTACGACCTTTACTGTCGTATTTTTGAAAAATTAAAAATACAGT
             GTTTAAAAACAAAAAAAAAAAAAAAAAAAAA
             ORF Start: ATG at 82      ORF Stop: TGA at 3649
             SEQ ID NO: 4              1189 aa   MW at 133608.9kD
NOV2a,       MDLPRGLVVAWALSLWPGFTDTFNMDTRKPRVIPGSRTAFFGYTVQQHDISGNKWLVVGAPLETNGYQ
CG106287-01
Protein      KTGDVYKCPVIHGNCTKLNLGRVTLSNVSERKDNMRLGLSLATNPKDNSFLACSPLWSHECGSSYYTT
Sequence
             GMCSRVNSNFRFSKTVAPALQRCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGVV
             QYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVITDG
             ESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAALKD
             IVDALGDRIFSLEGTNKNETSFGLENSQTGFSSHVVEDGVLLGAVGAYDWNGAVLKETSAGKVIPLRE
             SYLKEFPEELKNHGAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFTMHNNRSLTIHQAMRGQQI
             GSYFGSEITSVDIDGDGVTDVLLVGAPMYFNEGRERGKVYVYELRQNRFVYNGTLKDSHSYQNARFGS
             SIASVRDLNQDSYNDVVVGAPLEDNHAGAIYIFHGFRGSILKTPKQRITASELATGLQYFGCSIHGQL
             DLNEDGLIDLAVGALGNAVILWSRPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTPIFL
             APHFQTTTVGIRYNATMDERRYTPRAHLDEGGDRFTNRAVLLSSGQELCERINFHVLDTADYVKPVTF
             SVEYSLEDPDHGPMLDDGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYCQRVLRKPAQD
             CSAYTLSFDTTVFIIESTRQRVAVEATLENRGENAYSTVLNISOSANLQFASLIQKEDSDGSIECVNE
             ERRLQKQVCNVSYPFFRAKAKVAFRLDFEFSKSIFLHHLEIELAAGSDSNERDSTKEDNVAPLRFHLK
             YEADVLFTRSSSLSHYEVKLNSSLERYDGIGPPFSCIFRIQNLGLFPIHGIMMKITIPIATRSGNRLL
             KLRDFLTDEVANTSCNIWGNSTEYRPTPVEEDLRRAPQLNHSNSDVVSINCNIRLVPNQEINFHLLGN
             LWLRSLKALKYKSMKIMVNAALQRQFHSPFIFREEDPSRQIVFEISKQEDWQVPIWIIVGSTLGGLLL
             LALLVLALWKLGFFRSARRRREPGLDPTPKVLE
             SEQ ID NO: 5              4779 bp
NOV2b,       AGGAGGCTGCCGCTCTGGCTTGCCGCCCCCCGCCGCCGCTGCACACCGGACCCAGCCGCCGTGCCGC
CG106287-02
DNA Sequence GGGCCATGGACCTGCCCAGGGGCCTGGTGGTGGCCTGGGCGCTCAGCCTGTGCCCAGGTTTCACGGA
             CACCTTCAACATGGACACCAGGAAGCCCCGGGTCATCCCTGGCTCCAGGACCGCCTTCTTTGGCTAC
             ACAGTGCAGCAGCACGACATCAGTGGCAATAAGTGGCTGGTCGTGGGCGCCCCACTGGAAACCAATG
             GCTACCAGAAGACGGGAGACGTGTACAAGTGTCCAGTGATCCACGGGAACTGCACCAAACTCAACCT
             GGGGTGCCAGACCTACATGGACATCGTCATTGTCCTGGATGGCTCCAACAGCATCTACCCCTGGGTG
             GAGGTTCAGCACTTCCTCATCAACATCCTGAAAAAGTTTTACATTGGCCCAGGGCAGATCCAGGTTC
             GAGTTGTGCAGTATGGCGAAGATGTGGTGCATGAGTTTCACCTCAATGACTACAGGTCTGTAAAAGA
             TGTGGTGGAAGCTGCCAGCCACATTGAGCAGAGAGGAGGAACAGAGACCCGGACGGCATTTGGCATT
             GAATTTGCACGCTCAGAGGCTTTCCAGAAGGGTGGAAGGAAAGGAGCCAAGAAGGTGATGATTGTCA
             TCACAGATGGGGAGTCCCACGACAGCCCAGACCTGGAGAAGGTGATCCAGCAAAGCGAAAGAGACAA
             CGTAACAAGATATGCGGTGGCCGTCCTGGGCTACTACAACCGCAGGGGGATCAATCCAGAAACTTTT
             CTAAATGAAATCAAATACATCGCCAGTGACCCTGATGACAAGCACTTCTTCAATGTCACTGATGAGG
             CTGCCTTGAAGGACATTGTCGATGCCCTGGGGGACAGAATCTTCAGCCTGGAAGGCACCAACAAGAA
             CGAGACCTCCTTTGGGCTGGAGATGTCACAGACGGGCTTTTCCTCGCACGTGGTGGAGGATGGGGTT
             CTGCTGGGAGCCGTCGGTGCCTATGACTGGAATGGAGCTGTGCTAAAGGAGACGAGTGCCGGGAAGG
             TCATTCCTCTCCGCGAGTCCTACCTGAAAGAGTTCCCCGAGGAGCTCAAGAACCATGGTGCATACCT
             GGGGTACACAGTCACATCGGTCGTGTCCTCCAGGCAGGGGCGAGTGTACGTGGCCGGAGCCCCCCGG
             TTCAACCACACGGGCAAGGTCATCCTGTTCACCATGCACAACAACCGGAGCCTCACCATCCACCAGG
             CTATGCGGGGCCAGCAGATAGGCTCTTACTTTGGGAGTGAAATCACCTCGGTGGACATCGACGGCGA
             CGGCGTGACTGATGTCCTGCTGGTGGGCGCACCCATGTACTTCAACGAGGGCCGTGAGCGAGGCAAG
             GTGTACGTCTATGAGCTGAGACAGAACCGGTTTGTTTATAACGGAACGCTAAAGGATTCACACAGTT
             ACCAGAATGCCCGATTTGGGTCCTCCATTGCCTCAGTTCGAGACCTCAACCAGGATTCCTACAATGA
             CGTGGTGGTGGGAGCCCCCCTGGAGGACAACCACGCAGGAGCCATCTACATCTTCCACGGCTTCCGA
             GGCAGCATCCTGAAGACACCTAAGCAGAGAATCACAGCCTCAGAGCTGGCTACCGGCCTCCAGTATT
             TTGGCTGCAGCATCCACGGGCAATTGGACCTCAATGAGGATGGGCTCATCGACCTGGCAGTGGGAGC
             CCTTGGCAACGCTGTGATTCTGTGGTCCCGCCCAGTGGTTCAGATCAATGCCAGCCTCCACTTTGAG
             CCATCCAAGATCAACATCTTCCACAGAGACTGCAAGCGCAGTGGCAGGGATGCCACCTGCCTGGCCG
             CCTTCCTCTGCTTCACGCCCATCTTCCTGGCACCCCATTTCCAAACAACAACTGTTGGCATCAGATA
             CAACGCCACCATGGATGAGAGGCGGTATACACCGAGGGCCCACCTGGACGAGGGCGGGGACCGATTC
             ACCAACAGAGCCGTACTGCTCTCCTCCGGCCAGGAGCTCTGTGAGCGGATCAACTTCCATGTCCTGG
             ACACTGCTGACTACGTGAAGCCAGTGACCTTCTCAGTCGAGTATTCCCTGGAGGACCCTGACCATGG
             CCCCATGCTGGACGACGGCTGGCCCACCACTCTCAGAGTCTCGGTGCCCTTCTGGAACGGCTGCAAT
             GAGGATGAGCACTGTGTCCCTGACCTTGTGTTGGATGCCCGGAGTGACCTGCCCACGGCCATGGAGT
             ACTGCCAGAGGGTGCTGAGGAAGCCTGCGCAGGACTGCTCCGCATACACGCTGTCCTTCGACACCAC
             AGTCTTCATCATAGAGAGCACACGCCAGCGAGTGGCGGTGGAGGCCACACTGGAGAACAGGGGCGAG
             AACGCCTACAGCACGGTCCTAAATATCTCGCAGTCAGCAAACCTGCAGTTTGCCAGCTTGATCCAGA
             AGGAGGACTCAGACGGTAGCATTGAGTGTGTGAACGAGGAGAGGAGGCTCCAGAAGCAAGTCTGCAA
             CGTCAGCTATCCCTTCTTCCGGGCCAAGGCCAAGGTGGCTTTCCGTCTTGATTTTGAGTTCAGCAAA
             TCCATCTTCCTACACCACCTGGAGATCGAGCTCGCTGCAGGCAGTGACAGTAATGAGCGGGACAGCA
             CCAAGGAAGACAACGTGGCCCCCTTACGCTTCCACCTCAAATACGAGGCTGACGTCCTCTTCACCAG
             GAGCAGCAGCCTGAGCCACTACGAGGTCAAGCTCAACAGCTCGCTGGAGAGATACGATGGTATCGGG
             CCTCCCTTCAGCTGCATCTTCAGGATCCAGAACTTGGGCTTGTTCCCCATCCACGGGATTATGATGA
             AGATCACCATTCCCATCGCCACCAGGAGCGGCAACCGCCTACTGAAGCTGAGGGACTTCCTCACGGA
             CGAGGTAGCGAACACGTCCTGTAACATCTGGGGCAATAGCACTGAGTACCGGCCCACCCCAGTGGAG
             GAAGACTTGCGTCGTGCTCCACAGCTGAATCACAGCAACTCTGATGTCGTCTCCATCAACTGCAATA
             TACGGCTGGTCCCCAACCAGGAAATCAATTTCCATCTACTGGGGAACCTGTGGTTGAGGTCCCTAAA
             AGCACTCAAGTACAAATCCATGAAAATCATGGTCAACGCAGCCTTGCAGAGGCAGTTCCACAGCCCC
             TTCATCTTCCGTGAGGAGGATCCCAGCCGCCAGATCGTGTTTGAGATCTCCAAGCAAGAGGACTGGC
             AGGTCCCCATCTGGATCATTGTAGGCAGCACCCTGGGGGGCCTCCTACTGCTGGCCCTGCTGGTCCT
             GGCACTGTGGAAGCTCGGCTTCTTTAGAAGTGCCAGGCGCAGGAGGGAGCCTGGTCTGGACCCCACC
             CCCAAAGTGCTGGAGTGAGGCTCCAGAGGAGACTTTGAGTTGATGGGGGCCAGGACACCAGTCCAGG
             TAGTGTTGAGACCCAGGCCTGTGGCCCCACCGAGCTGGAGCGGAGAGGAAGCCAGCTGGCTTTGCAC
             TTGACCTCATCTCCCGAGCAATGGCGCCTGCTCCCTCCAGAATGGAACTCAAGCTGGTTTTAAGTGG
             AACTGCCCTACTGGGAGACTGGGACACCTTTAACACAGACCCCTAGGGATTTAAAGGGACACCCCTA
             CACACACCCAGGCCCACGCCAAGGCCTCCCTCAGGCTCTGTGGAGGGCATTTGCTGCCCCAGCTACT
             AAGGTGCTAGGAATTCGTAATCATCCCCATCCTCCAGAGAAACCCAGGGAGGAAGACTGTAAATACG
             AACCCAATCTGCACACTCCAGGCCTCTAGTTCCAGAAGGATCCAAGACAAAACAGATCTGAATTCTG
             CCCTTTTCTCTCACCCATCCCACCCCTCCATTGGCTCCCAAGTCACACCCACTCCCTTCCCCATAGA
             TAGGCCCCTGGGGCTCCCGAAGAATGAACCCAAGAGCAAGGGCTTGATGGTGACAGCTGCAAGCCAG
             GGATGAAGAAAGACTCTGAGATGTGGAGACTGATGGCCAGGCAAGTGGGACCAGGATACTGGACGCT
             GTCCTGAGATGAGAGGTAGCCGGGCTCTGCACCCACGTGCATTCACATTGACCGCAACTCACACATT
             CCCCCACCAGCTGCAGCCCCTTGCTCTCAGCTGCCAACCCTCCCGGGTCACTTTTGTTCCCAGGTAC
             CTCATGGGAAGCATGTGGATGACACAATCCCTGGGGCTGTGCATTCCCACGTCTTCTTGCTGCAGCC
             TGCCCCTAGACATGGACGCACCGGCCTGGCTGCAGCTGGGCAGCAGGGGTAGGGGTAGGGAGCCTCC
             CCTCCCTGTATCACCCCCTCCCTACACACACACACACACACACACACACACACTGCCTCCCATCCTT
             CCCTCATGCCCGCCAGTGCACAGGGAAGGGCTTGGCCAGCGCTGTTGAGGGGTCCCCTCTGGAATGC
             ACTGAATAAAGCACGTGCAAGGACTCCCGGAGCCTGTGCAGCCTTGGTGGCAAATATCTCATCTGCC
             GGCCCCCAGGACAAGTGGTATGACCAGTGATAATGCCCCAAGGACAAGGGGCGTGCCTGGCGCCCAG
             TGGAGTAATTTATGCCTTAGTCTTGTTTTGAGGTAGAAATGCAAGGGGGACACATGAAAGGCATCAG
             TCCCCCTGTGCATAGTACGACCTTTACTGTCGTATTTTTGAAAAATTAAAAATACAGTGTTTAAAAA
             CAAAAAAAAAAAAAAAAAAAAA
             ORF Start: ATG at 73      ORF Stop: TGA at 3433
             SEQ ID NO: 6              1120 aa   MW at 125924.3kD
NOV2b,       MDLPRGLVVAWALSLWPGFTDTFNMDTRKPRVIPGSRTAFFGYTVQQHDISGNKWLVVGAPLETNGY
CG106287-02
Protein      QKTGDVYKCPVIHGNCTKLNLGCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGV
Sequence
             VQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVIT
             DGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAA
             LKDIVDALGDRIFSLEGTNKNETSFGLEMSQTGFSSHVVEDGVLLGAVGAYDWNGAVLKETSAGKVI
             PLRESYLKEFPEELKNHGAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFTMHNNRSLTIHQAM
             RGQQIGSYFGSEITSVDIDGDGVTDVLLVGAPMYFNEGRERGKVYVYELRQNRFVYNGTLKDSHSYQ
             NARFGSSIASVRDLNQDSYNDVVVGAPLEDNHAGAIYIFHGFRGSILKTPKQRITASELATGLQYFG
             CSIHGQLDLNEDGLIDLAVGALGNAVILWSRPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAF
             LCFTPIFLAPHFQTTTVGIRYNATMDERRYTPRAHLDEGGDRFTNRAVLLSSGQELCERINFHVLDT
             ADYVKPVTFSVEYSLEDPDHGPMLDDGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYC
             QRVLRKPAQDCSAYTLSFDTTVFIIESTRQRVAVEATLENRGENAYSTVLNISQSANLQFASLIQKE
             DSDGSIECVNEERRLQKQVCNVSYPFFRAKAKVAFRLDFEFSKSIFLHHLEIELAAGSDSNERDSTK
             EDNVAPLRFHLKYEADVLFTRSSSLSHYEVKLNSSLERYDGIGPPFSCIFRIQNLGLFPIHGIMMKI
             TIPIATRSGNRLLKLRDFLTDEVANTSCNIWGNSTEYRPTPVEEDLRRAPOLNHSNSDVVSINCNIR
             LVPNQEINFHLLGNLWLRSLKALKYKSMKIMVNAALQRQFHSPFIFREEDPSRQIVFEISKQEDWQV
             PIWIIVGSTLGGLLLLALLVLALWKLGFFRSARRRREPGLDPTPKVLE

[0370] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 2B.

TABLE 2B
Comparison of NOV2a against NOV2b.
	Protein	NOV2a Residues/	Identities/Similarities
	Sequence	Match Residues	for the Matched Region
	NOV2b	159 . . . 1189	1017/1031 (98%)
		90 . . . 1120	1017/1031 (98%)

[0371] Further analysis of the NOV2a protein yielded the following properties shown in Table 2C.

TABLE 2C
Protein Sequence Properties NOV2a
PSort     0.6400 probability located in plasma membrane; 0.4600
analysis: probability located in Golgi body; 0.3700 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 23 and 24
analysis:

[0372] A search of the NOV2a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 2D.

TABLE 2D
Geneseq Results for NOV2a
			Identities/
		NOV2a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB25582	ITGA11 protein	1 . . . 1189	1189/1189	0.0
	encoded by human		(100%)
	secreted protein	1 . . . 1189	1189/1189
	gene #7—Homo		(100%)
	sapiens, 1189 aa.
	[WO200029435-A1,
	25 MAY 2000]
ABG12949	Novel human	1 . . . 1189	1188/1189	0.0
	diagnostic protein		(99%)
	#12940—Homo	1 . . . 1189	1189/1189
	sapiens, 1189 aa.		(99%)
	[WO200175067-A2,
	11 OCT. 2001]
AAU10551	Human A259 poly-	1 . . . 1189	1186/1189	0.0
	peptide—Homo		(99%)
	sapiens, 1188 aa.	1 . . . 1188	1187/1189
	[WO200181414-A2,		(99%)
	1 NOV. 2001]
AAB50085	Human A259—	1 . . . 1189	1186/1189	0.0
	Homo sapiens,		(99%)
	1188 aa.	1 . . . 1188	1187/1189
	[WO200073339-A1,		(99%)
	7 DEC. 2000]
AAU14231	Human novel	1 . . . 1189	1186/1189	0.0
	protein #102—		(99%)
	Homo sapiens,	1 . . . 1188	1187/1189
	1188 aa.		(99%)
	[WO200155437-A2,
	2 AUG. 2001]

[0373] In a BLAST search of public sequence datbases, the NOV2a protein was found to have homology to the proteins shown in the BLASTP data in Table 2E.

TABLE 2E
Public BLASTP Results for NOV2a
			Identities/
		NOV2a	Similarities
Protein		Residues/	for the
Accession	Protein/	Match	Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9UKX5	Integrin alpha-11	1 . . . 1189	1189/1189	0.0
	precursor—Homo		(100%)
	sapiens (Human),	1 . . . 1189	1189/1189
	1189 aa.		(100%)
CAD28200	Sequence 1	1 . . . 1189	1186/1189	0.0
	from Patent		(99%)
	WO0181414—	1 . . . 1188	1187/1189
	Homo sapiens		(99%)
	(Human),
	1188 aa.
CAD28203	Sequence 19	1 . . . 1189	1073/1189	0.0
	from Patent		(90%)
	WO0181414—	1 . . . 1188	1130/1189
	Mus musculus		(94%)
	(Mouse), 1188 aa.
Q8WY18	MSTP018—	366 . . . 1189	822/824	0.0
	Homo sapiens		(99%)
	(Human), 823 aa.	1 . . . 823	823/824
			(99%)
O75578	Integrin alpha-10	1 . . . 1170	513/1181	0.0
	precursor—Homo		(43%)
	sapiens (Human),	1 . . . 1150	723/1181
	1167 aa.		(60%)

[0374] PFam analysis predicts that the NOV2a protein contains the domains shown in the Table 2F.

TABLE 2F
Domain Analysis of NOV2a
Pfam	NOV2a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
FG-GAP	38 . . . 94	19/65 (29%)	2e−08
		39/65 (60%)
vwa	164 . . . 345	65/208 (31%)	8.1e−54
		155/208 (75%)
FG-GAP	422 . . . 475	13/65 (20%)	4.2e−06
		42/65 (65%)
FG-GAP	477 . . . 537	23/65 (35%)	2.6e−12
		48/65 (74%)
FG-GAP	539 . . . 598	24/67 (36%)	1.6e−15
		53/67 (79%)
FG-GAP	601 . . . 653	20/66 (30%)	3.2e−09
		42/66 (64%)

Example 3

[0375] The NOV3 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 3A.

TABLE 3A
NOV3 Sequence Analysis
             SEQ ID NO: 7              1915 bp
NOV3a,       CCCGGGGGACCCGCCGCCGCCGGTCATGTGGGCCGGACTGCTCCTTCGGGCCGCCTGTGTCGCGCTCC
CG106417-01
DNA Sequence TGCTGCCGGGGGCACCAGCCCGAGGCTACACCGGGAGGAAGCCGCCCGGGCACTTCGCGGCCGAGAGG
             AGACGCCGACTGGGCCCCCACGTCTGCCTCTCTGGGTTTGGGAGTGGCTGCTGCCCTGGCTGGGCGCC
             CTCTATGGGTGGTGGGCACTGCACCCTGCGTAAGCTCTGCTCCTTCGGCTGTGGGAGTGGCATCTGCA
             TCGCTCCCAATGTCTGCTCCTGCCAGGATGGAGAGCAAGGGGCCACCTGCCCAGAAACCCATGGACCA
             TGTGGGGAGTACGGCTGTGACCTTACCTGCAACCATGGAGGCTGTCAGGAGGTGGCCCGAGTGTGCCC
             CGTGGGCTTCTCGATGACGGAGACAGCTGTTGGCATCAGGTGTACAGACATTGACGAATGTGTAACCT
             CCTCCTGCGAGGGCCACTGTGTGAACACAGAAGGTGGGTTTGTGTGCGAGTGTGGGCCGGGCATGCAG
             CTGTCTGCCGACCGCCACAGCTGCCAAGACACTGACGAATGCCTAGGGACTCCCTGTCAGCAGAGATG
             TAAAAACAGCATTGGCAGCTACAAGTGTTCCTGTCGAACTGGCTTCCACCTTCATGGCAACCGGCACT
             CCTGTGTAGACGCAAACGAGTGTCGGACGCCATCGGAGACGCGAGTCTGTCACCATTCCTGCCACAAC
             ACCGTGGGCAGCTTCGTATGCACATGCGGACCTGGTTTCAGGTTCGGAGCTGACCGCGTGTCTGTTTC
             AGCTTTCCCGAAAGCCGTGCTGGCCCCATCTGCCATCCTGCAACCCCGGCAACACCCGTCCAAGATGC
             TTCTGTTGCTTCCTGAGGCCGGCCGGCCTGCCCTGTCCCCAGGACATAGCCCTCCTTCTGGGGCTCCA
             GGGCCCCCAGCCGGAGTCAGGACCACCCGCCTGCCATCTCCCACCCCACGACTACCCACATCCTCCCC
             TTCTGCCCTGCTGGCCACCCCAGTGCCTACTGCCTCCCTGCTGGGGAACCTCAGACCCCCCTCACTCC
             TTCAGGGGGAGGTGATGGGGACCCCTTCCTCACCCAGGGGCCCTGAGTCCCCCCGACTGGCAGCAGGG
             CCCTCTCCCTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTGGGTGTTC
             CCAGTGCTGGTGCGAGGTGGGTGGGCCTTGTGGTGGCGACGGGAAGGTGACCTGTGAAAAGGTGAGGT
             GTGAAGCTGCTTGTTCCCACCCAATTCCCTCCAGAGATGGTGGGTGCTGCCCATCGTGCACAGGTTCC
             TATTTGTCCTTCAAAGGCTGTTTTCACAGTGGTGTCGTCCGAGCTGAAGGGGATGTGTTTTCACCTCC
             CAATGAGAACTGCACCGTCTGTGTCTGTCTGGCTGGAAACGTGTCGTGCATGTTTCGTGAGTGTCCTT
             TTGGCCCGTGTGAGACCCCCCATAAAGACAGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCT
             GTGTTCAGTGGGGGTGGTGACGAGTGTACCACCTGTGTTTGCCAGCAGAATGGGGAGGTGGAGTGCTC
             CTTCATGCCCTGCCCTGAGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCT
             TCACCTGCCAGGAGCCCACACCCTCGACAGGTGGCTGCTCTCTTGACGACAACGGGGTTGAGTTTCCG
             ATTGGACAGATCTGGTCGCCTGGTGACCCCTGTCCAGGCAGATGGCTCGGTGAGCTGCAAGAGGACAG
             ACTGTGTGGACTCCTGCCCTCACCCGATCCGGATCCCTGGACAGTGCTGCCCAGACTGTTCAGCAGGT
             AATCCCCTGCC
             ORF Start: ATG at 26      ORF Stop: TAA at 1904
             SEQ ID NO: 8              626 aa    MW at 66006.2kD
NOV3a, MWAGLLLRAACVALLLPGAPARGYTGRKPPGHFAAERRRRLGPHVCLSGFGSGCCPGWAPSMGGGHCT
CG106417-01
Protein      LRKLCSFGCGSGICIAPNVCSCQDGEQGATCPETHGPCGEYGCDLTCNHGGCQEVARVCPVGFSMTET
Sequence
             AVGIRCTDIDECVTSSCEGHCVNTEGGFVCECGPGMQLSADRHSCQDTDECLGTPCQQRCKNSIGSYK
             CSCRTGFHLHGNRHSCVDANECRTPSETRVCHHSCHNTVGSFVCTCGPGFRFGADRVSVSAFPKAVLA
             PSAILQPRQHPSKMLLLLPEAGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLPTSSPSALLATPV
             PTASLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGAMHESRSRWTEPGCSQCWCEVGG
             PCGGDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGSYLSFKGCFHSGVVRAEGDVFSPPNENCTVCV
             CLAGNVSCMFRECPFGPCETPHKDRCYFHGRWYADGAVFSGGGDECTTCVCQQNGEVECSFMPCPELA
             CPREEWRLGPGQCCFTCQEPTPSTGGCSLDDNGVEFPIGQIWSPGDPCPGRWLGELQEDRLCGLLPSP
             DPDPWTVLPRLFSR
             SEQ ID NO: 9              12040 bp
NOV3b,       ATGTGGGCCGGACTGCTCCTTCGGGCCGCCTGTGTCGCGCTCCTGCTGCCGGGGGCACCAGCCCGAG
CG1064417-03
DNA Sequence GCTACACCGGGAGGAAGCCGCCCGGGCACTTCGCGGCCGAGAGGAGACGCCGACTGGGCCCCCACGT
             CTGCCTCTCTGGGTTTGGGAGTGGCTGCTGCCCTGGCTGGGCGCCCTCTATGGGTGGTGGGCACTGC
             ACCCTGCTCTGCTCCTTCGGCTGTGGGAGTGGCATCTGCATCGCTCCCAATGTCTGCTCCTGCCAGG
             ATGGAGAGCAAGGGGCCGAAACCCATGGACCATGTGGGGAGTACGGCTGTGACCTTACCTGCAACCA
             TGGAGGCTGTCAGGAGGTGGCCCGAGTGTGCCCCGTGGGCTTCTCGATGACGGAGACAGCTGTTGGC
             ATCAGGTGTGACATTGACGAATGTGTAACCTCCTCCTGCGAGGGCCACTGTGTGAACACAGAAGGTG
             GGTTTGTGTGCGAGTGTGGGCCGGGCATGCAGCTGTCTGCCGACCGCCACAGCTGCCAAGACACTGA
             CGAATGCCTAGGGACTCCCTGTCAGCAGAGATGTAAAAACAGCATTGGCAGCTACAAGTGTTCCTGT
             CGAACTGGCTTCCACCTTCATGGCAACCGGCACTCCTGTGTAGACGCAAACGAGTGTCGGACGCCAT
             CGGAGACGCGAGTCTGTCACCATTCCTGCCACAACACCGTGGGCAGCTTCGTATGCACATGCGGACC
             TGGTTTCAGGTTCGGAGCTGACCGCGTGCCATGTGAAGGTGAGCGCCAGGCCAGAGACCTCCGTGCT
             TCTGTTTCAGCTTTCCCGAAAGCCGTGCTGGCCCCATCTGCCATCCTGCAACCCCGGCAACACCCGT
             CCAAGATGCTTCTGTTGCTTCCTGAGGCCGGCCGGCCTGCCCTGTCCCCAGGACATAGCCCTCCTTC
             TGGGGCTCCAGGGCCCCCAGCCGGAGTCAGGACCACCCGCCTGCCATCTCCCACCCCACGACTACCC
             ACATCCTCCCCTTCTGCCCCTGTGTGGCTGCTGTCCACCCTGCTGGCCACCCCAGTGCCTACTGCCT
             CCCTGCTGGGGAACCTCAGACCCCCCTCACTCCTTCAGGGGGAGGTGATGGGGACCCCTTCCTCACC
             CAGGGGCCCTGAGTCCCCCCGACTGGCACCAGGGCCCTCTCCCTGCTGGCACCTGGGAGCCATGCAT
             GAATCAAGGAGTCGCTGGACAGAGCCTGGGTGTTCCCAGTGCTGGTGCGAGGGCTCTAACTCCTGCT
             TGTGCTTCGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCCAATTCC
             CTCCAGAGATGGTGGGTGCTGCCCATCGTGCACAGGTGGCTGTTTTCACAGTGGTGTCGTCCGAGCT
             GAAGGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTCTGTCTGGCTGGAAACGTGT
             CGTGCATGTTTCGTGAGTGTCCTTTTGGCCCGTGTGAGACCCCCCATAAAGACTGCAGGTGCCCACC
             TGGAAGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTGTTCAGTGGGGGTGGTGACGAG
             TGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTGCCCTGAGCTGGCCT
             GCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCAGGAGCCCACACCCTC
             GACAGGTCTTGACGACAACGGGGTTGAGTTTCCGATTGGACAGATCTGGTCGCCTGGTGACCCCTGT
             GAGAGATGGCTCGGTGAGCTGCAAGAGGACAGACTGTGTGGACTCCTGCCCTCACCCGATCCGGATC
             CCTGGACAGTGCTGCCCAGACTGTTCAGCAGGTAATCCCCTGCCTCTGCCCCAAGCCCCCAGGGCAG
             GGCATCTCAGGCATCGGGCTCCTTAAGCCCTATACAGCCTTCATCTCATGTCGTCCTAACAACCCCA
             AGGGACAACCCCATTGCACAGATAAGGAAA
             ORF Start: ATG at 1       ORF Stop: TAA at 1909
             SEQ ID NO: 10             636 aa    MW at 67370.7kD
NOV3b,       MWAGLLLRAACVALLLPGAPARGYTGRKPPGHFAAERRRRLGPHVCLSGFGSGCCPGWAPSMGGGHC
CG106417-03
Protein      TLLCSFGCGSGICIAPNVCSCQDGEQGAETHGPCGEYGCDLTCNHGGCQEVARVCPVGFSMTETAVG
Sequence
             IRCDIDECVTSSCEGHCVNTEGGFVCECGPGMQLSADRHSCQDTDECLGTPCQQRCKNSIGSYKCSC
             RTGFHLHGNRHSCVDANECRTPSETRVCHHSCHNTVGSFVCTCGPGFRFGADRVPCEGERQARDLRA
             SVSAFPKAVLAPSAILQPRQHPSKMLLLLPEAGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLP
             TSSPSAPVWLLSTLLATPVPTASLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGAMH
             ESRSRWTEPGCSQCWCEGSNSCLCFDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGGCFHSGVVRA
             EGDVFSPPNENCTVCVCLAGNVSCMFRECPFGPCETPHKDCRCPPGRCYFHGRWYADGAVFSGGGDE
             CTTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCFTCQEPTPSTGLDDNGVEFPIGQIWSPGDPC
             ERWLGELQEDRLCGLLPSPDPDPWTVLPRLFSR
             SEQ ID NO: 11             1821 bp
NOV3c,       ATGTGGGCCGGACTGCTCCTTCGGGCCGCCTGTGTCGTCTGCTCCTTCGGCTGTGGGAGTGGCATCTG
CG106417-04
DNA Sequence CATCGCTCCCAATGTCTGCTCCTGCCAGGATGGAGAGCAAGGGGCCGAAACCCATGGACCATGTGGGG
             AGTACGGCTGTGACCTTACCTGCAACCATGGAGGCTGTCAGGAGGTGGCCCGAGTGTGCCCCGTGGGC
             TTCTCGATGACGGAGACAGCTGTTGGCATCAGGTGTGACATTGACGAATGTGTAACCTCCTCCTGCGA
             GGGCCACTGTGTGAACACAGAAGGTGGGTTTGTGTGCGACTGTGGCCCGCCCATGCAGCTGTCTGCCG
             ACCGCCACAGCTGCCAAGACACTGACGAATGCCTAGGGACTCCCTGTCAGCAGAGATGTAAAAACAGC
             ATTGGCAGCTACAAGTGTTCCTGTCGAACTGGCTTCCACCTTCATGGCAACCGGCACTCCTGTGTAGA
             TGTAAACGAGTGTCGGAGGCCATTGGAGAGGCGAGTCTGTCACCATTCCTGCCACAACACCGTGGGCA
             GCTTCCTATGCACATGCCGACCTGGCTTCAGGCTCCGAGCTGACCGCGTGTCCTGTGAAGGTGAGCGC
             CAGGCTTTCCCGAAAGCCGTGCTGGCCCCATCTGCCATCCTGCAACCCCGGCAACACCCGTCCAAGAT
             GGTTCTGTTGCTTCCTGAGGCCGGCCGGCCTGCCCTGTCCCCAGGACATAGCCCTCCTTCTGGGGCTC
             CAGGGCCCCCAGCCGGAGTCAGGACCACCCGCCTGCCATCTCCCACCCCACGACTACCCACATCCTCC
             CCTTCTGCCCCTGTGTGGCTGCTGTCCACCCTGCTGGCCACCCCAGTGCCTACTGCCTCCCTGCTGGG
             GAACCTCAGACCCCCCTCACTCCTTCAGGGGGAGGTGATGGGGACCCCTTCCTCACCCAGGGGCCCTG
             AGTCCCCCCGACTGGCAGCAGGGCCCTCTCCCTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGT
             CGCTGGACAGAGCCTGGGTGTTCCCAGTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAG
             GTGTGAAGCTGCTTGTTCCCACCCAATTCCCTCCAGAGATGGTGGGTGCTGCCCATCGTGCACAGGTT
             GTTTTCACAGTGGTGTCGTCCGAGCTGAAGGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTG
             TGTGTCTGTCTGGCTGGAAACGTGTCCTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCAGACCCC
             CCCACAGACGGATTGCTGTACTTGTGTTCCAGGTAGATGCTATTTCCACGGCCGGTGGTACGCAGACG
             GGGCTGTGTTCAGTGGGGGTGGTGACGAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGC
             TCCTTCATGCCCTGCCCTGAGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTG
             CTTCACCTGCCAGGAGCCCACACCCTCGACAGGTCTTGACGACAACGGGGTTGAGTTTCCGATTGGAC
             AGATCTGGTCGCCTGGTGACCCCTGTGAGAGATGGCTCGGTGAGCTGCAAGAGGACAGACTGTGTGGA
             CTCCTGCCCTCACCCGATCCGGATCCCTGGACAGTGCTGCCCAGACTGTTCAGCAGGTAATCCCCTGC
             CTCTGCCCCAAGCCCCCAGGGCAGGGCATCTCAGGCATCGGGCTCCTTAAGCCCTATACAGCCTTCAT
             CTCATGTCGTCCTAACAACCCCAAGGGACAACCCCATTGCACAGATAAGGAAA
             ORF Start: ATG at 1       ORF Stop: TAA at 1690
             SEQ ID NO: 12             563 aa    MW at 59951.3kD
NOV3c,       MWAGLLLRAACVVCSFGCGSGICIAPNVCSCQDGEQGAETHGPCGEYGCDLTCNHGGCQEVARVCPVG
CG106417-04
Protein      FSMTETAVGIRCDIDECVTSSCEGHCVNTEGGFVCECGPGMQLSADRHSCQDTDECLGTPCQQRCKNS
Sequence
             IGSYKCSCRTGFHLHGNRHSCVDVNECRRPLERRVCHHSCHNTVGSFLCTCRPGFRLRADRVSCEGER
             QAFPKAVLAPSAILQPRQHPSKMLLLLPEAGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLPTSS
             PSAPVWLLSTLLATPVPTASLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGAMHESRS
             RWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVVRAEGDVFSPPNENCTV
             CVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPGRCYFHGRWYADGAVFSGGGDECTTCVCQNGEVEC
             SFMPCPELACPREEWRLGPGQCCFTCQEPTPSTGLDDNGVEFPIGQIWSPGDPCERWLGELQEDRLCG
             LLPSPDPDPWTVLPRLFSR
             SEQ ID NO: 13             534 bp
NOV3d,       AAGCTTTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTGGGTGTTCCC
209749357
DNA Sequence AGTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCC
             AATTCCCTCCAGAGATGGTGGGTGCTGCCCATCGTGCACAGGCTGTTTTCACAGTGGTGTCGTCCGA
             GCTGAAGGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTCTGTCTGGCTGGAAACG
             TGTCCTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCAGACCCCCCCACAGACGGATTGCTGTAC
             TTGTGTTCCAGTGAGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTGTTCAGTGGGGGT
             GGTGACGAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTGCCCTG
             AGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCTCGAC
             ORF Start: at 1           ORF Stop: end of sequence
             SEQ ID NO: 14             178 aa    MW at 19201.6kD
NOV3d,       KLCWHLGAMHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVVR
209749357
Protein      AEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPVRCYFHGRWYADGAVFSGG
Sequence
             GDECTTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCFTCLE
             SEQ ID NO: 15             534 bp
NOV3e,       AAGCTTTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTGGGTGTTCCCA
CG106417-02
DNA Sequence GTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCCAA
             TTCCCTCCAGAGATGGTGGGTGCTGCCCATCGTGCACAGGCTGTTTTCACAGTGGTGTCGTCCGAGCT
             GAAGGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTCTGTCTGGCTGGAAACGTGTC
             CTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCAGACCCCCCCACAGACGGATTGCTGTACTTGTG
             TTCCAGTGAGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTGTTCAGTGGGGGTGGTGAC
             GAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTGCCCTGAGCTGGC
             CTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCTCGAG
             ORF Start: at 7           ORF Stop: at 529
             SEQ ID NO: 16             174 aa    MW at 18718.0kD
NOV3e,       CWHLGAMHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVVRAEG
CG106417-02
Protein      DVFSPPNENCTVCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPVRCYFHGRWYADGAVFSGGGDEC
Sequence
             TTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCFTC

[0376] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 3B.

TABLE 3B
Comparison of NOV3a against NOV3b through NOV3e.
		NOV3a Residues/	Identities/Similarites
	Protein Sequence	Match Residues	for the Matched Region
	NOV3b	1 . . . 626	552/653 (84%)
		1 . . . 636	552/653 (84%)
	NOV3c	72 . . . 626	472/574 (82%)
		13 . . . 563	475/574 (82%)
	NOV3d	381 . . . 563	155/191 (81%)
		3 . . . 178	156/191 (81%)
	NOV3e	381 . . . 561	154/189 (81%)
		1 . . . 174	155/189 (81%)

[0377] Further analysis of the NOV3a protein yielded the following properties shown in Table 3C.

TABLE 3C
Protein Sequence Properties NOV3a
PSort analysis:   0.5947 probability located in outside; 0.1900 probability located in lysosome
                  (lumen); 0.1000 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 22 and 23

[0378] A search of the NOV3a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 3D.

TABLE 3D
Geneseq Results for NOV3a
		NOV3a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB85364	Novel Von	286 . . . 500	194/222 (87%)	e−113
	Willebrand/thrombosporin-	1 . . . 208	196/222 (87%)
	like polypeptide - Homo
	sapiens, 235 aa.
	[WO200153485-A1,
	Jul. 26, 2001]
AAM99920	Human polypeptide SEQ ID	384 . . . 592	185/217 (85%)	e−112
	NO 36 - Homo sapiens, 272	5 . . . 205	188/217 (86%)
	aa. [WO200155173-A2,
	Aug. 2, 2001]
AAM99933	Human polypeptide SEQ ID	384 . . . 592	181/217 (83%)	e−110
	NO 49 - Homo sapiens, 212	5 . . . 205	185/217 (84%)
	aa. [WO200155173-A2,
	Aug. 2, 2001]
AAB85365	Novel Von	304 . . . 500	176/204 (86%)	e−102
	Willebrand/thrombosporin-	1 . . . 190	178/204 (86%)
	like mature protein sequence -
	Homo sapiens, 217 aa.
	[WO200153485-A1,
	Jul. 26, 2001]
ABG15393	Novel human diagnostic	72 . . . 140	69/69 (100%)	8e−39
	protein #15384 - Homo	959 . . . 1027	69/69 (100%)
	sapiens, 1028 aa.
	[WO200175067-A2,
	Oct. 11, 2001]

[0379] In a BLAST search of public sequence datbases, the NOV3a protein was found to have homology to the proteins shown in the BLASTP data in Table 3E.

TABLE 3E
Public BLASTP Results for NOV3a
		NOV3a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q96DN2	CDNA FLJ32009 fis, clone	1 . . . 592	554/607 (91%)	0.0
	NT2RP7009498, weakly	1 . . . 589	558/607 (91%)
	similar to fibulin-1, isoform A
	precursor - Homo sapiens
	(Human), 955 aa.
Q9DBE2	1300015B04Rik protein - Mus	1 . . . 620	498/628 (79%)	0.0
	musculus (Mouse), 608 aa.	1 . . . 607	530/628 (84%)
Q9NPY3	Complement component C1q	82 . . . 371	103/295 (34%)	2e−32
	receptor precursor	300 . . . 566	132/295 (43%)
	(Complement component 1, q
	subcomponent, receptor 1)
	(C1qRp) (C1qR(p))
	(C1q/MBL/SPA receptor)
	(CD93 antigen) (CDw93) -
	Homo sapiens (Human), 652
	aa.
Q9CXD8	6130401L20Rik protein - Mus	54 . . . 260	78/219 (35%)	2e−29
	musculus (Mouse), 528 aa.	96 . . . 305	99/219 (44%)
Q91V88	POEM (NEPHRONECTIN	45 . . . 368	100/363 (27%)	3e−29
	short isoform) - Mus musculus	35 . . . 383	146/363 (39%)
	(Mouse), 561 aa.

[0380] PFam analysis predicts that the NOV3a protein contains the domains shown in the Table 3F.

TABLE 3F
Domain Analysis of NOV3a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV3a Match Region	Region	Value
EGF	148 . . . 181	16/47 (34%)	0.0045
		23/47 (49%)
EGF	187 . . . 220	12/47 (26%)	0.011
		25/47 (53%)
TIL	168 . . . 226	13/70 (19%)	0.53
		39/70 (56%)
vwc	381 . . . 442	20/84 (24%)	0.00069
		41/84 (49%)
vwc	452 . . . 502	18/84 (21%)	0.00017
		39/84 (46%)
vwc	503 . . . 561	21/84 (25%)	1.6e−05
		39/84 (46%)

Example 4

[0381] The NOV4 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 4A.

TABLE 4A
NOV4 Sequence Analysis
             SEQ ID NO: 17             1161 bp
NOV4a,       GAATTCCGCAGCCATGACCCCGCAGCTTCTCCTGGCCCTTGTCCTCTGGGCCAGCTGCCCGCCCTGCA
CG108901-01
DNA Sequence GTGGAAGGAAAGGGCCCCCAGCAGCTCTGACACTGCCCCGGGTGCAATGCCCAGCCTCTCGGTACCCG
             ATCGCCCTGGATTGCTCCTGGACCCTGCCGCCTGCTCCAAACTCCACCAGCCCCGTGTCCTTCATTGC
             CACGTACAGGCTCGGCATGGCTGCCCGGGGCCACAGCTGGCCCTGCCTGCAGCAGACGCCAACGTCCA
             CCAGCTGCACCATCACGGATGTCCAGCTGTTCTCCATGGCTCCCTACGTGCTCAATGTCACCGCCGTC
             CACCCCTGGGGCTCCAGCAGCAGCTTCGTGCCTTTCATAACAGAGCACATCATCAAGCCCGACCCTCC
             AGAAGGCGTGCGCCTAAGCCCCCTCGCTGAGCGCCAGCTACAGGTGCAGTGGGAGCCTCCCGGGTCCT
             GGCCCTTCCCAGAGATCTTCTCACTGAAGTACTGGATCCGTTACAAGCGTCAGGGAGCTGCGCGCTTC
             CACCGGGTGGGGCCCATTGAAGCCACGTCCTTCATCCTCAGGGCTGTGCGGCCCCGAGCCAGGTACTA
             CGTCCAAGTGGCGGCTCAGGACCTCACAGACTACGGGGAACTGAGTGACTGGAGTCTCCCCGCCACTG
             CCACAATGAGCCTGGGCAAGTAGCAAGGGCTTCCCGCTGCCTCCAGACAGCACCTGGGTCCTCGCCAC
             CCTAAGCCCCGGGACACCTGTTGGAGGGCGGATGGGATCTGCCTAGCCTGGGCTGGAGTCCTTGCTTT
             GCTGCTGCTGAGCTGCCGGGCAACCTCAGATGACCGACTTTTCCCTTTGAGCCTCAGTTTCTCTAGCT
             GAGAAATGGAGATGTACTACTCTCTCCTTTACCTTTACCTTTACCACAGTGCAGGGCTGACTGAACTG
             TCACTGTGAGATATTTTTTATTGTTTAATTAGAAAAGAATTGTTGTTGGGCTGGGCGCAGTGGATCGC
             ACCTGTAATCCCAGTCACTGGGAAGCCGACGTGGGTGGGTAGCTTGAGGCCAGGAGCTCGAAACCAGT
             CCGGGCCACACAGCAAGACCCCATCTCTAAAAAATTAATATAAATATAAAATAAAAAAAAAAAAAAGG
             AATTC
             ORF Start: ATG at 14      ORF Stop: TAG at 701
             SEQ ID NO: 18             229 aa    MW at 25396.0kD
NOV4a,       MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYRL
CG108901-01
Protein      GMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEGVR
Sequence
             LSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYVQVA
             AQDLTDYGELSDWSLPATATMSLGK
             SEQ ID NO: 19             528 bp
NOV4b,       CCATGACCCCGCAGCTTCTCCTGGCCCTTGTCCTCTGGGCCAGCTGCCCGCCCTGCAGTGGAAGGAA
CG108901-04
DNA Sequence AGGGCCCCCAGCAGCTCTGACACTGCCCCGGGTGCAATGCCGAGCCTCTCGGTACCCGATCGCCGTG
             GATTGCTCCTGGACCCTGCCGCCTGCTCCAAACTCCACCAGCCCCGTGCCTTTCATAACAGACCACA
             TCATCAAGCCCGACCCTCCAGAAGGCGTGCGCCTAAGCCCCCTCGCTGAGCGCCAGCTACAGGTGCA
             GTGGGAGCCTCCCGGGTCCTGGCCCTTCCCAGAGATCTTCTCACTGAAGTACTGGATCCGTTACAAG
             CGTCAGGGAGCTGCGCGCTTCCACCGGGTGGGGCCCATTGAAGCCACGTCCTTCATCCTCAGGGCTG
             TGCGGCCCCGAGCCAGGTACTACGTCCAAGTGGCGGCTCAGGACCTCACAGACTACGGGGAACTGAG
             TGACTGGAGTCTCCCCGCCACTGCCACAATGAGCCTGGGCAAGTAGCAAGGGCTTCCCG
             ORF Start: ATG at 3       ORF Stop: TAG at 513
             SEQ ID NO: 20             170 aa    MW at 18991.8kD
NOV4b,       MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVPFITDHI
CG108901-04
Protein      IKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAV
Sequence
             RPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK
             SEQ ID NO: 21             542 bp
NOV4c,       CATGACCCCGCAGCTTCTCCTGGCCCTTGTCCTCTGGGCCAGCTGCCCGCCCTGCAGTGGAAGGAAAG
CG108901-03
DNA Sequence GGCCCTGCCTGCAGCAGACGCCAACGTCCACCAGCTGCACCATCACGGATGTCCAGCTGTTCTCCATG
             GTTCCCTACGTGCTCAATGTCACCGCCGTCCACCCCTGGGGCTCCAGCAGCAGCTTCGTGCCTTTCAT
             AACAGAGCACATCATCAAGCCCGACCCTCCAGAAGGCGTGCGCCTAAGCCCCCTCGCTGAGCGCCAGC
             TACAGGTGCAGTGGGAGCCTCCTGGGTCCTGGCCCTTCCCAGAGATCTTCTCACTGAAGTACTGGATC
             CGTTACAAGCGTCAGGGAGCTGCGCGCTTCCACCGGGTGGGGCCCATTGAAGCCACGTCCTTCATCCT
             CAGGGCTGTGCGGCCCCGAGCCAGGTACTACATCCAAGTGGCGGCTCAGGACCTCACAGACTACGGGG
             AACTGAGTGACTGGAGTCTCCCCGCCACTGCCACAATGAGCCTGGGCAAGTAGCAAGGGCTTCCCG
             ORF Start: ATG at 2       ORF Stop: TAG at 527
             SEQ NO: 22                175 aa    MW at 19616.5kD
NOV4c,       MTPQLLLALVLWASCPPCSGRKGPCLQQTPTSTSCTITDVQLFSMVPYVLNVTAVHPWGSSSSFVPFI
CG108901-03
Protein      TEHIIKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFIL
Sequence
             RAVRPRARYYIQVAAQDLTDYGELSDWSLPATATMSLGK
             SEQ ID NO: 23               943 bp
NOV4d,       CGGGAAGCCCTTGCTACTTGCCCAGGCTCATCGTGGCAGTGGCGGGGAGACTCCAGTCACTCAGTTC
CG108901-02
DNA Sequence CCCGTAGTCTGTGAGGTCCTGAGCCGCCACTTGGATGTAGTACCTGGCTCGGGGCCGCACAGCCCTG
             AGGATGAAGGACGTGGCTTCAATGGGCCCCACCCGGTGGAAGCGCGCAGCTCCCTGACGCTTGTAAC
             GGATCCAGTACTTCAGTGAGAAGATCTCTGGGAAGGGCCATGACCCCGCAGCTTCTCCTGGCCCTTG
             TCCTCTGGGCCAGCTGCCCGCCCTGCAGTGGAAGGAAAGGGCCCCCAGCAGCTCTGACACTGCCCCG
             GGTGCAATGCCGAGCCTCTCGGTACCCGATCGCCGTGGATTGCTCCTGGACCCTGCCGCCTGCTCCA
             AACTCCACCAGCCCCGTGTCCTTCATTGCCACGTACAGGCTCGGCATGGCTGCCCGGGGCCACAGCT
             GGCCCTGCCTGCAGCAGACGCCAACGTCCACCAGCTGCACCATCACGGATGTCCAGCTGTTCTCCAT
             GGCTCCCTACGTGCTCAATGTCACCGCCGTCCACCCCTGGGGCTCCAGCAGCAGCTTCGTGCCTTTC
             ATAACAGAGCACATCATCAAGCCCGACCCTCCAGAAGGCGTGCGCCTAAGCCCCCTCGCTGAGCGCC
             AGCTACAGGTGCAGTGGGAGCCTCCCGGGTCCTGGCCCTTCCCAGAGATCTTCTCACTGAAGTACTG
             GATCCGTTACAAGCGTCAGGGAGCTGCGCGCTTCCACCGGGTGGGGCCCATTGAAGCCACGTCCTTC
             ATCCTCAGGGCTGTGCGGCCCCGAGCCAGGTACTACATCCAAGTGGCGGCTCAGGACCTCACAGACT
             ACGGGGAACTGAGTGACTGGAGTCTCCCCGCCACTGCCACGATGAGCCTGGGCAAGTAGCAAGGGCT
             TCCCG
             ORF Start: ATG at 241     ORF Stop: TAG at 928
             SEQ ID NO: 24             229 aa    MW at 25410.0kD
NOV4d,       MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYR
CG108901-02
Protein      LGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEG
Sequence
             VRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYI
             QVAAQDLTDYGELSDWSLPATATMSLGK

[0382] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 4B.

TABLE 4B
Comparison of NOV4a against NOV4b through NOV4d.
		NOV4a Residues/	Identities/Similarities
	Protein Sequence	Match Residues	for the Matched Region
	NOV4b	1 . . . 229	156/229 (68%)
		1 . . . 170	162/229 (70%)
	NOV4c	1 . . . 229	170/229 (74%)
		1 . . . 175	171/229 (74%)
	NOV4d	1 . . . 229	228/229 (99%)
		1 . . . 229	229/229 (99%)

[0383] Further analysis of the NOV4a protein yielded the following properties shown in Table 4C.

TABLE 4C
Protein Sequence Properties NOV4a
PSort analysis:   0.8650 probability located in lysosome (lumen); 0.3700 probability located in
                  outside; 0.1825 probability located in microbody (peroxisome); 0.1000
                  probability located in endoplasmic reticulum (membrane)
SignalP analysis: Cleavage site between residues 21 and 22

[0384] A search of the NOV4a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 4D.

TABLE 4D
Geneseq Results for NOV4a
		NOV4a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAW09779	Epstein Barr virus-induced	1 . . . 229	229/229 (100%)	e−137
	protein 3 (EBI3) - Homo	1 . . . 229	229/229 (100%)
	sapiens, 229 aa.
	[WO9713859-A1,
	Apr. 17, 1997]
ABB81683	Human clone LO81-19a	1 . . . 229	228/229 (99%)	e−136
	protein #1 - Homo sapiens,	1 . . . 229	229/229 (99%)
	229 aa. [WO200231114-A2,
	Apr. 18, 2002]
AAO14527	Human EBI-3 protein -	1 . . . 229	227/229 (99%)	e−136
	Homo sapiens, 229 aa.	1 . . . 229	228/229 (99%)
	[WO200212282-A2,
	Feb. 14, 2001]
AAB36652	Human cytokine receptor	1 . . . 229	227/229 (99%)	e−136
	subunit Eib3 protein SEQ ID	1 . . . 229	228/229 (99%)
	NO:9 - Homo sapiens, 229
	aa. [WO200073451-A1,
	Dec. 7, 2000]
AAW53624	Epstein Barr virus induced	1 . . . 229	227/229 (99%)	e−136
	gene 3 (EBI-3) - Homo	1 . . . 229	228/229 (99%)
	sapiens, 229 aa.
	U.S. Pat. No. 5,744,301-A]
	Apr. 28,1998]

[0385] In a BLAST search of public sequence datbases, the NOV4a protein was found to have homology to the proteins shown in the BLASTP data in Table 4E.

TABLE 4E
Public BLASTP Results for NOV4a
		NOV4a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q75269	Human cytokine receptor	1 . . . 229	229/229 (100%)	e−136
	(Epstein-Barr virus induced	1 . . . 229	229/229 (100%)
	gene 3) - Homo sapiens
	(Human), 229 aa.
Q14213	Cytokine receptor precursor-	1 . . . 229	227/229 (99%)	e−135
	Homo sapiens (Human), 229	1 . . . 229	228/229 (99%)
	aa.
O35228	Cytokine receptor-like	1 . . . 220	138/220 (62%)	5e−75
	molecule (Epstein-Barr virus	1 . . . 218	166/220 (74%)
	induced gene 3) - Mus
	musculus (Mouse), 228 aa.
CAD29041	Sequence 29 from Patent	1 . . . 67	67/67 (100%)	3e−34
	WO0214358 - Homo sapiens	1 . . . 67	67/67 (100%)
	(Human), 102 aa.
CAD44518	SI:bZ76A6.1 (novel protein	31 . . . 224	65/196 (33%)	5e−24
	similar to vertebrate ciliary	5 . . . 193	99/196 (50%)
	neurotrophic factor receptor
	alpha (CNTFR alpha)) -
	Brachydanio rerio (Zebrafish)
	(Danio rerio), 212 aa
	(fragment).

[0386] PFam analysis predicts that the NOV4a protein contains the domains shown in the Table 4F.

TABLE 4F
Domain Analysis of NOV4a
		Identities/
		Similarities
Pfam Domain	NOV4a Match Region	for the Matched Region	Expect Value
fn3	129 . . . 215	19/89 (21%)	0.0001
		56/89 (63%)

Example 5

[0387] The NOV5 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 5A.

TABLE 5A
NOV5 Sequence Analysis
             SEQ ID NO: 25             3971 bp
NOV5a,       GCTTTCAGGCGATCTGGAGAAAGAACGGCAGAACACACAGCAAGGAAAGGTCCTTTCTGGGGATCACC
CG112505-01
DNA Sequence CCATTGGCTGAAGATGAGACCATTCTTCCTCTTGTGTTTTGCCCTGCCTGGCCTCCTGCATGCCCAAC
             AAGCCTGCTCCCGTGGGGCCTGCTATCCACCTGTTGGGGACCTGCTTGTTGGGAGGACCCGGTTTCTC
             CGAGCTTCATCTACCTGTGGACTGACCAAGCCTGAGACCTACTGCACCCAGTATGGCGAGTGGCAGAT
             GAAATGCTGCAAGTGTGACTCCAGGCAGCCTCACAACTACTACAGTCACCGAGTAGAGAATGTGGCTT
             CATCCTCCGGCCCCATGCGCTGGTGGCAGTCCCAGAATGATGTGAACCCTGTCTCTCTGCAGCTGGAC
             CTGGACAGGAGATTCCAGCTTCAAGAAGTCATGATGGAGTTCCAGGGGCCCATGCCCGCCGGCATGCT
             GATTGAGCGCTCCTCAGACTTCGGTAAGACCTGGCGAGTGTACCAGTACCTGGCTGCCGACTGCACCT
             CCACCTTCCCTCGGGTCCGCCAGGGTCGGCCTCAGAGCTGGCAGGATGTTCGGTGCCAGTCCCTGCCT
             CAGAGGCCTAATGCACGCCTAAATGGGGGGAAGGTCCAACTTAACCTTATGGATTTAGTGTCTGGGAT
             TCCAGCAACTCAAAGTCAAAAAATTCAAGAGGTGGGGGAGATCACAAACTTGAGAGTCAATTTCACCA
             GGCTGGCCCCTGTGCCCCAAAGGGGCTACCACCCTCCCAGCGCCTACTATGCTGTGTCCCAGCTCCGT
             CTGCAGGGGAGCTGCTTCTGTCACGGCCATGCTGATCGCTGCGCACCCAAGCCTGGGGCCTCTGCAGG
             CCCCTCCACCGCTGTGCAGGTCCACGATGTCTGTGTCTGCCAGCACAACACTGCCGGCCCAAATTGTG
             AGCGCTGTGCACCCTTCTACAACAACCGGCCCTGGAGACCGGCGGAGGGCCAGGACGCCCATGAATGC
             CAAAGGTGCGACTGCAATGGGCACTCAGAGACATGTCACTTTGACCCCGCTGTGTTTGCCGCCAGCCA
             GGGGGCATATGGAGGTGTGTGTGACAATTGCCGGGACCACACCGAAGGCAAGAACTGTGAGCGGTGTC
             AGCTGCACTATTTCCGGAACCGGCGCCCGGGAGCTTCCATTCAGGAGACCTGCATCTCCTGCGAGTGT
             GATCCGGATGGGGCAGTGCCAGGGGCTCCCTGTGACCCAGTGACCGGGCAGTGTGTGTGCAAGGAGCA
             TGTGCAGGGAGAGCGCTGTGACCTATGCAAGCCGGGCTTCACTGGACTCACCTACGCCAACCCGCAGG
             GCTGCCACCGCTGTGACTGCAACATCCTGGGGTCCCGGAGGGACATGCCGTGTGACGAGGAGAGTGGG
             CGCTGCCTTTGTCTGCCCAACGTGGTGGGTCCCAAATGTGACCAGTGTGCTCCCTACCACTGGAAGCT
             GGCCAGTGGCCAGGGCTGTGAACCGTGTGCCTGCGACCCGCACAACTCCCCTCAGCCCACAGTGCAAC
             CAGTTCACAGGGCAGTGCCCTGTCGGGAAGGCTTTGGTGGCCTGATGTGCAGCGCTGCAGCCATCCGC
             CAGTGTCCAGACCGGACCTATGGAGACGTGGCCACAGGATGCCGAGCCTGTGACTGTGATTTCCGGGG
             AACAGAGGGCCCGGGCTGCGACAAGGCATCAGGCCGCTGCCTCTGCCGCCCTGGCTTGACCGGGCCCC
             GCTGTGACCAGTGCCAGCGAGGCTACTGCAATCGCTACCCGGTGTGCGTGGCCTGCCACCCTTGCTTC
             CAGACCTATGATGCGGACCTCCGGGAGCAGGCCCTGCGCTTTGGTAGACTCCGCAATGCCACCGCCAG
             CCTGTGGTCAGGGCCTGGGCTGGAGGACCGTGGCCTGGCCTCCCGGATCCTAGATGCAAAGAGTAAGA
             TTGAGCAGATCCGAGCAGTTCTCAGCAGCCCCGCAGTCACAGAGCAGGAGGTGGCTCAGGTGGCCAGT
             GCCATCCTCTCCCTCAGGCGAACTCTCCAGGGCCTGCAGCTGGATCTGCCCCTGGAGGAGGAGACGTT
             GTCCCTTCCGAGAGACCTGGAGAGTCTTGACAGAAGCTTCAATGGTCTCCTTACTATGTATCAGAGGA
             AGAGGGAGCAGTTTGAAAAAATAAGCAGTGCTGATCCTTCAGGAGCCTTCCGGATGCTGAGCACAGCC
             TACGAGCAGTCAGCCCAGGCTGCTCAGCAGGTCTCCGACAGCTCGCGCCTTTTGGACCAGCTCAGGGA
             CAGCCGGAGAGAGGCAGAGAGGCTGGTGCGGCAGGCGGGAGGAGGAGGAGGCACCGGCAGCCCCAAGC
             TTGTGGCCCTGAGGCTGGAGATGTCTTCGTTGCCTGACCTGACACCCACCTTCAACAAGCTCTGTGGC
             AACTCCAGGCAGATGGCTTGCACCCCAATATCATGCCCTGGTGAGCTATGTCCCCAAGACAATGGCAC
             AGCCTGTGGCTCCCGCTGCAGGGGTGTCCTTCCCAGGGCCGGTGGGGCCTTCTTGATGGCGGGGCAGG
             TGGCTGAGCAGCTGCGGGGCTTCAATGCCCAGCTCCAGCGGACCAGGCAGATGATTAGGGCAGCCGAG
             GAATCTGCCTCACAGATTCAATCCAGTGCCCAGCGCTTGGAGACCCAGGTGAGCGCCAGCCGCTCCCA
             GATGGAGGAAGATGTCAGACGCACACGGCTCCTAATCCAGCAGGTCCGGGACTTCCTAACAGACCCCG
             ACACTGATGCAGCCACTATCCAGGAGGTCAGCGAGGCCGTGCTGGCCCTGTGGCTGCCCACAGACTCA
             GCTACTGTTCTGCAGAAGATGAATGAGATCCAGGCCATTGCAGCCAGGCTCCCCAACGTGGACTTGGT
             GCTGTCCCAGACCAAGCAGGACATTGCGCGTGCCCGCCGGTTGCAGGCTGAGGCTGAGGAAGCCAGGA
             GCCGAGCCCATGCAGTGGAGGGCCAGGTGGAAGATGTGGTTGGGAACCTGCGGCAGGGGACAGTGGCA
             CTGCAGGAAGCTCAGGACACCATGCAAGGCACCAGCCGCTCCCTTCGGCTTATCCAGGACAGGGTTGC
             TGAGGTTCAGCAGGTACTGCGGCCAGCAGAAAAGCTGGTGACAAGCATGACCAAGCAGCTGGGTGACT
             TCTGGACACGGATGGAGGAGCTCCGCCACCAAGCCCGGCAGCAGGGGGCAGAGGCAGTCCAGGCCCAG
             CAGCTTGCGGAAGGTGCCAGCGAGCAGGCATTGAGTGCCCAAGAGGGATTTGAGAGAATAAAACAAAA
             GTATGCTGAGTTGAAGGACCGGTTGGGTCAGAGTTCCATGCTGGGTGAGCAGGGTGCCCGGATCCAGA
             GTGTGAAGACAGAGGCAGAGGAGCTGTTTGGGGAGACCATGGAGATGATGGACAGGATGAAAGACATG
             GAGTTGGAGCTGCTGCGGGGCAGCCAGGCCATCATGCTGCGCTCGGCGGACCTGACAGGACTGGAGAA
             GCGTGTGGAGCAGATCCGTGACCACATCAATGGGCGCGTGCTCTACTATGCCACCTGCAAGTGATGCT
             ACAGCTTCCAGCCCGTTGCCCCACTCATCTGCCGCCTTTGCTTTTGGTTGGGGGCAGATTGGGTTGGA
             ATGCTTTCCATCTCCAGGAGACTTTCATGCAGCCTAAAGTACAGCCTGGACCACCCCTGGTGTGTAGC
             TAGTAAGATTACCCTGAGCTGCAGCTGAGCCTGAGCCAATGGGACAGTTACACTTGACAGACAAAGAT
             GGTGGAGATTGGCATGCCATTGAAACTAAGAGCTCTCAAGTCAAGGAAGCTGGGCTGGGCAGTATCCC
             CCGCCTTTAGTTCTCCACTGGGGAGGAATCCTGGACCAAGCACAAAAACTTAACAAAAGTGATGTAAA
             AATGAAAAGCCAAATAAAAATCTTTGG
             ORF Start: ATG at 82      ORF Stop: TGA at 3598
             SEQ ID NO: 26             1172 aa   MW at 129574.1kD
NOV5a,       MRPFFLLCFALPGLLHAQQACSRGACYPPVGDLLVGRTRFLRASSTCGLTKPETYCTQYGEWQMKCCK
CG112505-01
Protein      CDSRQPHNYYSHRVENVASSSGPMRWWQSQNDVNPVSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERS
Sequence
             SDFGKTWRVYQYLAADCTSTFPRVRQGRPQSWQDVRCQSLPQRPNARLNGGKVQLNLMDLVSGIPATQ
             SQKIQEVGEITNLRVNFTRLAPVPQRCYHPPSAYYAVSQLRLQGSCFCHGHADRCAPKPGASAGPSTA
             VQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAECQDAHECQRCDCNGHSETCHFDPAVFAASQGAYG
             GVCDNCRDHTEGKNCERCQLHYFRNRRPGASIQETCISCECDPDGAVPGAPCDPVTGQCVCKEHVQGE
             RCDLCKPGFTGLTYANPQGCHRCDCNILGSRRDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKLASGQ
             GCEPCACDPHNSPQPTVQPVHRAVPCREGFGGLMCSAAAIRQCPDRTYGDVATGCRACDCDFRGTEGP
             GCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACHPCFQTYDADLREQALRFGRLRNATASLWSG
             PGLEDRGLASRILDAKSKIEQIRAVLSSPAVTEQSVAQVASAILSLRRTLQGLQLDLPLEEETLSLPR
             DLESLDRSFNGLLTMYQRKREQFEKISSADPSGAFRMLSTAYEQSAQAAQQVSDSSRLLDQLRDSRRE
             AERLVRQAGGGGGTGSPKLVALRLEMSSLPDLTPTFNKLCGNSRQMACTPISCPGELCPQDNGTACGS
             RCRGVLPRAGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEED
             VRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQT
             KQDIARARRLQAEAEEARSRAHAVECQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQ
             VLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAEL
             KDRLGQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQ
             IRDHINGRVLYYATCK
             SEQ ID NO: 27             3810 bp
NOV5b,       GCTTTCAGGCGATCTGGAGAAAGAACGGCAGAACACACAGCAAGGAAAGGTCCTTTCTGGGGATCAC
CG112505-02
DNA Sequence CCCATTGGCTGAAGATGAGACCATTCTTCCTCTTGTGTTTTGCCCTGCCTGGCCTCCTGCATGCCCA
             ACAAGCCTGCTCCCGTGGGGCCTGCTATCCACCTGTTGGGGACCTGCTTGTTGGGAGGACCCGGTTT
             CTCCGAGCTTCATCTACCTGTGGACTGACCAAGCCTGAGACCTACTGCACCCAGTATGGCGAGTGGC
             AGATGAAATGCTGCAAGTGTGACTCCAGGCAGCCTCACAACTACTACAGTCACCGAGTAGAGAATGT
             GGCTTCATCCTCCGGCCCCATGCGCTGGTGGCAGTCCCAGAATGATGTGAACCCTGTCTCTCTGCAG
             CTGGACCTGGACAGGAGATTCCAGCTTCAAGAAGTCATGATGGAGTTCCAGGGGCCCATGCCCGCCG
             GCATGCTGATTGACCGCTCCTCAGACTTCGGTAAGACCTGGCGAGTGTACCACTACCTCGCTGCCGA
             CTGCACCTCCACCTTCCCTCGGGTCCGCCAGGGTCGGCCTCAGAGCTGGCAGGATGTTCGGTGCCAG
             TCCCTGCCTCACAGGCCTAATGCACGCCTAAATGGGGGGAAGGTCCAACTTAACCTTATGGATTTAG
             TGTCTGGGATTCCAGCAACTCAAAGTCAAAAAATTCAAGAGGTGGGGGAGATCACAAACTTGAGAGT
             CAATTTCACCAGGCTGGCCCCTGTGCCCCAAAGGGGCTACCACCCTCCCAGCGCCTACTATGCTGTG
             TCCCAGCTCCGTCTGCAGGGGAGCTGCTTCTGTCACGGCCATGCTGATCGCTGCGCACCCAAGCCTG
             GGGCCTCTGCAGGCCCCTCCACCGCTGTGCAGGTCCACGATGTCTGTGTCTGCCAGCACAACACTGC
             CGGCCCAAATTGTGAGCGCTGTGCACCCTTCTACAACAACCGGCCCTGGAGACCGGCGGAGGGCCAG
             GACGCCCATGAATGCCAAAGGTGCGACTGCAATGGGCACTCAGAGACATGTCACTTTGACCCCGCTG
             TGTTTGCCGCCAGCCAGGGGGCATATGGAGGTGTGTGTGACAATTGCCGGGACCACACCGAAGGCAA
             GAACTGTGAGCGGTGTCAGCTGCACTATTTCCGGAACCGGCGCCCGGGAGCTTCCATTCAGGAGACC
             TGCATCTCCTGCGAGTGTGATCCGGATGGGGCAGTGCCAGGGGCTCCCTGTGACCCAGTGACCGGGC
             AGTGTGTGTGCAAGGAGCATGTGCAGGGAGAGCGCTGTGACCTATGCAAGCCGGGCTTCACTGGACT
             CACCTACGCCAACCCGCAGGGCTGCCACCGCTGTGACTGCAACATCCTGGGGTCCCGGAGGGACATG
             CCGTGTGACGAGGAGAGTGGGCGCTGCCTTTGTCTGCCCAACGTGGTGGGTCCCAAATGTGACCAGT
             GTGCTCCCTACCACTGGAAGCTGGCCAGTGGCCAGGGCTGTGAACCGTGTGCCTGCGACCCGCACAA
             CTCCCCTCAGCCCACAGTGCAACCAGTTCACAGGGCAGTGCCCTGTCGGGAAGGCTTTGGTGGCCTG
             ATGTGCAGCGCTGCAGCCATCCGCCAGTGTCCAGACCGGACCTATGGAGACGTGGCCACAGGATGCC
             GAGCCTGTGACTGTGATTTCCGGGGAACAGAGGGCCCGGGCTGCGACAAGGCATCAGGCCGCTGCCT
             CTGCCGCCCTGGCTTGACCGGGCCCCGCTGTGACCAGTGCCAGCGAGGCTACTGCAATCGCTACCCG
             GTGTGCGTGGCCTGCCACCCTTGCTTCCAGACCTATGATGCGGACCTCCGGGAGCAGGCCCTGCGCT
             TTGGTAGACTCCGCAATGCCACCGCCAGCCTGTGGTCAGGGCCTGGGCTGGAGGACCGTGGCCTGGC
             CTCCCGGATCCTAGATGCAAAGAGTAAGATTGAGCAGATCCGAGCAGTTCTCAGCAGCCCCGCAGTC
             ACAGAGCAGGAGGTGGCTCAGGTGGCCAGTGCCATCCTCTCCCTCAGGAGCCTTCCGGATGCTGAGC
             ACAGCCTACGAGCAGTCAGCCCAGGCTGCTCAGCAGGTCTCCGACAGCTCGCGCCTTTTGGACCAGC
             TCAGGGACAGCCGGAGAGAGGCAGAGAGGCTGGTGCGGCAGGCGGGAGGAGGAGGAGGCACCGGCAG
             CCCCAAGCTTGTGGCCCTGAGGCTGGAGATGTCTTCGTTGCCTGACCTGACACCCACCTTCAACAAG
             CTCTGTGGCAACTCCAGGCAGATGGCTTGCACCCCAATATCATGCCCTGGTGAGCTATGTCCCCAAG
             ACAATGGCACAGCCTGTGGCTCCCGCTGCAGGGGTGTCCTTCCCAGGGCCGGTGGGGCCTTCTTGAT
             GGCGGGGCAGGTGGCTGAGCAGCTGCGGGGCTTCAATGCCCAGCTCCAGCGGACCAGGCAGATGATT
             AGGGCAGCCGAGGAATCTGCCTCACAGATTCAATCCAGTGCCCAGCGCTTGGAGACCCAGGTGAGCG
             CCAGCCGCTCCCAGATGGAGGAAGATGTCAGACGCACACGGCTCCTAATCCAGCAGGTCCGGGACTT
             CCTAACAGACCCCGACACTGATGCAGCCACTATCCAGGAGGTCAGCGAGGCCGTGCTGGCCCTGTGG
             CTGCCCACAGACTCAGCTACTGTTCTGCAGAAGATGAATGAGATCCAGGCCATTGCAGCCAGGCTCC
             CCAACGTGGACTTGGTGCTGTCCCAGACCAAGCAGGACATTGCGCGTGCCCGCCGGTTGCAGGCTGA
             GGCTGAGGAAGCCAGGAGCCGAGCCCATGCAGTGGAGGGCCAGGTGGAAGATGTGGTTGGGAACCTG
             CGGCAGGGGACAGTGGCACTGCAGGAAGCTCAGGACACCATGCAAGGCACCAGCCGCTCCCTTCGGC
             TTATCCAGGACAGGGTTGCTGAGGTTCAGCAGGTACTGCGGCCAGCAGAAAAGCTGGTGACAAGCAT
             GACCAAGCAGCTGGGTGACTTCTGGACACGGATGGAGGAGCTCCGCCACCAAGCCCGGCAGCAGGGG
             GCAGAGGCAGTCCAGGCCCAGCAGCTTGCGGAAGGTGCCAGCGAGCAGGCATTGAGTGCCCAAGAGG
             GATTTGAGAGAATAAAACAAAAGTATGCTGAGTTGAAGGACCGGTTGGGTCAGAGTTCCATGCTGGG
             TGAGCAGGGTGCCCGGATCCAGAGTGTGAAGACAGAGGCAGAGGAGCTGTTTGGGGAGACCATGGAG
             ATGATGGACAGGATGAAAGACATGGAGTTGGAGCTGCTGCGGGGCAGCCAGGCCATCATGCTGCGCT
             CGGCGGACCTGACAGGACTGGAGAAGCGTGTGGAGCAGATCCGTGACCACATCAATGGGCGCGTGCT
             CTACTATGCCACCTGCAAGTGATGCTACAGCTTCCAGCCCGTTGCCCCACTCATCTGCCGCCTTTGC
             TTTTGGTTGGGGGCAGATTGGGTTGGAATGCTTTCCATCTCCAGGAGACTTTCATGCAGCCTAAAGT
             ACAGCCTGGACCACCCCTGGTGTGTAGCTAGTAAGATTACCCTGAGCTGCAGCTGAGCCTGAGCCAA
             TGGGACAGTTACACTTGACAGACAAAGATGGTGGAGATTGGCATGCCATTGAAACTAAGAGCTCTCA
             AGTCAAGGAAGCTGGGCTGGGCAGTATCCCCCGCCTTTAGTTCTCCACTGGGGAGGAATCCTGGACC
             AAGCACAAAAACTTAACAAAAGTGATGTAAAAATGAAAAGCCAAATAAAAATCTTTGG
             ORF Start: ATG at 82      ORF Stop: TGA at 2254
             SEQ ID NO: 28             724 aa    MW at 79264.7kD
NOV5b,       MRPFFLLCFALPGLLHAQQACSRGACYPPVGDLLVGRTRFLRASSTCGLTKPETYCTQYGEWQMKCC
CG112505-02
Protein      KCDSRQPHNYYSHRVENVASSSGPMRWWQSQNDVNPVSLQLDLDRRFQLQEVMMEFQGPMPAGMLIE
Sequence
             RSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSWQDVRCQSLPQRPNARLNGGKVQLNLMDLVSGIP
             ATQSQKIQEVGEITNLRVNFTRLAPVPQRGYHPPSAYYAVSQLRLQGSCFCHGHADRCAPKPGASAG
             PSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEGQDAHECQRCDCNGHSETCHFDPAVFAAS
             QGAYGGVCDNCRDHTEGKNCERCQLHYFRNRRPGASIQETCISCECDPDGAVPGAPCDPVTGQCVCK
             EHVQGERCDLCKPGFTGLTYANPQGCHRCDCNILGSRRDMPCDEESGRCLCLPNVVGPKCDQCAPYH
             WKLASGQGCEPCACDPHNSPQPTVQPVHRAVPCREGFGGLMCSAAAIRQCPDRTYGDVATGCRACDC
             DFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACHPCFQTYDADLREQALRFGRLR
             NATASLWSGPGLEDRGLASRILDAKSKIEQIRAVLSSPAVTEQEVAQVASAILSLRSLPDAEHSLRA
             VSPGCSAGLRQLAPFGPAQGQPERGREAGAAGGRRRRHRQPQACGPEAGDVFVA

[0388] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 5B.

TABLE 5B
Comparison of NOV5a against NOV5b.
		NOV5a Residues/	Identities/Similarities
	Protein Sequence	Match Residues	for the Matched Region
	NOV5b	1 . . . 659	647/659 (98%)
		1 . . . 659	647/659 (98%)

[0389] Further analysis of the NOV5a protein yielded the following properties shown in Table 5C.

TABLE 5C
Protein Sequence Properties NOV5a
PSort analysis:   0.3700 probability located in outside; 0.1900 probability located in lysosome
                  (lumen); 0.1000 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 18 and 19

[0390] A search of the NOV5a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 5D.

TABLE 5D
Geneseq Results for NOV5a
		NOV5a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAW37870	Human protein comprising	1 . . . 1172	1161/1172 (99%)	0.0
	secretory signal amino acid	1 . . . 1172	1161/1172 (99%)
	sequence 7 - Homo sapiens,
	1172 aa. [WO9811217-A2,
	Mar. 19, 1998]
AAB48466	Human laminin 5	4 . . . 1172	1151/1169 (98%)	0.0
	polypeptide, SEQ ID NO: 22 -	6 . . . 1174	1151/1169 (98%)
	Homo sapiens, 1174 aa.
	[WO200066731-A2,
	Nov. 9, 2000]
AAB48462	Human laminin 5	1 . . . 1172	1152/1172 (98%)	0.0
	polypeptide, SEQ ID NO: 14 -	1 . . . 1170	1155/1172 (98%)
	Homo sapiens, 1170 aa.
	[WO200066731-A2,
	Nov. 9, 2000]
AAB48464	Human laminin 5	4 . . . 1172	1152/1181 (97%)	0.0
	polypeptide, SEQ ID NO: 18 -	6 . . . 1186	1152/1181 (97%)
	Homo sapiens, 1186 aa.
	[WO200066731-A2,
	Nov. 9, 2000]
AAB48465	Human laminin 5	17 . . . 1172	1145/1156 (99%)	0.0
	polypeptide, SEQ ID NO: 20 -	12 . . . 1167	1145/1156 (99%)
	Homo sapiens, 1167 aa.
	[WO200066731-A2,
	Nov. 9, 2000]

[0391] In a BLAST search of public sequence datbases, the NOV5a protein was found to have homology to the proteins shown in the BLASTP data in Table 5E.

TABLE 5E
Public BLASTP Results for NOV5a
		NOV5a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q13751	Laminin beta-3 chain	1 . . . 1172	1161/1172 (99%)	0.0
	precursor (Laminin 5 beta 3)	1 . . . 1172	1161/1172 (99%)
	(Laminin B1k chain)
	(Kalinin B1 chain) - Homo
	sapiens (Human), 1172 aa.
CAC17363	Sequence 21 from Patent	4 . . . 1172	1151/1169 (98%)	0.0
	WO0066731 precursor -	6 . . . 1174	1151/1169 (98%)
	Homo sapiens (Human),
	1174 aa.
CAC17359	Sequence 13 from Patent	1 . . . 1172	1152/1172 (98%)	0.0
	WO0066731 precursor -	1 . . . 1170	1155/1172 (98%)
	Homo sapiens (Human),
	1170 aa.
CAC17361	Sequence 17 from Patent	4 . . . 1172	1152/1181 (97%)	0.0
	WO0066731 precursor -	6 . . . 1186	1152/1181 (97%)
	Homo sapiens (Human),
	1186 aa.
CAC17362	Sequence 19 from Patent	17 . . . 1172	1145/1156 (99%)	0.0
	WO0066731 - Homo sapiens	12 . . . 1167	1145/1156 (99%)
	(Human), 1167 aa
	(fragment).

[0392] PFam analysis predicts that the NOV5a protein contains the domains shown in the Table 5F.

TABLE 5F
Domain Analysis of NOV5a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV5a Match Region	Region	Value
laminin_Nterm	26 . . . 248	88/273 (32%)	1.6e−38
		150/273 (55%)
laminin_EGF	250 . . . 313	17/70 (24%)	4e−08
		50/70 (71%)
laminin_EGF	316 . . . 376	19/65 (29%)	1.7e−13
		50/65 (77%)
laminin_EGF	379 . . . 428	26/59 (44%)	9.4e−18
		43/59 (73%)
laminin_EGF	431 . . . 478	27/59 (46%)	3.9e−17
		39/59 (66%)
laminin_EGF	481 . . . 531	14/64 (22%)	0.79
		34/64 (53%)
laminin_EGF	534 . . . 578	20/59 (34%)	3.1e−10
		34/59 (58%)

Example 6

[0393] The NOV6 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 6A.

TABLE 6A
NOV6 Sequence Analysis
             SEQ ID NO: 29             2659 bp
NOV6a,       ACCCACGGGGCTGCCCTCCCCTGCGCACTCCCCTCGCTGCCCGGGCCCGGAGCGCAGTGGGGCCGCAC
CG121965-01
DNA Sequence AGATTCACAATGTTGAAAGCCCTTTTCCTAACTATGCTGACTCTGGCGCTGGTCAAGTCACAGGACAC
             CGAAGAAACCATCACGTACACGCAATGCACTGACGGATATGAGTGGGATCCTGTGAGACAGCAATGCA
             AAGATATTGATGAATGTGACATTGTCCCAGACGCTTGTAAAGGTGGAATGAAGTGTGTCAACCACTAT
             GGAGGATACCTCTGCCTTCCGAAAACAGCCCAGATTATTGTCAATAATGAACAGCCTCAGCAGGAAAC
             ACAACCAGCAGAAGGAACCTCAGGGGCAACCACCGGGGTTGTAGCTGCCAGCAGCATGGCAACCAGTG
             GAGTGTTGCCCGGGGGTGGTTTTGTGGCCAGTGCTGCTGCAGTCGCAGGCCCTGAAATGCAGACTGGC
             CGAAATAACTTTGTCATCCGGCGGAACCCAGCTGACCCTCAGCGCATTCCCTCCAACCCTTCCCACCG
             TATCCAGTGTGCAGCAGGCTACGAGCAAAGTGAACACAACGTGTGCCAAGACATAGACGAGTGCACTG
             CAGGGACGCACAACTGTAGAGCAGACCAAGTGTGCATCAATTTACGGGGATCCTTTGCATGTCAGTGC
             CCTCCTGGATATCAGAAGCGAGGGGAGCAGTGCGTAGACATAGATGAATGTACCATCCCTCCATATTG
             CCAGCAAAGATGCGTGAATACACCAGGCTCATTTTATTGCCAGTGCAGTCCTGGGTTTCAATTGGCAG
             CAAACAACTATACCTGCGTAGATATAAATGAATGTGATGCCAGCAATCAATGTGCTCAGCAGTGCTAC
             AACATTCTTGGTTCATTCATCTGTCAGTGCAATCAAGGATATGAGCTAAGCAGTGACAGGCTCAACTG
             TGAAGACATTGATGAATGCAGAACCTCAAGCTACCTGTGTCAATATCAATGTGTCAATGAACCTGGGA
             AATTCTGATGTATGTGCCCCCAGGGATACCAAGTGGTGAGAAGTAGAACATGTCAAGATATAAATGAG
             TGTGAGACCACAAATGAATGCCGGGAGGATGAAATGTGTTGGAATTATCATGGCGGCTTCCGTTGTTA
             TCCACGAAATCCTTGTCAAGATCCCTACATTCTAACACCAGAGAACCGATGTGTTTGCCCAGTCTCAA
             ATGCCATGTGCCGAGAACTGCCCCAGTCAATAGTCTACAAATACATGAGCATCCGATCTGATAGGTCT
             GTGCCATCAGACATCTTCCAGATACAGGCCACAACTATTTATGCCAACACCATCAATACTTTTCGGAT
             TAAATCTGGAAATGAAAATGGAGAGTTCTACCTACGACAAACAAGTCCTGTAAGTGCAATGCTTGTGC
             TCGTGAAGTCATTATCAGGACCAAGAGAACATATCGTGGACCTGGAGATGCTGACAGTCAGCAGTATA
             GGGACCTTCCGCACAAGCTCTGTGTTAAGATTGACAATAATAGTGGGGCCATTTTCATTTTAGTCTTT
             TCTAAGAGTCAACCACAGGCATTTAAGTCAGCCAAAGAATATTGTTACCTTAAAGCACTATTTTATTT
             ATAGATATATCTAGTGCATCTACATCTCTATACTGTACACTCACCCATAATTCAAACAATTACACCAT
             GGTATAAAGTGGGCATTTAATATGTAAAGATTCAAAGTTTGTCTTTATTACTATATGTAAATTAGACA
             TTAATCCACTAAACTGGTCTTCTTCAAGAGAGCTAAGTATACACTATCTGGTGAAACTTGGATTCTTT
             CCTATAAAAGTGGGACCAAGCAATGATGATCTTCTGTGGTGCTTAAGGAAACTTACTAGAGCTCCACT
             AACAGTCTCATAAGGAGGCAGCCATCATAACCATTGAATAGCATGCAAGGGTAAGAATGAGTTTTTAA
             CTGCTTTGTAAGAAAATGGAAAAGGTCAATAAAGATATATTTCTTTAGAAAATGGGGATCTGCCATAT
             TTGTGTTGGTTTTTATTTTCATATCCAGCCTAAAGGTGGTTGTTTATTATATAGTAATAAATCATTGC
             TGTACAATATGCTGGTTTCTGTAGGGTATTTTTAATTTTGTCAGAAATTTTAGATTGTGAATATTTTG
             TAAAAAACAGTAAGCAAAATTTTCCAGAATTCCCAAAATGAACCAGATATCCCCTAGAAAATTATACT
             ATTGAGAAATCTATGGGGAGGATATGAGAAAATAAATTCCTTCTAAACCACATTGGAACTGACCTGAA
             GAAGCAAACTCGGAAAATATAATAACATCCCTGAATTCAGGACTTCCACAAGATGCAGAACAAAATGG
             ATAAAAGGTATTTCACTGGAGAAGTTTTAATTTCTAAGTAAAATTTAAATCCTAACACTTCACTAATT
             TATAACTAAAATTTCTCATCTTCGTACTTGATGCTCACAGAGGAAGAAAATGATGATGGTTTTTATTC
             CTGGCATCCAGAGTGACAGTGAACTTAAGCAAATTACCCTCCTACCCAATTCTATGGAATATTTTATA
             CGTCTCCTTGTTTAAAATGTCACTGCTTTACTTTGATGTATCATATTTTTAAATAAAAATAAATATTC
             CTTTAGA
             ORF Start: ATG at 78      ORF Stop: TAG at 1557
             SEQ ID NO: 30             493 aa    MW at 54640.0kD
NOV6a,       MLKALFLTMLTLALVKSQDTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGY
CG121965-01
Protein      LCLPKTAQIIVNNEQPQQETQPAEGTSGATTGVVAASSMATSGVLPGGGFVASAAAVAGPEMQTGRNN
Sequence
             FVIRRNPADPQRIPSNPSHRTQCAAGYEQSEHNVCQDIDECTAGTHNCRADQVCINLRGSFACQCPPG
             YQKRGEQCVDIDECTIPPYCHQRCVNTPGSFYCQCSPGFQLAANNYTCVDINECDASNQCAQQCYNIL
             GSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECET
             TNECREDEMCWNYHGGFRCYPRNPCQDPYILTPENRCVCPVSNAMCRELPQSIVYKYMSIRSDRSVPS
             DIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLSGPREHIVDLEMLTVSSIGTF
             RTSSVLRLTIIVGPFSF
             SEQ ID NO: 31             2625 bp
NOV6b,       CTAGTATTCTACTAGAACTGGAAGATTGCTCTCCGAGTTTTGTTTTGTTATTTTGTTTAAAAAATAA
CG121965-02
DNA Sequence AAAGCTTGAGGCCAAGGCAATTCATATTGGCTCACAGGTATTTTTGCTGTGCTGTGCAAGGAACTCT
             GCTAGCTCAAGATTCACAATGTTGAAAGCCCTTTTCCTAACTATGCTGACTCTGGCGCTGGTCAAGT
             CACAGGACACCGAAGAAACCATCACGTACACGCAATGCACTGACGGATATGAGTGGGATCCTGTGAG
             ACAGCAATGCAAAGATATTGATGAATGTGACATTGTCCCAGACGCTTGTAAAGGTGGAATGAAGTGT
             GTCAACCACTATGGAGGATACCTCTGCCTTCCGAAAACAGCCCAGATTATTGTCAATAATGAACAGC
             CTCAGCAGGAAACACAACCAGCAGAAGGAACCTCAGGAGCAACCACCGGGGTTGTAGCTGCCAGCAG
             CATGGCAACCAGTGGAGTGTTGCCCGGGGGTGGTTTTGTGGCCAGTGCTGCTGCAGTCGCAGGCCCT
             GAAATGCAGACTGGCCGAAATAACTTTGTCATCCGGCGGAACCCAGCTGACCCTCAGCGCATTCCCT
             CCAACCCTTCCCACCGTATCCAGTGTGCAGCAGGCTACGAGCAAAGTGAACACAACGTGTGCCAAGA
             CATAGACGAGTGCACTGCAGGGACGCACAACTGTAGAGCAGACCAAGTGTGCATCAATTTACGGGGA
             TCCTTTGCATGTCAGTGCCCTCCTGGATATCAGAAGCGAGGGGAGCAGTGCGTAGATATAAATGAAT
             GTGATGCCAGCAATCAATGTGCTCAGCAGTGCTACAACATTCTTGGTTCATTCATCTGTCAGTGCAA
             TCAAGGATATGAGCTAAGCAGTGACAGGCTCAACTGTGAAGACATTGATGAATGCAGAACCTCAAGC
             TACCTGTGTCAATATCAATGTGTCAATGAACCTGGGAAATTCTCATGTATGTGCCCCCAGGGATACC
             AAGTGGTGAGAAGTAGAACATGTCAAGATATAAATGAGTGTGAGACCACAAATGAATGCCGGGAGGA
             TGAAATGTGTTGGAATTATCATGGCGGCTTCCGTTGTTATCCACGAAATCCTTGTCAAGATCCCTAC
             ATTCTAACACCAGAGAACCGATGTGTTTGCCCAGTCTCAAATGCCATGTGCCGAGAACTGCCCCAGT
             CAATAGTCTACAAATACATGAGCATCCGATCTGATAGGTCTGTGCCATCAGACATCTTCCAGATACA
             GGCCACAACTATTTATGCCAACACCATCAATACTTTTCGGATTAAATCTGGAAATGAAAATGGAGAG
             TTCTACCTACGACAAACAAGTCCTGTAAGTGCAATGCTTGTGCTCGTGAAGTCATTATCAGGACCAA
             GAGAACATATCGTGGACCTGGAGATGCTGACAGTCAGCAGTATAGGGACCTTCCGCACAAGCTCTGT
             GTTAAGATTGACAATAATAGTGGGGCCATTTTCATTTTAGTCTTTTCTAAGAGTCAACCACAGGCAT
             TTAAGTCAGCCAAAGAATATTGTTACCTTAAAGCACTATTTTATTTATAGATATATCTAGTGCATCT
             ACATCTCTATACTGTACACTCACCCATAACAAACAATTACACCATGGTATAAAGTGGGCATTTAATA
             TGTAAAGATTCAAAGTTTGTCTTTATTACTATATGTAAATTAGACATTAATCCACTAAACTGGTCTT
             CTTCAAGAGAGCTAAGTATACACTATCTGGTGAAACTTGGATTCTTTCCTATAAAAGTGGGACCAAG
             CAATGATGATCTTCTGTGGTGCTTAAGGAAACTTACTAGAGCTCCACTAACAGTCTCATAAGGAGGC
             AGCCATCATAACCATTGAATAGCATGCAAGGGTAAGAATGAGTTTTTAACTGCTTTGTAAGAAAATG
             GAAAAGGTCAATAAAGATATATTTCTTTAGAAAATGGGGATCTGCCATATTTGTGTTGGTTTTTATT
             TTCATATCCAGCCTAAAGGTGGTTGTTTATTATATAGTAATAAATCATTGCTGTACAACATGCTGGT
             TTCTGTAGGGTATTTTTAATTTTGTCAGAAATTTTAGATTGTGAATATTTTGTAAAAAACAGTAAGC
             AAAATTTTCCAGAATTCCCAAAATGAACCAGATACCCCCTAGAAAATTATACTATTGAGAAATCTAT
             GGGGAGGATATGAGAAAATAAATTCCTTCTAAACCACATTGGAACTGACCTGAAGAAGCAAACTCGG
             AAAATATAATAACATCCCTGAATTCAGGCATTCACAAGATGCAGAACAAAATGGATAAAAGGTATTT
             CACTGGAGAAGTTTTAATTTCTAAGTAAAATTTAAATCCTAACACTTCACTAATTTATAACTAAAAT
             TTCTCATCTTCGTACTTGATGCTCACAGAGGAAGAAAATGATGATGGTTTTTATTCCTGCCATCCAG
             AGTGACAGTGAACTTAAGCAAATTACCCTCCTACCCAATTCTATGGAATATTTTATACGTCTCCTTG
             TTTAAAATCTGACTGCTTTACTTTGATGTATCATATTTTTAAATAAAAATAAATATTCCTTTAGAAG
             ATCACTCTAAAA
             ORF Start: ATG at 153     ORF Stop: TAG at 1512
             SEQ ID NO: 32             453 aa    MW at 50198.0kD
NOV6b,       MLKALFLTMLTLALVKSQDTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGG
CG121965-02
Protein      YLCLPKTAQIIVNNEQPQQETQPAEGTSGATTGVVAASSMATSGVLPGGGFVASAAAVAGPEMQTGR
Sequence
             NNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTAGTHNCRADQVCINLRGSFACQC
             PPGYQKRGEQCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQ
             CVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPRNPCQDPYILTPEN
             RCVCPVSNAMCRELPQSIVYKYMSIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQT
             SPVSAMLVLVKSLSGPREHIVDLEMLTVSSIGTFRTSSVLRLTIIVGPFSF

[0394] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 6B.

TABLE 6B
Comparison of NOV6a against NOV6b.
		NOV6a Residues/	Identities/Similarities
	Protein Sequence	Match Residues	for the Matched Region
	NOV6b	1 . . . 493	440/493 (89%)
		1 . . . 453	440/493 (89%)

[0395] Further analysis of the NOV6a protein yielded the following properties shown in Table 6C.

TABLE 6C
Protein Sequence Properties NOV6a
PSort analysis:   0.3700 probability located in outside; 0.1900 probability located in lysosome
                  (lumen); 0.1000 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 18 and 19

[0396] A search of the NOV6a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 6D.

TABLE 6D
Geneseq Results for NOV6a
		NOV6a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAB48077	Human extracellular	1 . . . 493	493/493 (100%)	0.0
	signaling molecule (EXCS)	1 . . . 493	493/493 (100%)
	(ID 1359783CD1) - Homo
	sapiens, 493 aa.
	[WO200070049-A2,
	Nov. 23, 2000]
AAB72892	Human EFEMP1 - Homo	1 . . . 493	493/493 (100%)	0.0
	sapiens, 493 aa.	1 . . . 493	493/493 (100%)
	[WO200112823-A2,
	Feb. 22, 2001]
AAG68188	Extracellular protein SEQ ID	107 . . . 493	387/387 (100%)	0.0
	NO: 104 - Homo sapiens, 387	1 . . . 387	387/387 (100%)
	aa. [WO200177327-A1,
	Oct. 18, 2001]
AAY08066	Human EGF-like protein	144 . . . 493	350/350 (100%)	0.0
	S1-5 fragment #1 encoded by	1 . . . 350	350/350 (100%)
	GEN12205 cDNA - Homo
	sapiens, 350 aa.
	[WO9914241-A2,
	Mar. 25, 1999]
AAY08490	Human EGF-like protein	3 . . . 346	344/348 (98%)	0.0
	S1-5 fragment #2 encoded by	1 . . . 348	344/348 (98%)
	GEN12205 cDNA - Homo
	sapiens, 348 aa.
	[WO9914241-A2,
	Mar. 25, 1999]

[0397] In a BLAST search of public sequence datbases, the NOV6a protein was found to have homology to the proteins shown in the BLASTP data in Table 6E.

TABLE 6E
Public BLASTP Results for NOV6a
		NOV6a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q12805	EGF-containing fibulin-like	1 . . . 493	493/493 (100%)	0.0
	extracellular matrix protein 1	1 . . . 493	493/493 (100%)
	precursor (Fibulin-3)
	(FIBL-3) (Fibrillin-like
	protein) (Extracellular
	protein S1-5) - Homo sapiens
	(Human), 493 aa.
O35568	EGF-containing fibulin-like	1 . . . 493	459/493 (93%)	0.0
	extracellular matrix protein 1	1 . . . 493	476/493 (96%)
	precursor (Fibulin-3)
	(FIBL-3) (T16 protein) -
	Rattus norvegicus (Rat), 493
	aa.
I38449	extracellular protein - human,	107 . . . 493	387/387 (100%)	0.0
	387 aa.	1 . . . 387	387/387 (100%)
AAH31184	Hypothetical protein - Mus	107 . . . 493	371/387 (95%)	0.0
	musculus (Mouse), 387 aa.	1 . . . 387	379/387 (97%)
Q9JM06	EGF-containing fibulin-like	9 . . . 493	245/486 (50%)	e−148
	extracellular matrix protein 2 -	19 . . . 443	311/486 (63%)
	Mus musculus (Mouse),
	443 aa.

[0398] PFam analysis predicts that the NOV6a protein contains the domains shown in the Table 6F.

TABLE 6F
Domain Analysis of NOV6a
		Identities/
		Similarities
Pfam Domain	NOV6a Match Region	for the Matched Region	Expect Value
EGF	177 . . . 212	12/47 (26%)	0.0002
		29/47 (62%)
EGF	218 . . . 252	14/47 (30%)	0.0014
		30/47 (64%)
TIL	201 . . . 258	16/74 (22%)	0.78
		34/74 (46%)
EGF	258 . . . 292	13/47 (28%)	0.015
		23/47 (49%)

Example 7

[0399] The NOV7 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 7A.

TABLE 7A
NOV7 Sequence Analysis
             SEQ ID NO: 33             1503 bp
NOV7a,       GGACGCTGGATTAGAAGGCAGCAAAAAAAGATCTGTGCTGGCTGGAGCCCCCTCAGTGTGCAGGCTTA
CG126129-01
DNA Sequence GAGGGACTAGGCTGGGTGTGGAGCTGCAGCGTATCCACAGGCCCCAGGATGCAGGCCCTGGTGCTACT
             CCTCTGCATTGGAGCCCTCCTCGGGCACAGCAGCTGGCAGAACCCTGCCAGCCCCCCGGAGGAGGGCT
             CCCCAGACCCCGACAGCACAGGGGCGCTGGTGGAGGAGGAGGATCCTTTCTTCAAAGTCGCCGTGAAC
             AAGCTGGCAGCGGCTGTCTCCAACTTCGGCTATGACCTGTACCGGGTGCGATCCAGCATGAGCCCCAC
             GACCAACGTGCTCCTGTCTCCTCTCAGTGTGGCCACGGCCCTCTCGGCCCTCTCGCTGGGAGCGGACG
             AGCGAACAGAATCCATCATTCACCGGGCTCTCTACTATGACTTGATCAGCAGCCCAGACATCCATGGT
             ACCTATAAGGAGCTCCTTGACACGGTCACTGCCCCCCAGAAGAACCTCAAGAGTGCCTCCCGGATCGT
             CTTTGAGAAGAAGCTGCGCATAAAATCCAGCTTTGTGGCACCTCTGGAAAAGTCATATGGGACCAGGC
             CCAGAGTCCTGACGGGCAACCCTCGCTTGGACCTGCAAGAGATCAACAACTGGGTGCAGGCGCAGATG
             AAAGGGAAGCTCGCCAGGTCCACAAAGGAAATTCCCGATGAGATCAGCATTCTCCTTCTCGGTGTGGC
             GCACTTCAAGGGGCAGTGGGTAACAAAGTTTGACTCCAGAAAGACTTCCCTCGAGGATTTCTACTTGG
             ATGAAGAGAGGACCGTGAGGGTCCCCATGATGTCGGACCCTAAGGCTGTTTTACGCTATGGCTTGGAT
             TCAGATCTCAGCTGCAAGATTGCCCAGCTGCCCTTGACCGGAAGCATGAGTATCATCTTCTTCCTGCC
             CCTGAAAGTGACCCAGAATTTGACCTTGATAGAGGAGAGCCTCACCTCCGAGTTCATTCATGACATAG
             ACCGAGAACTGAAGACCGTGCAGGCGGTCCTCACTGTCCCCAAGCTGAAGCTGAGTTACGAAGGCGAA
             GTCACCAAGTCCCTGCAGGAGATGAAGCTGCAATCCTTGTTTGATTCACCAGACTTTAGCAAGATCAC
             AGGCAAACCCATCAAGCTGACTCAGGTGGAACACCGGGCTGGCTTTGAGTGGAACGAGGATGGGGCGG
             GAACCACCCCCAGCCCAGGGCTGCAGCCTGCCCACCTCACCTTCCCGCTGGACTATCACCTTAACCAG
             CCTTTCATCTTCGTACTGAGGGACACAGACACAGGGGCCCTTCTCTTCATTGGCAAGATTCTGGACCC
             CAGGGGCCCCTAATATCCCAGTTTAATATTCCAATACCCTAGAAGAAAACCCGAGGGACAGCAGATTC
             CACAGGACACGAAGGCTGCCCCTGTAAGGTTTCAATGCATACAATAAAAGAGCTTTATCCCTAAAAAA
             AAAAAAA
             ORF Start: ATG at 117     ORF Stop: TAA at 1371
             SEQ ID NO: 34             418 aa    MW at 46385.6kD
NOV7a,       MQALVLLLCIGALLGHSSWQNPASPPEEGSPDPDSTGALVEEEDPFFKVAVNKLAAAVSNFGYDLYRV
CG125129-01
Protein      RSSMSPTTNVLLSPLSVATALSALSLGADERTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNL
Sequence
             KSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDDQEINNWVQAQMKGKLARSTKEIPDEIS
             ILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSM
             SIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDS
             PDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLF
             IGKILDPRGP
             SEQ ID NO: 35             368 bp
NOV7b,       CTTAGAGGGACTAGGCTGGGTGTGGAGCTGCAGCGTATCCACAGGCCCCAGGATGCAGGCCCTGGTG
CG126129-02
DNA Sequence CTACTCCTCTGCATTGGAGCCCTCCTCGGGCACAGCAGCTGCCAGAACCCTGCCAGCCCCCCGGAGG
             AGGGCTCCCCAGACCCCGACAGCACAGGGGCGCTGGTGGAGGAGGAGGATCCTTTCTTCAAAGTCCC
             CGTGAACAAGCTGGCAGCGGCTGTCTCCAACTTCGGCTATGACCTGTACCGGGTGCGATCCAGCGAA
             CAGAATCCATCATTCACCGGGCTCTCTACTATGACTTGATCAGCAGCCCAGACATCCATGGTACCTA
             TAAGGAGCTCCTTGACACGGTCACTGCCCCCCA
             ORF Start: ATG at 53      ORF Stop: TGA at 305
             SEQ ID NO: 36             84 aa     MW at 8914.9kD
NOV7b,       MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYR
CG126129-02
Protein      VRSSEQNPSFTGLSTMT
Sequence

[0400] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 7B.

TABLE 7B
Comparison of NOV7a against NOV7b.
		NOV7a Residues/	Identities/Similarities
	Protein Sequence	Match Residues	for the Matched Region
	NOV7b	16 . . . 71	40/56 (71%)
		16 . . . 71	40/56 (71%)

[0401] Further analysis of the NOV7a protein yielded the following properties shown in Table 7C.

TABLE 7C
Protein Sequence Properties NOV7a
PSort analysis:   0.4600 probability located in plasma membrane; 0.1443 probability located in
                  microbody (peroxisome); 0.1000 probability located in endoplasmic reticulum
                  (membrane); 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 16 and 17

[0402] A search of the NOV7a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 7D.

TABLE 7D
Geneseq Results for NOV7a
		NOV7a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAR44800	Sequence of retinal	1 . . . 418	418/418 (100%)	0.0
	pigmented	1 . . . 418	418/418 (100%)
	epithelium-derived
	neurotrophic factor (PEDNF) -
	Homo sapiens, 418 aa.
	[WO9324529-A,
	Dec. 9, 1993]
AAE10306	Human pigment epithelium	1 . . . 418	416/418 (99%)	0.0
	derived growth factor (PEDF) -	1 . . . 418	416/418 (99%)
	Homo sapiens, 418 aa.
	[WO200162725-A2,
	Aug. 30, 2001]
AAR90287	Pigment epithelium-derived	1 . . . 418	416/418 (99%)	0.0
	factor - Homo sapiens, 418	1 . . . 418	416/418 (99%)
	aa. [WO9533480-A1,
	Dec. 14, 1995]
AAR90288	Modified pigment	44 . . . 418	371/375 (98%)	0.0
	epithelium-derived factor	5 . . . 379	374/375 (98%)
	(rPEDF) - Homo sapiens, 379
	aa. [WO9533480-A1,
	Dec. 14, 1995]
ABB57391	Rat mucocardial cell	1 . . . 415	343/416 (82%)	0.0
	proliferation associated	1 . . . 415	382/416 (91%)
	polypeptide SEQ ID NO 36 -
	Rattus norvegius, 418 aa.
	[WO200183705-A1,
	Nov. 8, 2001]

[0403] In a BLAST search of public sequence datbases, the NOV7a protein was found to have homology to the proteins shown in the BLASTP data in Table 7E.

TABLE 7E
Public BLASTP Results for NOV7a
		NOV7a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
A47281	pigment	1 . . . 418	416/418 (99%)	0.0
	epithelial-differentiating factor	1 . . . 418	416/418 (99%)
	precursor - human, 418 aa.
P36955	Pigment epithelium-derived	1 . . . 418	414/418 (99%)	0.0
	factor precursor (PEDF)	1 . . . 418	416/418 (99%)
	(EPC-1) - Homo sapiens
	(Human), 418 aa.
Q96CT1	Hypothetical 46.4 kDa protein -	1 . . . 418	413/418 (98%)	0.0
	Homo sapiens (Human), 418	1 . . . 418	415/418 (98%)
	aa.
O70629	Pigment epithelium-derived	1 . . . 415	357/415 (86%)	0.0
	factor (Serine (Or cysteine)	1 . . . 414	391/415 (94%)
	proteinase inhibitor, clade F
	(Alpha-2 antiplasmin, pigment
	epithelium derived factor).
	member 1) - Mus musculus
	(Mouse), 417 aa.
P97298	Pigment epithelium-derived	1 . . . 415	357/415 (86%)	0.0
	factor precursor (PEDF)	1 . . . 414	391/415 (94%)
	(Stromal cell- derived factor 3)
	(SDF-3) - Mus musculus
	(Mouse), 417 aa.

[0404] PFam analysis predicts that the NOV7a protein contains the domains shown in the Table 7F.

TABLE 7F
Domain Analysis of NOV7a
		Identities/
		Similarities
Pfam Domain	NOV7a Match Region	for the Matched Region	Expect Value
serpin	51 . . . 415	112/391 (29%)	4.8e−83
		262/391 (67%)

Example 8

[0405] The NOV8 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 8A.

TABLE 8A
NOV8 Sequence Analysis
             SEQ ID NO: 37             1154 bp
NOV8a,       ATGGGGCGGCTGGTTCTGCTGTGGGGAGCTGCGGTCTTTCTGCTGGGAGGCTGGATGGCTTTGGGGCA
CG142202-01
DNA Sequence AGGAGGAGCAGCAGAAGGAGTACAGATTCAGATCATCTACTTCAATTTAGAAACCGTGCAGGTGACAT
             GGAATGCCAGCAAATACTCCAGGACCAACCTGACTTTCCACTACAGATTCAACGGTGATGAGGCCTAT
             GACCAGTGCACCAACTACCTTCTCCAGGAAGGTCACACTTCGGGGTGCCTCCTAGACGCAGAGCAGCG
             AGACGACATTCTCTATTTCTCCATCAGGAATGGGACGCACCCCGTTTTCACCGCAAGTCGCTGGATGG
             TTTATTACCTGAAACCCAGTTCCCCGAAGCACGTGAGATTTTCGTGGCATCAGGATGCAGTGACGGTG
             ACGTGTTCTGACCTGTCCTACGGGGATCTCCTCTATGAGGTTCAGTACCGGAGCCCCTTCGACACCGA
             GTGGCAGTCCAAACAGGAAAATACCTGCAACGTCACCATAGAAGGCTTGGATGCCGAGAAGTGTTACT
             CTTTCTGGGTCAGGGTGAAGGCTATGGAGGATGTATATGGGCCAGACACATACCCAAGCGACTGGTCA
             GAGGTGACATGCTGGCAGAGAGGCGAGATTCGGGATGCCTGTGCAGAGACACCAACGCCTCCCAAACC
             AAAGCTGTCCAAATTTATTTTAATTTCCAGCCTGGCCATCCTTCTGATGGTGTCTCTCCTCCTTCTGT
             CTTTATGGAAATTATGGAGAGTGAGGAAGTTTCTCATTCCCAGCGTGCCAGACCCGAAATCCATCTTC
             CCCGGGCTCTTTGAGATACACCAAGGGAACTTCCAGGAGTGGATCACAGACACCCAGAACGTGGCCCA
             CCTCCACAAGATGGCAGGTGCAGAGCAAGAAAGTGGCCCCGAGGAGCCCCTGGTAGTCCAGTTGGCCA
             AGACTGAAGCCGAGTCTCCCAGGATGCTGGACCCACAGACCGAGGAGAAAGAGGCCTCTGGGGGATCC
             CTCCAGCTTCCCCACCAGCCCCTCCAAGGTGGTGATGTGGTCACAATCGGGGGCTTCACCTTTGTGAT
             GAATGACCGCTCCTACGTGGCGTTGTGATGGACACACCACTGTCAAAGTCAACGTCAGAAGGGCGA
             ORF Start: ATG at 1       ORE Stop: TGA at 1114
             SEQ ID NO: 38             371 aa    MW at 42040.3kD
NOV8a,       MGRLVLLWGAAVFLLGGWMALGQGGAAEGVQIQIIYFNLETVQVTWNASKYSRTNLTFHYRFNGDEAY
CG142202-01
Protein      DQCTNYLLQEGHTSGCLLDAEQRDDILYFSIRNGTHPVFTASRWMVYYLKPSSPKHVRFSWHQDAVTV
Sequence
             TCSDLSYGDLLYEVQYRSPFDTEWQSKQENTCNVTIEGLDAEKCYSFWVRVKAMEDVYGPDTYPSDWS
             EVTGWQRGEIRDACAETPTPPKPKLSKFILISSLAILLMVSLLLLSLWKLWRVRKFLIPSVPDPKSIF
             PGLFEIHQGNFQEWITDTQNVAHLHKMAGAEQESGPEEPLVVQLAKTEAESPRMLDPQTEEKEASGGS
             LQLPHQPLQGGDVVTIGGFTFVMNDRSYVAL
             SEQ ID NO: 39             1143 bp
NOV8b,       ATGGGGCGGCTGGTTCTGCTGTGGGGAGCTGCGGTCTTTCTGCTGGGAGGCTGGATGGCTTTGGGGC
CG142202-03
DNA Sequence AAGGAGGAGCAGAAGGAGTACAGATTCAGATCATCTACTTCAATTTAGAAACCGTGCAGGTGACATG
             GAATGCCAGCAAATACTCCAGGACCAACCTGACTTTCCACTACAGATTCAACGGTGATGAGGCCTAT
             GACCAGTGCACCAACTACCTTCTCCAGGAAGGTCACACTTCGGGGTGCCTCCTAGACGCAGAGCAGC
             GAGACGACATTCTCTATTTCTCCATCAGGAATGGGACGCACCCCGTTTTCACCGCAAGTCGCTGGAT
             GGTTTATTACCTGAAACCCAGTTCCCCGAAGCACGTGAGATTTTCGTGGCATCAGGATGCAGTGACG
             GTGACGTGTTCTGACCTGTCCTACGGGGATCTCCTCTATGAGGTTCAGTACCGGAGCCCCTTCGACA
             CCGAGTGGCAGTCCAAACAGGAAAATACCTGCAACGTCACCATAGAAGGCTTGGATGCCGAGAAGTG
             TTACTCTTTCTGGGTCAGGGTGAAGGCCATGGAGGATGTATATGGGCCAGACACATACCCAAGCGAC
             TGGTCAGAGGTGACATGCTGGCAGAGAGGCGAGATTCGGGATGCCTGTGCAGAGACACCAACGCCTC
             CCAAACCAAAGCTGTCCAAATTTATTTTAATTTCCAGCCTGGCCATCCTTCTGATGGTGTCTCTCCT
             CCTTCTGTCTTTATGGAAATTATGGAGAGTGAGGAAGTTTCTCATTCCCAGCGTGCCAGACCCGAAA
             TCCATCTTCCCCGGGCTCTTTGAGATACACCAAGGGAACTTCCAGGAGTGGATCACAGACACCCAGA
             ACGTGGCCCACCTCCACAAGATGGCAGGTGCAGAGCAAGAAAGTGGCCCCGAGGAGCCCCTGGTAGT
             CCAGTTGGCCAAGACTGAAGCCGAGTCTCCCAGGATGCTGGACCCACAGACCGAGGAGAAAGAGGCC
             TCTGGGGGATCCCTCCAGCTTCCCCACCAGCCCCTCCAAGGTGGTGATGTGGTCACAATCGGGGGCT
             TCACCTTTGTGATGAATGACCGCTCCTACGTGGCGTTGTGATGGACACACCACTGTCAAAGTCAACG
             TCAG
             ORF Start: ATG at 1       ORF Stop: TGA at 1111
             SEQ ID NO: 40             370 aa    MW at 41969.2kD
NOV8b,       MGRLVLLWGAAVFLLGGWMALGQGGAEGVQIQIIYFNLETVQVTWNASKYSRTNLTFHYRFNGDEAY
CG142202-03
Protein      DQCTNYLLQEGHTSGCLLDAEQRDDILYFSIRNGTHPVFTASRWMVYYLKPSSPKHVRFSWHQDAVT
Sequence
             VTCSDLSYGDLLYEVQYRSPFDTEWQSKQENTCNVTIEGLDAEKCYSFWVRVKAMEDVYGPDTYPSD
             WSEVTCWQRGEIRDACAETPTPPKPKLSKFILISSLAILLMVSLLLLSLWKLWRVRKFLIPSVPDPK
             SIFPGLFEIHQGNFQEWITDTQNVAHLHKMAGAEQESGPEEPLVVQLAKTEAESPRMLDPQTEEKEA
             SGGSLQLPHQPLQGGDVVTIGGFTFVMNDRSYVAL
             SEQ ID NO: 41             1154 bp
NOV8c,       ATGGGGCGGCTGGTTCTGCTGTGGGGAGCTGCGGTCTTTCTGCTGGGAGGCTGGATGGCTTTGGGGCA
CG142202-02
DNA Sequence AGGAGGAGCAGCAGAAGGAGTACAGATTCAGATCATCTACTTCAATTTAGAAACCGTGCAGGTGACAT
             GGAATGCCAGCAAATACTCCAGGACCAACCTGACTTTCCACTACAGATTCAACGGTGATGAGGCCTAT
             GACCAGTGCACCAACTACCTTCTCCAGGAAGGTCACACTTCGGGGTGCCTCCTAGACGCAGAGCAGCG
             AGACGACATTCTCTATTTCTCCATCAGGAATGGGACGCACCCCGTTTTCACCGCAAGTCGCTGGATGG
             TTTATTACCTGAAACCCAGTTCCCCGAAGCACGTGAGATTTTCGTGGCATCAGGATGCAGTGACGGTG
             ACGTGTTCTGACCTGTCCTACGGGGATCTCCTCTATGAGGTTCAGTACCGGAGCCCCTTCGACACCGA
             GTGGCAGTCCAAACAGGAAAATACCTGCAACGTCACCATAGAAGGCTTGGATGCCGAGAAGTGTTACT
             CTTTCTGGGTCAGGGTGAAGGCTATGGAGGATGTATATGGGCCAGACACATACCCAAGCGACTGGTCA
             GAGGTGACATGCTGGCAGAGAGGCGAGATTCGGGATGCCTGTGCAGAGACACCAACGCCTCCCAAACC
             AAAGCTGTCCAAATTTATTTTAATTTCCAGCCTGGCCATCCTTCTGATGGTGTCTCTCCTCCTTCTGT
             CTTTATGGAAATTATGGAGAGTGAGGAAGTTTCTCATTCCCAGCGTGCCAGACCCGAAATCCATCTTC
             CCCGGGCTCTTTGAGATACACCAAGGGAACTTCCAGGAGTGGATCACAGACACCCAGAACGTGGCCCA
             CCTCCACAAGATGGCAGGTGCAGAGCAAGAAAGTGGCCCCGAGGAGCCCCTGGTAGTCCAGTTGGCCA
             AGACTGAAGCCGAGTCTCCCAGGATGCTGGACCCACAGACCGAGGAGAAAGAGGCCTCTGGGGGATCC
             CTCCAGCTTCCCCACCAGCCCCTCCAAGGTGGTGATGTGGTCACAATCGGGGGCTTCACCTTTGTGAT
             GAATGACCGCTCCTACGTGGCGTTGTGATGGACACACCACTGTCAAAGTCAACGTCAGAAGGGCGA
             ORF Start: ATG at 1       ORF Stop: TGA at 1114
             SEQ ID NO: 42             371 aa    MW at 42040.3kD
NOV8c,       MGRLVLLWGAAVFLLGGWMALGQGGAAEGVQIQIIYFNLETVQVTWNASKYSRTNLTFHYRFNGDEAY
CG142202-02
Protein      DQCTNYLLQEGHTSGCLLDAEQRDDILYFSIRNGTHPVFTASRWMVYYLKPSSPKHVRFSWHQDAVTV
Sequence
             TCSDLSYGDLLYEVQYRSPFDTEWQSKQENTCNVTIEGLDAEKCYSFWVRVKAMEDVYGPDTYPSDWS
             EVTCWQRGEIRDACAETPTPPKPKLSKFILISSLAILLMVSLLLLSLWKLWRVRKFLIPSVPDPKSIF
             PGLFEIHQGNFQEWITDTQNVAHLHKMAGAEQESGPEEPLVVQLAKTEAESPRMLDPQTEEKEASGGS
             LQLPHQPLQGGDVVTIGGFTFVMNDRSYVAL

[0406] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 8B.

TABLE 8B
Comparison of NOV8a against NOV8b and NOV8c.
		NOV8a Residues/	Identities/Similarities
	Protein Sequence	Match Residues	for the Matched Region
	NOV8b	1 . . . 371	343/371 (92%)
		1 . . . 370	343/371 (92%)
	NOV8c	1 . . . 371	344/371 (92%)
		1 . . . 371	344/371 (92%)

[0407] Further analysis of the NOV8a protein yielded the following properties shown in Table 8C.

TABLE 8C
Protein Sequence Properties NOV8a
PSort analysis:   0.4600 probability located in plasma membrane; 0.2473 probability located in
                  microbody (peroxisome); 0.1000 probability located in endoplasmic reticulum
                  (membrane); 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 23 and 24

[0408] A search of the NOV8a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 5D.

TABLE 8D
Geneseq Results for NOV8a
		NOV8a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU77482	Human thymic stromal	1 . . . 371	370/371 (99%)	0.0
	lymphopoietin receptor	1 . . . 371	371/371 (99%)
	(TSLPR)-FLAG polypeptide -
	Homo sapiens, 379 aa.
	[WO200200724-A2,
	Jan. 3, 2002]
AAU77481	Human TSLPR (thymic	1 . . . 371	370/371 (99%)	0.0
	stromal lymphopoietin	1 . . . 371	371/371 (99%)
	receptor) polypeptide - Homo
	sapiens, 371 aa.
	[WO200200724-A2,
	Jan. 3, 2002]
AAU77220	Human thymic stromal	1 . . . 371	370/371 (99%)	0.0
	lymphopoietin	1 . . . 371	371/371 (99%)
	receptor(TSLPR)-FLAG
	protein sequence - Homo
	sapiens, 379 aa.
	[WO200200723-A2,
	Jan. 3, 2002]
AAU77219	Human thymic stromal	1 . . . 371	370/371 (99%)	0.0
	lymphopoietin receptor	1 . . . 371	371/371 (99%)
	(TSLPR) protein sequence -
	Homo sapiens, 371 aa.
	[WO200200723-A2,
	Jan. 3, 2002]
AAB71681	CRCGCL protein - Homo	1 . . . 371	370/371 (99%)	0.0
	sapiens, 371 aa.	1 . . . 371	371/371 (99%)
	[WO200112672-A2,
	Feb. 22, 2001]

[0409] In a BLAST search of public sequence datbases, the NOV8a protein was found to have homology to the proteins shown in the BLASTP data in Table 8E.

TABLE 8E
Public BLASTP Results for NOV8a
		NOV8a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
CAD26815	Sequence 7 from Patent	1 . . . 371	370/371 (99%)	0.0
	WO0200723 - synthetic	1 . . . 371	371/371 (99%)
	construct, 379 aa.
Q9HC73	Cytokine receptor CRL2	1 . . . 371	370/371 (99%)	0.0
	PRECUSOR (IL-XR)	1 . . . 371	371/371 (99%)
	(Thymic stromal
	LYMPHOPOIETIN protein
	receptor TSLPR) - Homo
	sapiens (Human), 371 aa.
Q9H5R3	CDNA: FLJ23147 fis, clone	1 . . . 176	161/176 (91%)	2e−93
	LNG09295 - Homo sapiens	1 . . . 175	166/176 (93%)
	(Human), 232 aa.
Q8R4S8	Thymic stromal	24 . . . 371	123/359 (34%)	5e−48
	lymphopoietin receptor -	28 . . . 360	183/359 (50%)
	Rattus norvegicus (Rat), 360
	aa.
Q9JMD5	Cytokine receptor delta1 -	6 . . . 371	135/380 (35%)	4e−43
	Mus musculus (Mouse), 359	1 . . . 359	186/380 (48%)
	aa.

[0410] PFam analysis predicts that the NOV8a protein contains the domains shown in the Table 8F.

TABLE 8F
Domain Analysis of NOV8a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV8a Match Region	Region	Value
T-box	167 . . . 192	7/26 (27%)	0.94
		22/26 (85%)

Example 9

The NOV9 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 9A.

[0411]

TABLE 9A
NOV9 Sequence Analysis
             SEQ ID NO: 43             828 bp
NOV9a,       CTTATTAAAAACATACTCTTATTTTTCAGG                                                        ATG                  TCAAACTTGGCACAATTTGACTCTGATTTTTACCA
CG142621-01
DNA Sequence ATCTAATTTTACTATTGATAACCAGGAGCAGAGTGGTAATGACTCTAATGCCTATGGAAATCTTTATG
             GATCTAGAAAGCAACAAGCTGGTGAGCAGCCTCAGCCTGCCTCCTTTGTTCCATCAGAGATGCTCATG
             TCATCGGGTTACGCAGGACAATTTTTTCAGCCAGCATCCAACTCAGATTATTATTCACAATCTCCTTA
             CATTGACAGTTTTGATGAAGAGCCTCCTTTGCTAGAAGAACTTGGAATCCATTTTGATCACATATGGC
             AAAAAACTTTGACAGTGTTAAACCCAATGAAGCCAGTAGATGGCAGCATTATGAATGAAACGGACCTC
             ACTGGACCCATTCTTTTTTGCGTAGCCCTGGGAGCCACCTTGCTTCTGGCAGGAAAAGTTCAGTTTGG
             TTATGTGTATGGCATGAGTGCCATTGGCTGCCTTGTGATTCATGCCTTGCTGAACCTGATGAGCTCTT
             CAGGGGTGTCGTACGGCTGTGTGGCCAGCGTGCTGGGTTACTGCCTGCTCCCCATGGTCATCCTGTCT
             GGTTGCGCCATGTTCTTTTCACTGCAGGGCATCTTTGGAATCATGTCATCCCTGGTCATCATTGGCTG
             GTGTAGTCTCTCAGCTTCCAAGATCTTCATTGCAGCCTTGCACATGGAAGGACAGCAGCTTCTTGTTG
             CCTACCCTTGTGCCATACTTTATGGACTTTTTGCCCTCCTAACAATTTTCTAAAGAATGTTTGAGATG
             GCATTTCAAGAC
             ORF Start: ATG at 31      ORF Stop: TAA at 799
             SEQ ID NO: 44             256 aa    MW at 27775.6kD
NOV9a,       MSNLAQFDSDFYQSNFTIDNQEQSGNDSNAYGNLYGSRKQQAGEQPQPASFVPSEMLMSSGYAGQFFQ
CG142621-01
Protein      PASNSDYYSQSPYIDSFDEEPPLLEELGIHFDHIWQKTLTVLNPMKPVDGSIMNETDLTGPILFCVAL
Sequence
             GATLLLAGKVQFGYVYGMSAIGCLVIHALLNLMSSSGVSYGCVASVLGYCLLPMVILSGCAMFFSLQG
             IFGIMSSLVIIGWCSLSASKIFIAALHMEGQQLLVAYPCAILYGLFALLTIF

[0412] Further analysis of the NOV9a protein yielded the following properties shown in Table 9B.

TABLE 9B
Protein Sequence Properties NOV9a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);
                  0.0300 probability located in mitochondrial inner membrane
SignalP analysis: No Known Signal Sequence Predicted

[0413] A search of the NOV9a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 9C.

TABLE 9C
Geneseq Results for NOV9a
		NOV9a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB07505	Human GTP-binding protein	1 . . . 256	160/259 (61%)	2e−86
	(GTPB) (ID: 4879308CD1) -	1 . . . 257	198/259 (75%)
	Homo sapiens, 257 aa.
	[WO200204510-A2,
	Jan. 17, 2002]
ABG34065	Human Pro peptide #36 -	1 . . . 256	160/259 (61%)	2e−86
	Homo sapiens, 257 aa.	1 . . . 257	198/259 (75%)
	[WO200224888-A2,
	Mar. 28, 2002]
AAM41786	Human polypeptide SEQ ID	1 . . . 256	160/259 (61%)	2e−86
	NO 6717 - Homo sapiens,	4 . . . 260	198/259 (75%)
	260 aa. [WO200153312-A1,
	Jul. 26, 2001]
AAM40000	Human polypeptide SEQ ID	1 . . . 256	160/259 (61%)	2e−86
	NO 3145 - Homo sapiens,	1 . . . 257	198/259 (75%)
	257 aa. [WO200153312-A1,
	Jul. 26, 2001]
AAG67008	Human Yip1p28 polypeptide -	1 . . . 256	2e−86
	Homo sapiens, 257 aa.	1 . . . 257	198/259 (75%)
	[WO200166769-A1,
	Sep. 13, 2001]

[0414] In a BLAST search of public sequence datbases, the NOV9a protein was found to have homology to the proteins shown in the BLASTP data in Table 9D.

TABLE 9D
Public BLASTP Results for NOV9a
		NOV9a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9JIM5	YIP1B (2310016N21RIK	1 . . . 256	207/256 (80%)	e−117
	protein) - Mus musculus	1 . . . 254	225/256 (87%)
	(Mouse), 254 aa.
Q9EQQ2	Hypothetical 27.9 kDa protein	1 . . . 256	160/259 (61%)	3e−86
	(2610311I19Rik protein)	1 . . . 257	196/259 (74%)
	(Similar to RIKEN cDNA
	2310016N21 gene) - Mus
	musculus (Mouse), 257 aa.
Q969M3	CDNA FLJ30014 fis, clone	1 . . . 256	160/259 (61%)	5e−86
	3NB692000330, weakly	1 . . . 257	198/259 (75%)
	similar to YIP1 protein
	(Similar to hypothetical
	protein AF140225)
	(Hypothetical 28.0 kDa
	protein) - Homo sapiens
	(Human), 257 aa.
AAK67644	Golgi membrane protein	1 . . . 256	159/259 (61%)	1e−84
	SB140 - Homo sapiens	1 . . . 257	197/259 (75%)
	(Human), 257 aa.
Q9H338	Hypothetical 28.0 kDa protein -	1 . . . 256	159/259 (61%)	2e−84
	Homo sapiens (Human), 257	1 . . . 257	195/259 (74%)
	aa.

[0415] PFam analysis predicts that the NOV9a protein contains the domains shown in the Table 9E.

TABLE 9E
Domain Analysis of NOV9a
Pfam Domain	NOV9a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 10

[0416] The NOV10 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 10A.

TABLE 10A
NOV10 Sequence Analysis
             SEQ ID NO: 45             1837 bp
NOV 10a,     GGCACGAGGAACCCTTCCTGTTGCCTTAGGGGAACGTGGCTTTCCCTGCAGAGCCGGTGTCTCCGCC
CG142761-01
DNA Sequence TGCGTCCCTGCTGCAGCAACCGGAGCTGGAGTCGGATCCCGAACGCACCCTCGCCATGGACTCGGCC
             CTCAGCGATCCGCATAACGGCAGTGCCGAGGCAGGCGGCCCCACCAACAGCACTACGCGGCCGCCTT
             CCACGCCCGAGGGCATCGCGCTGGCCTACGGCAGCCTCCTGCTCATGGCGCTGCTGCCCATCTTCTT
             CGGCGCCCTGCGCTCCGTACGCTGCGCCCGCGGCAAGAATGCTTCAGACATGCCTGAAACAATCACC
             AGCCGGGATGCCGCCCGCTTCCCCATCATCGCCAGCTGCACACTCTTGGGGCTCTACCTCTTTTTCA
             AAATATTCTCCCAGGAGTACATCAACCTCCTGCTGTCCATGTATTTCTTCGTGCTGGGAATCCTGGC
             CCTGTCCCACACCATCAGCCCCTTCATGAATAAGTTTTTTCCAGCCAGCTTTCCAAATCGACAGTAC
             CAGCTGCTCTTCACACAGGGTTCTGGGGAAAACAAGGAAGAGATCATCAATTATGAATTTGACACCA
             AGGACCTGGTGTGCCTGGGCCTGAGCAGCATCGTTGGCGTCTGGTACCTGCTGAGGAAGCACTGGAT
             TGCCAACAACCTTTTTGGCCTGGCCTTCTCCCTTAATGGAGTAGAGCTCCTGCACCTCAACAATGTC
             AGCACTGGCTGCATCCTGCTGGGCGGACTCTTCATCTACGATGTCTTCTGGGTATTTGGCACCAATG
             TGATGGTGACAGTGGCCAAGTTCTTCGAGGCACCAATAAAATTGGTGTTTCCCCAGGATCTGCTGGA
             GAAAGGCCTCGAAGCAAACAACTTTGCCATGCTGGGACTTGGAGATGTCGTCATTCCAGGGATCTTC
             ATTGCCTTGCTGCTGCGCTTTGACATCAGCTTGAAGAAGAATACCCACACCTACTTCTACACCAGCT
             TTGCAGCCTACATCTTCGGCCTGGGCCTTACCATCTTCATCATGCACATCTTCAAGCATGCTCAGCC
             TGCCCTCCTATACCTGGTCCCCGCCTGCATCGGTTTTCCTGTCCTGGTGGCGCTGGCCAAGGGAGAA
             GTGACAGAGATGTTCAGCTACGAGTCCTCGGCGGAAATCCTGCCTCATACCCCGAGGCTCACCCACT
             TCCCCACAGTCTCGGGCTCCCCAGCCAGCCTGGCCGACTCCATGCAGCAGAAGCTAGCTGGCCCTCG
             CCGCCGGCGCCCGCAGAATCCCAGCGCCATGTAATGCCCAGCGGGTGCCCACCTGCCCGCTTCCCCC
             TACTGCCCCGGGGCCCAAGTTATGAGGAGTCAAATCCTAAGGATCCAGCGGCAGTGACAGAATCCAA
             AGAGGGAACAGAGGCATCAGCATCGAAGGGGCTGGAGAAGAAAGAGAAATGATGCAGCTGGTGCCCG
             AGCCTCTCAGGGCCAGACCAGACAGATGGGGGCTGGGCCCACACAGGCGTGCACCGGTAGAGGGCAC
             AGGAGGCCAAGGGCAGCTCCAGGACAGGGCAGGGGGCAGCAGGATACCTCCAGCCAGGCCTCTGTGG
             CCTCTGTTTCCTTCTCCCTTTCTTGGCCCTCCTCTGCTCCTCCCCACACCCTGCAGGCAAAAGAAAC
             CCCCAGCTTCCCCCCTCCCCGGGAGCCAGGTGGGAAAAGTGGGTGTGATTTTTAGATTTTGTATTGT
             GGACTGATTTTGCCTCACATTAAAAACTCATCCCATGGCCAAAAAAAAAAAAAAAAAAAAAAAAAAA
             AAAAAAAAAAAAAAAAAAAAAAAAAAAA
             ORF Start: ATG at 123     ORF Stop: TAA at 1305
             SEQ ID NO: 46             394 aa    MW at 43482.2kD
NOV 10a,     MDSALSDPHNGSAEAGGPTNSTTRPPSTPEGIALAYGSLLLMALLPIFFGALRSVRCARGKNASDMP
CG142761-01
Protein      ETITSRDAARFPIIASCTLLGLYLFFKIFSQEYINLLLSMYFFVLGILALSHTISPFMNKFFPASFP
Sequence
             NRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSIVGVWYLLRKHWIANNLFGLAFSLNGVELLH
             LNNVSTGCILLGGLFIYDVFWVFGTNVMVTVAKFFEAPIKLVFPQDLLEKGLEANNFAMLGLGDVVI
             PGIFIALLLRFDISLKKNTHTYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVAL
             AKGEVTEMFSYESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAM

[0417] Further analysis of the NOV10a protein yielded the following properties shown in Table 10B.

TABLE 10B
Protein Sequence Properties NOV10a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);
                  0.0300 probability located in mitochondrial inner membrane
SignalP analysis: Cleavage site between residues 61 and 62

[0418] A search of the NOV10a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 10C.

TABLE 10C
Geneseq Results for NOV10a
		NOV10a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB88567	Human hydrophobic domain	1 . . . 379	353/379 (93%)	0.0
	containing protein clone	1 . . . 375	359/379 (94%)
	HP03010 #31 - Homo
	sapiens, 377 aa.
	[WO200112660-A2,
	Feb. 22, 2001]
AAB10549	Human aspartate protease ps1	1 . . . 379	353/379 (93%)	0.0
	3 protein - Homo sapiens,	1 . . . 375	359/379 (94%)
	377 aa. [WO200043505-A2,
	Jul. 27, 2000]
AAY27132	Human glioblastoma-derived	1 . . . 379	353/379 (93%)	0.0
	polypeptide (clone	1 . . . 375	359/379 (94%)
	OA004FG) - Homo sapiens,
	377 aa. [WO9933873-A1,
	Jul. 8, 1999]
AAM93670	Human polypeptide, SEQ ID	1 . . . 379	352/379 (92%)	0.0
	NO: 3554 - Homo sapiens,	1 . . . 375	359/379 (93%)
	377 aa. [EP1130094-A2,
	Sep. 5, 2001]
AAY27133	Human glioblastoma-derived	1 . . . 379	351/379 (92%)	0.0
	polypeptide (clone	1 . . . 375	357/379 (93%)
	OA004LD) - Homo sapiens,
	377 aa. [WO9933873-A1,
	Jul. 8, 1999]

[0419] In a BLAST search of public sequence datbases, the NOV10a protein was found to have homology to the proteins shown in the BLASTP data in Table 10D.

TABLE 10D
Public BLASTP Results for NOV10a
		NOV10a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q95H87	Similar to histocompatibility	1 . . . 379	354/379 (93%)	0.0
	13 - Homo sapiens (Human),	1 . . . 375	360/379 (94%)
	377 aa.
Q8TCT9	Signal peptide peptidase -	1 . . . 379	353/379 (93%)	0.0
	Homo sapiens (Human), 377	1 . . . 375	359/379 (94%)
	aa.
BAC11519	CDNA FLJ90802 fis, clone	1 . . . 379	352/379 (92%)	0.0
	Y79AA1000226 - Homo	1 . . . 375	359/379 (93%)
	sapiens (Human), 377 aa.
Q9D8V0	1200006009Rik protein -	1 . . . 349	335/349 (95%)	0.0
	Mus musculus (Mouse), 378	1 . . . 349	343/349 (97%)
	aa.
AAM22075	Minor histocompatibility	1 . . . 379	339/379 (89%)	0.0
	antigen H13 isoform 1 - Mus	1 . . . 376	352/379 (92%)
	musculus (Mouse), 378 aa.

[0420] PFam analysis predicts that the NOV10a protein contains the domains shown in the Table 10E.

TABLE 10E
Domain Analysis of NOV10a
Pfam Domain	NOV10a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 11

[0421] The NOV11 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 11A.

TABLE 11A
NOV11 Sequence Analysis
	SEQ ID NO:47	615bp
NOV11a,	CTCAGAGTCTCCTCAGACGCCGAGATGCGGGTCACGGCACCCCGAACCGTCCTCCTGCTGCTCTCGG
CG143926-01
DNA sequence	CGGCCCTGGCCCTGACCGAGTGCGTGGAGTGGCTCCGCAGATACCTGGAGAACGGGAAGGACAAGCT
	GGAGCGCGCTGACCCCCCAAAGACACACGTGACCCACCACCCCATCTCTGACCATGAGGCCACCCTG
	AGGTGCTGGGCCCTGGGTTTCTACCCTGCGGAGATCACACTGACCTGGCAGCGGGATGGCGAGGACC
	AAACTCAGGACACTGAGCTTGTGGAGACCAGACCAGCAGGAGATAGAACCTTCCAGAAGTGGGCAGC
	TGTGGTGGTGCCTTCTGGAGAAGAGCAGAGATACACATGCCATGTACAGCATGAGGGGCTGCCGAAG
	CCCCTCACCCTGAGATGGGAGCCGTCTTCCCAGTCCACCGTCCCCATCGTGGGCATTGTTGCTGGCC
	TGGCTGTCCTAGCAGTTGTGGTCATCGGAGCTGTGGTCGCTGCTGTGATGTGTAGGAGGAAGAGTTC
	AGGTGGAAAAGGAGGGAGCTACTCTCAGGCTGCGTGCAGCGACAGTGCCCAGGGCTCTGATGTGTCT
	TCTACAGCTTGA
	ORF Start: ATG at 25		ORF Stop: TGA at 613
	SEQ ID NO:48	196 aa	MW at 21301.0 kD
NOV11a,	MRVTAPRTVLLLLSAALALTECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFY
CG143926-01
Protein Sequence	PAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP

[0422] Further analysis of the NOV11a protein yielded the following properties shown in Table 11B.

TABLE 11B
Protein Sequence Properties NOV11a
PSort analysis:   0.4600 probability located in plasma membrane; 0.1000 probability located in
                  endoplasmic reticulum (membrane); 0.1000 probability located in
                  endoplasmic reticulum (lumen); 0.1000 probability located in outside
SignalP analysis: Cleavage site between residues 23 and 24

[0423] A search of the NOV11a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 11C.

TABLE 11C
Geneseq Results for NOV11a
		NOV11a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAP70155	Sequence encoded by	21 . . . 196	173/176 (98%)	e−100
	genomic DNA encoding	187 . . . 362	175/176 (99%)
	human histocompatibility
	antigen HLA-B 27 - Homo
	sapiens, 362 aa.
	[EP226069-A, Jun. 24, 1987]
AAP70590	Sequence of the human	21 . . . 196	172/176 (97%)	e−99
	histocompatibility antigen	162 . . . 337	174/176 (98%)
	HLA B27 - Homo sapiens,
	337 aa. [DE3542024-A,
	Jun. 4, 1987]
AAR03144	Sequence of HLA-B51	22 . . . 196	167/175 (95%)	4e−97
	antigen - Homo sapiens, 362	188 . . . 362	172/175 (97%)
	aa. [EP354580-A,
	Feb. 14, 1990]
AAR03142	Sequence of HLA-Bw52	22 . . . 196	167/175 (95%)	4e−97
	antigen - Homo sapiens, 362	188 . . . 362	172/175 (97%)
	aa. [EP354580-A,
	Feb. 14, 1990]
AAU32882	Novel human secreted	22 . . . 196	169/176 (96%)	1e−95
	protein #3373 - Homo	191 . . . 366	170/176 (96%)
	sapiens, 369 aa.
	[WO200179449-A2,
	Oct. 25, 2001]

[0424] In a BLAST search of public sequence datbases, the NOV11a protein was found to have homology to the proteins shown in the BLASTP data in Table 11D.

TABLE 11D
Public BLASTP Results for NOV11a
		NOV11a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q31603	Lymphocyte	21 . . . 196	176/176 (100%)	e−101
	antigen—Homo	187 . . . 362	176/176 (100%)
	sapiens (Human),
	362 aa.
Q29854	HLA-B alpha	21 . . . 196	176/176 (100%)	e−101
	chain antigen	187 . . . 362	176/176 (100%)
	precursor—Homo
	sapiens (Human),
	362 aa.
Q29861	HLA-BPOT	21 . . . 196	176/176 (100%)	e−101
	(classI)—Homo	187 . . . 362	176/176 (100%)
	sapiens (Human),
	362 aa.
Q29681	MHC class I	21 . . . 196	176/176 (100%)	e−101
	antigen heavy	187 . . . 362	176/176 (100%)
	chain precursor—
	Homo sapiens
	(Human), 362 aa.
Q29638	MHC class I	21 . . . 196	176/176 (100%)	e−101
	antigen—Homo	187 . . . 362	176/176 (100%)
	sapiens (Human),
	362 aa.

[0425] PFam analysis predicts that the NOV11a protein contains the domains shown in the Table 11E.

TABLE 11E
Domain Analysis of NOV11a
	Pfam	NOV11a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value
	MHC_I	20 . . . 37	15/18 (83%)	1.5e−07
			17/18 (94%)
	ig	54 . . . 119	15/67 (22%)	2.8e−09
			48/67 (72%)

Example 12

[0426] The NOV12 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 12A.

TABLE 12A
NOV12 Sequence Analysis
	SEQ ID NO:49	555 bp
NOV12a,	ATGATTTCCAGAATGGAGAAGATGACGATGATGATGAAGATATTGATTATGTTTGCTCTTGGAATGA
CG144193-01
DNA Sequence	ACTACTGGTCTTGCTCAGGTTTCCCAGTGTACGACTACGATCCATCCTCCTTAAGGGATGCCCTCAG
	TGCCTCTGTGGTAAAAGTGAATTCCCAGTCACTGAGTCCGTATCTGTTTCGGGCATTCAGAAGCTCA
	TTAAAAAGAGTTGAGGTCCTAGATGAGAACAACTTGGTCATGAATTTAGAGTTCAGCATCCGGGAGA
	CAACATGCAGGAAGGATTCTGGAGAAGATCCCGCTACATGTGCCTTCCAGAGGGACTACTATGTGTC
	CACGTCTGAGTCTTACAGCAGCGAAGAGATGATTTTTGGGGACATGTTGGGATCTCATAAATGGAGA
	AGCAATTATCTATTTGGTCTCATTTCAGACGAGTCCATAAGTGAACAATTTTATGATCGGTCACTTG
	GGATCATGAGAAGGGTATTGCCTCCTGGAAACAGAAGGTACCCAAACCACCGGCACAGAGCAAGAAT
	AAATACTGACTTTGAGTAA
	ORF Start: ATG at 1		ORF Stop: TAA AT 553
	SEQ ID NO:50	184 aa	MW at 21465.1 kD
NOV12a,	MISRMEKMTMMMKILIMFALGMNYWSCSGFPVYDYDPSSLRDALSASVVKVNSQSLSPYLFRAFRSS
CG144193-01
Protein Sequence	LKRVEVLDENNLVMNLEFSIRETTCRKDSGEDPATCAFQRDYYVSTSESYSSEEMIFGDMLGSHKWR
	SNYLFGLISDESISEQFYDRSLGIMRRVLPPGNRRYPNHRHRARINTDFE
	SEQ ID NO:51	636 bp
NOV12b,	ATGATTTCCAGAATGGAGAAGATGACGATGATGATGAAGATATTGATTATGTTTGCTCTTGGAATGA
CG144193-02
DNA Sequence	ACTACTGGTCTTGCTCAGGTTTCCCAGTGTACGACTACGATCCATCCTCCTTAAGGGATGCCCTCAG
	TGCCTCTGTGGTAAAAGTGAATTCCCAGTCACTGAGTCCGTATCTGTTTCGGGCATTCAGAAGCTCA
	TTAAAAAGAGTTGAGGTCCTAGATGAGAACAACTTGGTCATGAATTTAGAGTTCAGCATCCGGGAGA
	CAACATGCAGGAAGGATTCTGGAGAAGATCCCGCTACATGTGCCTTCCAGAGGGACTACTATGTGTC
	CACAGCTGTTTGCAGAAGCACCGTGAAGGTATCTGCCCAGCAGGTGCAGGGCGTGCATGCTCGCTGC
	AGCTGGTCCTCCTCCACGTCTGAGTCTTACAGCAGCGAAGAGATGATTTTTGGGGACATGTTGGGAT
	CTCATAAATGGAGAAACAATTATCTATTTGGTCTCATTTCAGACGAGTCCATAAGTGAACAATTTTA
	TGATCGGTCACTTGGGATCATGAGAAGGGTATTGCCTCCTGGAAACAGAAGGTACCCAAACCACCGG
	CACAGAGCAAGAATAAATACTGACTTTGAGTAA
	ORF Start: ATG at 1		ORF Stop: TAA at 634
	SEQ ID NO:52	211 aa	MW at 24337.4 kD
NOV12b,	MISRMEKMTMMMKILIMFALGMNYWSCSGFPVYDYDPSSLRDALSASVVKVNSQSLSPYLFRAFRSS
CG144193-02
Protein Sequence	LKRVEVLDENNLVMNLEFSIRETTCRKDSGEDPATCAFQRDYYVSTAVCRSTVKVSAQQVQGVHARC
	SWSSSTSESYSSEEMIFGDMLGSHKWRNNYLFGLISDESISEQFYDRSLGIMRRVLPPGNRRYPNHR
	HRARINTDFE

[0427] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 12B.

TABLE 12B
Comparison of NOV12a against NOV12b.
	Protein	NOV12a Residues/	Identities/Similarities
	Sequence	Match Residues	for the Matched Region
	NOV12b	1 . . . 184	176/211 (83%)
		1 . . . 211	180/211 (84%)

[0428] Further analysis of the NOV12a protein yielded the following properties shown in Table 12C.

TABLE 12C
Protein Sequence Properties NOV12a
PSort     0.5500 probability located in endoplasmic reticulum
analysis: (membrane); 0.1900 probability located in lysosome (lumen);
          0.1000 probability located in endoplasmic reticulum (lumen);
          0.1000 probability located in outside
SignalP   Cleavage site between residues 30 and 31
analysis:

[0429] A search of the NOV12a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 12D.

TABLE 12D
Geneseq Results for NOV12a
		NOV12a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAR10321	Human BMP—	1 . . . 184	183/211 (86%)	e−100
	Homo sapiens,	1 . . . 211	184/211 (86%)
	211 aa.
	[EP409472-A,
	23 JAN. 1991]
AAR10320	Human BMP—	1 . . . 184	183/211 (86%)	e−100
	Homo sapiens,	1 . . . 211	184/211 (86%)
	211 aa.
	[EP409472-A,
	23 JAN. 1991]
AAR10319	Bovine BMP—	5 . . . 184	117/206 (56%)	2e−55
	Bos taurus,	1 . . . 203	140/206 (67%)
	203 aa.
	[EP409472-A,
	23 JAN. 1991]
AAW02632	Bovine phospho-	10 . . . 184	113/201 (56%)	1e−54
	protein Spp24—	1 . . . 200	137/201 (67%)
	Bos taurus,
	200 aa.
	[WO9621006-A1,
	11 JUL. 1996]
AAR10317	Bovine BMP—	71 . . . 111	26/41 (63%)	2e−08
	exon 3—Bos	1 . . . 41	33/41 (80%)
	taurus, 41 aa.
	[EP409472-A,
	23 JAN. 1991]

[0430] In a BLAST search of public sequence datbases, the NOV12a protein was found to have homology to the proteins shown in the BLASTP data in Table 12E.

TABLE 12E
Public BLASTP Results for NOV12a
		NOV12a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q13103	Secreted	1 . . . 184	183/211 (86%)	3e−99
	phosphoprotein	1 . . . 211	184/211 (86%)
	24 precursor
	(SPP-24)—Homo
	sapiens (Human),
	211 aa.
AAH27494	RIKEN cDNA	11 . . . 184	121/200 (60%)	4e−59
	0610038O04	5 . . . 203	143/200 (71%)
	gene—Mus
	musculus
	(Mouse), 203 aa.
Q9DCG1	0610038O04Rik	11 . . . 184	121/200 (60%)	4e−59
	protein—Mus	5 . . . 203	143/200 (71%)
	musculus
	(Mouse), 203 aa.
Q27967	Secreted	10 . . . 184	114/201 (56%)	2e−54
	phosphoprotein	1 . . . 200	137/201 (67%)
	24 precursor
	(SPP-24)—Bos
	taurus (Bovine),
	200 aa.
Q62740	Secreted	30 . . . 184	109/181 (60%)	7e−51
	phosphoprotein	1 . . . 180	128/181 (70%)
	24 (SPP-24)—
	Rattus norvegicus
	(Rat), 180 aa.

[0431] PFam analysis predicts that the NOV12a protein contains the domains shown in the Table 12F.

TABLE 12F
Domain Analysis of NOV12a
Pfam	NOV12a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
Cathelicidins	37 . . . 104	18/69 (26%)	0.15
		33/69 (48%)
cystatin	30 . . . 106	17/83 (20%)	0.14
		51/83 (61%)

Example 13

[0432] The NOV13 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 13A.

TABLE 13A
NOV13 Sequence Analysis
	SEQ ID NO:53	835 bp
NOV13a,	CCTCTCTCTCTGACTGCCTGCTGGAAATGCCCCCATCTCCCTTTGAGTCCTCCTCCCGGGCGACTCC
CG144545-01
DNA Sequence	TGTGACCTGTAACCTCTGTCCTGAAATCATCACAATGGCCAGGGTGGCCTCAGCTCAGGGCCTCTGT
	GACATCACCAAGGGCCTGGCACCAGGTGCCCAGTCTCCCAGTTGCGAGGGCAAGCAAACCCGTCATG
	AGCAACTCCCTTCCCCATCTCTGCTCACCATGTGGACGCTGAAATCGTCCCTGGTCCTGCTTCTGTG
	CCTCACCTGCAGCTATGCCTTTATGTTCTCTTCTCTGAGACAGAAAACTAGCGAACCCCAGGGGAAG
	GTGCAATACGGAGAGCACTTTCGGATTCGGCAGAATCTACCAGAGCACACCCAAGGCTGGCTTGGGA
	GCAAATGGCTCTGGCTTCTTTTTGTTGTTGTGCCGTTTGTGATACTGCAGTGTCAAAGAGACAGTGA
	GAAGAATAAGGAGCAGAGTCCTCCTGGCCTTCGAGGCGGCCAACTTCACTCTCCATTAAAGAAAAAA
	AGAAATGCTTCCCCCAACAAAGACTGTGCATTCAATACCTTAATGGAACTCGAGGTGGAGCTTATGA
	AATTTGTGTCCGAAGTGCGGAATCTTAAAGGTGCCATGGCAACAGGTAGTGGCAGTAACCTCAGGCT
	TCGAAGGTCAGAGATGCCTGCAGATCCATACCATGTCACGATCTGTGAAATATGGGGAGAAGAAAGC
	TCTAGCTGAATGGATTTGTGTGTCAGGAGAGAAAAAAGTTGAGTGTTGACAAACTGTATGCAAACTA
	ATAAAACTATTCTGAAGAAAAGAAAAAAAAA
	ORF Start: ATG at 27		ORF Stop: TGA at 744
	SEQ ID NO:54	239 aa	MW at 26610.4 kD
NOV13a,	MPPSPFESSSRATPVTCNLCPEIITMARVASAQGLCDITKGLAPGAQSPSCEGKQTRHEQLPSPSLL
CG144545-01
Protein Sequence	TMWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVQYGEHFRIRQNLPEHTQGWLGSKWLWLLFV
	VVPFVILQCQRDSEKNKEQSPPGLRGGQLHSPLKKKRNASPNKDCAFNTLMELEVELMKFVSEVRNL
	KGAMATGSGSNLRLRRSEMPADPYHVTICEIWGEESSS

[0433] Further analysis of the NOV13a protein yielded the following properties shown in Table 13B.

TABLE 13B
Protein Sequence Properties NOV13a
PSort     0.6000 probability located in plasma membrane; 0.4000
analysis: probability located in Golgi body; 0.3000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in mitochondrial inner membrane
SignalP   No Known Signal Sequence Predicted
analysis:

[0434] A search of the NOV13a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 13C.

TABLE 13C
Geneseq Results for NOV13a
		NOV13a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU68550	Human novel	1 . . . 239	235/239 (98%)	e−137
	cytokine encoded	1 . . . 239	237/239 (98%)
	by cDNA
	790CIP2D_11
	#1—Homo
	sapiens, 239 aa.
	[WO200175093-
	A1, 11 OCT.
	2001]
AAY53032	Human secreted	69 . . . 239	168/171 (98%)	1e−96
	protein clone	1 . . . 171	170/171 (99%)
	di393_2 protein
	sequence SEQ ID
	NO: 70—Homo
	sapiens, 171 aa.
	[WO9957132-A1,
	11 NOV. 1999]
AAG00463	Human secreted	69 . . . 169	100/101 (99%)	5e−55
	protein, SEQ ID	1 . . . 101	100/101 (99%)
	NO: 4544—
	Homo sapiens,
	101 aa.
	[EP1033401-A2,
	6 SEP. 2000]
AAY12683	Human 5′ EST	69 . . . 169	100/101 (99%)	5e−55
	secreted protein	1 . . . 101	100/101 (99%)
	SEQ ID NO:
	273—Homo
	sapiens, 101 aa.
	[WO9906549-A2,
	11 FEB. 1999]
AAM87953	Human immune/	151 . . . 239	85/89 (95%)	4e−44
	haematopoietic	1 . . . 89	88/89 (98%)
	antigen SEQ ID
	NO: 15546—
	Homo sapiens,
	89 aa.
	[WO200157182-
	A2, 9 AUG.
	2001]

[0435] In a BLAST search of public sequence datbases, the NOV13a protein was found to have homology to the proteins shown in the BLASTP data in Table 13D.

TABLE 13D
Public BLASTP Results for NOV13a
		NOV13a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9HCV6	DJ1153D9.4 (Novel	102 . . . 239	120/138 (86%)	3e−66
	protein)—Homo	1 . . . 138	126/138 (90%)
	sapiens (Human),
	138 aa (fragment).
Q9D9T2	1700029J11Rik	72 . . . 238	101/168 (60%)	2e−46
	protein—Mus	5 . . . 169	122/168 (72%)
	musculus (Mouse),
	170 aa.
Q9HCV7	DJ1153D9.3 (novel	69 . . . 154	84/86 (97%)	4e−44
	protein)—Homo	1 . . . 86	84/86 (97%)
	sapiens (Human),
	94 aa.
Q96C09	Similar to neuronal	69 . . . 156	80/88 (90%)	8e−42
	thread protein—	1 . . . 88	82/88 (92%)
	Homo sapiens
	(Human), 106 aa.
Q8YR98	Hypothetical protein	9 . . . 61	18/53 (33%)	2.6
	A113550—	21 . . . 71	31/53 (57%)
	Anabaena sp.
	(strain PCC
	7120), 208 aa.

[0436] PFam analysis predicts that the NOV13a protein contains the domains shown in the Table 13E.

TABLE 13E
Domain Analysis of NOV13a
Pfam Domain	NOV13a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 14

[0437] The NOV14 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 14A.

TABLE 14A
NOV14 Sequence Analysis
	SEQ ID NO:55	855 bp
NOV14a,	CTGCGTTGCTGGGAAGTTCTGGAAGGAAGCATGTGCTCCAGAGGTTGGGATTCGTGTCTGGCTCTGG
CG144884-01
DNA Sequence	AATTGCTACTGCTGCCTCTGTCACTCCTGGTGACCAGCATTCAAGGTCACTTGGTACATATGACCGT
	GGTCTCCGGCAGCAACGTGACTCTGAACATCTCTGAGAGCCTGCCTGAGAACTACAAACAACTAACC
	TGGTTTTATACTTTCGACCAGAAGATTGTAGAATGGGATTCCAGAAAATCTAAGTACTTTGAATCCA
	AATTTAAAGGCAGGGTCAGACTTGATCCTCAGAGTGGCGCACTGTACATCTCTAAGGTCCAGAAAGA
	GGACAACAGCACCTACATCATGAGGGTGTTGAAAAAGACTGGGAATGAGCAAGAATGGAAGATCAAG
	CTGCAAGTGCTTGACCCTGTACCCAAGCCTGTCATCAAAATTGAGAAGATAGAAGACATGGATGACA
	ACTGTTATCTGAAACTGTCATGTGTGATACCTGGCGAGTCTGTAAACTACACCTGGTATGGGGACAA
	AAGGCCCTTCCCAAAGGAGCTCCAGAACAGTGTGCTTGAAACCACCCTTATGCCACATAATTACTCC
	AGGTGTTATACTTGCCAAGTCAGCAATTCTGTGAGCAGCAAGAATGGCACGGTCTGCCTCAGTCCAC
	CCTGTACCCTGGCCCGGTCCTTTGGAGTAGAATGGATTGCAAGTTGGCTAGTGGTCACGGTGCCCAC
	CATTCTTGGCCTGTTACTTACCTGAGATGAGCTCTTTTAACTCAAGCGAAACTTCAAGGCCAGAAGA
	TCTTGCCTGTTGGTGATCATGCTCCTCACCAGGACAGAGACTGTATAAAGG
	ORF Start: ATG at 31		ORF Stop: TGA at 760
	SEQ ID NO:56	243 aa	MW at 27682.8 kD
NOV 14a,	MCSRGWDSCLALELLLLPLSLLVTSIQGHLVHMTVVSGSNVTLNISESLPENYKQLTWFYTFDQKIV
CG144884-01
Protein Sequence	EWDSRKSKYFESKFKGRVRLDPQSGALYISKVQKEDNSTYIMRVLKKTGNEQEWKIKLQVLDPVPKP
	VIKIEKIEDMDDNCYLKLSCVIPGESVNYTWYGDKRPFPKELQNSVLETTLMPHNYSRCYTCQVSNS
	VSSKNGTVCLSPPCTLARSFGVEWIASWLVVTVPTILGLLLT
	SEQ ID NO:57	573 bp
NOV14b,	GGAAGTTCTGGAAGCAAGCATGTGCTCCAGAGGTTGGGATTCGTGTCTGGCTCTGGAATTGCTACTG
CG144884-02
DNA Sequence	CTGCCTCTGTCACTCCTGGTGACCAGCATTCAAGGTCACTTGGTACATATGACCGTGGTCTCCGGCA
	GCAACGTGACTCTGAACATCTCTGAGAGCCTGCCTGAGAACTACAAACAACTAACCTGGTTTTATAC
	TTTCGACCAGAAGATTGTAGAATGGGATTCCAGAAAATCTAAGTACTTTGAATCCAAATTTAAAGGC
	AGGGTCAGACTTGATCCTCAGAGTGGCGCACTGTACATCTCTAAGGTCCAGAAAGAGGACAACAGCA
	CCTACATCATGACGGTGTTGAAAAAGACTGGGAATGAGCAAGAATGGAAGATCAAGCTGCAAGTGCT
	TGCCCGGTCCTTTGGAGTAGAATGGATTGCAAGTTGGCTAGTGGTCACGGTGCCCACCATTCTTGGC
	CTGTTACTTACCTGAGATGAGCTCTTTTAACTCAAGCGAAACTTGAAGGCCAGAAGATCTTGCCTGT
	TGGTGATCATGCTCCTCACCAGGACAGACACTGTATA
	ORF Start: ATG at 20		ORF Stop: TGA at 482
	SEQ ID NO:58	154 aa	MW at 17670.4 kD
NOV14b,	MCSRGWDSCLALELLLLPLSLLVTSIQGHLVHMTVVSGSNVTLNISESLPENYKQLTWFYTFDQKIV
CG144884-02
Protein Sequence	EWDSRKSKYFESKFKGRVRLDPQSGALYISKVQKEDNSTYIMRVLKKTGNEQEWKIKLQVLARSFGV
	EWIASWLVVTVPTILGLLLT

[0438] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 14B.

TABLE 14B
Comparison of NOV14a against NOV14b.
	NOV14a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV14b	1 . . . 128	115/128 (89%)
	1 . . . 128	115/128 (89%)

[0439] Further analysis of the NOV14a protein yielded the following properties shown in Table 14C.

TABLE 14C
Protein Sequence Properties NOV14a
PSort analysis:   0.9190 probability located in plasma membrane; 0.2000 probability located in
                  lysosome (membrane); 0.1000 probability located in endoplasmic reticulum
                  (membrane); 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 29 and 30

[0440] A search of the NOV14a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 14D.

TABLE 14D
Geneseq Results for NOV14a
		NOV14a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAU74426	Human protein sequence #4,	1 . . . 243	242/243 (99%)	e−141
	related to isolation of genes	1 . . . 243	242/243 (99%)
	within SLE-1B - Homo
	sapiens, 243 aa.
	[WO200188200-A2,
	Nov. 22, 2001]
AAW35857	Human CD48 for use in T	27 . . . 220	194/194 (100%)	1e−113
	lymphocyte veto molecule -	1 . . . 194	194/194 (100%)
	Homo sapiens, 194 aa.
	[WO9737687-A1,
	Oct. 16, 1997]
AAU74427	Mouse protein sequence #4,	1 . . . 243	129/247 (52%)	2e−60
	related to isolation of genes	1 . . . 240	163/247 (65%)
	within SLE-1B - Mus
	musculus, 240 aa.
	[WO200188200-A2,
	Nov. 22, 2001]
AAG00342	Human secreted protein,	1 . . . 111	109/111 (98%)	4e−58
	SEQ ID NO: 4423 - Homo	1 . . . 111	109/111 (98%)
	sapiens, 111 aa.
	[EP1033401-A2,
	Sep. 6, 2000]
ABG47129	Human peptide encoded by	33 . . . 128	96/96 (100%)	4e−50
	genome-derived single exon	1 . . . 96	96/96 (100%)
	probe SEQ ID 36794 - Homo
	sapiens, 96 aa.
	[WO200186003-A2,
	Nov. 15, 2001]

[0441] In a BLAST search of public sequence datbases, the NOV14a protein was found to have homology to the proteins shown in the BLASTP data in Table 14E.

TABLE 14E
Public BLASTP Results for NOV14a
		NOV14a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
P09326	B-lymphocyte activation	1 . . . 243	243/243 (100%)	e−142
	marker BLAST-1 precursor	1 . . . 243	243/243 (100%)
	(BCM1 surface antigen)
	(Leucocyte antigen
	MEM-102) (TCT.1)
	(Antigen CD48) - Homo
	sapiens (Human), 243 aa.
AAH30224	Similar to B-lymphocyte	1 . . . 148	132/148 (89%)	1e−69
	activation marker BLAST-1	1 . . . 148	134/148 (90%)
	(BCM1 surface antigen)
	(Leucocyte antigen
	MEM-102) (TCT.1)
	(Antigen CD48) - Homo
	sapiens (Human), 169 aa.
P18181	MRC OX-45 surface antigen	1 . . . 243	129/247 (52%)	5e−60
	precursor (BCM1 surface	1 . . . 240	163/247 (65%)
	antigen) (BLAST-1) (CD48)
	(HM48-1) - Mus musculus
	(Mouse), 240 aa.
P10252	MRC OX-45 surface antigen	10 . . . 242	120/235 (51%)	2e−56
	precursor (BCM1 surface	10 . . . 239	155/235 (65%)
	antigen) (BLAST-1) (CD48) -
	Rattus norvegicus (Rat),
	240 aa.
Q8VE93	Similar to RIKEN cDNA	42 . . . 213	51/187 (27%)	1e−09
	2310026I04 gene - Mus	35 . . . 221	85/187 (45%)
	musculus (Mouse), 285 aa.

[0442] PFam analysis predicts that the NOV14a protein contains the domains shown in the Table 14F.

TABLE 14F
Domain Analysis of NOV14a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV14a Match Region	Region	Value
ig	147 . . . 198	10/56 (18%)	0.011
		36/56 (64%)

Example 15

[0443] The NOV15 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 15A.

TABLE 15A
NOV15 Sequence Analysis
	SEQ ID NO:59	700 bp
NOV15a,	GGGATCCGACTCTAGTCGTAATGGAGGCGGGCGGCTTTCTGGACTCGCTCATTTACGGAGCATGCGT
CG145122-01
DNA Sequence	GGTCTTCACCCTTGGCATGTTCTCCGCCGGCCTCTCGGACCTCAGGCACATGCGAATGACCCGGAGT
	GTGGACAACGTCCAGTTCCTGCCCTTTCTCACCACGGAAGTCAACAACCTGGGCTGGCTGAGTTATG
	GGGCTTTGAAGGGAGACGGGATCCTCATCGTCGTCAACACAGTGGGTGTTGTGCTCCTACAGACTGC
	AACCCTGCTAGGGGTCCTTCTCCTGGGTTATGGCTACTTTTGGCTCCTGGTACCCAACCCTGAGGCC
	CGGCTTCAGCAGTTGGGCCTCTTCTGCAGTGTCTTCACCATCAGCATGTACCTCTCACCACTGGCTG
	ACTTGGCTAAGGTGATTCAAACTAAATCAACCCAATGTCTCTCCTACCCACTCACCATTGCTACCCT
	TCTCACCTCTGCCTCCTGGTGCCTCTATGGGTTTCGACTCAGAGATCCCTATATCATGGTGTCCAAC
	TTTCCAGGAATCGTCACCAGCTTTATCCGCTTCTGGCTTTTCTGGAAGTACCCCCAGGAGCAAGACA
	GGAACTACTGGCTCCTGCAAACCTGAGGCTGCTCATCTGACCACTGGGCACCTTAGTGCCAACCTGA
	ACCAAAGAGACCTCCTTGTTTTATGCTGGG
	ORF Start: ATG at 21		ORF Stop: TGA at 627
	SEQ ID NO:60	202 aa	MW at 22754.5 kD
	NOV15a,	MEAGGFLDSLIYGACVVFTLGMFSAGLSDLRHMRMTRSVDNVQFLPFLTTEVNNLGWLSYGALKGDG
	CG145122-01
	Protein Sequence	ILIVVNTVGVVLLQTATLLGVLLLGYGYFWLLVPNPEARLQQLGLFCSVFTISMYLSPLADLAKVIQ
		TKSTQCLSYPLTIATLLTSASWCLYGFRLRDPYIMVSNFPGIVTSFIRFWLFWKYPQEQDRNYWLLQ
		T

[0444] Further analysis of the NOV15a protein yielded the following properties shown in Table 15B.

TABLE 15B
Protein Sequence Properties NOV15a
PSort analysis:   0.7300 probability located in plasma membrane; 0.6400 probability located in
                  endoplasmic reticulum (membrane); 0.3880 probability located in microbody
                  (peroxisome); 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 22 and 23

[0445] A search of the NOV15a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 15C.

TABLE 15C
Geneseq Results for NOV15a
		NOV15a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB90191	Human polypeptide SEQ ID	1 . . . 202	202/221 (91%)	e−112
	NO 2967 - Homo sapiens	66 . . . 286	202/221 (91%)
	286 aa. [WO200190304-A2,
	Nov. 29, 2001]
AAB75379	Human secreted protein #38 -	1 . . . 202	202/221 (91%)	e−112
	Homo sapiens, 221 aa.	1 . . . 221	202/221 (91%)
	[WO200100806-A2,
	Jan. 4, 2001]
AAE03982	Human gene 43 encoded	1 . . . 202	202/221 (91%)	e−112
	secreted protein fragment,	1 . . . 221	202/221 (91%)
	SEQ ID NO:180 - Homo
	sapiens, 221 aa.
	[WO200077022-A1,
	Dec. 21, 2000]
AAB25793	Human secreted protein SEQ	1 . . . 202	202/221 (91%)	e−112
	ID #105 - Homo sapiens, 221	1 . . . 221	202/221 (91%)
	aa. [W0200037491-A2,
	Jun. 29, 2000]
AAB53433	Human colon cancer antigen	1 . . . 102	202/221 (91%)	e−112
	protein sequence SEQ ID	28 . . . 248	202/221 (91%)
	NO:973 - Homo sapiens, 248
	aa. [WO200055351-A1,
	Sep. 21, 2000]

[0446] In a BLAST search of public sequence datbases, the NOV15a protein was found to have homology to the proteins shown in the BLASTP data in Table 15D.

TABLE 15D
Public BLASTP Results for NOV15a
		NOV15a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9BRV3	Stromal cell protein - Homo	1 . . . 202	202/221 (91%)	e−112
	sapiens (Human), 221 aa.	1 . . . 221	202/221 (91%)
Q9UHQ3	Stromal cell protein - Homo	1 . . . 202	201/221 (90%)	e−112
	sapiens (Human), 221 aa.	1 . . . 221	202/221 (90%)
Q95KW8	Uterine stromal cell protein -	1 . . . 202	197/221 (89%)	e−108
	Papio anubis (Olive baboon),	1 . . . 221	198/221 (89%)
	221 aa.
Q9UHQ2	Stromal cell protein isoform -	1 . . . 202	171/202 (84%)	1e−90
	Homo sapiens (Human), 179	1 . . . 179	175/202 (85%)
	aa.
Q9CXK4	Recombination activating	1 . . . 202	161/221 (72%)	4e−85
	gene 1 gene activation - Mus	1 . . . 221	174/221 (77%)
	musculus (Mouse), 221 aa.

[0447] PFam analysis predicts that the NOV15a protein contains the domains shown in the Table 15E.

TABLE 15E
Domain Analysis of NOV15a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV15a Match Region	Region	Value
MtN3_s1v	9 . . . 79	27/73 (37%)	5.6e−25
		61/73 (84%)
MtN3_s1v	108 . . . 194	35/89 (39%)	1.9e−35
77/89 (87%)

Example 16

[0448] The NOV16 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 16A.

TABLE 16A
NOV16 Sequence Analysis
	SEQ ID NO:61	568 bp
NOV16a,	CCGGCCGGGCCATGGATTCAATGCCTGAGCCCGCGTCCCGCTGTCTTCTGCTTCTTCCCTTGCTGCT
CG145198-01
DNA Sequence	GCTGCTGCTGCTGCTGCTGCCGGCCCCGGAGCTGGGCCCGAGCCAGGCCGGAGCTGAGGAGAACGAC
	TGGGTTCGCCTGCCCAGCAAATGCGAAGTGTGTAAATATGTTGCTGTGGAGCTGAAGTCAGCCTTTG
	AGGAAACCGGCAAGACCAAGGAGGTGATTGGCACGGGCTATGGCATCCTGGACCAGAAGGCCTCTGG
	AGTCAAATACACCAAGTCCATTTCAGATCCCCCAGACCAGATCACCTATCTTCCTTCCAGCTCTGAG
	TCACTTCCCATTGGGACTTGCGGTTAATCGAAGTCACTGAGACCATTTGCAAGAGGCTCCTGGATTA
	TAGCCTGCACAAGGAGAGGACCGGCAGCAATCGATTTGCCAAGGTTGGATTCGGGATTGTCCTTCAT
	CCGCTCTGGGGTCAGGCCTGCATGTATCTTAGTGTGTCTGCTGGTGTGAGTGTGATTTGAAGATGAC
	CACCTGGGATCTTCCCTCATTGCCTCTTCCCT
	ORF Start: ATG at 12		ORF Stop: TAA at 360
	SEQ ID NO:62	116 aa	MW at 12441.2 kD
NOV16a,	MDSMPEPASRCLLLLPLLLLLLLLLPAPELGPSQAGAEENDWVRLPSKCEVCKYVAVELKSAFEETG
CG145198-01	KTKEVIGTGYGILDQKASGVKYTKSISDPPDOMTYLPSSSESLPIGTCG
Protein Sequence
	SEQ ID NO:63	370 bp
NOV16b,	CACCGGATCCACCATGGATTCAATGCCTGAGCCCGCGTCCCGCTGTCTTCTGCTTCTTCCCTTGCTG
178498076 DNA
Sequence	CTGCTGCTGCTGCTGCTGCTGCCGGCCCCGGAGCTGGGCCCGAGCCAGGCCGGAGCTGAGGAGAACG
	ACTGGGTTCGCCTGCCCAGCAAATGCGAAGTGTGTAAATATGTTGCTGTGGAGCTGAAGTCAGCCTT
	TGAGGAAACCGGCAAGACCAAGGAGGTGATTGGCACGGGCTATGGCATCCTGGACCAGAAGGCCTCT
	GGAGTCAAATACACCAAGTCCATTTCAGATCCCCCAGACCAGATGACCTATCTTCCTTCCAGCTCTG
	AGTCACTTCCCATTGGGACTTGCGGTCTCGAGGGC
	ORF Start: at 2		ORF Stop: end of sequence
	SEQ ID NO:64	123 aa	MW at 13086.9 kD
NOV16b,	TGSTMDSMPEPASRCLLLLPLLLLLLLLLPAPELGPSQAGAEENDWVRLPSKCEVCKYVAVELKSAF
278498076
Protein Sequence	EETGKTKEVIGTGYGILDQKASGVKYTKSISDPPDQMTYLPSSSESLPIGTCGLEG
	SEQ ID NO:65	274 bp
NOV16c,	CACCGGATCCCCGAGCCAGGCCGGAGCTGAGGAGAACGACTGGGTTCGCCTGCCCAGCAAATGCGAA
278498091 DNA
Sequence	GTGTGTAAATATGTTGCTGTGGAGCTGAAGTCAGCCTTTGAGGAAACCGGCAAGACCAAGGAGGTGA
	TTGGCACGGGCTATGGCATCCTGGACCAGAAGGCCTCTGGAGTCAAATACACCAAGTCCATTTCAGA
	TCCCCCAGACCAGATGACCTATCTTCCTTCCAGCTCTGAGTCACTTCCCATTGGGACTTGCGGTCTC
	GAGGGC
	ORF Start: at 2		ORF Stop: end of sequence
	SEQ ID NO:66	91 aa	MW at 9647.7 kD
NOV16c,	TGSPSQAGAEENDWVRLPSKCEVCKYVAVELKSAFEETGKTKEVIGTGYGILDQKASGVKYTKSISD
278498091
Protein Sequence	PPDQMTYLPSSSESLPIGTCGLEG
	SEQ ID NO:67	1596 bp
NOV16d,	CCCAGGCCCAGACGCAGGCTTCTTCTCCTCGGGTCTTGGTCCTGCATCCTCTCTCTCCCAGAGCCTC
CG145198-02
DNA Sequence	CGTTAGGGGGTGGGAAAGGACTTTGCCATAGGTCGCTGAGGCCACCATCTGCTCTCTTACTGGCCAA
	GGGCGTAAAAAGATAGTCCTCCCATTAGCTAGAGAGCAAACCCCAGAAAGCCTATTGGCTGCGCCGT
	CCGCGGGCCTTGGTCCGCTTTGAAGGCGGGCTGCGGCTGCGAGAGGAGGGCGGGCGGGAGGCTAGCT
	GTTGTCGTGGTTGCTCGGAGGCACGTGTGCAGTCCCGGAAGCGGCGAGGGGAAACTGCTCCGCGCGC
	GCCGCGGGAGGAGGAACCGCCCGGTCCTTTAGGGTCCGGGCCCGGCCGGGCCATGGATTCAATGCCT
	GAGCCCGCGTCCCGCTGTCTTCTGCTTCTTCCCTTGCTGCTGCTGCTGCTGCTGCTGCTGCCGGCCC
	CGGAGCTGGGCCCGAGCCAGGCCGGAGCTGAGGAGAACGACTGGGTTCGCCTGCCCAGCAAATGCGA
	AGGGACTTGCGGTTAATCGAAGTCACTCAGACCATTGCAATAGGCTCCTGGATTATAGCCTGCACA
	AGGAGAGGACCGGCAGCAATCGATTTGCCAAGGGCATGTCAGAGACCTTTGAGACATTACACAACCT
	GGTACACAAAGGGGTCAAGGTGGTGATGGACATCCCCTATGAGCTGTGGAACGAGACTTCTGCAGAG
	GTGGCTGACCTCAAGAAGCAGTGTGATGTGCTGGTGGAAGAGTTTGAGGAGGTGATCGAGGACTGGT
	ACAGGAACCACCAGGAGGAAGACCTGACTGAATTCCTCTGCGCCAACCACGTGCTGAAGGGAAAAGA
	CACCAGTTGCCTGGCAGAGCAGTGGTCCGGCAAGAAGGGAGACACAGCTGCCCTGGGAGGGAAGAAG
	TCCAAGAAGAAGAGCAGCAGGGCCAAGGCAGCAGGCGGCAGGAGTAGCAGCAGCAAACAAAGGAAGG
	AGCTGGGTGGCCTTGAGGGAGACCCCAGCCCCGAGGAGGATGAGGGCATCCAGAAGGCATCCCCTCT
	CACACACAGCCCCCCTGATGAGCTCTGAGCCCACCCAGCATCCTCTGTCCTGAGACCCCTGATTTTG
	AAGCTGAGGAGTCAGGGGCATGGCTCTGGCAGGCCGGGATGGCCCCGCAGCCTTCAGCCCCTCCTTG
	CCTTGGCTGTGCCCTCTTCTGCCAAGGAAAGACACAAGCCCCAGGAAGAACTCAGAGCCGTCATGGG
	TAGCCCACGCCGTCCTTTCCCCTCCCCAAGTGTTTCTCTCCTGACCCAGGGTTCAGGCAGGCCTTGT
	GGTTTCAGGACTGCAAGGACTCCAGTGTGAACTCAGGAGGGGCAGGTGTCAGAACTGGGCACCAGGA
	CTGGAGCCCCCTCCGGAGACCAAACTCACCATCCCTCAGTCCTCCCCAACAGGGTACTAGGACTGCA
	GCCCCCTGTAGCTCCTCTCTGCTTACCCCTCCTGTGGACACCTTGCACTCTGCCTGGCCCTTCCCAG
	AGCCCAAAGAGTAAAAATGTTCTGGTTCTGAAAAAAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 388		ORF Stop: TAA at 550
	SEQ ID NO:68	54 aa	MW at 5772.7kD
NOV16d,	MDSMPEPASRCLLLLPLLLLLLLLLPAPELGPSQAGAEENDWVRLPSKCEGTCG
CG145198-02
Protein Sequence
	SEQ ID NO:69	901 bp
NOV16e,	GGAGGAGGAACCGCCCGGTCCTTTAGGGTCCGGGCCCGGCGGGCCATGGATTCAATGCCTGAGCCC
CG145198-03
DNA Sequence	GCGTCCCGCTGTCTTCTGCTTCTTCCCTTGCTGCTGCTGCTGCTGCTGCTGCTGCCGGCCCCGGAGC
	TGGGCCCGAGCCAGGCCGGAGCTGAGGAGAACGACTGGGTTCGCCTGCCCAGCAAATGCGAAGTGTG
	TAAATATGTTGCTGTGGAGCTGAAGTCAGCCTTTGAGGAAACCGGCAAGACCAAGGAGGTGATTGGC
	ACGGGCTATGGCATCCTGGACCAGAAGGCCTCTGGAGTCAAATACACCAAGTCGGACTTGCGGTTAA
	TCGAAGTCACTGAGACCATTTGCAAGAGGCTCCTGGATTATAGCCTGCACAAGGAGAGGACCGGCAG
	CAATCGATTTGCCAAGGGCATGTCAGAGACCTTTGAGACATTACACAACCTGGTACACAAAGGGGTC
	AAGGTGGTGATGGACATCCCCTATGAGCTGTGGAACGAGACTTCTGCAGAGGTGGCTGACCTCAAGA
	AGCAGTGTGATGTGCTGGTGGAAGAGTTTGAGGAGGTGATCGAGGACTGGTACAGGAACCACCAGGA
	GGAAGACCTGACTGAATTCCTCTGCGCCAACCACGTGCTGAAGGGAAAAGACACCAGTTGCCTGGCA
	GAGCAGTGGTCCGGCAAGAAGGGAGACACAGCTGCCCTGGGAGGGAAGAAGCCCAAGAAGAAGAGCA
	GCAGGGCCAAGGCAGCAGGCGGCAGGAGTAGCAGCAGCAAACAAAGGAAGGAGCTGGGTGGCCTTGA
	GGGAGACCCCAGCCCCGAGGAGGATGAGGGCATCCAGGCATCCCCCTCTCACACACACAGCCCCCCT
	GATGAGCTCTGAGCCCACCCAGCATCCTCT
	ORF Start: ATG at 47		ORF Stop: TGA at 881
	SEQ ID NO:70	278 aa	MW at 30757.7 kD
NOV16e,	MDSMPEPASRCLLLLPLLLLLLLLLPAPELGPSQAGAEENDWVRLPSKCEVCKYVAVELKSAFEETG
CG145198-03
Protein Sequence	KTKEVIGTGYGILDQKASGVKYTKSDLRLIEVTETICKRLLDYSLHKERTGSNRFAKGMSETFETLH
	NLVHKGVKVVMDIPYELWNETSAEVADLKKQCDVLVEEFEEVIEDWYRNHQEEDLTEFLCANHVLKG
	KDTSCLAEQWSGKKGDTAALGGKKPKKKSSRAKAAGGRSSSSKQRKELGGLEGDPSPEEDEGIQKAS
	PLTHSPPDEL

[0449] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 16B.

TABLE 16B
Comparison of NOV16a against NOV16b through NOV16e.
	NOV16a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV16b	1 . . . 116	101/116 (87%)
	5 . . . 120	101/116 (87%)
NOV16c	32 . . . 116	85/85 (100%)
	4 . . . 88	85/85 (100%)
NOV16d	1 . . . 50	35/50 (70%)
	1 . . . 50	35/50 (70%)
NOV16e	1 . . . 92	77/92 (83%)
	1 . . . 92	77/92 (83%)

[0450] Further analysis of the NOV16a protein yielded the following properties shown in Table 16C.

TABLE 16C
Protein Sequence Properties NOV16a
PSort analysis:   0.8200 probability located in outside; 0.1000 probability located in
                  endoplasmic reticulum (membrane); 0.1000 probability located in
                  endoplasmic reticulum (lumen); 0.1000 probability located in lysosome
                  (lumen)
SignalP analysis: Cleavage site between residues 32 and 33

[0451] A search of the NOV16a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 16D.

TABLE 16D
Geneseq Results for NOV16a
		NOV16a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABP41913	Human ovarian antigen	1 . . . 92	92/92 (100%)	2e−47
	HVVBT41, SEQ ID	76 . . . 167	92/92 (100%)
	NO:3045 - Homo sapiens,
	353 aa. [W0200200677-A1,
	Jan. 3, 2002]
AAU02499	Human trinucleotide repeat	1 . . . 92	92/92 (100%)	2e−47
	protein (TRP) - Homo	1 . . . 92	92/92 (100%)
	sapiens, 278 aa.
	[W0200130798-A1,
	May 3, 2001]
AAU12239	Human PRO4409	1 . . . 92	92/92 (100%)	2e−47
	polypeptide sequence - Homo	1 . . . 92	92/92 (100%)
	sapiens, 278 aa.
	[WO200140466-A2,
	Jun. 7, 2001]
AAW78312	Fragment of human secreted	1 . . . 92	82/92 (89%)	3e−39
	protein encoded by gene 67 -	1 . . . 91	83/92 (90%)
	Homo sapiens, 277 aa.
	[WO9856804-A1,
	Dec. 17, 1998]
AAU02498	Murine trinucleotide repeat	1 . . . 92	78/92 (84%)	4e−37
	protein (TRP) - Mus sp, 276	1 . . . 92	80/92 (86%)
	aa. [WO200130798-A1,
	May 3, 2001]

[0452] In a BLAST search of public sequence datbases, the NOV16a protein was found to have homology to the proteins shown in the BLASTP data in Table 16E.

TABLE 16E
Public BLASTP Results for NOV16a
		NOV16a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9BT09	Hypothetical 30.7 kDa protein	1 . . . 92	92/92 (100%)	4e−47
	(Unknown) (Protein for	1 . . . 92	92/92 (100%)
	MGC:4122) (Protein for
	MGC: 1220) (DJ475N16.1)
	(CTG4A) - Homo sapiens
	(Human), 278 aa.
O15412	CTG4a - Homo sapiens	1 . . . 92	92/92 (100%)	4e−47
	(Human), 143 aa.	1 . . . 92	92/92 (100%)
Q9DAU1	1600025D17Rik protein	1 . . . 92	78/92 (84%)	1e−36
	(Putative retinoic	1 . . . 92	80/92 (86%)
	acid-regulated protein)
	(RIKEN cDNA 1600025D17
	gene) - Mus musculus
	(Mouse), 276 aa.
CAC39850	Sequence 345 from Patent	19 . . . 76	24/58 (41%)	6e−06
	EP1067182 - Homo sapiens	8 . . . 65	35/58 (59%)
	(Human), 248 aa.
Q8WUN9	Hypothetical 29.4 kDa protein -	19 . . . 76	24/58 (41%)	6e−06
	Homo sapiens (Human), 257	19 . . . 76	35/58 (59%)
	aa (fragment).

[0453] PFam analysis predicts that the NOV16a protein contains the domains shown in the Table 16F.

TABLE 16F
Domain Analysis of NOV16a
Pfam Domain	NOV16a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 17

[0454] The NOV17 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 17A.

TABLE 17A
NOV17 Sequence Analysis
	SEQ ID NO:71	862 bp
NOV17a,	CCCCTCCCATTTGCCTGTCCTGGTCAGGCCCCCACCCCCCTTCCCACCTGACCAGCCATGGGGGCTG
CG145286-01
DNA Sequence	CGGTGTTTTTCGGCTGCACTTTCGTCGCGTTCGGCCCGGCCTTCGCGCTTTTCTTGATCACTGTGGC
	TGGGGACCCGCTTCGCGTTATCATCCTGGTCGCAGGGGCATTTTTCTGGCTGGTCTCCCTGCTCCTG
	GCCTCTGTGGTCTGGTTCATCTTGGTCCATGTGACCGACCGGTCAGATGCCCGGCTCCAGTACGGCC
	TCCTGATTTTTGGTGCTGCTGTCTCTGTCCTTCTACAGGAGGTGTTCCGCTTTGCCTACTACAAGCT
	GCTTAAGAAGGCAGATGAGGGGTTAGCATCGCTGAGTGAGGACGGAAGATCACCCATCTCCATCCGC
	CAGATGGCCTATGGTGTGGTTGGGATCCATGGAGACTCACCCTATTACTTCCTGACTTCAGCCTTTC
	TGACAGCAGCCATTATCCTGCTCCATACCTTTTGGGGAGTTGTGTTCTTTGATGCCTGTGAGAGGAG
	ACGGTACTGGGCTTTGGGCCTGGTGGTTGGGAGTCACCTACTGACATCGGGACTGACATTCCTGAAC
	CCCTGGTATGAGGCCAGCCTGCTGCCCATCTATGCAGTCACTGTTTCCATGGGGCTCTGGGCCTTCA
	TCACAGCTGGAGGGTCCCTCCGAAGTATTCAGCGCAGCCTCTTGTGCCGACGGCAGGAGGACAGTCG
	GGTGATGGTGTATTCTGCCCTGCGCATCCCACCCGAGGACTGAGGGAACCTAGGGGGGACCCCTGGG
	CCTGGGGTGCCCTCCTGATGTCCTCGCCCTGTATTTCTCCATCTCCAGTTCTGGACAG
	ORF Start: ATG at 58		ORF Stop: TGA at 778
	SEQ ID NO:72	240 aa	MW at 26566.8 kD
NOV17a,	MGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVTDRSDARL
CG145286-01
Protein Sequence	QYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYGVVGIHGDSPYYFLT
	SAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGL
	WAFITAGGSLRSIQRSLLCRRQEDSRVMVYSALRIPPED
	SEQ ID NO:73	942 bp
NOV17b,	CCTTCCCCTCCCATTTGCCTGTCCTGGTCAGGCCCCCCACCCCCCTTCCCACCTGACCAGCCATGGG
CG145286-02
DNA Sequence	GGCTGCGGTGTTTTTCGGCTGCACTTTCGTCCCGTTCGGCCCGGGCCTTCCGCTTTTCTTGATCACT
	GTGGCTGGGGACCCGCTTCGCGTTATCATCCTGGTCGCAGGGGCATTTTCCTGGCTGGTCTCCCTGC
	TCCTGGCCTCTGTGGTCTGGTTCATCTTGGTCCATGTGACCGACCGGTCAGATGCCCGGCTCCAGTA
	CGGCCTCCTGATTTTTGGTGCTGCTGTCTCTGTCCTTCTACAGGAGGTGTTCCGCTTTGCCTACTAC
	AAGCTGCTTAAGAAGGCAGATGAGGGGTTAGCATCGCTGAGTGAGGACGGAAGATCACCCATCTCCA
	TCCGCCAGATGGCCTATGTTTCTGGTCTCTCCTTCGGTATCATCAGTGGTGTCTTCTCTGTTATCAA
	TATTTTGGCTGATGCACTTGGGCCAGGTGTGGTTGGGATCCATGGAGACTCACCCTATTACTTCCTG
	ACTTCAGCCTTTCTGACAGCAGCCATTATCCTGCTCCATACCTTTTGGGGAGTTGTGTTCTTTGATG
	CCTGTGAGAGGAGACGGTACTGGGCTTTGGGCCTGGTGGTTGGGAGTCACCTACTGACATCGGGACT
	GACATTCCTGAACCCCTGGTATGAGGCCAGCCTGCTGCCCATCTATGCAGTCACTGTTTCCATGGGG
	CTCTGGGCCTTCATCACAGCTGGAGGGTCCCTCCGAAGTATTCAGCGCAGCCTCTTGTGCCGACGGC
	AGGAGGACAGTCGGGTGATGGTGTATTCTGCCCTGCGCATCCCACCCGAGGACTGAGGGAACCTAGG
	GGGGACCCCTGGGCCTGGGGTGCCCTCCTGATGTCCTCGTCCTGTATTTCTCCATCTCCAGTTCTGG
	ACAG
	ORF Start: ATG at 63		ORF Stop: TGA at 858
	SEQ ID NO:74	265 aa	MW at 28935.5 kD
NOV17b,	MGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFSWLVSLLLASVVWFILVHVTDRSDARL
CG145286-02
Protein Sequence	QYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYVSGLSFGIISGVFSV
	INILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTS
	GLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQRSLLCRRQEDSRVMVYSALRJPPED

[0455] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 17B.

TABLE 17B
Comparison of NOV17a against NOV17b.
	NOV17a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV17b	1 . . . 240	224/265 (84%)
	1 . . . 265	224/265 (84%)

[0456] Further analysis of the NOV17a protein yielded the following properties shown in Table 17C.

TABLE 17C
Protein Sequence Properties NOV17a
PSort analysis:   0.6400 probability located in plasma membrane; 0.4600 probability located in
                  Golgi body; 0.3700 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 63 and 64

[0457] A search of the NOV17a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 17D.

TABLE 17D
Geneseq Results for NOV17a
		NOV17a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB65248	Human PRO1141 (UNQ579)	1 . . . 221	220/246 (89%)	e−120
	protein sequence SEQ ID	1 . . . 246	221/246 (89%)
	NO:303 - Homo sapiens, 247
	aa. [WO200073454-A1,
	Dec. 7, 2000]
AAB94784	Human protein sequence	1 . . . 221	220/246 (89%)	e−120
	SEQ ID NO: 15888 - Homo	1 . . . 246	221/246 (89%)
	sapiens, 247 aa.
	[EP1074617-A2,
	Feb. 7, 2001]
AAM93680	Human polypeptide, SEQ ID	1 . . . 221	220/246 (89%)	e−120
	NO: 3574 - Homo sapiens,	1 . . . 246	221/246 (89%)
	247 aa. [EP1130094-A2,
	Sep. 5, 2001]
AAU29137	Human PRO polypeptide	1 . . . 221	220/246 (89%)	e−120
	sequence #114 - Homo	1 . . . 246	221/246 (89%)
	sapiens, 247 aa.
	[WO200168848-A2,
	Sep. 20, 2001]
AAY57881	Human transmembrane	1 . . . 221	220/246 (89%)	e−120
	protein HTMPN-5 - Homo	1 . . . 246	221/246 (89%)
	sapiens, 247 aa.
	[W09961471-A2,
	Dec. 2, 1999]

[0458] In a BLAST search of public sequence datbases, the NOV17a protein was found to have homology to the proteins shown in the BLASTP data in Table 17E.

TABLE 17E
Public BLASTP Results for NOV17a
		NOV17a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q96B13	Hypothetical 29.0 kDa	1 . . . 240	240/265 (90%)	e−131
	protein (CGI-78 protein) -	1 . . . 265	240/265 (90%)
	Homo sapiens (Human), 265
	aa.
Q9BVG0	Similar to CGI-78 protein -	1 . . . 240	239/265 (90%)	e−131
	Homo sapiens (Human), 265	1 . . . 265	240/265 (90%)
	aa.
Q8R1T3	CGI-78 protein - Mus	1 . . . 240	238/265 (89%)	e−130
	musculus (Mouse), 265 aa.	1 . . . 265	239/265 (89%)
Q969R6	CGI-78 protein - Homo	1 . . . 221	220/246 (89%)	e−119
	sapiens (Human), 247 aa.	1 . . . 246	221/246 (89%)
CAC39761	Sequence 159 from Patent	1 . . . 221	219/246 (89%)	e−118
	EP1067182 - Homo sapiens	1 . . . 246	220/246 (89%)
	(Human), 247 aa.

[0459] PFam analysis predicts that the NOV17a protein contains the domains shown in the Table 17F.

TABLE 17F
Domain Analysis of NOV17a
Pfam Domain	NOV17a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 18

[0460] The NOV18 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 18A.

TABLE 18A
NOV18 Sequence Analysis
	SEQ ID NO:75	644 bp
NOV18a,	GTAATTTACCACCATCTTTGGTTCCTGTTTATAAGATGTTTTAAGAAAGATTTGAAACAGATTTTCT
CG145650-01
DNA Sequence	GAAGAAAGCAGAAGCTCTCTTCCCATTATGACTTCGGAAATCACTTATGCTGAAGTGAGGTTCAAAA
	ATGAATTCAAGTCCTCAGGCATCAACACAGCCTCTTCTGCAGAGACAGCCTGGAGCTGTTGCCCAAA
	GAATTGGAAGTCATTTAGTTCCAACTGCTACTTTATTTCTACTGAATCAGCATCTTGGCAAGACAGT
	GAGAAGGACTGTGCTAGAATGGAGGCTCACCTGCTGGTGATAAACACTCAAGAAGAGCAGGATTTCA
	TCTTCCAGAATCTGCAAGAAGAATCTGCTTATTTTTTGGGGCTCTCAGATCCAGAAGGTCAGCGACA
	TTGGCAATGGGTTGATCAGACGCCATACAATGAAAGTTCCACATTCTGGCATCCACGTGAGCCCAGT
	GATCCCAATGAGCGCTGCGTTGTGCTAAATTTTCGTAAATCACCCAAAAGATGGGGCTGGAATGATG
	TTAATTGTCTTGGTCCTCAAAGGTCAGTTTGTGAGATGATGAAGATCCACTTATGAACTGAACATTC
	TCCATGAACAGGTGGTTGGATTGGTATCTGTCATTGTAGGG
	ORF Start: ATG at 95		ORF Stop: TGA at 590
	SEQ ID NO:76	165 aa	MW at 19294.2 kD
NOV18a,	MTSEITYAEVRFKNEFKSSGINTASSAETAWSCCPKNWKSFSSNCYFISTESASWQDSEKDCARMEA
CG145650-01
Protein Sequence	HLLVINTQEEQDFIFQNLQEESAYFLGLSDPEGQRHWQWVDQTPYNESSTFWHPREPSDPNERCVVL
	NFRKSPKRWGWNDVNCLGPQRSVCEMMKIHL
	SEQ ID NO:77	763 bp
NOV18b,	GTAATTTACCACCATGTTTGGTTCCTGTTTATAAGATGTTTTAAGAAAGATTTGAAACAGATTTTCT
CG145650-02
DNA Sequence	GAAGAAAGCAGAAGCTCTCTTCCCATTATGACTTCGGAAATCACTTATGCTGAAGTGAGGTTCAAAA
	ATGAATTCAAGTCCTCAGGCATCAACACAGCCTCTTCTGCAGCTTCCAAGGAGAGGACTGCCCCTCT
	CAAAAGTAATACCGGATTCCCCAAGCTGCTTTGTGCCTCACTGTTGATATTTTTCCTGCTATTGCCA
	ATCTCATTCTTTATTCCTTTTGTCATTTTCTTTCAAATATTTTTCTCCCCCCAGCTTCTTGAGACTA
	CAAAAGAGCTGGTTCATACAACATTGGAGTGTGTGAAAAAAAATATGCCCGTGGAAGAGACAGCCTG
	GAGCTGTTGCCCAAAGAATTGGAAGTCATTTAGTTCCAACTGCTACTTTATTTCTACTGAATCAGCA
	TCTTGGCAAGACAGTGAGAAGGACTGTGCTAGAATGGAGGCTCACCTGCTGGTGATAAACACTCAAG
	AAGAGCAGGATTTCATCTTCCAGAATCTGCAAGAAGAATCTGCTTATTTTGTGGGGCTCTCAGATCC
	AGAAGGTCAGCGACATTGGCAATGGGTTGATCAGACACCATACAATGATGTTAATTGTCTTGGTCCT
	CAAAGGTCAGTTTGTGAGATGATGAAGATCCACTTATGAACACATTCTCCCATGAAACAGGTGG
	TTGGATTGGTATCTGTCATTGTAGGG
	ORF Start: ATG at 95		ORF Stop: TGA at 707
	SEQ ID NO:78	204 aa	MW at 23462.5 kD
NOV18b,	MTSEITYAEVRFKNEFKSSGINTASSAASKERTAPLKSNTGFPKLLCASLLIFFLLLAISFFIAFVI
CG145650-02
Protein Sequence	FFQKYSQLLEKKTTKELVHTTLECVKKNMPVEETAWSCCPKNWKSFSSNCYFISTESASWQDSEKDC
	ARMEAHLLVINTQEEQDFIFQNLQEESAYFVGLSDPEGQRHWQWVDQTPYNDVNCLGPQRSVCEMMK
	IHL
	SEQ ID NO:79	1308 bp
NOV18c,	CTCACTATACTGGTCCTGAGGAAAGGGCTTCTGTGAACTGCGGTTTTTAGTTTTTATTGTGGTTCTT
CG145650-03
DNA Sequence	AGTTCTCATGAGACCCCTCTTGAGGATATGTGCCTATCTGGTGCCTCTGCTCTCCACTAGTTGAGTG
	AAAGGAAGGAGGTAATTTACCACCATGTTTGGTTCCTGTTTATAAGATGTTTTAAGAAAGATTTGAA
	ACAGATTTTCTGAAGAAAGCAGAAGCTCTCTTCCCATTATGACTTCGGAAATCACTTATGCTGAAGT
	GAGGTTCAAAAATGAATTCAAGTCCTCAGGCATCAACACAGCCTCTTCTGCAGCTTCCAAGGAGAGG
	ACTGCCCCTCTCAAAAGTAATACCGGATTCCCCAAGCTGCTTTGTGCCTCACTGTTGATATTTTTCC
	TGCTATTGGCAATCTCATTCTTTATTGCTTTTGTCATTTTCTTTCAAAAATATTCTCAGCTTCTTGA
	AAAAAAGACTACAAAAGAGCTGGTTCATACAACATTGGAGTGTGTGAAAAAAAATATGCCCGTGGAA
	GAGACAGCCTGGAGCTGTTGCCCAAAGAATTGGAAGTCATTTAGTTCCAACTGCTACTTTATTTCTA
	CTGAATCAGCATCTTGGCAAGACAGTGAGAAGGACTGTGCTAGAATGGAGGCTCACCTGCTGGTGAT
	AAACACTCAAGAAGAGCAGGATTTCATCTTCCAGAATCTGCAAGAAGAATCTGCTTATTTTGTGGGG
	CTCTCAGATCCAGAAGGTCAGCGACATTGGCAATGGGTTGATCAGACACCATACAATGAAAGTTCCA
	CATTCTGGCATCCACGTGAGCCCAGTGATCCCAATGAGCGCTGCGTTGTGCTAAATTTTCGTAAATC
	ACCCAAAAGATGGGGCTGGAATGATGTTAATTGTCTTGGTCCTCAAAGGTCCAGTTTGTGAGATGAT
	GAAGATCCACTTATGAACTGAACATTCTCCATGAACAGGTGGTTGGATTGGTATCTGTCATTGTAGG
	GATAGATAATAAGCTCTTCTTATTCATGTGTAAGGGAGGTCCATAGAATTTAGGTGGTCTGTCAACT
	ATTCTACTTATGAGAGAATTGGTCTGTACATTGACTGATTCACTTTTTCATAAAGTGAGCATTTATT
	GAGCATTTTTTCATGTGCCAGAGCCTGTACTGGAGGCCCCCATTGTGCACACATGGAGAGAACATGA
	GTCTCTCTTAATTTTTATCTGGTTGCTAAAGAATTATTTACCAATAAAATTATATGATGTGGTGAAA
	AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 240		ORF Stop: TGA at 930
	SEQ ID NO:80	230 aa	MW at 26602.8 kD
NOV18c,	MTSEITYAEVRFKNEFKSSGINTASSAASKERTAPLKSNTGFPKLLCASLLIFFLLLAISFFIAFVI
CG145650-03
Protein Sequence	FFQKYSQLLEKKTTKELVHTTLECVKKNMPVEETAWSCCPKNWKSFSSNCYFISTESASWQDSEKDC
	ARMEAHLLVINTQEEQDFIFQNLQEESAYFVGLSDPEGQRHWQWVDQTPYNESSTFWHPREPSDPNE
	RCVVLNFRKSPKRWGWNDVNCLGPQRSSL

[0461] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 18B.

TABLE 18B
Comparison of NOV18a against NOV18b and NOV18c.
	NOV18a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV18b	28 . . . 165	104/138 (75%)
	100 . . . 204	105/138 (75%)
NOV18c	28 . . . 156	128/129 (99%)
	100 . . . 228	129/129 (99%)

[0462] Further analysis of the NOV18a protein yielded the following properties shown in Table 18C

TABLE 18C
Protein Sequence Properties NOV18a
PSort analysis:   0.6868 probability located in microbody (peroxisome); 0.1000 probability
                  located in mitochondrial matrix space; 0.1000 probability located in lysosome
                  (lumen); 0.0000 probability located in endoplasmic reticulum (membrane)
SignalP analysis: No Known Signal Sequence Predicted

[0463] A search of the NOV18a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 18D.

TABLE 18D
Geneseq Results for NOV18a
		NOV18a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABP48034	Human polypeptide SEQ ID	28 . . . 165	137/138 (99%)	3e-84
	NO 464 - Homo sapiens, 243	106 . . . 243	138/138 (99%)
	aa. [US2002042386-A1,
	11-APR-2002]
ABP47873	Human polypeptide SEQ ID	28 . . . 165	137/138 (99%)	3e-84
	NO 303 - Homo sapiens, 246	109 . . . 246	138/138 (99%)
	aa. [US2002042386-A1,
	11-APR-2002]
AAU98014	Human dendritic cell	28 . . . 165	137/138 (99%)	3e-84
	immunoreceptor AJ133532 -	100 . . . 237	138/138 (99%)
	Homo sapiens, 237 aa.
	[WO200232958-A2,
	25-APR-2002]
ABB90277	Human polypeptide SEQ ID	28 . . . 165	137/138 (99%)	3e-84
	NO 2653 - Homo sapiens,	100 . . . 237	138/138 (99%)
	237 aa. [WO200190304-A2,
	29-NOV-2001]
AAU19814	Human novel extracellular	28 . . . 165	137/138 (99%)	3e-84
	matrix protein, Seq ID No	106 . . . 243	138/138 (99%)
	464 - Homo sapiens, 243 aa.
	[WO200155368-A1,
	02-AUG-2001]

[0464] In a BLAST search of public sequence datbases, the NOV18a protein was found to have homology to the proteins shown in the BLASTP data in Table 18E.

TABLE 18E
Public BLASTP Results for NOV18a
		NOV18a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9H2Z9	C-type lectin DDB27 short	1 . . . 165	163/204 (79%)	8e-93
	form - Homo sapiens	1 . . . 204	165/204 (79%)
	(Human), 204 aa.
Q9UMR7	Dendritic cell	28 . . . 165	137/138 (99%)	9e-84
	immunoreceptor - Homo	100 . . . 237	138/138 (99%)
	sapiens (Human), 237 aa.
Q9UI34	C-type lectin superfamily 6 -	28 . . . 165	137/138 (99%)	9e-84
	Homo sapiens (Human), 237	100 . . . 237	138/138 (99%)
	aa.
Q9NS33	HDCGC13P - Homo sapiens	28 . . . 165	136/138 (98%)	3e-83
	(Human), 237 aa.	100 . . . 237	137/138 (98%)
Q8WXW9	Fc-epsilon receptor III -	28 . . . 156	128/129 (99%)	5e-78
	Homo sapiens (Human), 230	100 . . . 228	129/129 (99%)
	aa.

[0465] PFam analysis predicts that the NOV18a protein contains the domains shown in the Table 18F.

TABLE 18F
Domain Analysis of NOV18a
		Identities/
		Similarities
Pfam Domain	NOV18a Match Region	for the Matched Region	Expect Value
lectin_c	51 . . . 160	34/127 (27%)	5.8e-28
			85/127 (67%)

Example 19

[0466] The NOV19 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 19A.

TABLE 19A
NOV19 Sequence Analysis
	SEQ ID NO:81	661 bp
NOV19a,	CTCCTGTAACCCTCCTCCAGGATGAACCACCTGCCAGAAGACATGGAGAACGCTCTCACCGGGAGCC
CG145836-01
DNA Sequence	AGAGCTCCCATGCTTCTCTGCGCAATATCCATTCCATCAACCCCACACAACTCATGGCCAGGATTGA
	GTCCTATGAAGGAAGGGAAAAGAAAGGCATATCTGATGTCAGGAGGACTTTCTGTTTGTTTGTCACC
	TTTGACCTCTTATTCGTAACATTACTGTGGATAATAGAGTTAAATGTGAATGGAGGCATTGAGAACA
	CATTAGAGAAGGAGGTGATGCAGTATGACTACTATTCTTCATATTTTGATATATTTCTTCTGGCAGT
	TTTTCGATTTAAAGTGTTAATACTTGCATATGCTGTGTGCAGACTGCCCATCATTTCATTCATCCTT
	GCCTGGATTGAGACGTGGTTCCTGGATTTCAAAGTGTTACCTCAAGAAGCAGAAGAAGAAAACAGAC
	TCCTGATAGTTCAGGATGCTTCAGAGAGGGCAGCACTTATACCTGGTGGTCTTTCTGATGGTCAGTT
	TTATTCCCCTCCTGAATCCGAAGCAGGATCTGAAGAAGCTGAAGAAAAACAGGACAGTGAGAAACCA
	CTTTTAGAACTATGAGTACTACTTTTGTTAAATGTGAAAAACCCTCACAGAAAGTCAT
	ORF Start: ATG at 22		ORF Stop: TGA at 616
	SEQ ID NO:82	198 aa	MW at 22691.5 kD
NOV19a,	MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVT
CG145836-01
Protein Sequence	LLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLPIISFILAWIETWF
	LDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL
	SEQ ID NO:83	768 bp
NOV19b,	CTCCTGTAACCCTCCTCCAGGATGAACCACCTGCCAGAAGACATGGAGAACGCTCTCACCGGGAGCC
CG145836-02
DNA Sequence	AGAGCTCCCATGCTTCTCTGCGCAATATCCATTCCATCAACCCCACACAACTCATGGCCAGGATTGA
	GTCCTATGAAGGAAGGGAAAAGAAAGGCATATCTGATGTCGGGAGGACTTTCTGTTTGTTTGTCACC
	TTTGACCTCTTATTCGTAACATTACTGTGGATAATAGAGTTAAATGTGAATGGAGGCATTGAGAACA
	CATTAGAGAAGGAGGTGATGCAGTATGACTACTATTCTTCATATTTTGATATATTTCTTCTGGCAGT
	TTTTCGATTTAAAGTGTTAATACTTGCATATGCTGTGTGCAGACTGCGCCATTGGTGGGCAATAGCG
	TTGACAACGGCAGTGACCAGTGCCTTTTTACTAGCAAAAGTGATCCTTTCGAAGCTTTTCTCTCAAG
	GGGCTTTTGGCTATGTGCTGCCCATCATTTCATTCATCCTTGCCTGGATTGAGACGTGGTTCCTGGA
	TTTCAAAGTGTTACCTCAAGAAGCAGAAGAAGAAAACAGACTCCTGATAGTTCAGGATGCTTCAGAG
	AGGGCAGCACTTATACCTGGTGGTCTTTCTGATGGTCAGTTTTATTCCCCTCCTGAATCCGAAGCAG
	GATCTGAAGAAGCTGAAGAAAAACAGGACAGTGAGAAACCACTTTTAGAACTATGAGTACTACTTTT
	GTTAAATGTGAAAAACCCTCACAGAAAGTCAT
	ORF Start: ATG at 22		ORF Stop: TGA at 724
	SEQ ID NO:84	234 aa	MW at 26555.1 kD
NOV19b,	MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVGRTFCLFVTFDLLFVT
CG145836-02
Protein Sequence	LLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALTTAVTS
	AFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPG
	GLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL

[0467] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 19B.

TABLE 19B
Comparison of NOV19a against NOV19b.
	NOV19a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV19b	1 . . . 198	167/234 (71%)
	1 . . . 234	167/234 (71%)

[0468] Further analysis of the NOV19a protein yielded the following properties shown in Table 19C.

TABLE 19C
Protein Sequence Properties NOV19a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in mitochondrial inner membrane
SignalP analysis: Cleavage site between residues 3 and 4

[0469] A search of the NOV19a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 19D.

TABLE 19D
Geneseq Results for NOV19a
		NOV19a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAM39930	Human polypeptide SEQ ID	1 . . . 198	198/216 (91%)	e-107
	NO 3075 - Homo sapiens,	1 . . . 216	198/216 (91%)
	216 aa. [WO200153312-A1,
	26-JUL-2001]
ABB84847	Human PRO1864 protein	1 . . . 198	198/234 (84%)	e-105
	sequence SEQ ID NO:62 -	1 . . . 234	198/234 (84%)
	Homo sapiens, 234 aa.
	[WO200200690-A2,
	03-JAN-2002]
ABB95453	Human angiogenesis related	1 . . . 198	198/234 (84%)	e-105
	protein PRO1864 SEQ ID	1 . . . 234	198/234 (84%)
	NO: 62 - Homo sapiens, 234
	aa. [WO200208284-A2,
	31-JAN-2002]
AAB87532	Human PRO 1864 - Homo	1 . . . 198	198/234 (84%)	e-105
	sapiens, 234 aa.	1 . . . 234	198/234 (84%)
	[WO200116318-A2,
	08-MAR-2001]
AAM41716	Human polypeptide SEQ ID	1 . . . 198	198/234 (84%)	e-105
	NO 6647 - Homo sapiens,	5 . . . 238	198/234 (84%)
	238 aa. [WO200153312-A1,
	26-JUL-2001]

[0470] In a BLAST search of public sequence datbases, the NOV19a protein was found to have homology to the proteins shown in the BLASTP data in Table 19E.

TABLE 19E
Public BLASTP Results for NOV19a
		NOV19a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
O95772	H_NH1021A09.1 protein	1 . . . 198	198/234 (84%)	e-105
	(Unknown) (Protein for	1 . . . 234	198/234 (84%)
	MGC: 14607) (Similar to
	steroidogenic acute regulatory
	protein related) - Homo
	sapiens (Human), 234 aa.
Q99J63	Similar to RIKEN cDNA	1 . . . 198	186/235 (79%)	1e-96
	0610035N01 gene - Mus	1 . . . 235	191/235 (81%)
	musculus (Mouse), 235 aa.
Q9DCI3	0610035N01Rik protein - Mus	1 . . . 198	185/235 (78%)	3e-96
	musculus (Mouse), 235 aa.	1 . . . 235	190/235 (80%)
Q9D356	6530409L22Rik protein - Mus	30 . . . 193	145/200 (72%)	2e-73
	musculus (Mouse), 272 aa.	39 . . . 238	151/200 (75%)
Q61542	MLN 64 protein (ES 64	7 . . . 193	105/224 (46%)	1e-45
	protein) (StarD3) - Mus	11 . . . 229	133/224 (58%)
	musculus (Mouse), 446 aa.

[0471] PFam analysis predicts that the NOV19a protein contains the domains shown in the Table 19F.

TABLE 18F
Domain Analysis of NOV19a
		Identities/
		Similarities
		for the Matched
Pfam Domain	NOV19a Match Region	Region	Expect Value

Example 20

[0472] The NOV20 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 20A.

TABLE 20A
NOV20 Sequence Analysis
	SEQ ID NO:85	3157 bp
NOV20a,	GCGGCAGTAGCAGCCATGCTGCCCTTTCTGCTGGCCACACTGGGCACCACAGCCCTCAACAACAGCA
CG145978-01
DNA Sequence	ACCCCAAGGACTACTGCTACAGCGCCCGCATCCGCAGCACTGTCCTGCAGGGCCTGCCCTTTGGGGG
	CGTCCCCACCGTGCTGGCTCTCGACTTCATGTGCTTCCTTTTCCCTCAGGCACTGCTGTTCTTATTC
	TCTATCCTCCGGAAGGTGGCCTGGGACTATGGGCGGCTGGCCTTGGTGACAGATGCAGACAGCCATG
	ACCGGTATGAGCGTCTCACCTCTGTCTCCAGCTCCGTTGACTTTGACCAAAGGGACAATGTGGGTTT
	CTGTTCCTGGCTGACAGCCATCTTCAGGATAGATGATGAGATCCGGGACAAATGTGGGGGCGATGCC
	GTGCACTACCTGTCCTTTCAGCGGCACATCATCGGGCTGCTGGTGGTTGTGGGCGTCCTCTCCGTAG
	GCATCGTGCTGCCTGTCAACTTCTCAGGGGACCTGCTGGAGAACAATGCCTACAGCTTTGGGAGAAC
	CACCATTGCCAACTTGAAATCAGGGAACAACCTGCTATGGCTGCACACCTCCTTCGCCTTCCTGTAT
	CTGCTGCTCACCGTCTACAGCATGCGTAGACACACCTCCAAGATGCGCTACAAGGAGGATGATCTGG
	TGCGTCGGACCCTCTTCATCAATGGAATCTCCAAATATGCAGAGTCAGAAAAGATCAAGAAGCATTT
	TAGGGAAGCCTACCCCAACTGCACAGTTCTCGAAGCCCGCCCGTGTTACAACGTGGCTCGCCTAATG
	TTCCTCGATGCAGAGAGGAAGAAGGCCGAGCGGGGAAAGCTGTACTTCACAAACCTCCAGAGCAAGG
	AGAACGTGCCTACCATGATCAACCCCAAGCCCTGTGGCCACCTCTGCTGCTGTGTGGTGCGAGGCTG
	TGAGGAGGCCATTGAGTACTACACAAAGCTGGAGCAGAAGCTGAAGGAAGACTACAAGCGGGAGAAG
	GAGAAGGTGAATGAGAAGCCTCTTGGCATGGCCTTTGTCACCTTCCACAATGAGACTATCATCCTGA
	AGGACTTCAACGTGTGTAAATGCCAGGGCTCCACCTGCCGTGGGGACCCACGCCCCTCATCCTGCAG
	CGACTCCCTCCACATCTCCAACTGGACCGTGTCCTATGCCCCTGACCCTCAGAACATCTACTGGGAG
	CACCTCTCCATCCGACGCTTCATCTCGTGGCTGCGCTGCCTGGTCATCAATGTCGTCCTCTTCATCC
	TCCTCTTCTTCCTCACCACTCCAGCCATCATCATCACCACCATGGACAAGTTCAACGTCACCAAGCC
	TGTGGAGTACCTCAACAACCCCATCATCACCCAGTTCTTCCCCACCCTGCTCCTGTGGTGCTTCTCG
	GCCCTCCTTCCCACCATCGTCTACTACTCAGCCTTCTTTGAAGCCCACTGGACACGGTCCAGCTCTG
	GGGAGAACAGGACAACCATGCACAAGTGCTACACTTTCCTCATCTTCATGGTGCTGCTCCTACCCTC
	GCTGGGACTGAGCAGCCTGGACCTCTTCTTCCGCTGGCTCTTTGATAAGAAATTCTTGGCTGAGGCA
	GCTATTCGGTTTGAGTGTGTGTTCCTGCCCGACAACGGCGCCTTCTTCGTGAACTACGTCATTGCCT
	CAGCCTTTATCGGCAACGCCATGGACCTGCTGCGCATCCCAGGCCTGCTCATGTACATGATCCGGCT
	CTGCCTGGCGCGCTCGGCCGCCGACAGGCGCAACGTGAAGCAGCATCAGGCCTACGAGTTCCAGTTT
	GGCGCAGCCTACGCCTGGATGATGTGCGTCTTCACGGTGGTCATGACCTACAGTATCACCTGCCCCA
	TCATCGTGCCCTTCGGGCTCATGTACATGCTGCTGAAGCACCTGGTAGACAGCTACAATCTCTACTA
	CGCCTACCTGCCGGCCAAGCTGGACAACAAGATCCACTCGGGGGCTGTGAACCAGGTGGTGGCCCCG
	CCCATCCTCTGCCTCTTCTGGCTGCTCTTCTTTTCCACCATGCGCACGGGGTTCCTAGCTCCCACGT
	CTATGTTCACATTTGTCGTCCTGGTCATCACCATCGTCATCTGTCTCTGCCACGTCTGCTTTCGACA
	CTTCAAATACCTCAGTGCCCACAACTACAAGATTGACCACACGGAGACAGATACTGTGGACCCCAGA
	AGCAATGGACGGCCCCCCACTGCTGCTGCTGTCCCCAAATCTGCGAAATACATCGCTCAGGTGCTGC
	AGGACTCAGAGGTGGACGGGGATGGGGATGGGGCTCCTGGGAGCTCAGGGGATGAGCCCCCATCATC
	CTCATCCCAAGATGAGGAGTTGCTGATGCCACCCGACGCCCTCACGGACACAGACTTCCAGTCTTGC
	GAGGACAGCCTCATAGAGAATGAGATTCACCAGTAAGGGGAGGGAGGGGCCCTGGAGGCCACATCCT
	GCCCCACCCCACCCCCACTCCCACGGACACTAAAACGCTAATAATTTATTAGATCTAAAGCCCCTTC
	CTCCCCAGCCCCTGCTTTCATTAAGGTATTTAAACTTGGGGGTTTCACTGCTCTCCCCCCATGATGG
	AGGGAGGGAGCCCCCCAACCTCAGTGAGGAGAGCCCAGAGCCGGCCCCGGGGCAAAGAGGCGTGCAG
	AGGGAGTTCCCCCAGATCAGTACCCCCAACACCTCACCACATAGTAGCAAGCACCAAAACAGGGTTA
	ATGAGAGCCAAGAGGAGTACCTGGTGCACCTGGTGCCGGTGGCTGGAGACCTGGGGGGCAGGTGGAT
	CTGGGGCTGTTCCCCCCCCTCCGTTTTTTCCACCCCACAGTTCCTCCTGGCATCTGGCCCTCCAGGG
	AAGTGGAGCCTCCAGCCCCTAGGGGATGCATGAGGGGGGAGGGGGTGCTGAGTGGCAGGAAGAGTCA
	GGCTCACAGCTGGGGTGGCCTGGGGGTGGGGGTGGGCAAGGCTGACACTGGAAAATGGGTTTTTGCA
	CTGTTTTTTTTTTGGTTTTTTTGTTCTTTTTTGTTTTTTTCCTTTAAAATAAAAACAAAGAAAAGCT
	CTGAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
	AAAAAAAG
	ORF Start: ATG at 16		ORF Stop: TAA at 2446
	SEQ ID NO:86	810 aa	MW at 92305.1 kD
NOV20a,	MLPFLLATLGTTALNNSNPKDYCYSARIRSTVLQGLPFGGVPTVLALDFMCFLFPQALLFLFSILRK
CG145978-01
Protein Sequence	VAWDYGRLALVTDADSHDRYERLTSVSSSVDFDQRDNVGFCSWLTAIFRIDDEIRDKCGGDAVHYLS
	FQRHIIGLLVVVGVLSVGIVLPVNFSGDLLENNAYSFGRTTIANLKSGNNLLWLHTSFAFLYLLLTV
	YSMRRHTSKMRYKEDDLVRRTLFINGISKYAESEKIKKHFREAYPNCTVLEARPCYNVARLMFLDAE
	RKKAERGKLYFTNLQSKENVPTMINPKPCGHLCCCVVRGCEEAIEYYTKLEQKLKEDYKREKEKVNE
	KPLGMAFVTFHNETIILKDFNVCKCOGCTCRGEPRPSSCSESLHISNWTVSYAPDPONIYWEHLSIR
	GFIWWLRCLVINVVLFILLFFLTTPAIIITTMDKFNVTKPVEYLNNPIITQFFPTLLLWCFSALLPT
	IVYYSAFFEAHWTRSSSGENRTTMHKCYTFLIFMVLLLPSLGLSSLDLFFRWLFDKKFLAEAAIRFE
	CVFLPDNGAFFVNYVIASAFIGNAMDLLRIPGLLMYMIRLCLARSAAERRNVKQHQAYEFQFGAAYA
	WMMCVFTVVMTYSITCPIIVPFGLMYMLLKHLVDRYNLYYAYLPAKLDKKIHSGAVNQVVAAPILCL
	FWLLFFSTMRTGFLAPTSMFTFVVLVITIVICLCHVCFGHFKYLSAHNYKIEHTETDTVDPRSNGRP
	PTAAAVPKSAKYIAQVLQDSEVDGDGDGAPGSSGDEPPSSSSQDEELLMPPDALTDTDFQSCEDSLI
	ENEIHQ
	SEQ ID NO:87	1864 bp
NOV20b	GCCGCCCAGCGACTCCCCCTCCCCCTCCCCCAGCCCCGCCCCGCCCCAACCCGGGGCTCCGAGCCGG
CG145978-02	AGCCGAGTCTGCGCCTGGGGGAGGACCATGCGGCAGTAGCAGCCATGCTGCCCTTTCTGCTGGCCAC
DNA Sequence
	ACTGGGCACCACAGCCCTCAACAACAGCAACCCCAAGGACTACTGCTACAGCGCCCGCATCCGCAGC
	ACTGTCCTGCAGGGCCTGCCCTTTGGGGGCGTCCCCACCGTGCTGGCTCTCGACTTCATGTGCTTCC
	TTCCTCAGGCACTGCTGTTCTTATTCTCTATCCTCCGGAAGGTGGCCTGGGACTATGGGCGGCTGGC
	CTTGGTGACAGATGCAGACAGGCTTCGGCGGCAGGAGAGGGACCGAGTGGAACAGGAATATGTGGCT
	TCAGCTATGCACGGGGACAGCCATGACCGGTATGAGCGTCTCACCTCTGTCTCCAGCTCCGTTGACT
	TTGACCAAAGGGACAATGTGGGTTTCTGTTCCTGGCTGACAGCCATCTTCAGGATAAAGGATGATGA
	GATCCGGGACAAATGTGGGGGCGACGCCGTGCACTACCTGTCCTTTCAGCGGCACATCATCGGGCTG
	CTGGTGGTTGTGGGCGTCCTCTCCGTAGGCATCGTGCTGCCTGTCAACTTCTCAGGGGACCTGCTGG
	AGAACAATGCCTACAGCTTTGGGAGAACCACCATTGCCAACTTGAAATCAGGGAACAACCTGCTATG
	GCTGCACACCTCCTTCGCCTTCCTGTATCTGCTGCTCACCGTCTACAGCATGCGTAGACACACCTCC
	AAGATGCGCTACAAGGAGGATGATCTGGTGCGTCGGACCCTCTTCATCAATGGAATCTCCAAATATG
	CAGAGTCAGAAAAGATCAAGAAGCATTTTAGGGAAGCCTACCCCAACTGCACAGTTCTCGAAGCCCG
	CCCGTGTTACAACGTGGCTCGCCTAATGTTCCTCGATGCAGAGAGGAAGAAGGCCGAGCGGGGAAAG
	CTGTACTTCACAAACCTCCAGAGCAAGGAGAACGTGCCTACCATGATCAACCCCAAGCCCTGTGGCC
	ACCTCTGCTGCTGTGTGGTGCGAGGCTGTCAGCAGGTGGACCCCATTGAGTACTACACAAAGCTGGA
	GCAGAAGCTGAAGGAAGACTACAAGCGGGAGAATTGGAGGGTGAATGAGAAGCCTCTTGGCATGGCC
	TTTGTCACCTTCCACAATGAGACTATCACCGCCATGATCCCCTGGGACTTCAACGTGTGTAAATGCC
	AGGGCTGCACCTGCCGTGGGGAGCCACGCCCCTCATCCTGCAGCGAGTCCCTGCACATCTCCAACTG
	GACCGTGTCCTATGCCCCTGACCCTCAGAACATCTACTGGGAGCACCTCTCCATCCGAGGCTTCATC
	TGGTGGCTGCGCTGCCTGGTCATCAATGTCGTCCTCTTCATCCTCCTCTTCTTCCTCACCACTCCAG
	CCATCATCATCACCACCATGGACAAGTTCAACGTCACCAAGCCTGTGGAGTACCTCAACGTGAGGCC
	TCATGCCCCTGTCACTTTCCACGCTGGGTCACAACACACAGATACCAGGCCCTGATCCCTCTTCCAC
	TTGCCCAGCCCAGCCCGTTCTGCTTGTTCCAACCCCGTGCCACCAACCAGCTCCCAAAAACCCCTGT
	GTGCACTTCCCTTGGGCTCCCTGCCACCTTCCCCCTGAGAGAGGCCACCCTCAGGTGTGCAACACCT
	GGAGAAACACCCAGGTAAGAGAGAGAGCCTGCATTTAGTCCTGATCTCAGAGAAGTCCCCTTCCCTC
	ACCCCTCAGTCTAACTGAAAAAATGGAAAGGTTTGACTAGAAAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 112		ORF Stop: TGA at 1594
	SEQ ID NO:88	494 aa	MW at 56686.9 kD
NOV20b,	MLPFLLATLGTTALNNSNPKDYCYSARIRSTVLQGLPFGGVPTVLALDFMCFLPQALLFLFSILRKV
CG145978-02
Protein Sequence	AWDYGRLALVTDADRLRRQERDRVEQEYVASAMHGDSHDRYERLTSVSSSVDFDQRDNVGFCSWLTA
	IFRIKDDEIRDKCGGDAVHYLSFQRHIIGLLVVVGVLSVGIVLPVNFSGDLLENNAYSFGRTTIANL
	KSGNNLLWLHTSFAFLYLLLTVYSMRRHTSKMRYKEDDLVRRTLFINGISKYAESEKIKKHFREAYP
	NCTVLEARPCYNVARLMFLDAERKKAERGKLYFTNLQSKENVPTMINPKPCGHLCCCVVRGCEQVEA
	IEYYTKLEQKLKEDYKREKEKVNEKPLGMAFVTFHNETITAIILKDFNVCKCQGCTCRGEPRPSSCS
	ESLHISNWTVSYAPDPQNIYWEHLSIRGFIWWLRCLVINVVLFILLFFLTTPAIIITTMDKFNVTKP
	VEYLNVRPHAPVTFHAGSQHTDTRP

[0473] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 20B.

TABLE 20B
Comparison of NOV20a against NOV20b.
	NOV20a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV20b	1 . . . 447	394/475 (82%)
	1 . . . 474	394/475 (82%)

[0474] Further analysis of the NOV20a protein yielded the following properties shown in Table 20C.

TABLE 20C
Protein Sequence Properties NOV20a
PSort analysis:   0.6400 probability located in plasma membrane; 0.4600 probability located in
                  Golgi body; 0.3700 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 14 and 15

[0475] A search of the NOV20a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 20D.

TABLE 20D
Geneseq Results for NOV20a
		NOV20a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB97369	Novel human protein SEQ ID	291 . . . 792	499/507 (98%)	0.0
	NO: 637 - Homo sapiens, 541	1 . . . 505	500/507 (98%)
	aa. [WO200222660-A2,
	Mar. 21, 2002]
AAB94004	Human protein sequence	19 . . . 745	445/735 (60%)	0.0
	SEQ ID NO: 14117 - Homo	27 . . . 755	565/735 (76%)
	sapiens, 807 aa.
	[EP1074617-A2,
	Feb. 7, 2001]
AAB42245	Human ORFX ORF2009	19 . . . 472	440/482 (91%)	0.0
	polypeptide sequence SEQ	3 . . . 480	442/482 (91%)
	ID NO:4018 - Homo sapiens,
	480 aa. [WO200058473-A2,
	Oct. 5, 2000]
ABG63456	Human albumin fusion	493 . . . 810	316/318 (99%)	0.0
	protein #131 - Homo sapiens,	1 . . . 318	318/318 (99%)
	318 aa. [WO200177137-A1,
	Oct. 18, 2001]
AAG71250	Human gene 8-encoded	493 . . . 810	316/318 (99%)	0.0
	secreted protein HCEIE80,	1 . . . 318	318/318 (99%)
	SEQ ID NO:98 - Homo
	sapiens, 318 aa.
	[WO200132674-A1,
	May 10, 2001]

[0476] In a BLAST search of public sequence datbases, the NOV20a protein was found to have homology to the proteins shown in the BLASTP data in Table 20E.

TABLE 20E
Public BLASTP Results for NOV20a
		NOV20a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
CAD38916	Hypothetical protein - Homo	167 . . . 681	510/520 (98%)	0.0
	sapiens (Human), 519 aa	1 . . . 518	512/520 (98%)
	(fragment).
AAH30245	KIAA0792 gene product -	19 . . . 745	449/735 (61%)	0.0
	Homo sapiens (Human), 807	27 . . . 755	570/735 (77%)
	aa.
O94886	KIAA0792 protein - Homo	19 . . . 745	448/735 (60%)	0.0
	sapiens (Human), 807 aa.	27 . . . 755	569/735 (76%)
Q91YT8	Hypothetical 91.9 kDa	19 . . . 745	446/735 (60%)	0.0
	protein - Mus musculus	27 . . . 754	570/735 (76%)
	(Mouse), 804 aa.
BAC04207	CDNA FLJ36310 fis, clone	1 . . . 447	440/475 (92%)	0.0
	THYMU2005001 - Homo	1 . . . 471	441/475 (92%)
	sapiens (Human), 491 aa.

[0477] PFam analysis predicts that the NOV20a protein contains the domains shown in the Table 20F.

TABLE 20F
Domain Analysis of NOV20a
		Identities/
		Similarities
Pfam Domain	NOV20a Match Region	for the Matched Region	Expect Value
DUF221	327 . . . 787	109/493 (22%)	1.1e−84
		365/493 (74%)

Example 21

[0478] The NOV21 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 21A.

TABLE 21A
NOV21 Sequence Analysis
	SEQ ID NO: 89	8700 bp
NOV21a,	GCTGATTGAGACACTATGTTGAGTCTACAGGATTCTGTGTTTTTTGAAATTAGCATAAAGTCCTTGT
CG145997-01
DNA Sequence	TAAAGTCCTGGAGCAGCAGCATGTCAAACATTACGATTGACCCAGATGTCAAACCTGGTGAATATGT
	CATCAAGAGCCTCTTTGCAGAATTTGCTGTTCAAGCTGAAAAGAAAATTGAAGTTGTAATGGCCGAA
	CCCTTGGAGAAGCTATTGTCCAGATCTCTTCAGAGGGGTGAAGATCTTCAGTTTGATCAGGTAATAA
	GCTCTATGAGCTCAGTAGCAGAGCACTGTCTCCCTTCCTTACTTCGCACCTTGTTTGACTGGTACAG
	ACGCCAAAATGGAACGGAAGATGAATCTTATGAATATAGGCCTCGGTCTAGCACAAAGTCTAAGGAT
	GAACAGCAACGTGAAAGAGATTATCTTCTTGAAAGGAGGGACTTAGCAGTAGACTTCATTTTTTGTT
	TAGTTTTAGTTGAAGTTCTAAAGCAGATTCCTGTTCATCCTGTACCCGATCCCTTAGTTCATGAAGT
	TCTAAACTTAGCTTTTAAGCACTTTAAACATAAGGAAGGGGGAACCAACACTGGGAATGTGCATATT
	ATTGCTGATTTATATGCAGAGGTGATAGGGGTTCTTGCCCAATCAAAGTTTCAGGCTGTAAGGAAGA
	AGTTTGTGACAGAATTAAAAGAACTGCGACAAAAGGAACAAAGCCCACATGTGGTACAAAGTGTCAT
	CAGCTTAATAATGGGAAATGAATTTTTTCGAGTAAAAATGTATCCTGTAGAAGATTTTGAAGCATCA
	TTTCAATTTATGCAGGAATGTGCTCAGTATTTCTTAGAAGTGAAAGATAAAGATATAAAACATGCAC
	TTGCTGGTTTATTTGTGGAGATTCTTATCCCTGTAGTTAAAAATGAAGTGAATGTTCCCTGTTTGAA
	AAATTTTGTGGAGATGCTTTATCAGACTACTTTTGAACTGAGCTCGAGAAAGAAGCATTCATTGGTA
	TTAAATAAAGATCCGAAAATGTCTCGAGTTGCACTGGAATCTTTGTATAGATTATTGTGGGTTTATG
	TAATTAGAATAAAATGTGAAAGCAACACTGTAACTCAAAGTCGTCTTATGAGCATAGTGTCAGCACT
	TTTTCCAAAAGGCTCACGAAGTGTGGTTCCTCGTGACACACCTCTCAATATATTTGTGAAGATTATT
	CAGTTCATTGCTCAGGAACGCTTGGATTTTGCAATGAAAGAAATAATATTTGATCTTCTCAGTGTTG
	GAAAATCTACTAAAACTTTCACCATTAATCCAGAGTGTCTAGCATATGTAATATGTTTCTTATTAAA
	TCCTGTTGTATTTTTCACGGGGGAAAGAAAACCCAAGATTGATTTGTTTAGAACTTGTATTGCTGCG
	ATTCCAAGGTTGATTCCTGACGGTATGAGCAGAACTGACCTGATTGAATTGTTAGCAAGGCTCACAA
	TTCATATGGATGAAGAACTGCGTGCTCTGGCTTTCAATACTCTGCAGGCACTAATGCTTGATTTTCC
	AGATTGGCGGGAGGATGTTCTTTCAGGATTTGTTTATTTTATTGTTCGTGAAGTGACTGATGTCCAT
	CCCACACTTCTTGATAATGCCGTAAAGATGTTGGTACAATTAATAAATCAGTGGAAACAAGCAGCCC
	AAATGCATAATAAAAACCAGGACACTCAGGTACCAGATTCTTTTCTAGTAGCTAATGGAGCTTCTCA
	TCCCCCTCCTCTGGAAAGGAGCCCATATTCCAATGTATTCCATGTGGTTGAAGGCTTTGCGCTTCTC
	ATTCTCTGTAGCAGTCGACCTGCCACTAGGAGACTAGCCGTCAGTGTCCTTAGAGAAATACGGGCTT
	TATTTGCACTTCTGGAAATACCTAAGGGTGATGATGAATTAGCCATAGATGTGATGGACAGGCTAAG
	CCCATCCATTCTTGAGAGTTTCATACATCTCACTGGGGCTGATCAGGTAACTATATCGATAGATTTA
	CAAACTTTAGCAGAATGGAACTCTTCTCCTATTAGCCACCAGTTTGATGTGATTAGTCCATCACATA
	TATGGATATTTGCACATGTGACCCAAGGCCAAGACCCATGGATTATAAGTCTCTCCAGTTTTTTAAA
	GCAAGAAAATCTTCCTAAACACTGCTCTACAGCTGTGAGCTATGCTTGGATGTTTGCATACACAAGA
	CTTCAGTTGTTGTCCCCTCAGGTCGATAGTAGCCCCATCAATGCTAAGAAAGTAAATACCACCACAA
	GCAGTGACTCATACATTGGCCTGTGGAGAAACTATCTGATCCTTTGCTGCAGTGCAGCAACATCGTC
	ATCTTCCACATCTGCAGGTTCTGTGAGATGTTCTCCTCCTGAGACGCTGGCGTCTACCCCAGATAGC
	GGCTATAGCATTGATTCTAAAATTGGCATCCCATCCCCTTCATCCTTGTTTAAGCACATAGTTCCAA
	TGATGCGTTCTGAGAGCATGGAAATCACAGAATCCCTTGTTCTAGGTCTTGGCAGGACCAACCCAGG
	AGCTTTTAGGAATATGAAACGGCGCAGGCGTCGAGACATTTTACGAGTACAACTGGTACGAATATTT
	GAACTGCTGGCAGATGCTGGTGTCATTAGTAGTGCAAGTGGTGGCCTTGATAATGAAACACATTTTC
	TCAACAACACTTTATTGGAATATGTAGATTTAACTAGACAACTCCTGGAAGCAGAAAATGAAAAAGA
	CTCTGACACACTGAAGGATATACGATGCCATTTTAGTGCCTTAGTGGCGAATATTATTCAGAATGTT
	CCAGTGCACCAGAGAAGAAGTATTTTTCCTCAACAGAGCCTTCGTCACAGTCTATTTATGCTGTTCA
	GTCACTGGGCAGGTCCTTTTAGCATCATGTTTACGCCCTTGGACAGATACAGTGATAGAAATATGCA
	AATTAATAGACATCAATACTGTGCGTTAAAGGCTATGTCTGCTGTACTGTGTTGTGGCCCTGTTGCA
	GATAATGTAGGACTTTCATCAGATGGCTATTTGTACAAATGGTTGGATAACATTTTGGATTCTCTGG
	ACAAAAAGGTTCACCAGCTGGGCTGTGAAGCAGTTACGTTGTTACTGGAGCTGAACCCTGATCAGAA
	CAACCTGATGTACTGGGCCAGGGATTATCAATGTGACACAGTGATGCTTCTAAATCTGATACTGTTT
	AAAGCAGCTGATTCTTCTAGAAGTATCTATGAAGTTGCTATGCAACTTTTACAGATTCTGGAACCGA
	AGATGTTTCGCTATGCTCACAAATTGGAGGTTCAGAGAACAGATGGAGTACTCAGCCAGCTGTCTCC
	TCTACCACATCTCTATTCTGTTTCATATTATCAGTTGTCCGAGGAACTAGCAAGGGCGTATCCTGAG
	CTAACTCTCGCCATATTCTCAGGTAAGCCAGAGAATCCAGACAGCTCACCCTGCTGGGCGGCAGGTG
	ATGCTGCACTACCTGCTACCATGGATGAACAACATCGAGCTGGTGGACTGCAAGCTCCGCCTCCCGG
	GTTCACGCCATTCTCCGATGATTCCTTAAAAGACCGAGAACTTATGGTGACTAGTAGGCGCTGGTTA
	CGGGGAGAAGGATGGGGATCTCCACAAGCCACTGCAATGGTTTTGAACAATCTGATGTATATGACAG
	CAAAGTATGGCGATGAACTGGCCTGGTCGGAGGTGGAGAATGTGTGGACCACACTTGCAGATGGCTG
	GCCCAAAAACCTGAAAATAATTTTGCACTTTTTGATCAGCATTTGTGGGGTGAATAGCGAACCAAGC
	CTCTTGCCTTACGTAAAGAAGGTCATTGTATATTTAGGTAGAGATAAAACAATGCAGTTGCTAGAAG
	AGCTGGTGAGTGAGCTTCAGCTGACCGATCCTGTCAGTTCAGGGGTCACTCACATGGATAATCCCCC
	GTATTATCGCATCACTTCCAGCGCTTTGTCTTTGATTACAGGAACTACTTCCAGTAGCAATACAATG
	GTAGCTCCCACAGATGGCAATCCTGATAATAAGCCCATTAAAGAGAATATTGAAGAGAGGACCAGTC
	ATTTGAATCGGCAACATCCCAGCCTAGAATCCCGATACAGTAGCAGCTCTGGAGGATCTTATGAAGA
	AGAAAAAAGTGATTCAATGCCACTTTATTCTAATTGGCGACTGAAAGTGATGGAGCATAACCAAGGA
	GAGCCACTGCCCTTCCCACCAGCTGGAGGCTGCTGGTCACCACTGGTGGATTACGTGCCTGAAACGT
	CATCACCTGGATTACCTCTTCACAGGTGTAACATAGCAGTGATCCTTTTGACTGATCTCATCATTGA
	TCATAGTGTGAAGGTGGAATGGGGAAGCTACCTCCATCTTCTTCTTCATGCAATTTTTTTAGGGTTT
	GACCACTGCCACCCTGAGGTGTATGAACATTGTAAACGCCTGCTTCTGCACTTATTAATAGTAATGG
	GACCCAATAGTAACATCCGAACTGTTGCTTCTGTCCTTCTCAGGAACAAGGAGTTTAATGAGCCCAG
	GGTGCTTACAGTCAAACAAGTTGCACACTTAGATTATAATTTCACAGGTATTAACGATTTTATACCT
	GATTACCAGCCCTCCCCTATGACTGACTCAGGGCTTAGCTCAAGTTCTACCTCTTCTAGTATCAGCT
	TAGGAAATAACAGTGCTGCCATTTCACATCTGCACACCACTATCCTCAATGAGGTTGACATCTCAGT
	GGAGCAGGATGGAAAAGTCAAAACCCTCATGGAATTCATTACCTCAAGGAAAAGAGGGCCCCTTTGG
	AACCATGAGGATGTTTCTGCCAAGAATCCTAGCATAAAGAGTGCTGAACAGTTAACTACATTTTTGA
	AACATGTGGTTTCTGTTTTTAAGCAGTCAAGCTCAGAAGGAATTCATCTGGAACATCATCTTAGTGA
	AGTTGCTCTGCAAACAGCACTTTCCTGTTCTTCTCGACACTATGCTGGGAGATCCTTTCAGATTTTC
	AGGGCCCTAAAGCAGCCTCTCACTGCAACTACACTTTCTGATGTTCTCTCCAGACTTGTAGAAACTG
	TAGGGGATCCAGGAGAAGATGCACAGGGATTTGTGATTGAGCTTCTTCTCACATTGGAATCTGCAAT
	TGATACTTTGGCTGAAACCATGAAGCATTATGATCTTCTTTCTGCCCTTTCTCAAACCTCATATCAT
	GATCCTATAATGGGAAACAAGTATGCAGCTAACAGGAAAAGCACTGGACAACTCAATCTAAGCACAA
	GTCCCATTAATAGTAGCAGTTATTTGGGATATAACAGTAATGCAAGAAGTAACTCTTTGAGATTAAG
	TTTGATTGGTGACCGACGAGGTGACCGGCGGCGGAGTAACACACTGGATATAATGGATGGACGGATA
	AACCATAGCAGTAGTTTAGCAAGGACTAGAAGCCTTTCCTCTCTAAGAGAGAAAGGAATGTATGACG
	TGCAGTCCACTACTGAGCCTACCAACTTGATGGCCACCATTTTTTGGATAGCAGCATCTTTATTAGA
	ATCAGATTATGAATATGAATACCTCCTGGCTCTCAGGCTTCTCAACAAACTGCTTATCCATTTGCCT
	TTGGATAAATCAGAGAGTCGAGAGAAGATTGAAAATGTACAAAGCAAATTGAAATGGACTAATTTTC
	CAGGACTTCAGCAGCTCTTCCTTAAGGGTTTTACCTCAGCATCTACACAAGAAATGACCGTGCACCT
	CCTCAGTAAACTCATTTCTGTCTCCAAACATACATTGGTGGATCCTTCCCAATTGTCAGGCTTTCCT
	CTTAACATCCTTTGCTTATTGCCTCACTTAATCCAGCATTTTGACAGCCCAACTCAGTTTTGCAAAG
	AAACAGCTAGTCGAATAGCAAAGGTTTGTGCAGAAGAAAAATGCCCAACACTTGTCAATCTGGCACA
	CATGATGAGTTTGTACAGTACACACACGTATTCCAGAGACTGTTCTAACTGGATCAATGTCGTGTGC
	AGATACCTGCATGACTCCTTCTCAGATACAACATTTAATCTTGTGACTTATCTTGCAGAGCTGTTAG
	AGAAAGGATTGTCCAGTATGCAGCAATCATTACTACAGATTATTTATAGTCTATTGAGTCATATTGA
	CCTGTCTGCAGCCCCAGCCAAGCAGTTTAATCTGGAGATCATAAAGATTATTGGCAAATATGTACAG
	AGTCCTTACTGGAAGGAAGCCCTTAACATATTAAAGCTGGTGGTGTCACGCTCTGCGAGTCTTGTCG
	TACCCAGTGATATCCCCAAGACCTATGGAGGAGATACAGGTTCTCCTGAAATATCCTTCACTAAAAT
	TTTTAATAATGTTTCTAAGGAGTTGCCTGGGAAGACCTTAGATTTTCATTTTGATATATCTGAGACA
	CCAATTATTGGAAACAAATATGGTGATCAGCACAGTGCGGCTGGAAGAAATGGGAAACCAAAAGTTA
	TTGCTGTCACTAGAAGTACTTCCTCAACTTCTTCTGGTTCTAATTCTAATGCCTTGGTTCCTGTTAG
	TTGGAAAAGGCCACAGTTATCACAGCGAAGAACAAGAGAAAAGCTAATGAATGTGCTTTCTCTCTGT
	GGTCCAGAATCTGGCCTCCCAAAGAACCCATCAGTTGTATTTTCTTCTAATGAGGATTTGGAAGTCG
	GTGACCAACAGACTAGCCTAATTTCTACAACAGAAGACATAAATCAAGAGGAAGAAGTAGCTGTGGA
	AGATAATAGCAGTGAACAACAGTTTGGTGTTTTTAAGGATTTTGACTTTTTAGATGTTGAATTGGAA
	GATGCAGAGGGTGAAAGTATGGACAATTTCAACTGGGGAGTTCGCAGGCGCTCACTGGACAGTATTG
	ACAAAGGGGACACTCCATCCCTCCAGGAGTACCAGTGCTCTAGTAGCACCCCCAGCCTGAACCTCAC
	CAATCAGGAGGATACAGATGAGTCCTCGGAAGAAGAAGCGGCACTTACAGCAAGCCAGATACTCTCA
	CGCACACAGATGTTAAACAGTGATTCTGCCACTGATGAAACAATACCAGACCATCCTGACTTACTTC
	TCCAGTCTGAAGATTCCACTGGCAGCATCACAACAGAGGAAGTGCTTCAAATCAGGGATGAGACCCC
	AACTTTGGAGGCTTCTCTAGATAATGCTAACAGCCGGCTGCCTGAGGATACAACTTCAGTATTAAAG
	GAGGAACATGTTACAACCTTTGAAGATGAAGGATCCTATATAATTCAAGAACAGCAGGAATCTCTTG
	TGTGTCAAGGAATTCTTGATTTAGAAGAAACTGAAATGCCAGAGCCTCTAGCTCCTGAAAGTTACCC
	CGAGTCAGTCTGTGAAGAGGATGTTACCTTAGCTCTGAAAGAGCTAGATGAAAGATGTGAAGAAGAA
	GAAGCGGATTTCTCCGGACTGTCTAGTCAAGATGAAGAAGAGCAAGATGGTTTTCCAGAAGTACAGA
	CGTCGCCTCTGCCGTCACCATTTCTTTCTGCCATCATAGCCGCCTTTCAGCCCGTGGCATATGATGA
	TGAAGAGGAAGCCTGGCGCTGCCACGTCAATCAGATGCTGTCTGACACCGACGGGTCCTCTGCAGTG
	TTTACTTTTCATGTGTTTTCTAGGCTGTTTCAGACAATTCAAAGAAAGTTTGGAGAAATAACTAATG
	AGGCAGTCAGCTTTCTTGGTGATAGTCTGCAACGCATTGGTACCAAATTTAAAAGTTCCTTGGAAGT
	GATGATGCTGTGTTCAGAATGCCCAACAGTCTTTGTGGATGCTGAAACACTGATGTCATGTGGTTTG
	CTGGAAACACTCAAGTTTGGTGTTTTGGAGTTGCAAGAACACCTGGATACATACAATGTGAAAAGAG
	AAGCCGCTGAGCAGGAATTGGAGCTCTGCCGAAGATTATACAAATTGCATTTTCAATTGCTGCTTCT
	GTTCCAGGCCTACTGTAAACTTATCAACCAAGTAAATACGATAAAAAATGAAGCAGAGGTCATCAAC
	ATGTCAGAGGAACTTGCCCAACTGGAAAGTATCCTCAAAGAAGCTGAGTCCGCTTCCGAAAACGAAG
	AAATTGACATTTCCAAAGCTGCACAAACTACTATAGAAACTGCCATTCATTCTTTAATTGAAACTTT
	GAAAAATAAAGAATTTATATCAGCTGTAGCACAAGTCAAAGCTTTCAGATCTCTCTGGCCCAGTGAT
	ATCTTTGGCAGTTGTGAAGATGACCCTGTACAGACACTGTTACATATATATTTCCATCATCAGACGC
	TGGGCCAGACAGGAAGCTTTGCAGTTATAGGCTCTAACCTGGACATGTCAGAAGCCAACTACAAACT
	GATGGAACTTAATCTGGAAATAAGAGAGTCTCTACGCATGGTGCAATCATACCAACTTCTAGCACAG
	GCCAAACCAATGGGAAATATGGTGAGCACTGGATTCTGAGACACTTCAGGCCTTTAGGAAAGAAACT
	AAACTGAAGATGATGAAGAATATTAACCAAGCACCTTTTATGGACCCTTGCATTCACTGATAACTTT
	CTGCCAGCATCTACTTTTTAGTGTAACTAATGTCAAACTGTATCATCAAAAACAAAGATCTGAAAGA
	AAAAAACATCTGATATTTTAACAGCTGCCAATATCTCCCACAATAACTGCGTGAAGA
	ORF Start: ATG at 16		ORF Stop: TGA at 8479
	SEQ ID NO:90	2821 aa	MW at 316987.5 kD
NOV21a,	MLSLQDSVFFEISIKSLLKSWSSSMSNITIDPDVKPGEYVIKSLFAEFAVQAEKKIEVVMAEPLEKL
CG145997-10
Protein Sequence	LSRSLQRGEDLQFDQVISSMSSVAEHCLPSLLRTLFDWYRRQNGTEDESYEYRPRSSTKSKDEQQRE
	RDYLLERRDLAVDFIFCLVLVEVLKQIPVHPVPDPLVHEVLNLAFKHFKHKEGGTNTGNVHIIADLY
	AEVIGVLAQSKFQAVRKKFVTELKELRQKEQSPHVVQSVISLIMGMKFFRVKMYPVEDFEASFQFMQ
	ECAQYFLEVKDKDIKHALAGLFVEILIPVVKNEVNVPCLKNFVEMLYQTTFELSSRKKHSLVLNKDP
	KMSRVALESLYRLLWVYVIRIKCESNTVTQSRLMSIVSALFPKGSRSVVPRDTPLNIFVKIIQFIAQ
	ERLDFAMKEIIFDLLSVGKSTKTFTINPECLAYVICFLLNPVVFFTGERKPKIDLFRTCIAAIPRLI
	PDGMSRTDLIELLARLTIHMDEELRALAFNTLQALMLDFPDWREDVLSGFVYFIVREVTDVHPTLLD
	NAVKMLVQLINQWKQAAQMHNKNQDTQVPDSFLVANGASHPPPLERSPYSNVFHVVEGFALVILCSS
	RPATRRLAVSVLREIRALFALLEIPKGDDELAIDVMDRLSPSILESFIHLTGADQVTISISLQTLAE
	WNSSPISHQFDVISPSHIWIFAHVTQGQDPWIISLSSFLKQENLPKHCSTAVSYAWMFAYTRLQLLS
	PQVDSSPINAKKVNTTTSSDSYIGLWRNYLILCCSAATSSSSTSAGSVRCSPPETLASTPDSGYSID
	SKIGIPSPSSLFKHIVPMMRSESMEITESLVLGLGRTNPGAFRNMKRRRRRDILRVQLVRIFELLAD
	AGVISSASGGLDNETHFLNNTLLEYVDLTRQLLEAENEKDSDTLKDIRCHFSALVANIIQNVPVHQR
	RSIFPQQSLRHSLFMLFSHWAGPFSIMFTPLDRYSDRNMQINRHQYCALKAMSAVLCCGPVADNVGL
	SSDGYLYKWLDNILDSLDKKVHQLGCEAVTLLLELNPDQNNLMYWARDYQCDTVMLLNLILFKAADS
	SRSIYEVAMOLLOILEPKMFRYAHKLEVORTDGVLSOLSPLPHLYSVSYYOLSEELARAYPELTLAI
	FSGKPENPDSSPCWAAGDAALPATMDEQHRAGGLQAPPPGFTPFSDDSLKDRELMVTSRRWLRGEGW
	GSPQATAMVLNNLMYMTAKYGDELAWSEVENVMTTLADGWPKNLKIILHFLISICGVNSEPSLLPYV
	KKVIVYLGRDKTMQLLEELVSELQLTDPVSSGVTHMDNPPYYRITSSALSLITGTTSSSNTMVAPTD
	GNPDNKPIKENIEERTSHLNRQHPSLESRYSSSSGGSYEEEKSDSMPLYSNWRLKVMEHNQGEPLPF
	PPAGGCWSPLVDYVPETSSPGLPLHRCNIAVILLTDLIIDHSVKVEWGSYLHLLLHAIFLGFDHCHP
	EVYEHCKRLLLHLLIVMGPNSNIRTVASVLLRNKEFNEPRVLTVKQVAHLDYNFTGINDFIPDYQPS
	PMTDSGLSSSSTSSSISLGNNSAAISHLHTTILNEVDISVEQDGKVKTLMEFITSRKRGPLWNHEDV
	SAKNPSIKSAEQLTTFLKHVVSVFKQSSSEGIHLEHHLSEVALQTALSCSSRHYAGRSFQIFRALKQ
	PLTATTLSDVLSRLVETVGDPGEDAQGFVIELLLTLESAIDTLAETMKHYDLLSALSQTSYHDPIMG
	NKYAANRKSTGQLNLSTSPINSSSYLGYNSNARSNSLRLSLIGDRRGDRRRSNTLDIMDGRINHSSS
	LARTRSLSSLREKGMYDVQSTTEPTNLMATIFWIAASLLESDYEYEYLLALRLLNKLLIHLPLDKSE
	SREKIENVQSKLKWTNFPGLQQLFLKGFTSASTQEMTVHLLSKLISVSKHTLVDPSQLSGFPLNILC
	LLPHLIQHFDSPTQFCKETASRIAKVCAEEKCPTLVNLAHMMSLYSTHTYSRDCSNWINVVCRYLHD
	SFSDTTFNLVTYLAELLEKGLSSMQQSLLQIIYSLLSHIDLSAAPAKQFNLEIIKIIGKYVQSPYWK
	EALNILKLVVSRSASLVVPSDIPKTYGGDTGSPEISFTKIFNNVSKELPGKTLDFHFDISETPIIGN
	KYGDQHSAAGRNGKPKVIAVTRSTSSTSSGSNSNALVPVSWKRPQLSQRRTREKLMNVLSLCGPESG
	LPKNPSVVFSSNEDLEVGDQQTSLISTTEDINQEEEVAVEDNSSEQQFGVFKDFDFLDVELEDAEGE
	SMDNFNWGVRRRSLDSIDKGDTPSLQEYQCSSSTPSLNLTNQEDTDESSEEEAALTASQILSRTQML
	NSDSATDETIPDHPDLLLQSEDSTGSITTEEVLQIRDETPTLEASLDNANSRLPEDTTSVLKEEHVT
	TFEDEGSYIIQEQQESLVCQGILDLEETEMPEPLAPESYPESVCEEDVTLALKELDERCEEEEADFS
	GLSSQDEEEQDGFPEVQTSPLPSPFLSAIIAAFQPVAYDDEEEAWRCHVNQMLSDTDGSSAVFTFHV
	FSRLFQTIQRKFGEITNEAVSFLGDSLQRIGTKFKSSLEVMMLCSECPTVFVDAETLMSCGLLETLK
	FGVLELQEHLDTYNVKREAAEQELELCRRLYKLHFQLLLLFQAYCKLINQVNTIKNEAEVINMSEEL
	AQLESILKEAESASENEEIDISKAAQTTIETAIHSLIETLKNKEFISAVAQVKAFRSLWPSDIFGSC
	EDDPVQTLLHIYFHHQTLGQTGSFAVIGSNLDMSEANYKLMELNLEIRESLRMVQSYQLLAQAKPMG
	NMVSTGF

[0479] Further analysis of the NOV21a protein yielded the following properties shown in Table 21B.

TABLE 21B
Protein Sequence Properties NOV21a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3538 probability located in mitochondrial inner membrane;
                  0.3000 probability located in endoplasmic reticulum (membrane)
SignalP analysis: No Known Signal Sequence Predicted

[0480] A search of the NOV21a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 21C.

TABLE 21C
Geneseq Results for NOV21a
		NOV21a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
ABG04763	Novel human diagnostic	432 . . . 2819	1382/2497 (55%)	0.0
	protein #4754 - Homo	609 . . . 3046	1762/2497 (70%)
	sapiens, 3048 aa.
	[WO200175067-A2,
	Oct. 11, 2001]
ABB97274	Novel human protein SEQ	1591 . . . 2821	1231/1254 (98%)	0.0
	ID NO: 549 - Homo sapiens	1 . . . 1254	1231/1254 (98%)
	1254 aa.
	[WO200222660-A2,
	Mar. 21, 2002]
ABG04764	Novel human diagnostic	567 . . . 2276	893/1794 (49%)	0.0
	protein #4755 - Homo	293 . . . 1962	1155/1794 (63%)
	sapiens, 2035 aa.
	[WO200175067-A2,
	Oct. 11, 2001]
AAB65130	Gene #26 associated peptide	2144 . . . 2821	675/701 (96%)	0.0
	#21 - Homo sapiens, 703 aa.	3 . . . 703	677/701 (96%)
	[WO200075375-A1,
	Dec. 14, 2000]
AAB65110	Gene #26 associated peptide	2144 . . . 2820	675/700 (96%)	0.0
	#1 - Homo sapiens, 702 aa.	3 . . . 702	677/700 (96%)
	[WO200075375-A1,
	Dec. 14, 2000]

[0481] In a BLAST search of public sequence datbases, the NOV21a protein was found to have homology to the proteins shown in the BLASTP data in Table 21D.

TABLE 21D
Public BLASTP Results for NOV21a
		NOV21a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q9Y3N6	Hypothetical 338.2 kDa	432 . . . 2819	1385/2493 (55%)	0.0
	protein - Homo sapiens	577 . . . 3010	1764/2493 (70%)
	(Human), 3012 aa.
O94915	KIAA0826 protein - Homo	1615 . . . 2821	1207/1236 (97%)	0.0
	sapiens (Human), 1236 aa	1 . . . 1236	1207/1236 (97%)
	(fragment).
O14572	WUGSC:H_248015.1	449 . . . 2276	1090/1892 (57%)	0.0
	protein - Homo sapiens	1 . . . 1849	1375/1892 (72%)
	(Human), 1849 aa
	(fragment).
Q91ZH1	DM505L19.1 (Novel	1226 . . . 2819	877/1652 (53%)	0.0
	protein) - Mus musculus	1 . . . 1593	1152/1652 (69%)
	(Mouse), 1595 aa (fragment).
O95640	Hypothetical 88.4 kDa	1591 . . . 2385	795/795 (100%)	0.0
	protein - Homo sapiens	1 . . . 795	795/795 (100%)
	(Human), 795 aa (fragment).

[0482] PFam analysis predicts that the NOV21a protein contains the domains shown in the Table 21E.

TABLE 21E
Domain Analysis of NOV21a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV21a Match Region	Region	Value
PFK	1028 . . . 1039	7/12 (58%)	0.52
		10/12 (83%)

Example 22

[0483] The NOV22 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 22A.

TABLE 22A
NOV22 Sequence Analysis
	SEQ ID NO: 91	4170 bp
NOV22a,	ACGCGTTCCCCGGGAACAACACGTTGAGGGCGCCCACCCTGCGTGCCCGGGGCCACCCGGTCCCTGC
CG146119-01
DNA Sequence	CCTCGGGCGGCAGGAGAGGTCGAGCTTCCACGGCCCTCGGAGTAGCCCCGTGACCAGACCCGGACTG
	GCCTTGGAGTTGAAGGGGTTGTTTGCCACCAAATGAACCGAAAAAACTGAACTTTTCAGACTTCGGA
	ATGGCAGATATGGGCTTGGAGTTCAGTGAAATTGCAGCGGAGGCGGTGGTGTTCTGAGCTGAGATGC
	GGCTGCTCCTGCTCGTGCCGCTGCTGCTGGCTCCAGCGCCCGGGTCCTCGGCTCCCAAGGTGAGGCG
	GCAGAGTGACACCTGGGGACCCTGGAGCCAGTGGAGCCCCTGCAGCCGGACCTGTGGAGGGGGTGTC
	AGCTTCCGGGAGCGCCCCTGCTACTCCCAGAGGAGAGATGGAGGCTCCAGCTGCGTGGGCCCCGCCC
	GCAGAGTGACACCTGGGGACCCTGGAGCCAGTGGAGCCCCTGCAGCCGGACCTGTGGAGGGGGTGTC
	GGAGCCACCGCTCTTGTCGCACGGAGAGCTGCCCCGACGGCGCCCGGGACTTCCGGGCCGAGCAGTG
	CGCGGAGTTCGACGGAGCGGAGTTCCAGGGGCGGCGGTATCGGTGGCTGCCCTACTACAGCGCCCCA
	AACAAGTGTGAACTGAACTGCATTCCCAAGGGGGAGAACTTCTACTACAAGCACAGGGAGGCTGTGG
	TTGATGGGACGCCCTGCGAGCCTGGCAAGAGGGATGTCTGTGTGGATGGCAGCTGCCGGGTTGTCGG
	CTGTGATCACGAGCTGGACTCGTCCAAGCAGGAGGACAAGTGTCTGCGGTGTGGGGGTGACGGCACG
	ACCTGCTACCCCGTCGCAGGCACCTTTGACGCTAATGACCTCAGCCGAGGCTACAACCAGATCCTCA
	TAGTTCCCATGGGTGCCACCAGCATCCTCATCGACGAGGCTGCTGCCAGCAGGAACTTCCTGGCTGT
	GAAGAATGTTCGTGGGGAATACTACCTCAATGGGCACTGGACCATCGAGGCGGCCCGGGCCCTGCCA
	GCAGCCAGCACCATCCTGCATTACGAGCGGGGTGCTGAGGGGGACCTGGCCCCTGAGCGACTCCATG
	CCCGGGGCCCCACCTCGGAGCCCCTGGTCATCGAGCTCATCAGCCAGGAGCCCAACCCCGGTGTGCA
	CTATGAGTACCACCTGCCCCTGCGCCGCCCCAGCCCCGGCTTCAGCTGGAGCCACGGCTCATGGAGT
	GACTGCAGCGCGGAGTGTGGCGGAGGTCACCAGTCCCGCCTGGTGTTCTGCACCATCGACCATGAGG
	CCTACCCCGACCACATGTGCCAGCGCCAGCCACGGCCAGCTGACCGGCGTTCCTGCAATCTTCACCC
	TTGCCCGGAGACCAAGCGCTGGAAGGCAGGGCCATGGGCACCCTGCTCAGCCTCCTGTGGAGGAGGC
	TCCCAGTCCCGCTCCGTGTACTGCATCTCGTCTGACGGGGCCGGCATCCAGGAGGCCGTGGAGGAGG
	CTGAGTGTGCCGGGCTGCCTGGGAAGCCCCCTGCCATTCAGGCCTGTAACCTGCAGCGCTGTGCAGC
	CTGGAGCCCGGAGCCCTGGGGAGAGTGTTCTGTCAGTTGTGGCGTTGGCGTCCGGAAGCGGAGCGTT
	ACTTGCCGGGGTGAAAGGGGTTCTTTGCTCCATACCGCAGCGTGCTCCTTGGAAGACCGGCCACCTC
	TGACTGAGCCCTGTGTGCATGAGGACTGCCCCCTCCTCAGTGACCAGGCCTGGCATGTTGGCACCTG
	GGGTCTATGCTCCAAGAGCTGCAGCTCGGGCACTCGGAGGCGACAGGTCATCTGTGCCATTGGGCCG
	CCCAGCCACTGCGGGAGCCTGCAGCACTCCAAGCCTGTGGATGTGGAGCCTTGTAACACGCAGCCCT
	GTCATCTCCCCCAGGAGGTCCCCAGCATGCAGGATGTGCACACCCCTGCCAGCAACCCCTGGATGCC
	GTTGGGCCCTCAGGAGTCCCCTGCCTCAGACTCCAGAGGCCAGTGGTGGGCAGCCCAGGAACACCCC
	TCAGCCAGGGGTGACCACAGGGGAGAACGAGGTGACCCCAGGGGCGACCAAGGCACCCACCTGTCAG
	CCCTGGGCCCCGCTCCCTCTCTGCAGCAGCCCCCATACCAGCAACCCCTGCGGTCGGGCTCAGGGCC
	CCACGACTGCAGACACAGTCCTCACGGGTGCTGCCCCGATGGCCACACGGCATCTCTCGGGCCTCAG
	TGGCAAGGCTGCCCTGGGGCCCCCTGTCAGCAGAGCAGGTACGGGTGCTGCCCTGACAGGGTATCTG
	TCGCTGAGGGGCCCCATCACGCTGGCTGCACAAAGTCGTATGGTGGTGACAGCACCGGGGGCATGCC
	CAGGTCAAGGGCAGTGGCTTCTACAGTAAGTGTCTGGAACACCCACCAGCCCCAGGCCCAGCAGAAT
	GAGCCCAGTGAGTGCCGGGGCTCCCAGTTTGGCTGTTGCTATGACAACGTGGCCACTGCAGCCGGTC
	CTCTTGGGGAAGGCTGTGTGGGCCAGCCCAGCCATGCCTACCCCGTGCGGTGCCTGCTGCCCAGTGC
	CCATGGCTCTTGCGCAGACTGGGCTGCCCGCTGGTACTTCGTTGCCTCTGTGGGCCAATGTAACCGC
	TTCTGGTATGGCGGCTGCCATGGCAATGCCAATAACTTTGCCTCGGAGCAAGAGTGCATGAGCAGCT
	GCCAGGGATCTCTCCATGGGCCCCGTCGTCCCCAGCCTGGGGCTTCTGGAAGGAGCACCCACACGGA
	TGGTGGCGGCAGCAGTCCTGCAGGCGAGCAGGAACCCAGCCAGCACAGGACAGGGGCCGCGGTGCAG
	AGAAAGCCCTGGCCTTCTGGTGGTCTCTGGCGGCAAGACCAACAGCCTGGGCCAGGGGAGGCCCCCC
	ACACCCAGGCCTTTGGAGAATGGCCATGGGGGCAGGAGCTTGGGTCCAGGGCCCCTGGACTGGGTGG
	AGATGCCGGATCACCAGCGCCACCCTTCCACAGCTCCTCCTACAGGATTAGCTTGGCAGGTGTGGAG
	CCCTCGTTGGTGCAGGCAGCCCTGGGGCAGTTGGTGCGGCTCTCCTGCTCAGACGACACTGCCCCGG
	AATCCCAGGCTGCCTGGCAGAAAGATGGCCAGCCCATCTCCTCTGACAGGCACAGGCTGCAGTTCGA
	CGGATCCCTGATCATCCACCCCCTGCAGGCAGAGGACGCGGGCACCTACAGCTGTGGCAGCACCCGG
	CCAGGCCGCGACTCCCAGAAGATCCAACTTCGCATCATAGGGGGTGACATGGCCGTGCTGTCTGAGG
	CTGAGCTGAGCCGCTTCCCTCAGCCCAGGGACCCAGCTCAGGACTTTGGCCAAGCGGGGGCTGCTGG
	GCCCCTGGGGGCCATCCCCTCTTCACACCCACAGCCTGCAAACAGGCTGCGTTTGGACCAGAACCAG
	CCCCGGGTGGTGGATGCCAGTCCAGGCCAGCGGATCCGGATGACCTGCCGTGCCGAAGGCTTCCCGC
	CCCCAGCCATCGAGTGGCAGAGAGATGGGCAGCCTGTCTCTTCTCCCAGACACCAGCTGCAGCCTGA
	TGGCTCCCTGGTCATTAGCCGAGTGGCTGTAGAAGATGGCGGCTTCTACACCTGTGTCGCTTTCAAT
	GGGCAGGACCGAGACCAGCGATGGGTCCAGCTCAGAGTTCTGGGGGAGCTGACAATCTCAGGACTGC
	CCCCTACTGTGACAGTGCCAGAGGGTGATACGGCCAGGCTATTGTGTGTGGTAGCAGGAGAAAGTGT
	GAACATCAGGTGGTCCAGGAACGGGCTACCTGTGCAGGCTGATGGCCACCGTGTCCACCAGTCCCCA
	GATGGCACGCTGCTCATTTACAACTTGCGGGCCAGGGATGAGGGCTCCTACACGTGCAGTGCCTACC
	AGGGGAGCCAGGCAGTCAGCCGCAGCACCGAGGTGAAGGTGGTCTCACCAGCACCCACCGCCCAGCC
	CAGGGACCCTGGCAGGGACTGCGTCGACCAGCCAGAGCTGGCCAACTGTGATTTGATCCTGCAGGCC
	CAGCTTTGTGGCAATGAGTATTACTCCAGCTTCTGCTGTGCCAGCTGTTCACGTTTCCAGCCTCACG
	CTCAGCCCATCTGGCAGTAGGGATGAAGGCTAGTTCCAGCCCCAGTCCAAAATAGTTCATAGGGCTA
	GGGAGAAAGGAAGATG
	ORF Start: ATG at 265		ORF Stop: TAG at 4105
	SEQ ID NO: 92	1280 aa	MW at 137933.8 kD
NOV22a,	MRLLLLVPLLLAPAPGSSAPKVRRQSDTWGPWSQWSPCSRTCGGGVSFRERPCYSQRRDGGSSCVGP
CG146119-01
Protein Sequence	ARSHRSCRTESCPDGARDFRAEQCAEFDGAEFQGRRYRWLPYYSAPNKCELNCIPKGENFYYKHREA
	VVDGTPCEPGKRDVCVDGSCRVVGCDHELDSSKQEDKCLRCGGDGTTCYPVAGTFDANDLSRGYNQI
	LIVPMGATSILIDEAAASRNFLAVKNVRGEYYLNGHWTIEAARALPAASTILHYERGAEGDLAPERL
	HARGPTSEPLVIELISQEPNPGVHYEYHLPLRRPSPGFSWSHGSWSDCSAECGGGHQSRLVFCTIDH
	EAYPDHMCQRQPRPADRRSCNLHPCPETKRWKAGPWAPCSASCGGGSQSRSVYCISSDGAGIQEAVE
	EAECAGLPGKPPAIQACNLQRCAAWSPEPWGECSVSCGVGVRKRSVTCRGERGSLLHTAACSLEDRP
	PLTEPCVHEDCPLLSDQAWHVGTWGLCSKSCSSGTRRRQVICAIGPPSHCGSLQHSKPVDVEPCNTQ
	PCHLPQEVPSMQDVHTPASNPWMPLGPQESPASDSRGQWWAAQEHPSARGDHRGERGDPRGDQGTHL
	SALGPAPSLQQPPYQQPLRSGSGPHDCRHSPHGCCPDGHTASLGPQWQGCPGAPCQQSRYGCCPDRV
	SVAEGPHHAGCTKSYGGDSTGGMPRSRAVASTVSVWNTHQPQAQQNEPSECRGSQFGCCYDNVATAA
	GPLGEGCVGQPSHAYPVRCLLPSAHGSCADWAARWYFVASVGQCNRFWYGGCHGNANNFASEQECMS
	SCQGSLHGPRRPQPGASGRSTHTDGGGSSPAGEQEPSQHRTGAAVQRKPWPSGGLWRQDQQPGPGEA
	PHTQAFGEWPWGQELGSRAPGLGGDAGSPAPPFHSSSYRISLAGVEPSLVQAALGQLVRLSCSDDTA
	PESQAAWQKDGQPISSDRHRLQFDGSLIIHPLQAEDAGTYSCGSTRPGRDSQKIQLRIIGGDMAVLS
	EAELSRFPQPRDPAQDFGQAGAAGPLGAIPSSHPQPANRLRLDQNQPRVVDASPGQRIRMTCRAEGF
	PPPAIEWQRDGQPVSSPRHQLQPDGSLVISRVAVEDGGFYTCVAFNGQDRDQRWVQLRVLGELTISG
	LPPTVTVPEGDTARLLCVVAGESVNIRWSRNGLPVQADGHRVHQSPDGTLLIYNLRARDEGSYTCSA
	YQGSQAVSRSTEVKVVSPAPTAQPRDPGRDCVDQPELANCDLILQAQLCGNEYYSSFCCASCSRFQP
	HAQPIWQ

[0484] Further analysis of the NOV22a protein yielded the following properties shown in Table 22B.

TABLE 22B
Protein Sequence Properties NOV22a
PSort analysis:   0.4896 probability located in outside; 0.1800 probability located in nucleus;
                  0.1000 probability located in endoplasmic reticulum (membrane); 0.1000
                  probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 19 and 20

[0485] A search of the NOV22a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 22C.

TABLE 22C
Geneseq Results for NOV22a
			Identities/
		NOV22a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU12196	Human PRO4799	899 . . . 1280	375/384	0.0
	polypeptide		(97%)
	sequence—Homo	94 . . . 477	377/384
	sapiens, 477 aa.		(97%)
	[WO200140466-
	A2, 7 JUN.
	2001]
ABB71150	Drosophila	27 . . . 538	209/529	e−110
	melanogaster		(39%)
	polypeptide SEQ	18 . . . 536	282/529
	ID NO 40242—		(52%)
	Drosophila
	melanogaster,
	2858 aa.
	[WO200171042-
	A2, 27 SEP.
	2001]
ABB58064	Drosophila	27 . . . 538	209/529	e−110
	melanogaster		(39%)
	polypeptide SEQ	18 . . . 536	282/529
	ID NO 984—		(52%)
	Drosophila
	melanogaster,
	3060 aa.
	[WO200171042-
	A2, 27 SEP.
	2001]
AAU72890	Human metallo-	29 . . . 549	201/529	e−105
	partial protein		(37%)
	sequence #2—	550 . . . 1064	272/529
	Homo sapiens,		(50%)
	1103 aa.
	[WO200183782-
	A2, 8 NOV.
	2001]
AAB74945	Human ADAM	29 . . . 549	201/529	e−105
	type metal		(37%)
	protease MDTS2	550 . . . 1064	272/529
	protein SEQ ID		(50%)
	NO: 10—Homo
	sapiens, 1103 aa.
	[JP2001008687-
	A, 16 JAN.
	2001]

[0486] In a BLAST search of public sequence datbases, the NOV22a protein was found to have homology to the proteins shown in the BLASTP data in Table 22D.

TABLE 22D
Public BLASTP Results for NOV22a
			Identities/
		NOV22a	Similarities
Protein		Residues/	for the
Accession	Protein/	Match	Matched	Expect
Number	Organism/Length	Residues	Portion	Value
O95428	Hypothetical 133.5	1 . . . 1280	1136/1321	0.0
	kDa protein—Homo		(85%)
	sapiens (Human),	1 . . . 1235	1146/1321
	1235 aa.		(85%)
Q9EPX2	Papilin—Mus	5 . . . 1280	952/1283	0.0
	musculus (Mouse),		(74%)
	1280 aa.	6 . . . 1278	1052/1283
			(81%)
Q99JQ8	Hypothetical 52.5	803 . . . 1280	340/483	0.0
	kDa protein—Mus		(70%)
	musculus (Mouse),	1 . . . 482	382/483
	484 aa.		(78%)
Q9U8G8	Lacunin precursor—	29 . . . 538	211/530	e−113
	Manduca sexta		(39%)
	(Tobacco hawk-	63 . . . 582	288/530
	moth) (Tobacco		(53%)
	hornworm),
	3198 aa.
Q9VAV4	CG1540 protein—	27 . . . 538	209/529	e−109
	Drosophila		(39%)
	melanogaster	18 . . . 536	282/529
	(Fruit fly), 3060 aa.		(52%)

[0487] PFam analysis predicts that the NOV22a protein contains the domains shown in the Table 22E.

TABLE 22E
Domain Analysis of NOV22a
Pfam	NOV22a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
tsp_1	30 . . . 79	23/55 (42%)	3.7e−10
		39/55 (71%)
tsp_1	309 . . . 360	14/58 (24%)	0.042
		34/58 (59%)
tsp_1	366 . . . 424	15/65 (23%)	0.0013
		39/65 (60%)
tsp_1	425 . . . 480	19/61 (31%)	0.0013
		40/61 (66%)
tsp_1	488 . . . 538	14/54 (26%)	0.0095
		36/54 (67%)
Kunitz_BPTI	756 . . . 806	24/62 (39%)	2e−27
		41/62 (66%)
ig	926 . . . 982	17/60 (28%)	2.9e−07
		41/60 (68%)
ig	1060 . . . 1116	20/60 (33%)	4.1e−12
		45/60 (75%)
ig	1149 . . . 1206	15/62 (24%)	1.2e−09
		42/62 (68%)

Example 23

[0488] The NOV23 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 23A.

TABLE 23A
NOV23 Sequence Analysis
	SEQ ID NO. 93	1088 BP
NOV23a,	CTCCTGGAGGAGGAACAGCTGAGAGGCCTTGGATTCCGACAGACTCGAGGATACAAGAGCTTAGCAG
CG146202-01
DNA Sequence	GGTGTCTTGGCCATGGTCCCCTGGTGCTGCAACTCCTCTCCTTCACGCTCTTGGCTGGGCTCCTTGT
	CCAAGTGTCCAAGGTCCCCAGCTCCATAAGTCAGGAACAATCCAGGCAAGACGCGATCTACCAGAAC
	CTGACCCAGCTTAAAGCTGCAGTGGGTGAGCTCTCAGAGAAATCCAAGCTGCAGGAGATCTACCAGG
	AGCTGACCCAGCTGAAGGCTGCAGTGGGTGAGCTTCCAGAGAAATCTAAGCTGCAGGAGATCTACCA
	GGAGCTGACCCGGCTGAAGGCTGCAGTGGGTGAGCTTCCAGAGAAATCTAAGCTGCAGGAGATCTAC
	CAGGAGCTGACCTGGCTGAAGGCTGCAGTGGGTGAGCTTCCAGAGAAATCTAAGATGCAGGAGATCT
	ACCAGGAGCTGACTCGGCTGAAGGCTGCAGTGGGTGAGCTTCCAGAGAAATCTAAGCAGCAGGAGAT
	CTACCAGGAGCTGACCCGGCTGAAGGCTGCAGTGGAACGCCTGTGCCACCCCTGTCCCTGGGAATGG
	ACATTCTTCCAAGGAAACTGTTACTTCATGTCTAACTCCCAGCGGAACTGGCACGACTCCATCACCG
	CCTGCAAAGAAGTGGGGGCCCAGCTCGTCGTAATCAAAAGTGCTGAGGAGCAGAACTTCCTACAGCT
	GCAGTCTTCCAGAAGTAACCGCTTCACCTGGATGGGACTTTCAGATCTAAATCAGGAAGGCACGTGG
	CAATGGGTGGACGGCTCACCTCTGTTGCCCAGCTTCAAGCAGTATTGGAACAGAAGAGAGCCCAACA
	ACGTTGGGGAGGAAGACTGCGCGGAATTTAGTGGCAATGGCTGGAACGACGACAAATGTAATCTTGC
	CAAATTCTGGATCTGCAAAAAGTCCGCAGCCTCCTGCTCCAGGGATGAAGAACAGTTTCTTTCTCCA
	GCCCCTGCCACCCCAAACCCCCCTCCTGCGTAGCAGAACTTCACCCCCTTTTAAGCTACAGTTCCTT
	CTCTCCATCCTTCGAC
	ORF Start: at 1		ORF Stop: TAG at 1036
	SEQ ID NO: 94	345 aa	MW at 39149.0 kD
NOV23a,	LLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSISQEQSRQDAIYQN
CG146202-01
Protein Sequence	LTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIY
	QELTWLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVERLCHPCPWEW
	TFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTW
	QWVDGSPLLPSFKQYWNRREPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSP
	APATPNPPPA

[0489] Further analysis of the NOV23a protein yielded the following properties shown in Table 23B.

TABLE 23B
Protein Sequence Properties NOV23a
PSort     0.7900 probability located in plasma membrane; 0.3000
analysis: probability located in microbody (peroxisome); 0.3000
          probability located in Golgi body; 0.2000 probability
          located in endoplasmic reticulum (membrane)
SignalP   Cleavage site between residues 50 and 51
analysis:

[0490] A search of the NOV23a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 23C.

TABLE 23C
Geneseq Results for NOV23a
		NOV23a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU88025	Mouse OtS1-B7	1 . . . 345	344/391 (87%)	0.0
	ORF protein—	14 . . . 404	344/391 (87%)
	Mus sp, 404 aa.
	[WO200214366-
	A2, 21 FEB.
	2002]
AAG79086	Human DC-	1 . . . 345	344/391 (87%)	0.0
	SIGN, a dendritic	14 . . . 404	344/391 (87%)
	cell-speciific
	C-type lectin—
	Homo sapiens,
	404 aa.
	[WO200164752-
	A2, 7 SEP.
	2001]
AAB28614	Human C-type	1 . . . 345	344/391 (87%)	0.0
	lectin receptor—	14 . . . 404	344/391 (87%)
	Homo sapiens,
	404 aa.
	[WO200063251-
	A1, 26 OCT.
	2000]
AAB19714	Dendritic cell	1 . . . 345	344/391 (87%)	0.0
	specific C-type	14 . . . 404	344/391 (87%)
	lectin DC-
	SIGN—Homo
	sapiens, 404 aa.
	[EP1046651-A1,
	25 OCT. 2000]
AAR32188	Sequence of a	1 . . . 345	338/391 (86%)	0.0
	non-CD4 glyco-	14 . . . 404	340/391 (86%)
	protein gp120
	receptor protein—
	Homo sapiens,
	404 aa.
	[WO9301820-A,
	4 FEB. 1993]

[0491] In a BLAST search of public sequence datbases, the NOV23a protein was found to have homology to the proteins shown in the BLASTP data in Table 23D.

TABLE 23D
Public BLASTP Results for NOV23a
		NOV23a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9NNX6	Membrane-	1 . . . 345	344/391 (87%)	0.0
	associated lectin	14 . . . 404	344/391 (87%)
	type-C (Probable
	mannose-binding
	C-type lectin DC-
	SIGN) (MDC-
	SIGN1A type I
	isoform)—Homo
	sapiens (Human),
	404 aa.
Q96QQ1	MDC-SIGN1B type	3 . . . 345	342/389 (87%)	0.0
	I isoform—Homo	16 . . . 404	342/389 (87%)
	sapiens (Human),
	404 aa.
Q96QQ8	MDC-SIGN1A type	1 . . . 345	338/391 (86%)	0.0
	II isoform—Homo	14 . . . 398	338/391 (86%)
	sapiens (Human),
	398 aa.
Q95LC6	Dendritic cell-	1 . . . 345	319/368 (86%)	0.0
	specific ICAM-3	14 . . . 381	332/368 (89%)
	grabbing non-
	integrin—
	Macaca nemestrina
	(Pig-tailed
	macaque), 381 aa.
Q95LA8	Dendritic cell-	1 . . . 345	317/368 (86%)	0.0
	specific ICAM-3	14 . . . 381	331/368 (89%)
	grabbing non-
	integrin—
	Macaca mulatta
	(Rhesus macaque),
	381 aa.

[0492] PFam analysis predicts that the NOV23a protein contains the domains shown in the Table 23E.

TABLE 23E
Domain Analysis of NOV23a
Pfam	NOV23a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
integrin_B	65 . . . 83	13/21 (62%)	0.25
		19/21 (90%)
lectin_c	214 . . . 320	45/127 (35%)	3.6e−34
		87/127 (69%)

Example 24

[0493] The NOV24 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 24A.

TABLE 24A
NOV24 Sequence Analysis
	SEQ ID NO: 95	1191 bp
NOV24a,	GAGTACGTATCGTCCACTCTGAGCCTTAGAGGTGGGGGTTCATCAGGAGCACTTCGAGGAGGAGGAG
CG146250-01
DNA Sequence	GAGGAGGCCGGGGTGGAGGGGTGGGCTCTGGCGGCCTCTGTCGAGCCCTCCGCTCCTATGCGCTCTG
	CACTCGGCGCACCGCCCGCACCTGCCGCGGGGACCTCGCCTTCCATTCGGCGGTACATGGCATCGAA
	GACCTGATGATCCAGCACAACTGCTCCCGCCAGGGCCCTACAGCCCCTCCCCCGCCCCGGGCCCCG
	CCCTTCCAGGCGCGGGCTCCGGCCTCCCTGCCCCGGACCCTTGTGACTATGAAGGCCGGTTTTCCCG
	GCTGCATGGTCGTCCCCCGGGGTTCTTGCATTGCGCTTCCTTCGGGGACCCCCATGTGCGCAGCTTC
	CACCATCACTTTCACACATGCCGTGTCCAAGGAGCTTGGCCTCTACTGGATAATGACTTCCTCTTTG
	TCCAAGCCACCAGCTCCCCCATGGCGTTGGGGGCCAACGCTACCGCCACCCGGAAGGTCACCATCAT
	ATTTAAGAACATGCAGGAATGCATTGATCAGAAGGTGTATCAGGCTGAGGTGGATAATCTTCCTGTA
	GCCTTTGAAGATGGTTCTATCAATGGAGGTGACCGACCTGGGGGATCCAGTTTGTCGATTCAAACTG
	CTAACCCTGGGAACCATGTGGAGATCCAAGCTGCCTACATTGGCACAACTATAATCATTCGGCAGAC
	AGCTGGGCAGCTCTCCTTCTCCATCAAGGTAGCAGAGGATGTGGCCATGGCCTTCTCAGCTGAACAG
	GACCTGCAGCTCTGTGTTGGGGGGTGCCCTCCAAGTCAGCGACTCTCTCGATCAGAGCGCAATCGTC
	GGGGAGCTATAACCATTGATACTGCCAGACGGCTGTGCAAGGAAGGGCTTCCAGTGGAAGATGCTTA
	CTTCCATTCCTGTGTCTTTGATGTTTTAATTTCTGGTGATCCCAACTTTACCGTGGCAGCTCAGGCA
	GCACTGGAGGATGCCCGAGCCTTCCTGCCAGACTTAGAGAAGCTGCATCTCTTCCCCTCAGATGCTG
	GGGTTCCTCTTTCCTCAGCAACCCTCTTAGCTCCACTCCTTTCTGGGCTCTTTGTTCTGTGGCTTTG
	CATTCAGTAAGGGGACCATCAGTCCCATTACTAGTTTGGAAATGATTTGGAG
	ORF Start: ATG at 208		ORF Stop: TAA at 1147
	SEQ ID NO: 96	313 aa	MW at 33664.8 kD
NOV24a,	MIQHNCSRQGPTAPPPPRGPALPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPHVRSFHH
CG146250-01
Protein Sequence	HFHTCRVQGAWPLLDNDFLFVQATSSPMALGANATATRKVTIIFKNMQECIDQKVYQAEVDNLPVAF
	EDGSINGGDRPGGSSLSIQTANPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDL
	QLCVGGCPPSQRLSRSERNRRGAITIDTARRLCKEGLPVEDAYFHSCVFDVLISGDPNFTVAAQAAL
	EDARAFLPDLEKLHLFPSDAGVPLSSATLLAPLLSGLFVLWLCIQ
	SEQ ID NO: 97	974 bp
NOV24b,	AAGACCTGATGATCCAGCACAACTGCTCCCGCCAGGGCCCTACAGCCCCTCCCCCGCCCCGGGGCCC
CG146250-02
DNA Sequnece	CGCCCTTCCAGGCGCGGGCTCCGGCCTCCCTGCCCCGGACCCTTGTGACTATGAAGGCCGGTTTTCC
	CGGCTGCATGGTCGTCCCCCGGGGTTCTTGCATTGCGCTTCCTTCGGGGACCCCCATGTGCGCAGCT
	TCCACCATCACTTTCACACATGCCGTGTCCAAGGAGCTCGGCCTCTACTGGATAATGACTTCCTCTT
	TGTCCAAGCCACCAGCTCCCCCATGGCGTTGGGGGCCAACGCTACCGCCACCCGGAAGCTCACCATC
	ATATTTAAGAACATGCAGGAATGCATTGATCAGAAGGTGTATCAGGCTGAGGTGGATAATCTTCCTG
	TAGCCTTTGAAGATGGTTCTATCAATGGAGGTGACCGACCTGGGGGATCCAGTTTGTCGATTCAAAC
	TGCTAACCCTGGGAACCATGTGGAGATCCAAGCTGCCTACATTGGCACAACTATAATCATTCGGCAG
	ACAGCTGGGCAGCTCTCCTTCTCCATCAAGGTAGCAGAGGATGTGGCCATGGCCTTCTCAGCTGAAC
	AGGACCTGCAGCTCTGTGTTGGGGGGTGCCCTCCAAGTCAGCGACTCTCTCGATCAGAGCGCAATCG
	TCGGGGAGCTATAACCATTGATACTGCCAGACGGCTGTGCAAGGAAGGGCTTCCAGTGGAAGATGCT
	TACTTCCATTCCTGTGTCTTTGATGTTTTAATTTCTGGTGATCCCAACTTTACCGTGGCAGCTCAGG
	CAGCACTGGAGGATGCCCGAGCCTTCCTGCCAGACTTAGAGAAGCTGCATCTCTTCCCCTCAGATGC
	TGGGGTTCCTCTTTCCTCAGCAACCCTCTTAGCTCCACTCCTTTCTGGGCTCTTTGTTCTGTGGCTT
	TGCATTCAGTAAGGGGAACCATCAGTACAGGGCGAT
	ORF Start: ATG at 9		ORF Stop: TAA at 948
	SEQ ID NO: 98	313 aa	MW at 33648.8 kD
NOV24b,	MIQHNCSRQGPTAPPPPGPALPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPLHVRSFHH
CG146250-02
Protein Sequence	HFHTCRVQGARPLLDNDFLFVQATSSPMALGANATATRKLTIIFKNMQECIDQKVYQAEVDNLPVAF
	EDGSINGGDRPGGSSLSIQTANPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDL
	QLCVGGCPPSQRLSRSERNRRGAITIDTARRLCKEGLPVEDAYFHSCVFDVLISGDPNFTVAAQAAL
	EDARAFLPDLEKLHLFPSDAGVPLSSATLLAPLLSGLFVLWLCIQ
	SEQ ID NO: 99	1338 bp
NOV24c,	CCGGCGCCTGGGAAACCTGGCTGAATAGGTATGGGGGAGCCAGGCCAGTCCCCTAGTCCCAGGTCCT
CG146250-03
DNA Sequence	CCCATGGCAGTCCCCCAACTCTAAGCACTCTCACTCTCCTGCTGCTCCTCTGTGGATTAGCTCATTC
	TCAATGCAAGATCCTCCGCTGCAATGCTGAGTACGTATCGTCCACTCTGAGCCTTAGAGGTGGGGGT
	TCATCAGGAGCACTTCGAGGAGGAGGAGGAGGAGGCCGGGGTGGAGGGGTGGGCTCTGGCGGCCTCT
	GTCGAGCCCTCCGCTCCTATGCGCTCTGCACTCGGCGCACCGCCCGCACCTGCCGCGGGGACCTCGC
	CTTCCATTCGGCGGTACATGGCATCGAAGACCTGATGATCCAGCACAACTGCTCCCGCCAGGGCCCT
	ACAGCCCCTCCCCCGCCCCGGGGCCCCGCCCTTCCAGGCGCGGGCTCCGGCCTCCCTGCCCCGGACC
	CTTGTGACTATGAAGGCCGGTTTTCCCGGCTGCATGGTCGTCCCCCGGGGTTCTTGCATTGCGCTTC
	CTTCGGGGACCCCCATGTGCGCAGCTTCCACCATCACTTTCACACATGCCGTGTCCAAGGAGCTTGG
	CCTCTACTGGATAATGACTTCCTCTTTGTCCAAGCCACCAGCTCCCCCATGGCGTTGGGGGCCAACG
	CTACCGCCACCCGGAAGGTCACCATCATATTTAAGAACATGCAGGAATGCATTGATCAGAAGGTGTA
	TCAGGCTGAGGTGGATAATCTTCCTGTAGCCTTTGAAGATGGTTCTATCAATGGAGGTGACCGACCT
	GGGGGATCCAGTTTGTCGATTCAAACTGCTAACCCTGGGAACCATGTGGAGATCCAAGCTGCCTACA
	TTGGCACAACTATAATCATTCGGCAGACAGCTGGGCAGCTCTCCTTCTCCATCAAGGTAGCAGAGGA
	TGTGGCCATGGCCTTCTCAGCTGAACAGGACCTGCAGCTCTGTGTTGGGGGGTGCCCTCCAAGTCAG
	CGACTCTCTCGATCAGAGCGCAATCGTCGGGGAGCTATAACCATTGATACTGCCAGACGGCTGTGCA
	AGGAAGGGCTTCCAGTGGAAGATGCTTACTTCCATTCCTGTGTCTTTGATGTTTTAATTTCTGGTGA
	TCCCAACTTTACCGTGGCAGCTCAGGCAGCACTGGAGGATGCCCGAGCCTTCCTGCCAGACTTAGAG
	AAGCTGCATCTCTTCCCCTCAGATGCTGGGGTTCCTCTTTCCTCAGCAACCCTCTTAGCTCCACTCC
	TTTCTGGGCTCTTTGTTCTGTGGCTTTGCATTCAGTAAGGGGACCATCAGTCCCATTACTAGTTT
	ORF Start: ATG at 31		ORF Stop: TAA at 1309
	SEQ ID NO: 100	426 aa	MW at 45041.5 kD
NOV24c,	MGEPGQSPSPRSSHGSPPTLSTLTLLLLLCGLAHSQCKILRCNAEYVSSTLSLRGGGSSGALRGGGG
CG146250-03
Protein Sequence	GGRGGGVGSGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPPRGPA
	LPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPHVRSFHHHFHTCRVQGAWPLLDNDFLFV
	QATSSPMALGANATATRKVTIIFKNMQECIDQKVYQAEVDNLPVAFEDGSINGGDRPGGSSLSITQTA
	NPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDLQLCVGGCPPSQRLSRSERNRR
	GAITIDTARRLCKEGLPVEDAYFHSCVFDVLISGDPNFTVAAOAALEDARAFLPDLEKLHLFPSDAG
	VPLSSATLLAPLLSGLFVLWLCIQ

[0494] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 24B.

TABLE 24B
Comparison of NOV24a against NOV24b and NOV24c.
	Protein	NOV24a Residues/	Identities/Similarities
	Sequence	Match Residues	for the Matched Region
	NOV24b	1 . . . 313	271/313 (86%)
		1 . . . 313	272/313 (86%)
	NOV24c	1 . . . 313	273/313 (87%)
		114 . . . 426	273/313 (87%)

[0495] Further analysis of the NOV24a protein yielded the following properties shown in Table 24C.

TABLE 24C
Protein Sequence Properties NOV24a
PSort     0.7000 probability located in plasma membrane; 0.3740
analysis: probability located in microbody (peroxisome); 0.2000
          probability located in endoplasmic reticulum (membrane);
          0.1000 probability located in mitochondrial inner membrane
SignalP   No Known Signal Sequence Predicted
analysis:

[0496] A search of the NOV24a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 24D.

TABLE 24D
Geneseq Results for NOV24a
		NOV24a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU70169	Rat secreted	1 . . . 313	273/313 (87%)	e−161
	factor protein	110 . . . 422	284/313 (90%)
	encoded by DNA
	clone
	P0248_B04—
	Rattus
	norvegicus,
	422 aa.
	[WO200174901-
	A2, 11 OCT.
	2001]
AAM93823	Human poly-	1 . . . 308	158/340 (46%)	1e−76
	peptide, SEQ ID	110 . . . 446	206/340 (60%)
	NO: 3881—
	Homo sapiens,
	450 aa.
	[EP1130094-A2,
	5 SEP. 2001]
ABG65106	Human albumin	1 . . . 308	157/340 (46%)	4e−76
	fusion protein	94 . . . 430	205/340 (60%)
	#1781—Homo
	sapiens, 434 aa.
	[WO200177137-
	A1, 18 OCT.
	2001]
AAE07112	Human gene 6	1 . . . 308	157/340 (46%)	4e−76
	encoded secreted	131 . . . 467	205/340 (60%)
	protein fragment,
	SEQ ID NO:
	129—Homo
	sapiens, 471 aa.
	[WO200154708-
	A1, 2 AUG.
	2001]
AAE07056	Human gene 6	1 . . . 308	157/340 (46%)	4e−76
	encoded secreted	94 . . . 430	205/340 (60%)
	protein
	HARMJ38, SEQ
	ID NO: 73—
	Homo sapiens,
	434 aa.
	[WO200154708-
	A1, 2 AUG.
	2001]

[0497] In a BLAST search of public sequence datbases, the NOV24a protein was found to have homology to the proteins shown in the BLASTP data in Table 24E.

TABLE 24E
Public BLASTP Results for NOV24a
			Identities/
		NOV24a	Similarities
Protein		Residues/	for the
Accession	Protein/	Match	Matched	Expect
Number	Organism/Length	Residues	Portion	Value
BAC03944	CDNA FLJ35363	1 . . . 313	311/313	0.0
	fis, clone		(99%)
	SKMUS2000679—	1 . . . 313	313/313
	Homo sapiens		(99%)
	(Human), 313 aa.
BAC05248	CDNA FLJ40846	1 . . . 313	273/313	e−161
	fis, clone		(87%)
	TRACH2014544—	110 . . . 422	284/313
	Homo sapiens		(90%)
	(Human), 422 aa.
Q8WVJ5	Similar to	114 . . . 313	200/200	e−111
	RIKEN cDNA		(100%)
	2310035L15 gene—	1 . . . 200	200/200
	Homo sapiens		(100%)
	(Human), 200 aa.
AAH22603	Hypothetical	114 . . . 311	177/198	1e−97
	protein—Mus		(89%)
	musculus (Mouse),	1 . . . 198	182/198
	201 aa.		(91%)
Q9D741	2310035L15Rik	114 . . . 311	177/198	2e−97
	protein—Mus		(89%)
	musculus (Mouse),	1 . . . 198	182/198
	201 aa.		(91%)

[0498] PFam analysis predicts that the NOV24a protein contains the domains shown in the Table 24F.

TABLE 24F
Domain Analysis of NOV24a
	Pfam	NOV24a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value

Example 25

[0499] The NOV25 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 25A.

TABLE 25A
NOV25 Sequence Analysis
	SEQ ID NO: 101	381 bp
NOPV25a,	ATTCCTGGTGGTGAAAGGATGTGGCCCCAGGACCCATCCCGGAAGGAGGTGCTGAGGTTTGCAGTCA
CG146625-01
DNA Sequence	GCTGCCGTATCCTGACTCTGATGCTGCAGGTTCTCACCAGGTTTTTGGGCTCCTCCACTCCTATTAT
	GTACTGGTTTCCAGCTCACTTGCTTCAGGATCAAGAGCCGCTGTTGAGATCCTTAAAGACTGTGCCT
	TGGAAGCCTCTTGCAGAGGACTCCCCACCAGGACAAAAGGTCCCCAGAAATCCTATCATGGGACTTT
	TGTATCACTGGAAAACCTGTTCTCCAGTCACACGATACATTCTAGGCTACTTCCTGACTTACTGGCT
	CCTGGGACTACTCCTACATTGCAACTTCCTGCCTTGGACATGACCT
	ORF Start: ATG at 19		ORF Stop: TGA at 376
	SEQ ID NO: 102	119 aa	MW at 13984.5 kD
NOV25a,	MWPQDPSRKEVLRFAVSCRILTLMLQVLTRFLGSSTPIMYWFPAHLLQDQEPLLRSLKTVPWKPLAE
CG146625-01
Protein Sequence	DSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWLLGLLLHCNFLPWT
	SEQ ID NO: 103	906 bp
NOV25b,	GGAGCTCAATCCTGGTAGCAACACCCCTGAATTCCTGGTGGTGAAAGGATGTGGCCCCAGGACCCAT
CG146625-02
DNA Sequence	CCCGGAAGGAGGTGCTGAGGTTTGCAGTCAGCTGCCGTATCCTGACTCTGATGCTGCAGGCCCTCTT
	CAATGCCATCATCCCAGATCACCATGCAGAAGCCTTCTCTCCTCCTCGCCTGGCCCCCTCAGGCTTT
	GTGGACCAACTCGTGGAAGGCTCAGCCCGCCCCATTCCTGAGCCTTTGGTACAGTTAGCTGTAGACA
	AGGGCTACCGGATTGCAGAGGGAAATGAACCGCCTTGGTGCTTCTGGGATGTTCCACTAATATACAG
	CTATATCCAGGATGTCTGCTGGAATGTTGGCTTTTTGAAATACTATGAGCTCAAGCAGGTGCCCAAT
	TTTCTACTGGCTGCACCAGTGGCTATACTGGTTGCCTGGGCAACTTGGACATACGTGACCACTCACC
	CTTGGCTCTGCCTTACACTTGGGCTGCAAAGGAGCAAGAACAATAAGACCCTAGAGAAGCCCGATCT
	TGGATTCCTCAGTCCTCAGGTGTTTGTGTACGTGGTCCACGCTGCAGTGCTGCTGCTGTTTGGAGGT
	CTGTGCATGCATGTTCAGGTTCTCACCAGGTTTTTGGGCTCCTCCACTCCTATTATGTACTGGTTTC
	CAGCTCACTTGCTTCAGGATCAAGAGCCGCTGTTGAGATCCTTAAAGACTGTGCCTTGGAAGCCTCT
	TGCAGAGGACTCCCCACCAGGACAAAAGGTCCCCAGAAATCCTATCATGGGACTTTTGTATCACTGG
	AAAACCTGTTCTCCAGTCACACGATACATTCTAGGCTACTTCCTGACTTACTGGCTCCTGGGACTAC
	TCCTACATTGCAACTTCCTGCCTTGGACATGACCT
	ORF Start: ATG at 49		ORF Stop: TGA at 901
	SEQ ID NO: 104	284 aa	MW at 32499.9 kD
NOV25b,	MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGSARPIPEPL
CG146625-02
Protein Sequence	VQLAVDKGYRIAEGNEPPWCFWDVPLIYSYIQDVCWNVGFLKYYELKQVPNFLLAAPVAILVAWATW
	TYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSST
	PIMYWFPAHLLQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLT
	YWLLGLLLHCNFLPWT
	SEQ ID NO: 105	2114 bp
NOV25c,	CTCGTCTGCTTCCGGCCCTGTGGCCTGGTGGGGCTCTGCAGGCTCCCTCGGGAGTGGTCCTTGGGCC
CG146625-03
DNA Sequence	GTGGCCCCTCTGGGAGGCCTGAGGGAGCTCAATCCTGGTAGCAACACCCCTGAATTCCTGGTGGTGA
	AAGGATGTGGCCCCAGGACCCATCCCGGAAGGAGGTGCTGAGGTTTGCAGTCAGCTGCCGTATCCTG
	ACTCTGATGCTGCAGGCCCTCTTCAATGCCATCACCCCAGATCACCATGCAGAAGCCTTCTCTCCTC
	CTCGCCTGGCCCCCTCAGGCTTTGTGGACCAACTCGTGGAAGGTCTTCTGGGCGGCCTGTCTCACTG
	GGATGCTGAACACTTCTTGTTCATTGCTGAGCATGGCTACCTGTATGAGCACAACTTTGCCTTCTTT
	CCTGGTTTCCCCTTGGCCCTGCTGGTGGGGACTGAACTGTTGAGACCCTTACGGGGGTTACTGAGTC
	TACGCAGTTGCCTGCTGATTTCGGTAGCATCACTCAATTTCTTGTTCTTCATGTTGGCTGCAGTTGC
	ACTTCATGACCTGGGTTGTCTGGTTTTGCACTGTCCCCACCAGTCCTTTTATGCAGCTCTGCTTTTC
	TGTCTCAGCCCTGCCAATGTCTTCCTGGCAGCTGGTTACTCAGAAGCTTTGTTTGCCCTCCTGACAT
	TCAGTGCCATGGGGCAGCTGGAGAGGGGCCGAGTCTGGACTAGTGTACTCCTCTTTGCCTTTGCCAC
	TGGGGTACGCTCCAACGGGCTGGTCAGTGTTGGCTTCCTCATGCATTCTCAATGCCAAGGCTTTTTC
	TCTTCTCTAACGATGCTGAATCCTCTGAGACAGCTCTTTAAGCTGATGGCCTCTCTGTTTCTGTCGG
	TGTTCACACTTGGCCTTCCCTTTGCCCTCTTTCAGTATTATGCCTACACCCAATTCTGTCTGCCAGG
	CTCAGCCCGCCCCATTCCTGAGCCTTTGGTACAGTTAGCTGTAGACAAGGGCTACCGGATTGCAGAG
	GGAAATGAACCGCCTTGGTGCTTCTGGGATGTTCCACTAATATACAGCTATATCCAGGATGTCTACT
	GGAATGTTGGCTTTTTGAAATACTATGAGCTCAAGCAGGTGCCCAATTTTCTACTGGCTGCACCAGT
	GGCTATACTGGTTGCCTGGGCAACTTGGACATACGTGACCACTCACCCTTGGCTCTGCCTTACACTT
	GGGCTGCAAAGGAGCAAGAACAATAAGACCCTAGAGAAGCCCGATCTTGGATTCCTCAGTCCTCAGG
	TGTTTGTGTACGTGGTCCACGCTGCAGTGCTGCTGCTGTTTGGAGGTCTGTGCATGCATGTTCAGGT
	TCTCACCAGGTTTTTGGGCTCCTCCACTCCTATTATGTACTGGTTTCCAGCTCACTTGCTTCAGGAT
	CAAGAGCCGCTGTTGAGATCCTTAAAGACTGTGCCTTGGAAGCCTCTTGCAGAGGACTCCCCACCAG
	GACAAAAGGTCCCCAGAAATCCTATCATGGGACTTTTGTATCACTGGAAAACCTGTTCTCCAGTCAC
	ACGATACATTCTAGGCTACTTCCTGACTTACTGGCTCCTGGGACTACTCCTACATTGCAACTTCCTG
	CCTTGGACATGACCTGGACTCTCCAGGGACAGGTTGGAAGCCAACTTAACCCAGGGGTCTGAAAGTA
	AAAATACACATTGGAACTGCCTCTGCTGCCCTGGGATCATTACTGTGTCCATTATAAATCTTTCTCTT
	TCTCTTTGAAAGCTGGTCAGGAATGGGAGAAGTGTCAGACACTAGAGAGCCCCTTCTGGTCCTGGCT
	AGGGCAAATTTTAGACAACTATTTTCTCTGTAAGTGAAGATTGTCGTATTCCAAGTCTAAAATACAC
	CTGGATCTGTCTAGTCAATCAACATAGCAGAGACAGTCTTAAACCTACCATTGACCTGTGTGTAAAT
	TTAAATGTCAATTTATTGAAGTGTAAATTTCATCAAAGGCATTAGCTGACAGGCTGGTAACAGTCCA
	CACAAGATGGTATAGGCCTGAACAGTGTAGTGGCAGTAATAAAGTGGGACCATTTTTTCCAAAAAAA
	AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 139		ORF Stop: TGA at 1618
	SEQ ID NO: 106	493 aa	MW at 55699.9 kD
NOV25c,	MWPQDPSRKEVLRFAVSCRILTLMLQALFNAITPDHHAEAFSPPRLAPSGFVDQLVEGLLGGLSHWD
CG146625-03
Protein Sequence	AEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVAL
	HDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATG
	VRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGS
	ARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVA
	ILVAWATWTYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVL
	TRFLGSSTPIMYWFPAHLLQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTR
	YILGYFLTYWLLGLLLHCNFLPWT

[0500] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 25B.

TABLE 25B
Comparison of NOV25a against NOV25b and NOV25c.
	Protein	NOV25a Residues/	Identities/Similarities
	Sequence	Match Residues	for the Matched Region
	NOV25b	21 . . . 119	81/99 (81%)
		186 . . . 284	83/99 (83%)
	NOV25c	21 . . . 119	81/99 (81%)
		395 . . . 493	83/99 (83%)

[0501] Further analysis of the NOV25a protein yielded the following properties shown in Table 25C.

TABLE 25C
Protein Sequence Properties NOV25a
PSort     0.8025 probability located in lysosome (lumen); 0.7480
analysis: probability located in microbody (peroxisome); 0.4715
          probability located in mitochondrial matrix space; 0.1742
          probability located in mitochondrial inner membrane
SignalP   Cleavage site between residues 34 and 35
analysis:

[0502] A search of the NOV25a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 25D.

TABLE 25D
Geneseq Results for NOV25a
		NOV25a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABG65069	Human albumin	21 . . . 119	95/99 (95%)	8e−55
	fusion protein	182 . . . 280	97/99 (97%)
	#1744—Homo
	sapiens, 280 aa.
	[WO200177137-
	A1, 18 OCT.
	2001]
ABB89811	Human poly-	21 . . . 119	95/99 (95%)	8e−55
	peptide SEQ ID	75 . . . 173	97/99 (97%)
	NO 2187—Homo
	sapiens, 173 aa.
	[WO200190304-
	A2, 29 NOV.
	2001]
ABB97380	Novel human	21 . . . 119	95/99 (95%)	8e−55
	protein SEQ ID	395 . . . 493	97/99 (97%)
	NO: 648—Homo
	sapiens, 493 aa.
	[WO200222660-
	A2, 21 MAR.
	2002]
AAE07114	Human gene 9	21 . . . 119	95/99 (95%)	8e−55
	encoded secreted	213 . . . 311	97/99 (97%)
	protein fragment,
	SEQ ID NO:
	131—Homo
	sapiens, 311 aa.
	[WO200154708-
	A1, 2 AUG.
	2001]
AAE07059	Human gene 9	21 . . . 119	95/99 (95%)	8e−55
	encoded secreted	182 . . . 280	97/99 (97%)
	protein
	HTEGF16, SEQ
	ID NO: 76—
	Homo sapiens,
	280 aa.
	[WO200154708-
	A1, 2 AUG.
	2001]

[0503] In a BLAST search of public sequence datbases, the NOV25a protein was found to have homology to the proteins shown in the BLASTP data in Table 25E.

TABLE 25E
Public BLASTP Results for NOV25a
		NOV25a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9NUD9	DJ50O24.5.1	21 . . . 119	95/99 (95%)	2e−54
	(Novel protein	395 . . . 493	97/99 (97%)
	(Translation of
	cDNA KAT07271
	(Em: AK000484)))
	(Hypothetical 55.7
	kDa protein)—
	Homo sapiens
	(Human), 493 aa.
Q9NX26	CDNA FLJ20477	21 . . . 119	95/99 (95%)	2e−54
	fis, clone	395 . . . 493	97/99 (97%)
	KAT07271—Homo
	sapiens (Human),
	493 aa.
Q9U3X2	VEGETABLE	9 . . . 119	38/123 (30%)	0.057
	precursor—	361 . . . 449	50/123 (39%)
	Drosophila
	melanogaster
	(Fruit fly), 449 aa.
Q9V7W1	CG6657 protein—	9 . . . 119	38/123 (30%)	0.057
	Drosophila	361 . . . 449	50/123 (39%)
	melanogaster
	(Fruit fly), 449 aa.
Q95TV6	GM14315p—	9 . . . 119	38/123 (30%)	0.057
	Drosophila	185 . . . 273	50/123 (39%)
	melanogaster
	(Fruit fly), 273 aa.

[0504] PFam analysis predicts that the NOV25a protein contains the domains shown in the Table 25F.

TABLE 25F
Domain Analysis of NOV25a
	Pfam	NOV25a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value

Example 26

[0505] The NOV26 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 26A.

TABLE 26A
NOV26 Sequence Analysis
	SEQ ID NO: 107	1139 bp
NOV26a,	GCACTCACTACGCACAGACTCGACGGTGCCATCAGCATGAGAACTTACCGCTACTTCTTGCTGCTCT
CG147284-01
DNA Sequence	TTTGGGTGGGCCAGCCCTACCCAACTCTCTCAACTCCACTATCAAAGAGGACTAGTGGTTTCCCAGC
	AAAGAAAAGGGCCCTGGAGCTCTCTGGAAACAGCAAAAATGAGCTGAACCGTTCAAAAAGGAGCTGG
	ATGTGGAATCAGTTCTTTCTCCTGGAGGAATACACAGGATCCGATTATCAGTATGTGGGCAAGTTAC
	ATTCAAACTTTACCATTCAAGACAACAAAGACAACACGGCGGGAATCTTAACTCGGAAAAATGGCTA
	TAATAGACACGAGATGAGCACCTATCTCTTGCCTGTGGTCATTTCAGACAACGACTACCCAGTTCAA
	AGCAGCACTGGGACAGTGACTGTCCGGGTCTGTGCATCTGACCACCACGGGAACATGCAATCCTGCC
	ACGCGGAGGCGCTCATCCACCCCACGGGACTGAGCACGGGGGCTCTGGTTGCCATCCTTCTGTGCAT
	CGTGATCCTACTAGTGACAGTGGTGCTGTTTGCAGCTCTGAGGCGGCAGCGAAAAAAAGAGCCTTTG
	ATCATTTCCAAAGAGGACATCAGAGATAACATTGTCAGTTACAACGACGAAGGTGGTGGAGAGGAGG
	ACACCCAGGCTTTTGATATCGGCACCCTGAGGAATCCTGAAGCCATAGAGGACAACAAATTACGAAG
	GGACATTGTGCCCGAAGCCCTTTTCCTACCCCGACGGACTCCAACAGCTCGCGACAACACCGATGTC
	AGAGATTTCATTAACCAAAGGTTAAAGGAAAATGACACGGACCCCACTGCCCCGCCATACGACTCCT
	TGGCCACTTACGCCTATGAAGGCACTGGCTCCGTGGCGGATTCCCTGAGCTCGCTGGAGTCAGTGAC
	CACGGATGCAGATCAAGACTATGATTACCTTAGTGACTGGGGACCTCGATTCAAAAAGCTTGCAGAT
	ATGTATGGAGGAGTGGACAGTGACAAAGACTCCTAATCTGTTGCCTTTTTCATTTTCCAATACGACA
	CTGAAATATGTGAAGTGGCTATTTCTTTATATTTATCCACTACTCCGTGAAGGCTTCTCTGTTCTAC
	ORF Start: ATG at 37		ORF Stop: TAA at 1039
	SEQ ID NO: 108	334 aa	MW at 37675.7 kD
NOV26a,	MRTYRYFLLLFWVGQPYPTLSTPLSKRTSGFPAKKRALELSGNSKNELNRSKRSWMWNQFFLLEEYT
CG14728-01
Protein Sequence	GSDYQYVGKLHSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCA
	CDHHGNMQSCHAEALIHPTGLSTGALVAILLCIVILLVTVVLFAALRRQRKKEPLIISKEDIRDNIV
	SYNDEGGGEEDTQAFDIGTLRNPEAIEDNKLRRDIVPEALFLPRRTPTARDNTDVRDFINQRLKEND
	TDPTAPPYDSLATYAYEGTGSVADSLSSLESVTTDADQDYDYLSDWGPRFKKLADMYGGVDSDKDS

[0506] Further analysis of the NOV26a protein yielded the following properties shown in Table 26B.

TABLE 26B
Protein Sequence Properties NOV26a
PSort     0.7300 probability located in plasma membrane; 0.6400
analysis: probability located in endoplasmic reticulum (membrane);
          0.1000 probability located in endoplasmic reticulum (lumen);
          0.1000 probability located in outside
SignalP   Cleavage site between residues 22 and 23
analysis:

[0507] A search of the NOV26a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 26C.

TABLE 26C
Geneseq Results for NOV26a
			Identities/
		NOV26a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAW13131	Partial human	79 . . . 334	256/256	e−148
	cadherin-6—Homo		(100%)
	sapiens, 414 aa.	159 . . . 414	256/256
	[US5597725-A,		(100%)
	28 JAN. 1997]
AAW25659	Human cadherin-	79 . . . 334	256/256	e−148
	6—Homo		(100%)
	sapiens, 414 aa.	159 . . . 414	256/256
	[US5646250-A,		(100%)
	8 JUL. 1997]
AAR43564	Human cadherin-	79 . . . 311	233/233	e−133
	6—Homo		(100%)
	sapiens, 391 aa.	159 . . . 391	233/233
	[WO9321302-A,		(100%)
	28 OCT. 1993]
ABP47864	Human polypeptide	77 . . . 334	212/258	e−125
	SEQ ID NO 294—		(82%)
	Homo sapiens,	101 . . . 358	238/258
	358 aa.		(92%)
	[US2002042386-
	A1, 11 APR.
	2002]
AAU19644	Human novel extra-	77 . . . 334	212/258	e−125
	cellular matrix		(82%)
	protein, Seq ID No	101 . . . 358	238/258
	294—Homo		(92%)
	sapiens, 358 aa.
	[WO200155368-A1,
	2 AUG. 2001]

[0508] In a BLAST search of public sequence datbases, the NOV26a protein was found to have homology to the proteins shown in the BLASTP data in Table 26D.

TABLE 26D
Public BLASTP Results for NOV26a
		NOV26a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
P55285	Cadherin-6	79 . . . 334	256/256 (100%)	e−147
	precursor	535 . . . 790	256/256 (100%)
	(Kidney-cadherin)
	(K-cadherin)—
	Homo sapiens
	(Human), 790 aa.
P97326	Cadherin-6	79 . . 334	246/256 (96%)	e−143
	precursor	535 . . . 790	253/256 (98%)
	(Kidney-cadherin)
	(K-cadherin)—
	Mus musculus
	(Mouse), 790 aa.
P55280	Cadherin-6	79 . . . 334	239/256 (93%)	e−136
	precursor	535 . . . 789	246/256 (95%)
	(Kidney-cadherin)
	(K-cadherin)—
	Rattus norvegicus
	(Rat), 789 aa.
Q90762	Cadherin-6	79 . . . 334	232/256 (90%)	e−134
	precursor	535 . . . 790	243/256 (94%)
	(Cadherin-6B)
	(c-cad6B)—
	Gallus gallus
	(Chicken),
	790 aa.
Q9DFS1	Cadherin-6—	80 . . . 334	227/255 (89%)	e−132
	Xenopus laevis	538 . . . 792	240/255 (94%)
	(African clawed
	frog), 792 aa.

[0509] PFam analysis predicts that the NOV26a protein contains the domains shown in the Table 26E.

TABLE 26E
Domain Analysis of NOV26a
		Identities/
		Similarities
	NOV26a Match	for the Matched	Expect
Pfam Domain	Region	Region	Value
Cadherin_C_term	182 . . . 328	108/156 (69%)	6.6e−102
		142/156 (91%)

Example 27

[0510] The NOV27 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 27A.

TABLE 27A
NOV27 Sequence Analysis
	SEQ ID NO: 109	1082 bp
NOV27a,	AAGTGGCTTCATTTCAGTGGCTGACTTCCAGAGAGCAAATGGCTGGTTCCCCAACATGCCTCACC
CG147937-01
DNA Sequence	TCATCTATATCCTTTGGCAGCTCACAGGTCAGCAGCCTCTGGACCCGTGAAAGAGCTGGTCGGTTC
	CGTTGGTGGGGCCGTGACTTTCCCCCTGAAGTCCAAAGTAAGCAAGTTGACTCTATTGTCTGGACC
	TTCAACACAACCCCTCTTGTCACCATACAGCCAGAAGGGGGCACTATCATAGTGACCCAAAATCGTA
	ATAGGGAGAGAGTAGACTTCCCAGATGGAGGCTACTCCCTGAAGCTCAGCAAACTGAAGAAGAATGA
	CTCAGGGATCTACTATGTGGGGATATACAGCTCATCACTCCAGCAGCCCTCCACCCAGGAGTACGTG
	CTGCATGTCTACGAGCACCTGTCAAAGCCTAAAGTCACCATGGGTCTGCAGAGCAATAAGAATGGCA
	CCTGTGTGACCAATCTGACATGCTGCATGGAACATGGGGAAGAGGATGTGATTTATACCTGGAAGGC
	CCTGGGGCAAGCAGCCAATGAGTCCCATAATGGGTCCATCCTCCCCATCTCCTGGAGATGGGGAGAA
	AGTGATATGACCTTCATCTGCGTTGCCAGGAACCCTGTCAGCAGAAACTTCTCAAGCCCCATCCTTG
	CCAGGAAGCTCTGTGAAGGTGCTGCTGATGACCCAGATTCCTCCATGGTCCTCCTGTGTCTCCTGTT
	GGTGCCCCTCCTGCTCAGTCTCTTTGTACTGGGGCTATTTCTTTGGTTTCTGAAGAGAGAGAGACAA
	GAAGAGTACATTGAAGAGAAGAAGAGAGTGGACATTTGTCGGGAAACTCCTAACATATGCCCCCATT
	CTGGAGAGAACACAGAGTACGACACAATCCCTCACACTAATAGAACAATCCTAAAGGAAGATCCAGC
	AAATACGGTTTACTCCACTGTGGAAATACCGAAAAAGATGGAAAATCCCCACTCACTGCTCACGATG
	CCAGACACACCAAGGCTATTTGCCTATGAGAATGTTATCTAGACAGCAGTGCACTCCCCTAAGTCTC
	TGCTCAAAAA
	ORF Start: ATG at 40		ORF Stop: TAG at 1045
	SEQ ID NO: 110	335 aa	MW at 37420.5 kD
NOV27a,	MAGSPTCLTLIYILWQLTGSAASGPVKELVGSVGGAVTFPLKSKVKQVDSIVWTFNTTPLVTIQPEG
CG147937-01
Protein Sequence	GTIIVTQNRNRERVDFPDGGYSLKLSKLKKNDSGIYYVGIYSSSLQQPSTQEYVLHVYEHLSKPKVT
	MGLQSNKNGTCVTNLTCCMEHGEEDVIYTWKALGQAANESHNGSILPISWRWGESDMTFICVARNPV
	SRNFSSPILARKLCEGAADDPDSSMVLLCLLLVPLLLSLFVLGLFLWFLKRERQEEYIEEKKRVDIC
	RETPNICPHSGENTEYDTIPHTNRTILKEDPLANTVYSTVEIPKKEMPLHSLLTMPDTPRLFAYENVI
	SEQ ID NO:111	1121 bp
NOV27b,	AAGTGGCTTCATTTCAGTGGCTGACTTCCAGAGAGCAATATGGCTGGTTCCCCAACATGCCTCACCC
CG147937-01
DNA Sequence	TCATCTATATCCTTTGGCAGCTCACAGGGTCAGCAGCCTCTGGACCCGTGAAAGAGCTGGTCGGTTC
	CGTTGGTGGGGCCGTGACTTTCCCCCTGAAGTCCAAAGTAAAGCAAGTTGACTCTATTGTCTGGACC
	TTCAACACAACCCCTCTTGTCACCATACAGCCAGAAGGGGGCACTATCATAGTGACCCAAAATCGTA
	ATAGGGAGAGAGTAGACTTCCCAGATGGAGGCTACTCCCTGAAGCTCAGCAAACTGAAGAAGAATGA
	CTCAGGGATCTACTATGTGGGGATATACAGCTCATCACTCCAGCAGCCCTCCACCCAGGAGTACGTG
	CTGCATGTCTACGAGCACCTGTCAAAGCCTAAAGTCACCATGGGTCTGCAGAGCAATAAGAATGGCA
	CCTGTGTGACCAATCTGACATGCTGCATGGAACATGGGGAAGAGGATGTGATTTATACCTGGAAGGC
	CCTGGGGCAAGCAGCCAATGAGTCCCATAATGGGTCCATCCTCCCCATCTCCTGGAGATGGGGAGAA
	AGTGATATGACCTTCATCTGCGTTGCCAGGAACCCTGTCAGCAGAAACTTCTCAAGCCCCATCCTG
	CCAGGAAGCTCTGTGAAGGTGACTGCCTCTCCCTCTCCACAGGAGACTCTGCCCAGGTGCTGCTGA
	TGACCCAGATTCCTCCATGGTCCTCCTGTGTCTCCTGTTGGTGCCCCTCCTGCTCAGTCTCTTTGTA
	CTGGGGCTATTTCTTTGGTTTCTGAAGAGAGAGAGACAAGAAGAGTACATTGAAGAGAAGAAGAGAG
	TGGACATTTGTCGGGAAACTCCTAACATATGCCCCCATTCTGGAGAGAACACAGAGTACGACACAAT
	CCCTCACACTAATAGAACAATCCTAAAGGAAGATCCAGCAAATACGGTTTACTCCACTGTGGAAATA
	CCGAAAAAGATGGAAAATCCCCACTCACTGCTCACGATGCCAGACACACCAAGGCTATTTGCCTATG
	AGAATGTTATCTAGACAGCAGTGCACTCCCCTAAGTCTCTGCTCAAAAA
	ORF Start: ATG at 40		ORF Stop: TAG at 1084
	SEQ ID NO: 112	348 aa	MW at 38869.2 kD
NOV27b,	MAGSPTCLTLIYILWQLTGSAASGPVKELVGSVGGAVTFPLKSKVKQVDSIVWTFNTTPLVTIQPEG
CG147937-02
Protein Sequence	GTIIVTQNRNRERVDFPDGGYSLKLSKLKKNDSGIYYVGIYSSSLQQPSTQEYVLHVYEHLSKPKVT
	MGLQSNKNGTCVTNLTCCMEHGEEDVIYTWKALGQAANESHNGSILPISWRWGESDMTFICVARNPV
	SRNFSSPILARKLCEGDCLSPLHRRLCPGAADDPDSSMVLLCLLLVPLLLSLFVLGLFLWFLKRERQ
	EEYIEEKKRVDICRETPNICPHSGENTEYDTIPHTNRTILKEDPANTVYSTVEIPKKMENPHSLLTM
	PDTPRLFAYENVI

[0511] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 27B.

TABLE 27B
Comparison of NOV27a against NOV27b.
	NOV27a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV27b	1 . . . 335	290/348 (83%)
	1 . . . 348	290/348 (83%)

[0512] Further analysis of the NOV27a protein yielded the following properties shown in Table 27C.

TABLE 27C
Protein Sequence Properties NOV27a
PSort analysis:   0.4600 probability located in plasma membrane; 0.1000 probability located in
                  endoplasmic reticulum (membrane); 0.1000 probability located in
                  endoplasmic reticulum (lumen); 0.1000 probability located in outside
SignalP analysis: Cleavage site between residues 23 and 24

[0513] A search of the NOV27a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 27D.

TABLE 27D
Geneseq Results for NOV27a
		NOV27a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAB65224	Human PRO1138 (UNQ576)	1 . . . 335	335/335 (100%)	0.0
	protein sequence SEQ ID	1 . . . 335	335/335 (100%)
	NO:253 - Homo sapiens, 335
	aa. [WO200073454-A1,
	Dec. 7, 2000]
AAB87548	Human PRO1138 - Homo	1 . . . 335	335/335 (100%)	0.0
	sapiens, 335 aa.	1 . . . 335	335/335 (100%)
	[WO200116318-A2,
	Mar. 8, 2001]
AAB47321	APEX-1 - Homo sapiens,	1 . . . 335	335/335 (100%)	0.0
	335 aa. [WO200146260-A2.	1 . . . 335	335/335 (100%)
	Jun. 28, 2001]
AAU29119	Human PRO polypeptide	1 . . . 335	335/335 (100%)	0.0
	sequence #96 - Homo	1 . . . 335	335/335 (100%)
	sapiens, 335 aa.
	[WO200168848-A2,
	Sep. 20, 2001]
AAY66701	Membrane-bound protein	1 . . . 335	335/335 (100%)	0.0
	PRO1138 - Homo sapiens,	1 . . . 335	335/335 (100%)
	335 aa. [WO9963088-A2,
	Dec. 9, 1999]

[0514] In a BLAST search of public sequence datbases, the NOV27a protein was found to have homology to the proteins shown in the BLASTP data in Table 27E.

TABLE 27E
Public BLASTP Results for NOV27a
		NOV27a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q9NQ25	BA404F10.4 (Novel LY9	1 . . . 335	335/335 (100%)	0.0
	(Lymphocyte antigen 9) like	1 . . . 335	335/335 (100%)
	protein) (NK cell receptor)
	(Membrane protein
	FOAP-12) (CD2-like
	receptor activating cytotoxic
	cells) - Homo sapiens
	(Human), 335 aa.
Q9NY08	19A protein - Homo sapiens	1 . . . 335	334/335 (99%)	0.0
	(Human), 335 aa.	1 . . . 335	335/335 (99%)
Q9NY23	19A24 protein - Homo	1 . . . 316	273/316 (86%)	e−152
	sapiens (Human), 328 aa.	1 . . . 281	276/316 (86%)
AAH27867	19A24 protein - Homo	1 . . . 257	257/257 (100%)	e−149
	sapiens (Human), 296 aa.	1 . . . 257	257/257 (100%)
CAD39085	Hypothetical protein - Homo	120 . . . 335	212/217 (97%)	e−123
	sapiens (Human), 228 aa.	12 . . . 228	214/217 (97%)

[0515] PFam analysis predicts that the NOV27a protein contains the domains shown in the Table 27F.

TABLE 27F
Domain Analysis of NOV27a
Pfam Domain	NOV27a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 28

[0516] The NOV28 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 28A.

TABLE 28A
NOV28 Sequence Analysis
	SEQ ID NO: 113	561 bp
NOV28a,	CTTGTGGCCCCCGGCTGCAGCCTCAGTGGCATGGGGGTGAAGCGGAGCCTCCAGAGTGGGGGCATTC
CG148221-01
DNA Sequence	TGCTCAGCCTCGTGGCCAACGTCCTCATGGTGCTCTCCACGGCCACCAACTACTGGACCCGCCAACA
	AGAGGGCCACAGTGGCCTGTGGCAGGAATGCAACCACGGCATCTGCTCCAGCATCCCCTGCCAGAGT
	ACGCTGGCGGTGACTGTGGCGTGCATGGTGCTGGCGGTGGGTGTCGGCGTGGTGGGCATGGTGATGG
	GACTGCGGATTCGGTGCGACGAGGGCGAGTCGCTGCGGGGCCAGACCACGAGCGCCTTCCTCTTCCT
	CGGCGGACTGCTGCTGCTGACCGCCTTGATAGGCTACACCGTGAAGAATGCGTGGAAGAACAACGTC
	TTCTTCTCTTGGTCCTATTTTTCTGGGTGGCTGGCCTTACCCTTCTCAATTCTCGCGGGCTTCTGCT
	TTCTGCTGGCAGACATGATCATGCAGAGCACCGACGCCATCAGTGGATTCCCCGTGTGTCTGTGACT
	GCAGCCTGCCTGGGGCAGAATAAAG
	ORF Start: ATG at 31		ORF Stop: TGA at 532
	SEQ ID NO: 114	167 aa	MW at 17970.0 kd
NOV28a,	MGVKRSLQSGGILLSLVANVLMVLSTATNYWTRQQEGHSGLWQECNHGICSSIPCQSTLAVTVACMV
CG148221-01
Protein Sequence	LAVGVGVVGMVMGLRIRCDEGESLRGQTTSAFLFLGGLLLLTALIGYTVKNAWKNNVFFSWSYFSGW
	LALPFSILAGFCFLLADMIMQSTDAISGFPVCL
	SEQ ID NO: 115	561 bp
NOV28b,	CTTGTGGCCCCCGGCTGCAGCCTCAGTGGCATGGGGGTGAAGCGGAGCCTCCAGAGTGGGGGCATTC
CG148221-02
DNA Sequence	TGCTCAGCCTCGTGGCCAACGTCCTCATGGTGCTCTCCACGGCCACCAACTACTGGACCCGCCAACA
	AGAGGGCCACAGTGGCCTGTGGCAGGAATGCAACCACGGCATCTGCTCCAGCATCCCCTGCCAGAGT
	ACGCTGGCGGTGACTGTGGCGTGCATGGTGCTGGCGGTGGGTGTCGGCGTGGTGGGCATGGTGATGG
	GACTGCGGATTCGGTGCGACGAGGGCGAGTCGCTGCGGGGCCAGACCACGAGCGCCTTCCTCTTCCT
	CGGCGGACTGCTGCTGCTGACCGCCTTGATAGGCTACACCGTGAAGAATGCGTGGAAGAACAACGTC
	TTCTTCTCTTGGTCCTATTTTTCTGGGTGGCTGGCCTTACCCTTCTCAATTCTCGCGGGCTTCTGCT
	TTCTGCTGGCAGACATGATCATGCAGAGCACCGACGCCATCAGTGGATTCCCCGTGTGTCTGTGACT
	GCAGCCTGCCTGGGGCAGAATAAAG
	ORF Start: ATG at 31		ORF Stop: TGA at 532
	SEQ ID NO: 116	167 aa	MW at 17970.0 kD
NOV28b,	MGVKRSLQSGGILLSLVANVLMVLSTATNYWTRQQEGHSGLWQECNHGICSSIPCQSTALVTVACMW
CG148221-02
Protein Sequence	LAVGVGVVGMVMGLRIRCDEGESLRGQTTSAFLFLGGLLLLTALIGYTVKNAWKNNVFFSWSYFSGW
	LALPFSILAGFCFLLADMIMQSTDAISGFPVCL

[0517] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 28B.

TABLE 28B
Comparison of NOV28a against NOV28b.
	NOV28a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV28b	1 . . . 167	134/167 (80%)
	1 . . . 167	134/167 (80%)

[0518] Further analysis of the NOV28a protein yielded the following properties shown in Table 28C.

TABLE 28C
Protein Sequence Properties NOV28a
PSort analysis:   0.6850 probability located in endoplasmic reticulum (membrane); 0.6760
                  probability located in plasma membrane; 0.4600 probability located in Golgi
                  body; 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 28 and 29

[0519] A search of the NOV28a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 28D.

TABLE 28D
Geneseq Results for NOV28a
		NOV28a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU74822	Human REPTR 5 protein -	6 . . . 150	42/158 (26%)	2e−07
	Homo sapiens, 173 aa.	3 . . . 160	71/158 (44%)
	[WO200198354-A2,
	Dec. 27, 2001]
AAR30057	Rat PMP - Rattus rattus, 160	10 . . . 149	37/149 (24%)	1e−06
	aa. [WO9221694-A,	7 . . . 155	66/149 (43%)
	Dec. 10, 1992]
AAB48599	Mouse PMP-22 - Mus sp, 161	10 . . . 149	38/149 (25%)	3e−06
	aa. [U.S. Pat. NO. 6,150,136-A,	7 . . . 155	66/149 (43%)
	Nov. 21, 2000]
AAR30058	Mouse PMP - Mus musculus,	10 . . . 149	38/149 (25%)	3e−06
	160 aa. [WO9221694-A,	7 . . . 155	66/149 (43%)
	Dec. 10, 1992]
AAR30059	Bovine PMP - Bos taurus,	10 . . . 149	37/150 (24%)	2e−05
	160 aa. [WO9221694-A,	7 . . . 155	69/150 (45%)
	Dec. 10, 1992]

[0520] In a BLAST search of public sequence datbases, the NOV28a protein was found to have homology to the proteins shown in the BLASTP data in Table 28E.

TABLE 28E
Public BLASTP Results for NOV28a
		NOV28a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
AAH29518	Similar to RIKEN cDNA	1 . . . 167	166/167 (99%)	2e−93
	1700071E18 gene - Homo	1 . . . 167	167/167 (99%)
	sapiens (Human), 167 aa.
Q9D9H2	1700071E18Rik protein -	1 . . . 167	117/167 (70%)	2e−65
	Mus musculus (Mouse), 167	1 . . . 167	136/167 (81%)
	aa.
P54825	Lens fiber membrane	6 . . . 150	46/159 (28%)	4e−08
	intrinsic protein (MP17)	3 . . . 160	73/159 (44%)
	(MP18) (MP19) (MP20) -
	Rattus norvegicus (Rat), 173
	aa.
P56563	Lens fiber membrane	6 . . . 150	46/159 (28%)	4e−08
	intrinsic protein (MP17)	3 . . . 160	73/159 (44%)
	(MP18) (MP19) (MP20) -
	Mus musculus (Mouse), 173
	aa.
P20274	Lens fiber membrane	6 . . . 150	45/159 (28%)	6e−07
	intrinsic protein (MP18)	3 . . . 160	72/159 (44%)
	(MP19) (MP21) (MP23) -
	Bos taurus (Bovine), 173 aa.

[0521] PFam analysis predicts that the NOV28a protein contains the domains shown in the Table 28F.

TABLE 28F
Domain Analysis of NOV28a
		Identities/
		Similarities
	NOV28a Match	for the Matched	Expect
Pfam Domain	Region	Region	Value
PMP22_Claudin	5 . . . 147	36/188 (19%)	1.5e−05
		108/188 (57%)

Example 29

[0522] The NOV29 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 29A.

TABLE 29A
NOV29 Sequence Analysis
	SEQ ID NO: 117	2603 bp
NOV29a,	CGTGGGCCGGGGTCGCGCAGCGGGCTGTGGGCGCGCCCGGAGGAGCGACCGCCGCAGTTCTCGAGCT
CG148476-01
DNA Sequence	CCAGCTGCATTCCCTCCGCGTCCGCCCCACGCTTCTCCCGCTCCGGGCCCCGCAATGGCCCAGGCAG
	TGTGGTCGCGCCTCGGCCGCATCCTCTGGCTTGCCTGCCTCCTGCCCTGGGCCCCGGCAGGGGTGGC
	CGCAGGCCTGTATGAACTCAATCTCACCACCGATAGCCCTGCCACCACGGGAGCGGTGGTGACCATC
	TCGGCCAGCCTGGTGGCCAAGGACAACGGCAGCCTGGCCCTGCCCGCTGACGCCCACCTCTACCGCT
	TCCACTGGATCCACACCCCGCTGGTGCTTACTGGCAAGATGGAGAAGGGTCTCAGCTCCACCATCCG
	TGTGGTCGGCCACGTGCCCGGGGAATTCCCGGTCTCTGTCTGGGTCACTGCCGCTGACTGCTGGATG
	TGCCAGCCTGTGGCCAGGGGCTTTGTGGTCCTCCCCATCACAGAGTTCCTCGTGGGGGACCTTGTTG
	TCACCCAGAACACTTCCCTACCCTGGCCCAGCTCCTATCTCACTAAGACCGTCCTGAAAGTCTCCTT
	CCTCCTCCACGACCCGAGCAACTTCCTCAAGACCGCCTTGTTTCTCTACAGCTGGGACTTCGGGGAC
	GGGACCCAGATGGTGACTGAAGACTCCGTGGTCTATTATAACTATTCCATCATCGGGACCTTCACCG
	TGAAGCTCAAAGTGGTGGCGGAGTGGGAAGAGGTGGAGCCGGATGCCACGAGGGCTGTGAAGCAGAA
	GACCGGGGACTTCTCCGCCTCGCTGAAGCTGCAGGAAACCCTTCGAGGCATCCAAGTGTTGGGGCCC
	ACCCTAATTCAGACCTTCCAAAAGATGACCGTGACCTTGAACTTCCTGGGGAGCCCTCCTCTGACTG
	TGTGCTGGCGTCTCAAGCCTGAGTGCCTCCCGCTGGAGGAAGGGGAGTGCCACCCTGTGTCCGTGGC
	CAGCACAGCGTACAACCTGACCCACACCTTCAGGGACCCTGGGGACTACTGCTTCAGCATCCGGGCC
	GAGAATATCATCAGCAAGACACATCAGTACCACAAGATCCAGGTGTGGCCCTCCAGAATCCAGCCGG
	CTGTCTTTGCTTTCCCATGTGCTACACTTATCACTGTGATGTTGGCCTTCATCATGTACATGACCCT
	GCGGAATGCCACTCAGCAAAAGGACATGGTGGAGGTGGCTGATTTTGACTTTTCCCCCATGTCTGAC
	AAGAACCCGGAGCCACCCTCTGGGGTCAGGTGCTGCTGCCAGATGTGCTGTGGGCCTTTCTTGCTGG
	AGACTCCATCTGAGTACCTGGAAATTGTTCGTGAGAACCACGGGCTGCTCCCGCCCCTCTATAAGTC
	TGTCAAAACTTACACCGTGTGA+E,UN GCACTCCCCCTCCCCACCCCATCTCAGTGTTAACTGACTGCTGAC
	TTGGAGTTTCCAGCAGGGTGGTGTGCACCACTGACCAGGAGGGGTTCATTTGCGTGGGGCTGTTGGC
	CTGGATCATCCATCCATCTGTACAGTTCAGCCACTGCCACAAGCCCCTCCCTCTCTGTCACCCCTGA
	CCCCAGCCATTCACCCATCTGTACAGTCCAGCCACTGACATAAGCCCCACTCGGTTACCACCCCCTT
	GACCCCCTACCTTTGAAGAGGCTTCGTGCAGGACTTTGATGCTTGGGGTGTTCCGTGTTGACTCCTA
	GGTGGGCCTGGCTGCCCACTGCCCATTCCTCTCATATTGGCACATCTGCTGTCCATTGGGGGTTCTC
	AGTTTCCTCCCCCAGACAGCCCTACCTGTGCCAGAGAGCTAGAAAGAAGGTCATAAAGGGTTAAAAA
	TCCATAACTAAAGGTTGTACACATAGATGGGCACACTCACAGAGAGAAGTGTGCATGTACACACACC
	ACACACACACACACACACACACACACAGAAATATAAACACATGCGTCACATGGGCATTTCAGATGAT
	CAGCTCTGTATCTGGTTAAGTCGGTTGCTGGGATGCACCCTGCACTAGAGCTGAAAGGAAATTTGAC
	CTCCAAGCAGCCCTGACAGGTTCTGGGCCCGGGCCCTCCCTTTGTGCTTTGTCTCTGCAGTTCTTGC
	GCCCTTTATAAGGCCATCCTAGTCCCTGCTGGCTGGCAGGGGCCTGGATGGGGGGCAGGACTAATAC
	TGAGTGATTGCAGAGTGCTTTATAAATATCACCTTATTTTATCGAAACCCATCTGTGAAACTTTCAC
	TGAGGAAAAGGCCTTGCAGCGGTAGAAGAGGTTGAGTCAAGGCCGGGCGCGGTGGCTCACGCCTGTA
	ATCCCAGCACTTTGGGAGGCCGAGGCGGGTGGATCACGAGATCAGGAGATCGAGACCACCCTGGCTA
	ACACGGTGAAACCCCGTCTCTACTAAAAAAATACAAAAAGTTAGCCGGGCGTGGTGGTGGGTGCCTG
	TAGTCCCAGCTACTCGGGAGGCTGAGGCAGGAGAATGGTGCGAACCCGGGAGGCGGAGCTTGCAGTG
	AGCCCAGATGGCGCCACTGCACTCCAGCCTGAGTGACAGAGCGAGACTCTGTCTCCA
	ORF Start: ATG at 122		ORF Stop: TGA at 1427
	SEQ ID NO: 118	435 aa	MW at 48328.6 kD
NOV29a,	MAQAVWSRLGRILWLACLLPWAPAGVAAGLYELNLTTDSPATTGAVVTISASLVAKDNGSLALPADA
CG148476-01
Protein Sequence	HLYRFHWIHTPLVLTGKMEKGLSSTIRVVGHVPGEFPVSVWVTAADCWMCQPVARGFVVLPITEFLV
	GDLVVTQNTSLPWPSSYLTKTVLKVSFLLHDPSNFLKTALFLYSWDFGDGTQMVTEDSVVYYNYSII
	GTFTVKLKVVAEWEEVEPDATRAVKQKTGDFSASLKLQETLRGIQVLGPTLIQTFQKMTVTLNFLGS
	PPLTVCWRLKPECLPLEEGECHPVSVASTAYNLTHTFRDPGDYCFSIRAENIISKTHQYHKIQVWPS
	RIQPAVFAFPCATLITVMLAFIMYMTLRNATQQKDMVEVADFDFSPMSDKNPEPPSGVRCCCQMCCG
	PFLLETPSEYLEIVRENHGLLPPLYKSVKTYTV

[0523] Further analysis of the NOV29a protein yielded the following properties shown in Table 29B.

TABLE 29B
Protein Sequence Properties NOV29a
PSort analysis:   0.6400 probability located in plasma membrane; 0.4600 probability located in
                  Golgi body; 0.3700 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 25 and 26

[0524] A search of the NOV29a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 29C.

TABLE 29C
Geneseq Results for NOV29a
		NOV29a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB65220	Human PRO1383 (UNQ719)	1 . . . 435	423/435 (97%)	0.0
	protein sequence SEQ ID	1 . . . 423	423/435 (97%)
	NO:241 - Homo sapiens, 423
	aa. [WO200073454-A1,
	Dec. 7, 2000]
AAM25558	Human protein sequence	1 . . . 435	423/435 (97%)	0.0
	SEQ ID NO: 1073 - Homo	46 . . . 468	423/435 (97%)
	sapiens, 468 aa.
	[WO200153455-A2,
	Jul. 26, 2001]
AAU29113	Human PRO polypeptide	1 . . . 435	423/435 (97%)	0.0
	sequence #90 - Homo	1 . . . 423	423/435 (97%)
	sapiens, 423 aa.
	[WO200168848-A2,
	Sep. 20, 2001]
AAY66697	Membrane-bound protein	1 . . . 435	423/435 (97%)	0.0
	PRO1383 - Homo sapiens,	1 . . . 423	423/435 (97%)
	423 aa. [WO9963088-A2,
	Dec. 9, 1999]
ABG43580	Human peptide encoded by	185 . . . 239	55/55 (100%)	7e−24
	genome-derived single exon	1 . . . 55	55/55 (100%)
	probe SEQ ID 33245 - Homo
	sapiens, 55 aa.
	[WO200186003-A2,
	Nov. 15, 2001]

[0525] In a BLAST search of public sequence datbases, the NOV29a protein was found to have homology to the proteins shown in the BLASTP data in Table 29D.

TABLE 29D
Public BLASTP Results for NOV29a
		NOV29a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
CAD39014	Hypothetical protein - Homo	1 . . . 435	435/435 (100%)	0.0
	sapiens (Human), 435 aa.	1 . . . 435	435/435 (100%)
AAH30793	Similar to QNR-71 protein -	1 . . . 435	423/435 (97%)	0.0
	Homo sapiens (Human), 423	1 . . . 423	423/435 (97%)
	aa.
CAD38628	Hypothetical protein - Homo	27 . . . 435	396/409 (96%)	0.0
	sapiens (Human), 397 aa	1 . . . 397	396/409 (96%)
	(fragment).
AAM31285	Surface layer protein B -	177. . . 339	40/166 (24%)	1e−04
	Methanosarcina mazei	331 . . . 476	64/166 (38%)
	(Methanosarcina frisia), 879
	aa.
AAH32783	Similar to glycoprotein	150 . . . 212	23/64 (35%)	0.001
	(transmembrane) nmb -	254 . . . 317	36/64 (55%)
	Homo sapiens (Human), 572
	aa.

[0526] PFam analysis predicts that the NOV29a protein contains the domains shown in the Table 29E.

TABLE 29E
Domain Analysis of NOV29a
Pfam Domain	NOV29a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 30

[0527] The NOV30 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 30A.

TABLE 30A
NOV30 Sequence Analysis
	SEQ ID NO: 119	3273 bp
NOV30a,	CTCCCGGAGATGCCCCGCGGCAGCCGCGCTCGGGCTCTAAGAGAAAAAGGAGTTGGAATACAGAAT
CG148818-01
DNA Sequence	GCCCATCCTTTCCAGGAGAAAGACCACTGCAGGTCAGAAGAGCAGGTCTCAGGACAGCAGGGGCAGC
	TGCCTCTCTCTCTGAAGCATGGCTCAGGTGTGGAGAAGGGTTTCAGAACACTTCTGGGAATCCGTCA
	TTAACAGCTGAAGAGAAGACGATTACAGAAAAGCACCTTGAATTATGCCCTAGACCCAAGCAAGAAA
	CCACCACATCTAAAAGCACCAGTGGGCTTACAGACATAACATGGAGCTCCAGTGGAAGTGATTTGTC
	GGATGAAGATAAGACACTTTCTCAGTTACAGAGAGATGAATTACAGTTTATCGACTGGGAGATTGAC
	AGTGACAGGGCAGAGGCTAGTGACTGTGATGAATTTGAAGATGACGAGGGTGCTGTGGAAATCTCAG
	ACTGTGCTTCTTGTGCAAGTAATCAGTCTTTGACAAGTGATGAGAAGCTGTCGGAGCTTCCCAAGCC
	AAGTTCTATAGAAATTTTAGAGTATTCATCAGATAGTGAAAAAGAAGATGATTTGGAAAATGTCCTA
	CTCATTGATTCAGAATCCCCTCACAAATACCACGTGCAGTTTGCATCGGATGCAAGACAGATTATGG
	AGAGACTGATAGATCCAAGGACAAAATCAACAGAGACCATTTTGCATACACCTCAGAAACCCACAGC
	TAAGTTTCCCAGGACTCCAGAAAATTCAGCAAAGAAGAAGCTTTTAAGAGGTGGACTAGCAGAAAGA
	CTAAATGGACTGCAGAATCGAGAGAGATCTGCTATTTCTTTGTGGAGACATCAATGTATTTCTTACC
	AAAAGACACTTTCAGGTAGAAAATCTGGTGTATTAACTGTGAAAATTTTAGAGCTGCATGAGGAATG
	TGCCATGCAAGTTGCCATGTGTGAGCAGTTATTGGGGTCACCAGCCACCAGCTCCTCCCAAAGTGTG
	GCTCCCAGGCCTGGAGCTGGCCTGAAAGTTCTCTTCACCAAGGAGACTGCAGGCTACCTCAGGGGCC
	GTCCCCAGGACACTGTCCGGATCTTCCCTCCCTGGCAAAAACTGATTATTCCAAGTGGAAGTTGCCC
	TGTTATTCTGAATACTTACTTTTGTGAGAAAGTTGTTGCCAAAGAAGATTCAGAAAAAACTTGTGAA
	GTGTACTGTCCGGACATACCCCTTCCAAGAAGAAGCATCTCTTTGGCCCAGATGTTTGTAATTAAGG
	GTCTAACAAATAATTCACCTGAAATCCAGGTTGTGTGTAGTGGTGTAGCCACTACAGGGACAGCCTG
	GACCCATGGGCACAAAGAAGCAAAACAGCGCATCCCAACCAGCACTCCCCTGAGGGATTCTCTCCTG
	GATGTGGTGGAAAGCCAGGGAGCTGCCTCGTGGCCAGGAGCTGGAGTCCGAGTGGTGGTGCAAAGAG
	TGTATTCTCTTCCCAGCAGAGACAGCACCAGGGGTCAGCAGGGGGCCAGCTCAGGACACACAGACCC
	AGCTGGAACTCGAGCCTGCCTTCTGGTACAAGATGCCTGTGGAATGTTCGGTGAAGTGCACTTGGAG
	TTCACCATGTCGAAGGCAAGACAGTTGGAAGGGAAGTCTTGCAGCCTGGTGGGAATGAAGGTTCTAC
	AGAAAGTCACCAGAGGAAGGACAGCGGGGATTTTCAGTTTGATTGACACCCTGTGGCCCCCAGCGAT
	ACCTCTGAAAACACCTGGCCGCGACCAGCCCTGTGAAGAGATAAAAACTCATCTGCCTCCTCCAGCC
	TTGTGTTACATCCTCACAGCTCATCCAAATCTGGGACAAATTGATATAATTGACGAAGACCCCATTT
	ATAAGCTTTACCAGCCTCCAGTTACCCGCTGCTTAAGAGACATTCTCCAGATGAATGATCTTGGTAC
	CCGTTGCAGTTTCTATGCCACGGTGATTTACCAAAAACCACAGCTGAAGAGTCTGCTGCTTCTGGAG
	CAAAGGGAGATCTGGCTGCTAGTGACCGATGTCACTCTGCAAACGAAGGAGGAGAGAGACCCCAGGC
	TCCCCAAAACCCTGCTGGTCTATGTGGCCCCCTTGTGTGTGCTGGGCTCTGAAGTCCTGGAGGCACT
	CGCTGGGGCTGCCCCTCACAGCCTCTTCTTCAAGGACGCTCTCCGTGACCAGGGTCGGATTGTTTGT
	GCTGAACGAACTGTCCTCTTGCTTCAGAAGCCCCTTTTGAGTGTGGTCTCTGGTGCAAGTTCCTGTG
	AGCTGCCTGGCCCGGTGATGCTCGACAGCCTGGACTCTGCAACACCTGTCAACTCCATCTGCAGTGT
	TCAAGGCACTGTGGTTGGCGTGGACGAGAGCACTGCTTTCTCATGGCCTGTGTGTGACATGTGTGGC
	AACGGGAGATTGGAACAGAGGCCGGAAGACAGAGGCGCCTTTTCCTGTGGGGACTGCTCCCGGGTGG
	TCACATCTCCTGTTCTCAAGAGGCACCTGCAGGTCTTCCTGGACTGCCGCTCAAGACCGCAGTGCAG
	AGTGAAGGTCAAGGTAGGAGCCAGGCCAGAGCACGCACGCACTCCTAGCTCACTCCAACATAGCGAA
	GCTGTTGCAGCGCAGCATTTCCTCCCTGCTGAGGTTTGCCGCCGGTGAAGATGGGAGCTACGAAGTG
	AAGAGTGTCCTCGGAAAGGAAGTGGGGTTGTTAAATTGTTTTGTCCAGTCCGTAACCGCCCACCCGA
	CCAGCTGCATTGGATTGGAGGAAATCGAGCCTCTGAGTGCAGGAGGGGCCTCTGCAGAACACTAGCG
	GTTGCCGCAGGATCTGTGAACTTTGCAATGTGGCTGCAAGGGTGGTGGTGGTGGTGGTGATTTGGGG
	TAGTTATTTGTTAACTATGGACACAGTGAACGTAGTTTACGATCTTGAAATGAAACTTAGATTTTTC
	TGGGGAAATGTTCAGATACAGTTTTGTGAACTGTAAATCAAAATACCTTTTTCTACAGTTTATCTTT
	TATTTTCTGCAAATTTAGGAACATATTTACTCGTTTTCACATTGAATCTTAAGTTTAAGCTCTTCAT
	TTGGTATTTAGGCAATATATGAGAAAAAAATTTTTTTTGTTCATTTGTAATTTTAACAAGTTGAACA
	TTTTACCATGATTGAACATGTTTTTATTACAGTATTTAACATTCCCCCAAAGAATACCCTGCAAAGT
	GTAAACCTTTGTCCCATACTGTGATATTACTGTTCTGCTACAATAAATGTCAAACCT
	ORF Start: ATG at 10		ORF Stop: TGA at 2659
	SEQ ID NO: 120	883 aa	MW at 97134.4 kD
NOV30a,	MPRGSRARGSKRKRSWNTECPSFPGERPLQVRRAGLRTAGAAASLSEAWLRCGEGFQNTSGNPSLTA
CG148818-01
Protein Sequence	EEKTITEKHLELCPRPKQETTTSKSTSGLTDITWSSSGSDLSDEDKTLSQLQRDELQFIDWEIDSDR
	AEASDCDEFEDDEGAVEISDCASCASNQSLTSDEKLSELPKPSSIEILEYSSDSEKEDDLENVLLID
	SESPHKYHVQFASDARQIMERLIDPRTKSTETILHTPQKPTAKFPRTPENSAKKKLLRGGLAERLNG
	LQNRERSAISLWRHQCISYQKTLSGRKSGVLTVKILELHEECAMQVAMCEQLLGSPATSSSQSVAPR
	PGAGLKVLFTKETAGYLRGRPQDTVRIFPPWQKLIIPSGSCPVILNTYFCEKVVAKEDSEKTCEVYC
	PDIPLPRRSISLAQMFVIKGLTNNSPEIQVVCSGVATTGTAWTHGHKEAKQRIPTSTPLRDSLLDVV
	ESQGAASWPGAGVRVVVQRVYSLPSRDSTRGQQGASSGHTDPAGTRACLLVQDACGMFGEVHLEFTM
	SKARQLEGKSCSLVGMKVLQKVTRGRTAGIFSLIDTLWPPAIPLKTPGRDQPCEEIKTHLPPPALCY
	ILTAHPNLGQIDIIDEDPIYKLYQPPVTRCLRDILQMDLGTRCSFYATVIYQKPQLKSLLLLLEQRE
	IWLLVTDVTLQTKEERDPRLPKTLLVYVAPLCVLGSEVLEALAGAAPHSLFFKDALRDQGRIVCAER
	TVLLLQKPLLSVVSGASSCELPGPVMLDSLDSATPVNSICSVQGTVVGVDESTAFSWPVCDMCGNGR
	LEQRPEDRGAFSCGDCSRVVTSPVLKRHLQVFLDCRSRPQCRVKVKVGARPEHARTPSSLQHSEAVA
	AQHFLPAEVCRR

[0528] Further analysis of the NOV30a protein yielded the following properties shown in Table 30B.

TABLE 30B
Protein Sequence Properties NOV30a
PSort analysis:   0.4400 probability located in plasma membrane; 0.4284 probability located in
                  mitochondrial inner membrane; 0.2397 probability located in mitochondrial
                  matrix space; 0.2397 probability located in mitochondrial intermembrane
                  space
SignalP analysis: No Known Signal Sequence Predicted

[0529] A search of the NOV30a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 30C.

TABLE 30C
Geneseq Results for NOV30a
		NOV30a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAG76160	Human colon cancer antigen	175 . . . 206	29/32 (90%)	5e−08
	protein SEQ ID NO:6924 -	12 . . . 43	30/32 (93%)
	Homo sapiens, 43 aa.
	[WO200122920-A2,
	Apr. 5, 2001]
ABB60641	Drosophila melanogaster	59 . . . 255	51/199 (25%)	0.004
	polypeptide SEQ ID NO	284 . . . 462	85/199 (42%)
	8715 - Drosophila
	melanogaster, 476 aa.
	[WO200171042-A2,
	Sep. 27, 2001]
ABP39618	Staphylococcus epidermidis	17 . . . 237	52/224 (23%)	0.017
	ORF amino acid sequence	1831 . . . 2048	88/224 (39%)
	SEQ ID NO:4463 -
	Staphylococcus epidermidis,
	2137 aa. [U.S. Pat. No. 6,380,370-B1,
	Apr. 30, 2002]
AAB30809	Amino acid sequence of a	64 . . . 196	32/133 (24%)	0.030
	prion-like amyloidogenic	30 . . . 154	61/133 (45%)
	protein - Saccharomyces
	cerevisiae, 414 aa.
	[WO200075324-A2,
	Dec. 14, 2000]
AAW10529	Saccharomyces cerevisiae	64 . . . 196	32/133 (24%)	0.030
	nucleolin like protein, NOL1 -	30 . . . 154	61/133 (45%)
	Saccharomyces cerevisiae
	(S288C), 414 aa.
	[U.S. Pat. No. 5,470,971-A,
	Nov. 28, 1995]

[0530] In a BLAST search of public sequence datbases, the NOV30a protein was found to have homology to the proteins shown in the BLASTP data in Table 30D.

TABLE 30D
Public BLASTP Results for NOV30a
		NOV30a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q14159	KIAA0146 protein - Homo	1 . . . 851	850/851 (99%)	0.0
	sapiens (Human), 918 aa	4 . . . 854	851/851 (99%)
	(fragment).
Q8R305	Hypothetical 43.0 kDa protein -	527 . . . 851	223/325 (68%)	e−125
	Mus musculus (Mouse), 393	6 . . . 325	258/325 (78%)
	aa.
Q96BI5	Hypothetical 23.1 kDa protein -	701 . . . 851	150/151 (99%)	1e−82
	Homo sapiens (Human), 218	4 . . . 154	151/151 (99%)
	aa (fragment).
P97399	Dentin sialophosphoprotein	86 . . . 196	29/112 (25%)	0.029
	precursor (Dentin matrix	581 . . . 692	50/112 (43%)
	protein-3) (DMP-3)
	[Contains: Dentin
	phosphoprotein (Dentin
	phosphophoryn) (DPP) Dentin
	sialoprotein (DSP)] - Mus
	musculus (Mouse), 934 aa.
Q01538	Myelin transcription factor I	67 . . . 193	32/136 (23%)	0.051
	(MYT1) (MYTI) (Proteolipid	221 . . . 355	65/136 (47%)
	protein binding protein)
	(PLPB1) - Homo sapiens
	(Human), 1121 aa.

[0531] PFam analysis predicts that the NOV30a protein contains the domains shown in the Table 30E.

TABLE 30E
Domain Analysis of NOV30a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV30a Match Region	Region	Value
zf-B_box	792 . . . 837	11/49 (22%)	0.48
		32/49 (65%)

Example 31

[0532] The NOV31 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 31A.

TABLE 31A
NOV31 Sequence Analysis
	SEQ ID NO: 121	144 bp
NOV31a,	ACCATGAACCACACTGTCCAAACCCTCTTCACTCCTGCCAACACCGGCCGCTCCACCAACCATGAGA
CC149332-01
DNA Sequence	TGCTCAAGGAGAAGCATGAGGTGGCTGTGCTGGGGGCACCCCACAACCCTGTGCCTCCAGCGTTCAC
	CATGATCCACATCTGCAGTGAGACCTCCCTGCCCGACCATGTCGTCTGGTCCCTATTCCCACCCTC
	TTCAAGAATTCCTGCTGCCCGGACTTCATAGCATTCATCTACTCTGTGAAGTCTAGGGACAGGAAGA
	TGGTTGGTGACCTGACTGGGGCCCAGGCCTGTGTCTCCACTGCCAAGTGCCTGAACATCTGGGCCCT
	GGCTCTGGGCATCCTCCTGACCATTCTGCTCATCATCATCTCAGTGCTGATCTTCCAAGTCTCTCGA
	TAGAACAGGAGACAGCATCCGGGCCAGGAGCTCTGCCCAACCT
	ORF Start: ATG at 4		ORF Stop: TAG at 403
	SEQ ID NO: 122	133 aa	MW at 14678.1 kD
NOV31a,	MNHTVQTLFTPANTGRSTNHEMLKEKHEVAVLGAPHNPVPPAFTMIHICSETSVPDHVVWSLFNTLF
CG149332-01
Protein Sequence	KNSCCPDFIAFIYSVKSRDRKMVGDLTGAQACVSTAKCLNIWALALGILLTILLIIISVLIFQVSR

[0533] Further analysis of the NOV31a protein yielded the following properties shown in Table 31B.

TABLE 31B
Protein Sequence Properties NOV31a
PSort analysis:   0.7000 probability located in plasma membrane; 0.2000 probability located in
                  endoplasmic reticulum (membrane); 0.1242 probability located in microbody
                  (peroxisome); 0.1000 probability located in mitochondrial inner membrane
SignalP analysis: No Known Signal Sequence Predicted

[0534] A search of the NOV31a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 31C.

TABLE 31C
Geneseq Results for NOV31a
		NOV31a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABP43105	Human ovarian antigen	1 . . . 130	104/130 (80%)	3e−56
	HVCBB19, SEQ ID	11 . . . 140	113/130 (86%)
	NO:4237 - Homo sapiens,
	143 aa. [WO200200677-A1,
	Jan. 3, 2002]
AAE13797	Human lung tumour-specific	1 . . . 130	104/130 (80%)	3e−56
	protein SALT-T8 - Homo	1 . . . 130	113/130 (86%)
	sapiens, 133 aa.
	[WO200172295-A2,
	Oct. 4, 2001]
AAB44456	Human lung tumour-specific	1 . . . 130	104/130 (80%)	3e−56
	antigen encoded by cDNA	1 . . . 130	113/130 (86%)
	#71 - Homo sapiens, 133 aa.
	[WO200060077-A2,
	Oct. 12, 2000]
AAY29544	Human lung tumour protein	1 . . . 130	104/130 (80%)	3e−56
	SALT-T8 predicted amino	1 . . . 130	113/130 (86%)
	acid sequence - Homo
	sapiens, 133 aa.
	[WO9938973-A2,
	Aug. 5, 1999]
AAY93594	Protein encoded by I-8U gene	1 . . . 130	102/130 (78%)	3e−55
	from interferon-inducible	1 . . . 130	112/130 (85%)
	gene family - Homo sapiens,
	133 aa. [WO200035473-A2,
	Jun. 22, 2000]

[0535] In a BLAST search of public sequence datbases, the NOV31a protein was found to have homology to the proteins shown in the BLASTP data in Table 31D.

TABLE 31D
Public BLASTP Results for NOV31a
		NOV31a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q01628	Interferon-induced	1 . . . 130	104/130 (80%)	7e−56
	transmembrane protein 3	1 . . . 130	113/130 (86%)
	(Interferon-inducible protein
	1-8U) - Homo sapiens
	(Human), 133 aa.
AAH22439	Interferon induced	1 . . . 130	103/130 (79%)	6e−55
	transmembrane protein 3	1 . . . 130	112/130 (85%)
	(1-8U) - Homo sapiens
	(Human), 133 aa.
S17182	interferon-induced protein	1 . . . 130	102/130 (78%)	8e−55
	1-8U - human, 133 aa.	1 . . . 130	112/130 (85%)
Q01629	Interferon-induced	1 . . . 133	98/133 (73%)	2e−51
	transmembrane protein 2	1 . . . 132	110/133 (82%)
	(Interferon-inducible protein
	1-8D) - Homo sapiens
	(Human), 132 aa.
Q95MQ3	Interferon-induced protein	1 . . . 124	78/124 (62%)	9e−39
	1-8U - Bos taurus (Bovine),	1 . . . 124	97/124 (77%)
	146 aa.

[0536] PFam analysis predicts that the NOV31a protein contains the domains shown in the Table 31E.

TABLE 31E
Domain Analysis of NOV31a
Pfam Domain	NOV31a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 32

[0537] The NOV32 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 32A.

TABLE 32A
NOV32 Sequence Analysis
	SEQ ID NO: 123	702 bp
NOV32a,	GGTGGTCAGGGCGCCATGGCGCTGTCCTGGCTGCACCCCGTCGAGCTTGCGCTCTTTGCTGCCGCCT
CG149649-01
DNA Sequence	TCCTGTGCGGGGGCCGTGGCGGCCGCGGCGATGACTCGGACCCAGGGCTCCTTCAGTGGTAGATGTCC
	TGCTACTTTGTAGCTGGGGCCTCTGGCCTCTTGGCCCTCTACTGCCTCCTGCTTTTGCTCTTCTGGA
	TCTACAGCAGCTGCATCGAGGACTCCCACAGGGGTGCTATAGGGCTGCGCATTGCACTGGCCATCTC
	AGCTATAGCCGTCTTCCTGGTCTTGGTGTCTGCCTGTATCCTTCGATTTGGCACCAGGTCTCTCTGC
	AACTCCATCATCTCCTTGAACACTACAATTAGCTGTTCTGAAGCCCAGAAAATTCCATGGACACCCC
	CTGGAACTGCTCTGCAGTTTTACTCCAACCTACACAATGCTGAAACCTCTTCTTGGGTGAATTTGGT
	ATTGTGGTGTGTGGTCTTGGTGCTCCAGGTCGTGCAGTGGAAGTCTGAAGCCACCCCATACCGGCCT
	CTGGAGAGGGGTGACCCTGAGTGGAGCTCTGAGACAGATGCTCTCGTTGGGTCACGCCTTTCCCATT
	CCTGAAGAATAAGCGGAGTGCTTCCTGCAGCC
	ORF Start: ATG at 16		ORF Stop: TGA at 673
	SEQ ID NO: 124	219 aa	MW at 23550.0 kD
NOV32a,	MALSWLQRVELALFAAAFLCGAVAAAAMTRTQGSFSGRCPLYGVATLNGSSLALSRPSAPSLCYFVA
CG149649-01
Protein Sequence	GASGLLALYCLLLLLFWIYSSCIEDSHRGAIGLRIALAISAIAVFLVLVSACILRFGTRSLCNSIISC
	LNTTISCSEAQKIPWTPPGTALQFYSNLHNAETSSWVNLVLWCVVLVLQVVQWKSEATPYRPLERCD
	PEWSSETDALVGSRLSHS
	SEQ ID NO: 125	708bp
NOV32b,	GTGCTGCAATTCGCCCTTCATGGCGCTGTCCTGGCTGCAGCGCGTCGAGCTTGCGCTCTTTGCTCCC
CG149649-02
DNA Sequence	GCCTTCCTGTCCGGGGCCGTCGCGGCCGCGGCGATGACTCGGACCCAGGGCTCCTTCAGTGGTAGAT
	GTCCCCTGTATGGTGTGGCCACCCTGAATGGCTCCTCCCTCGCCTTATCCCGTCCCTCAGCACCATC
	CCTGTGCTACTTTGTAGCTGGGGCCTCTCGCCTCTTGGCCCTCTACTGCCTCCTGCTTTTGCTCTTC
	TGGATCTACACCAGCTGCATCGAGGACTCCCACAGAGGTGCTATAGGGCTGCGCATTGCACTGGCCA
	TCTCAGCTATAGCCGTCTTCCTGGTCTTGCTGTCTCCCTGTATCCTTCGATTTGGCACCAGGTCTCT
	CTGCAACTCCATCATCTCTTTGAACACTACAATTAGCTGTTCTCAAGCCCAGAAAATTCCATCGACA
	CCCCCTGGAACTGCTCTGCAGTTTTACTCCAACCTACACAATGCTGAAACCTCTTCTTGGCTGAATT
	TGGTATTGTGGTGTGTGGTCTTGGTGCTCCAGGTCGTGCAGTGGAAGTCTGAAGCCACCCCATACCG
	GCCTCTGCAGAGGGGTGACCCTGAGTCGAGCTCTGACACAGATGCTCTCGTTGGGTCACGCCTTTCC
	CATTCCTGAACAATAAGCGGAGTGCTAAGGGCCATTCC
	ORF Start: ATG at 20		ORF Stop: TGA at 677
	SEQ ID NO: 126	219aa	MW at 23550.0 kD
NOV32b,	MALSWLQRVELALFAAAFLCGAVAAAAMTRTQGSFSGRCPLYGVATLNGSSLALSRPSAPSLCYFVA
CG149649-02
Protein Sequence	GASGLLALYCLLLLLFWIYSSCIEDSHRGAICLRIALAISAIAVFLVLVSACILRFGTRSLCNSIIS
	LNTTISCSEAQKIPWTPPGTALQFYSNLHNAETSSNVNLVLWCVVLVLQVVQWKSEATPYRPLERGD
	PEWSSETDALVGSRLSHS

[0538] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 32B.

TABLE 32B
Comparison of NOV32a against NOV32b.
	NOV32a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV32b	1 . . . 219	160/219 (73%)
	1 . . . 219	160/219 (73%)

[0539] Further analysis of the NOV32a protein yielded the following properties shown in Table 32C.

TABLE 32C
Protein Sequence Properties NOV32a
PSort analysis:   0.6400 probability located in plasma membrane; 0.4600 probability located in
                  Golgi body; 0.3700 probability located in endoplasmic reticulum (membrane);
                  0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 25 and 26

[0540] A search of the NOV32a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 32D.

TABLE 32D
Geneseq Results for NOV32a
		NOV32a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU12071	Human PHT1 variant protein	19 . . . 138	40/134 (29%)	3.3
	from Caco-2 cells - Homo	14 . . . 142	54/134 (39%)
	sapiens, 577 aa.
	[WO200192468-A2,
	Dec. 6, 2001]
AAU12070	Human PHT1 variant protein	19 . . . 138	40/134 (29%)	3.3
	from BeWo cells - Homo	14 . . . 142	54/134 (39%)
	sapiens, 577 aa.
	[WO200192468-A2,
	Dec. 6, 2001]
AAU12069	Human PHT1 protein splice	19 . . . 138	40/134 (29%)	3.3
	variant - Homo sapiens, 295	14 . . . 142	54/134 (39%)
	aa. [WO200192468-A2,
	Dec. 6, 2001]
AAU12068	Human PHT1 protein isolated	19 . . . 138	40/134 (29%)	3.3
	from Caco-2 cells - Homo	14 . . . 142	54/134 (39%)
	sapiens, 577 aa.
	[WO200192468-A2,
	Dec. 6, 2001]
ABB91559	Herbicidally active	32 . . . 125	20/94 (21%)	5.6
	polypeptide SEQ ID NO 770 -	603 . . . 689	42/94 (44%)
	Arabidopsis thaliana, 763
	aa. [WO200210210-A2,
	Feb. 7, 2002]

[0541] In a BLAST search of public sequence datbases, the NOV32a protein was found to have homology to the proteins shown in the BLASTP data in Table 32E.

TABLE 32E
Public BLASTP Results for NOV32a
		NOV32a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9CY24	1810059G22Rik protein -	1 . . . 219	177/219 (80%)	e−100
	Mus musculus (Mouse), 219	1 . . . 219	191/219 (86%)
	aa.
Q9D8L7	1810059G22Rik protein -	1 . . . 219	176/219 (80%)	e−100
	Mus musculus (Mouse), 219	1 . . . 219	191/219 (86%)
	aa.
Q9FLD9	Similarity to	114 . . . 182	24/69 (34%)	0.60
	hedgehog-interacting protein -	611 . . . 676	35/69 (49%)
	Arabidopsis thaliana
	(Mouse-ear cress), 677 aa.
O83823	Hypothetical protein TP0851 -	96 . . . 143	20/48 (41%)	1.4
	Treponema pallidum, 724 aa.	280 . . . 326	28/48 (57%)
Q9JVM8	Hypothetical protein	132 . . . 188	15/58 (25%)	5.2
	NMA0774 - Neisseria	156 . . . 213	30/58 (50%)
	meningitidis (serogroup A),
	352 aa.

[0542] PFam analysis predicts that the NOV32a protein contains the domains shown in the Table 32F.

TABLE 32F
Domain Analysis of NOV32a
Pfam Domain	NOV32a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 33

[0543] The NOV33 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 33A.

TABLE 33A
NOV33 Sequence Analysis
	SEQ ID NO: 127	2105 bp
NOV33a,	AGGTGCAAAGCCTGGTGCCCCCGAGCCCTGCGGAGCTCGGGGCCAGCATGGCCCCCACGCTGCAACAG
CG149680-01
DNA Sequence	GCGTACCGGAGGCGCTGGTGCATGGCCTGCACGGCTGTGCTGGAGAACCTCTTCTTCTCTCCTGTAC
	TCCTGGGCTGGGGCTCCCTGTTGATCATTCTGAAGAACGAGGGCTTCTATTCCAGCACGTGCCCAGC
	TGAGAGCAGCACCAACACCACCCAGGATGAGCAGCGCAGGTGCCCTTGCTTCACTGCGTCCTGCACC
	CTCATGGCCCTGGCCTCCCGGGACGTCGAAGCTCTGTCTCCGTTGATATTCCTGGCGCTGTCCCTGA
	ATGGCTTTGGTGGCATCTGCCTAACGTTCACTTCACTCACGCTGCCCAACATGTTTGGCAACCTGCG
	CTCCACGTTAATGGCCCTCATGATTGGCTCTTACGCCTCTTCTGCCATTACGTTCCCAGGAATCAAG
	CTGATCTACGATGCCGGTGTGGCCTTCGTGGTCATCATGTTCACCTGGTCTGGCCTGGCCTGCCTTA
	TCTTTCTGAACTGCACCCTCAACTGGCCCATCGAAGCCTTTCCTGCCCCTGAGGAAOTCAATTACAC
	GAAGAAGATCAAGCTCAGTGGGCTGGCCCTGGACCACAAGGTGACAGGTGACCTCTTCTACACCCAT
	GTGACCACCATGGGCCAGAGGCTCAGCCAGAAGGCCCCCAGCCTGGAGGACGGTTCOGATGCCTTCA
	TGTCACCCCAGGATGTTCGGGGCACCTCAGAAAACCTTCCTGAGAGGTCTGTCCCCTTACGCAAGAG
	CCTCTGCTCCCCCACTTTCCTGTGGAGCCTCCTCACCATGGGCATGACCCAGCTGCGGATCATCTTC
	TACATGGCTGCTGTGAACAAGATGCTGGAGTACCTTGTGACTGGTGGCCAGGAGCATGAGACAAATG
	AACAGCAACAAAAGGTCGCAGAGACAGTTGGGTTCTACTCCTCCGTCTTCGGGGCCATGCAGCTGTT
	GTGCCTTCTCACCTGCCCCCTCATTCGCTACATCATGGACTGCCGGATCAAGGACTGCGTGGACGCC
	CCAACTCAGGGCACTGTCCTCGCAGATGCCAGGGACGGGGTTGCTACCAAATCCATCAGACCACGCT
	ACTGCAAGATCCAAAAGCTCACCAATGCCATCAGTGCCTTCACCCTGACCAACCTGCTGCTTGTGGG
	TTTTGGCATCACCTGTCTCATCAACAACTTACACCTCCAGTTTGTGACCTTTGTCCTGCACACCATT
	GTTCGACGTTTCTTCCACTCAGCCTGTGGGAGTCTCTATGCTGCAGTGTTCCCATCCAACCACTTTG
	GGACGCTGACAGGCCTGCAGTCCCTCATCAGTGCTGTGTTCGCCTTGCTTCAGCAGCCACTTTTCAT
	GGCGATGGTGGGACCCCTGAAAOGACAGCCCTTCTGGGTGAATCTGCGCCTCCTCCTATTCTCACTC
	CTGGGATTCCTGTTGCCTTCCTACCTCTTCTATTACCGTGCCCGGCTCCAGCAGGAGTACGCCGCCA
	ATGGGATGGGCCCACTCAAGGTCCTTAGCGGCTCTGAGGTGACCCCATAGACTTCTCAGACCAAGGG
	CCTCTGCTCCCCCACTTTCCTGTGGAGCCTCCTCACCATGGGCATGACCCAGCTGCGGATCATCTTC
	TACATGCACATAGAGCCATGGCCGTAGATTTATAAATACCAAGAGAAGTTCTATTTTTGTAAAGACT
	GCAAAAAGGAGGAAAAAAAAACCTTCAAAAACGCCCCCTAAGTCAACGCTCCATTGACTGAAGACAC
	TCCCTATCCTAGAGGGCTTGAGCTTTCTTCCTCCTTGGGTTGCAGGACACCAGGGTGCCTCTTATCT
	CCTTCTAGCGGTCTGCCTCCTGGTACCTCTTGGGGCGATCGGCAAACAGGCTACCCCTGAGGTCCCA
	TGTGCCATGAGTGTGCACACATGCATGTGTCTGTGTATGTGTGAATGTGAGAGAGACACAGCCCTCC
	TTTCAGAAGGAAAGGGGCCTGAGGTGCCAGCTGTCTCCTCGGTTACGGGTTGGCCGTCGGCCCCTTC
	CAGGGCCAGGAGGTCAGGTTCCTCAGCG
	ORF Start: ATG at 47		ORF Stop: TAG at 1589
	SEQ ID NO: 128	514 aa	MW at 56699.6 kD
NOV33a,	MAPTLQQAYRRRWWMACTAVLENLFFSAVLLGWGSLLIILKNEGFYSSTCPAESSTNTTQDEQRRWP
CG149680-01
Protein Sequence	CFTASCTLMALASRDVEALSPLIFLALSLNGFGGICLTFTSLTLPNMFGNLRSTLMALMIGSYASSA
	ITFPGIKLIYDAGVAFVVIMFTWSGLACLTFLNCTLNWPIEAFPAPEEVNYTKKIKLSGLALDHKVT
	GDLFYTHVTTMGQRLSQKAPSLEDGSDAFMSPQDVRGTSENLPERSVPLRKSLCSPTFLWSLLTMGM
	TQLRIIFYMAAVNKMLEYLVTGGQEHETNEQQQKVAETVGFYSSVFGAMQLLCLLTCPLIGYIMDWR
	IKDCVDAPTQGTVLGDARDGVATXSIRPRYCKIQKLTNAISAFTLTNLLLVGFGITCLINNLHLQFV
	TFVLHTIVRFGGHSACGSLYAAVFPSNHFGTLTGLQSLISAVFALLQQPLFMAMVGPLKGEPFWVNL
	GLLLFSLLGFLLPSYLFYYRARLQQEYAANGMGPLKVLSGSEVTA
	SEQ ID NO: 129	2284 bp
NOV33b,	AGGTGCAAAGCCTGGTGCCCCGAGCCCTGCGGAGCTCGGCCCAGCATGCCCCCCACGCTGCAACAC
CG149680-02
DNA Sequnce	GCGTACCGGAGGCGCTGGTGGATGGCCTCCACGGCTGTGCTGGAGAACCTCTTCTTCTCTGCTGTAC
	TCCTGGGCTGGGGCTCCCTGTTGATCATTCTGAAGAACGAGGGCTTCTATTCCAGCACGTGCCCAGC
	TGTTCCTGGTGTCATGTCCTGCGCCCTCCCTTCCCCCTCCTCAGCTGAGAGCAGCACCAACACCACC
	CAGGATGAGCAGCGCAGGTCGCCAGGCTGTGACCAGCAGGACGAGATGCTCAACCTGGGCTTCACCA
	TTGCTTCCTTCGTGCTCAGCGCCACCACCCTGCCACTGGGGATCCTCATGGACCGCTTTGGCCCCCG
	ACCCGTGCGGCTGGTTGGCAGTGCCTGCTTCACTGCGTCCTGCACCCTCATGGCCCTGCCCTCCCGG
	GACGTGGAAGCTCTGTCTCCGTTGATATTCCTGGCGCTGTCCCTGAATGGCTTTGGTGGCATCTGCC
	TAACGTTCACTTCACTCACGCTGCCCAACATGTTTGGGAACCTGCGCTCCACGTTAATGGCCCTCAT
	GATTGGCTCTTACGCCTCTTCTGCCATTACGTTCCCAGGAATCAAGCTGATCTACGATGCCGCTGTG
	GCCTTCGTGGTCATCATGTTCACCTGGTCTGGCCTGGCCTGCCTTATCTTTCTGAACTGCACCCTCA
	ACTGGCCCATCGAAGCCTTTCCTGCCCCTGAGGAAGTCAATTACACCAAGAAGATCAAGCTCAGTGG
	GCTGGCCCTGGACCACAAGGTGACAGGTGACCTCTTCTACACCCATGTGACCACCATGGGCCAGAGG
	CTCAGCCAGAAGGCCCCCAGCCTGGAGGACGGTTCGGATGCCTTCATGTCACCCCAGGATGTTCGGG
	GCACCTCAGAAAACCTTCCTGAGAGGTCTGTCCCCTTACGCAAGAGCCTCTGCTCCCCCACTTTCCT
	GTGGAGCCTCCTCACCATGGGCATGACCCAGCTGCGGATCATCTTCTACATGGCTGCTGTGAACAAG
	ATGCTGGAGTACCTTGTGACTGGTGGCCAGGAGCATGACACAAATCAACAGCAACAAAAGGTGGCAG
	AGACAGTTGGGTTCTACTCCTCCGTCTTCGGGGCCATGCAGCTGTTGTGCCTTCTCACCTGCCCCCT
	CATTGGCTACATCATGGACTGGCGGATCAAGGACTGCGTGGACGCCCCAACTCAGGCCACTGTCCTC
	GCAGATGCCAGGGACGGGGTTGCTACCAAATCCATCAGACCACGCTACTGCAACATCCAAAAGCTCA
	CCAATGCCATCAGTGCCTTCACCCTGACCAACCTGCTGCTTGTGGGTTTTGGCATCACCTGTCTCAT
	CAACAACTTACACCTCCAGTTTGTGACCTTTGTCCTGCACACCATTGTTCGAGGTTTCTTCCACTCA
	GCCTGTGGGAGTCTCTATGCTGCAGTGTTCCCATCCAACCACTTTGGGACGCTGACAGGCCTGCAGT
	CCCTCATCAGTGCTGTGTTCGCCTTGCTTCAGCAGCCACTTTTCATGGCGATGGTGGGACCCCTGAA
	AGGAGAGCCCTTCTGGGTGAATCTGGGCCTCCTGCTATTCTCACTCCTGGGATTCCTGTTGCCTTCC
	TACCTCTTCTATTACCGTGCCCGGCTCCAGCAGGAGTACGCCGCCAATGGGATGGGCCCACTGAAGG
	TGCTTAGCGGCTCTGAGGTGACCGCATAGACTTCTCAGACCAAGGGACCTGGATGACAGGCAATCAA
	GGCCTGAGCAACCAAAAGGAGTGCCCCATATGGCTTTTCTACCTGTAACATGCACATAGAGCCATCG
	CCGTAGATTTATAAATACCAAGACAAGTTCTATTTTTCTAAAGACTGCAAAAAGGAGGAAAAAAAAC
	CTTCAAAAACGCCCCCTAAGTCAACGCTCCATTGACTGAAGACAGTCCCTATCCTAGAGGGGTTGAG
	CTTTCTTCCTCCPTGGGTTGGAGGAGACCAGGGTGCCTCTTATCTCCTTCTAGCGGTCTGCCTCCTG
	CTTTCTTCCTCCTTGGGTTGGAGGAGACCAGGGTGCCTCTTATCTCCTTCTAGCGGTCTGCCTCCTG
	GTACCTCTTGGGGGGATCGGCAAACAGGCTACCCCTGAGGTCCCATGTGCCATGAGTGTGCACACAT
	GCATGTGTCTGTGTATGTGTGAATCTGAGAGAGACACAGCCCTCCTTTCAGAAGGAAAGGGGCCTGA
	GGTGCCAGCTGTGTCCTGGGTTAGGGGTTGGGGGTCGGCCCCTTCCAGGGCCAGGAGGTCAGGTTCC
	TCAGCG
	ORF Start: ATG at 47		ORF Stop: TAG at 1769
	SEQ ID NO: 130	574 aa	MW at 62959.8 kD
NOV33b,	MAPTLQQAYRRRWWMACTAVLENLFFSAVLLGWGSLLIILKNEGFYSSTCPAVPGVMCWALPSPSSA
CG149680-02
Protein Sequence	ESSTNTTQDEQRRWPGCDQQDEMLNLGFTIGSVLSATTLPLGILMDRFGPRPVRLVGSACFTASCT
	LMALASRDVEALSPLIFLALSLNGFGGICLTFTSLTLPNMFGNLRSTLMALMIGSYASSAITFPGIK
	LIYDAGVAFVVIMFTWSGLACLIFLNCTLNWPTEAFPAPEEVNYTKKIKLSGLALDHKVTGDLFYTH
	VTTMGQRLSQKAPSLEDGSDAFMSPQDVRGTSENLPERSVPLRKSLCSPTFLWSLLTMGMTQLRIIF
	YMAAVNKMLEYLVTGGQEHETNEQQQKVAETVGFYSSVFGAMQLLCLLTCPLIGYIMDWRIKDCVDA
	PTQGTVLGDARDGVATKSIRPRYCKIQKLTNAISAFTLTNLLLVGFCITCLINNLHLQFVTFVLHTI
	VRGFFHSACGSLYAAVFPSNHFGTLTGLQSLISAVFALLQQPLFMAMVGPLKGEPFWVNLGLLLFSL
	LGFLLPSYLFYYRARLQQEYAANGMCPLKVLSGSEVTA

[0544] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 33B.

TABLE 33B
Comparison of NOV33a against NOV33b.
	NOV33a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV33b	1 . . . 514	494/574 (86%)
	1 . . . 574	494/574 (86%)

[0545] Further analysis of the NOV33a protein yielded the following properties shown in Table 33C.

TABLE 33G
Protein Sequence Properties NOV33a
PSort analysis:   0.6450 probability located in mitochondrial inner membrane; 0.6000
                  probability located in plasma membrane; 0.5634 probability located in
                  mitochondrial intermembrane space; 0.4367 probability located in
                  mitochondrial matrix space
SignalP analysis: Cleavage site between residues 45 and 46

[0546] A search of the NOV33a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 33D.

TABLE 33D
Geneseq Results for NOV33a
		NOV33a	Identities/
Geneseq	Protein/Organism/length	Residues/Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAY44897	Human PB39 protein	1 . . . 514	514/559 (91%)	0.0
	dysregulated in prostate	1 . . . 559	514/559 (91%)
	cancer - Homo sapiens, 559
	aa. [W0200005376-A1,
	03 Feb. 2000]
AAW64554	Human liver cell clone	1 . . . 514	514/559 (91%)	0.0
	HP10301 protein - Homo	1 . . . 559	514/559 (91%)
	sapiens, 559 aa.
	[W09821328-A2,
	22 May 1998]
AAY44898	Human PB39 variant protein	1 . . . 467	467/512 (91%)	0.0
	dysregulated in prostate	1 . . . 512	467/512 (91%)
	cancer - Homo sapiens, 560
	aa. [W0200005376-A1,
	03 Feb. 2000]
AAB94537	Human protein sequence	68 . . . 514	447/447 (100%)	0.0
	SEQ ID NO: 15277 - Homo	39 . . . 485	447/447 (100%)
	sapiens, 485 aa.
	[EP1074617-A2,
	07 Feb. 2001]
AAE05505	Mature human HC-like	68 . . . 495	250/436 (57%)	e−38
	protein #2 - Homo sapiens,	85 . . . 505	320/436 (73%)
	529 aa. [W0200155435-A2,
	02 Aug. 2001]

[0547] In a BLAST search of public sequence datbases, the NOV33a protein was found to have homology to the proteins shown in the BLASTP data in Table 33E.

TABLE 33E
Public BLASTP Results for NOV33a
Protein		NOV33a	Identities/
Accession		Residues/Match	Similarities for	Expect
Number	Protein/Organism/Length	Residues	the Matched Portion	Value
O75387	PB39 (Prostate cancer	1 . . . 514	514/559 (91%)	0.0
	OVEREXPRESSED gene 1)	1 . . . 559	514/559 (91%)
	- Homo sapiens (Human),
	559 aa.
Q9D0H7	2610016F07Rik protein -	11 . . . 512	417/552 (75%)	0.0
	Mus musculus (Mouse), 654	101 . . . 652	453/552 (81%)
	aa.
AAH27923	Hypothetical 62.7 kDa	1 . . . 495	297/560 (53%)	e−154
	protein - Homo sapiens	1 . . . 545	374/560 (66%)
	(Human), 569 aa.
BAC11450	CDNA FLJ90692 fis, clone	68 . . . 495	250/436 (57%)	e−138
	PLACE1006443, weakly	16 . . . 436	320/436 (73%)
	similar to Homo sapiens
	PB39 mRNA - Homo sapiens
	(Human), 460 aa.
BAC11383	CDNA FLJ90587 fis, clone	68 . . . 495	249/436 (57%)	e−137
	PLACE1000914, weakly	16 . . . 436	320/436 (73%)
	similar to Homo sapiens
	PB39 mRNA - Homo sapiens
	(Human), 460 aa.

[0548] PFam analysis predicts that the NOV33a protein contains the domains shown in the Table 33F.

TABLE 33F
Domain Analysis of NOV33a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV33a Match Region	Region	Value

Example 34

[0549] The NOV34 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 34A.

TABLE 34A
NOV34 Sequence Analysis
	SEQ ID NO: 131	458 bp
NOV34a,	AATCGCCTTACATGATGTGGCCCATGCACACCCCACTGCTGCTGCTGACTGCCTTGATGGTGGCCGT
CG149777-01
DNA Sequence	GGCCGGGAGTGCCTCGGCCCAATCTAGGACCTTGGCAGGTGGCATCCATGCCACAGACCTCAATGAC
	AAGAGTGTGCAGCGTGCCCTGGACTTTGCCATCAGCGAGTACAACAAGGTCATTAATAAGGATGAGT
	ACTACAGCCGCCCTCTGCAGGTGATGGCTGCCTACCAGCAGATCGTGGGTGGGGTGAACTACTACTT
	CAATGTGAAGTTCGGTCGAACCACATGCACCAAGTCCCAGCCCAACTTGGACAACTGTCCCTTCAAT
	GACCAGCCAAAACTGAAAGAGGAAGAGTTCTGCTCTTTCCAGATCAATGAAGTTCCCTCGGAGGATA
	AAATTTCCATTCTGAACTACAAGTGCCGGAAAGTCTAGGGGTCTGTGCAAGGCCTG
	ORF Start: ATG at 12		ORF Stop: TAG at 438
	SEQ ID NO: 132	142 aa	MW at 16133.4 kD
NOV34a,	MMWPMHTPLLLLTALMVAVAGSASAQSRTLAGCIHATDLNDKSVQRALDFAISEYNKVINKDEYYSR
CG149777-01
Protein Sequence	PLQVMAAYQQIVGGVNYYFNVKFGRTTCTKSQPNLDNCPFNDQPKLKEEEFCSFQIMEVPWEDKISI
	LNYKCRKV
	SEQ ID NO: 133	285 bp
NOV34b,	AACATGATGTGGCCCATGCACACCCCACTGCTGCTGCTGACTGCCTTGATGGTGGCCGTGGCCGGGA
CG149777-02
DNA Sequence	GTGCCTCGGCCCAATCTAGGACCTTGGCAGGTGGCATCCATGCCACAGACCTCAATGACAAGAGTGT
	GCAGCGTGCCCTGGACTTTGCCTTCAATGACCAGCCAAAACTGAAAGAGGAAGAGTTCTGCTCTTTC
	CAGATCAATGAAGTTCCCTGGGAGGATAAAATTTCCATTCTGAACTACAAGTGCCGGAAAGTCTAGG
	GGTCTCTGCAAGGCCTG
	ORF Start: ATG at 4		ORF Stop: TAG at 265
	SEQ ID NO: 134	87 aa	MW at 9781.2 kD
NOV34b,	MMWPMHTPLLLLTALMVAVAGSASAQSRTLAGGIHATDLNDKSVQRALDFAFNDQPKLKEEEFCSFQ
CG149777-02
Protein Sequence	INEVPWEDKISILNYKCRKV
	SEQ ID NO: 135	280 bp
NOV34c,	CACCAACCTTATGATGTCGCCCATGCACACCCCACTGCTGCTGCTGACTGCCTTGATCGTGGCCGTG
257474374 DNA
Sequence	GCCGGGAGTCCCTCGGCCCAATCTAGGACCTTGGCAGGTGGCATCCATGCCACAGACCTCAATGACA
	AGAGTGTGCAGCGTGCCCTGGACTTTGCCTTCAATGACCAGCCAAAACTGAAAGAGGAAGAGTTCTG
	CTCTTTCCAGATCAATGAAGTTCCCTGGGAGGATAAAATTTCCATTCTGAACTACAAGTGCCGGAAA
	GTCCTCGAGGGC
	ORF Start: at 2		ORF Stop: end of sequence
	SEQ ID NO: 136	93 aa	MW at 10423.0 kD
NOV34c,	TKLMMWPMHTPLLLLTALMVAVAGSASAQSRTRLAGGIHATDLNDKSVQRALDFAFNDQPKLKEEEFC
257474374
Protein Sequence	SFQINEVPWEDKISILNYKCRKVLEG
	SEQ ID NO: 137	205 bp
NOV34d,	cACCAAGCTTCAATCTAGGACCTTGGCAGGTGGCATCCATGCCACAGACCTCAATGACAAGAGTGTG
257474386 DNA
Sequence	CAGCGTGCCCTGGACTTTGCCTTCAATGACCAGCCAAAACTGAAAGAGGAGAGTTCTGCTCTTTCC
	AGATCAATGAAGTTCCCTGGGAGGATAAAATTTCCATTCTGAACTACAAGTGCCGGAAAGTCCTCGA
	GGGC
	ORF Start: at 2		ORF Stop: end of sequence
	SEQ ID NO: 138	68 aa	MW at 7827.8 kD
NOV34d,	TKLQSRTLAGGIHATDLNDKSVQRALDFAFNDQPKLKEEEFCSFQINEVPWEDKISILNYKCRKVLE
257474386
Protein Sequence	G

[0550] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 34B.

TABLE 34B
Comparison of NOV34a against NOV34b through NOV34d.
		Identities/
	NOV34a Residues/	Similarities for
Protein Sequence	Match Residues	the Matched Region
NOV34b	1 . . . 142	67/142 (47%)
	1 . . . 87	69/142 (48%)
NOV34c	1 . . . 142	67/142 (47%)
	4 . . . 90	69/142 (48%)
NOV34d	26 . . . 142	58/117 (49%)
	4 . . . 65	60/117 (50%)

[0551] Further analysis of the NOV34a protein yielded the following properties shown in Table 34C.

TABLE 34C
Protein Sequence Properties NOV34a
PSort analysis:   0.7857 probability located in outside; 0.1000 probability located in
                  endoplasmic reticulum (membrane); 0.1000 probability located in
                  endoplasmic reticulum (lumen); 0.1000 probability located in lysosome
                  (lumen)
SignalP analysis: Cleavage site between residues 26 and 27

[0552] A search of the NOV34a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 34D.

TABLE 34D
Geneseq Results for NOV34a
		NOV34a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAO15149	Human cystatin D protein	1 . . . 142	142/142 (100%)	2e−80
	sequence - Homo sapiens,	1 . . . 142	142/142 (100%)
	142 aa. [US2002052476-A1,
	02 May 2002]
AAE02408	Human cystatin D precursor	1 . . . 142	142/142 (100%)	2e−80
	protein - Homo sapiens, 142	1 . . . 142	142/142 (100%)
	aa. [US6235708-B1,
	22 May 2001]
AAE04437	Human cystatin D	1 . . . 142	142/142 (100%)	2e−80
	homologue protein - Homo	1 . . . 142	142/142 (100%)
	sapiens, 142 aa.
	[US6245529-B1,
	12 Jun. 2001]
AAE11210	Human cystatin D (CysD)	1 . . . 142	142/142 (100%)	2e−80
	protein - Homo sapiens, 142	1 . . . 142	142/142 (100%)
	aa. [US6300477-B1,
	09 Oct. 2001]
AAY81137	Human wild-type cystatin D	21 . . . 142	122/122 (100%)	3e−68
	- Homo sapiens, 122 aa.	1 . . . 122	122/122 (100%)
	[WO200008159-A2,
	17 Feb. 2000]

[0553] In a BLAST search of public sequence datbases, the NOV34a protein was found to have homology to the proteins shown in the BLASTP data in Table 34E.

TABLE 34E
Public BLASTP Results for NOV34a
Protein		NOV34a	Identities/
Accession		Residues/Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
A47142	cystatin D precursor - human,	1 . . . 142	142/142 (100%)	7e−80
	142 aa.	1 . . . 142	142/142 (100%)
P28325	Cystatin D precursor - Homo	1 . . . 142	141/142 (99%)	6e−79
	sapiens (Human), 142 aa.	1 . . . 142	141/142 (99%)
P09228	Cystatin SA precursor	1 . . . 141	80/141 (56%)	2e−42
	(Cystatin S5) - Homo sapiens	1 . . . 141	108/141 (75%)
	(Human), 141 aa.
P01036	Cystatin S precursor (Salivary	1 . . . 141	79/141 (56%)	2e−41
	acidic protein-1) (Cystatin	1 . . . 140	109/141 (77%)
	SA-III) - Homo sapiens
	(Human), 141 aa.
P01037	Cystatin SN precursor	5 . . . 141	78/137 (56%)	5e−40
	(Salivary cystatin SA-1)	5 . . . 140	105/137 (75%)
	(Cystain SA-I) - Homo
	sapiens (Human), 141 aa.

[0554] PFam analysis predicts that the NOV34a protein contains the domains shown in the Table 34F.

TABLE 34F
Domain Analysis of NOV34a
		Identities/
	NOV34a	Similarities	Expect
Pfam Domain	Match Region	for the Matched Region	Value
cystatin	32 . . . 138	45/113 (40%)	1.6e-39
		99/113 (88%)

Example 35

[0555] The NOV35 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 35A.

TABLE 35A
NOV35 Sequence Analysis
	SEQ ID NO: 139	1733 bp
NOV35a,	GACACCGTGCGTACCGGCCTCCGGCCCCCGGCCACCGGGGCGGACCGCGGACCCCAGGCCATGTC
CG150005-01
DNA Sequence	CCATGAAAAGAGTTTTTTGGTGTCTGGGGACAACTATCCTCCCCCCAACCCTGGATATCCGGGGGGG
	CCCCACCCACCCATGCCCCCCTATGCTCAGCCTCCCTACCCTGGGGCCCCTTACCCACAGCCCCCTT
	TCCAGCCCTCCCCCTACGGTCAGCCAGGGTACCCCCATGGCCCCAGCCCCTACCCCCAAGCCCTACC
	CCCAGGGCCCCTACCCACAAGAGGGCTACCCACAGCCCCCCTACCCCCAGAGCCCCTTCCCCCCCAA
	CCCCTATGGACAGCCATTCCCAGGACAACACCCTGACTCACCCCAGCATGGAAACTACCAGGAGGAG
	GGTCCCCCATCCTACTATGACAACCAGGACTTCCCTGCCACCAACTGGGATAAGAGCATCCGACAGG
	CCTTCATCCGCAAGGTCTTCCTAGTGCTGACCTTGCAGCTGTCGGTGACCCTGTCCACGGTGTCTGT
	GTTCACTTTTGTTGCGGAGGTGAAGGGCTTTGTCCGGGAGAATGTCTGGACCTACTATGTCTCCTAT
	GCTGTCTTCTTCATCTCTCTCATCGTCCTCAGCTGTTGTGCGGACTTCCGGCGAAAGCACCCCTGGA
	ACCTTCTTGCACTGTCGGTCCTCACCGCCAGCCTGTCGTACATGGTGGGGATGATCGCCAGCTTCTA
	CAACACCGAGGCAGTCATCATGGCCGTGGGCATCACCACAGCCGTCTGCTTCACCGTCGTCATCTTC
	TCCATGCAGACCCGCTACGACTTCACCTCATGCATGGGCGTGCTCCTGGTGAGCATGGTGGTGCTCT
	TCATCTTCGCCATTCTCTGCATCTTCATCCGGAACCGCATCCTGGAGATCGTGTACGCCTCAACTGG
	GGCTCTGCTGCTGACCTGCTTCCTCGCAGTGCACACCCAGCTGCTGCTGGGGAACAAGCAGCTGTCC
	CTGACCCCAGAAGAGTATGTGTTTGCTGCGCTGAACCTGTACACAGACATCATCAACATCTTCCTGT
	ACATCCTCACCATCATTGGCCCGCCAAGGAGTAGCCGAGCTCCAGCTCGCTGTCCCCGCTCAGGTGG
	CACGGCTGCCCCTGGCACGGCAGTGCCAGCTGTACTTCCCCTCTCTCTTGTCCCCAGGCACAGCCTA
	GGCAAAAGGATGCCTCTCTCCAACCCTCCTGTATGTACACTGCAGATACTTCCATTTGGACCCGCTG
	TGGCCACAGCATGGGCCCCTTTAGTCCTCCCGCCCCCGCCAAGGGGCACCAAGGCCACCTTTCCGTG
	CCACCTCCTGTCTACTCATTGTTGCATGAGCCCTGTCTGCCAGCTTCCACCCCAGGGACTGGGGGTC
	AGCGAACAGGTCCAAGGATTGAGCTCAATGGGTGAGGGTGCACGTCTTCCCTCCTGTCCCAGCTCCC
	CAGCCTGCCGTAGAGCACCCCTCCCCTCCCCCCCAAGTGCTGCCCTCTGGGGACATGGCGGAGTGGG
	GGTCTTATCCCCTCAGGGCAGAGGATCGCATGTTTCAGGGCAGAGAGGAAGCCTTCCTCTCAATTTG
	TTGTCAGTGAAATTCCAATAAATGGGATTTGCTCTCTGCAAAAAAAAAAAAAAAAAAAAAAAAAGGA
	AGCAAAGCCCCCAACCGACAGCACCATCAAATCAGCAACTCACAACCGACCGACACCA
	ORF Start: ATG at 70		ORF Stop: TAA at 1627
	SEQ ID NO: 140	519 aa	MW AT 56107.8 kD
NOV35a,	MKRVFWCLGTTILPPTLDIRGGPSHPCPPMLSLPTLGPLTHSPLSSPPPTVSQGTPMAPPAPTPKPYP
CG150005-01
Protein Sequence	QGPYPQEGYPQGPYPQSPFPPNPYGQPFPGQDPDSPQHGNYQEEGPPSYYDNQDFPATNWDKSIRQA
	FIRKVFLVLTLQLSVTLSTVSVFTFVAEVKGFVRENVWTYYVSYAVFFISLIVLSCCGDFRRKHPWN
	LVALSVLTASLSYMVGMIASFYNTEAVINAVGITTAVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLF
	IFAILCIFIRNRILEIVYASTGALLLTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLY
	ILTIIGFPRSSRAPARCARSGGTAAPGTAVPAVLPLSLVPRHSLGKRMPLSNPPVCTLQILPFGPAV
	ATAWAPLVLPPPPRGTKATFPCHLLSTHCCMSPVCQLPPQGLGVSEQVQGLSSMGEGARLPSCPSSP
	AWRRAPLPSPPSAALWGHGGVGVLSPEGRGWHVSGERGSLPLNLLSVKFQ

[0556] Further analysis of the NOV35a protein yielded the following properties shown in Table 35B.

TABLE 35B
Protein Sequence Properties NOV35a
PSort analysis:   0.6000 probability located in plasma membrane; 0.5510 probability located in
                  mitochondrial inner membrane; 0.4000 probability located in Golgi body;
                  0.3000 probability located in endoplasmic reticulum (membrane)
SignalP analysis: Cleavage site between residues 22 and 23

[0557] A search of the NOV35a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 35C.

TABLE 35C
Geneseq Results for NOV35a
		NOV35a	Identities/
Geneseq	Protein/Organism/Length	Residues/Match	Similarities for	Expect
Identifier	[Patent #, Date]	Residues	the Matched Region	Value
AAW62612	Human glutamate-binding	1 . . . 341	337/365 (92%)	0.0
	protein (HGLUBP) - Homo	1 . . . 365	337/365 (92%)
	sapiens, 369 aa.
	[W09821241-A1,
	22 May 1998]
ABB12050	Human leukocyte HP00804	49 . . . 496	339/463 (73%)	e−180
	protein homologue, SEQ ID	1 . . . 461	350/463 (75%)
	NO:2420 - Homo sapiens,
	461 aa. [WO200157188-A2,
	09 Aug. 2001]
AAW64535	Human leukocyte cell clone	2 . . . 341	293/364 (80%)	e−161
	HP00804 protein - Homo	4 . . . 367	297/364 (81%)
	sapiens, 371 aa.
	[WO9821328-A2,
	22 May 1998]
AAY48255	Human prostate	50 . . . 328	240/304 (78%)	e−129
	cancer-associated protein 41	1 . . . 304	246/304 (79%)
	- Homo sapiens, 321 aa.
	[DE19811193-A1,
	16 Sep. 1999]
ABB60180	Drosophila melanogaster	67 . . . 344	134/291 (46%)	1e−65
	polypeptide SEQ ID NO	36 . . . 323	190/291 (65%)
	7332 - Drosophila
	melanogaster, 324 aa.
	[WO200171042-A2,
	27 Sep. 2001]

[0558] In a BLAST search of public sequence datbases, the NOV35a protein was found to have homology to the proteins shown in the BLASTP data in Table 35D.

TABLE 35D
Public BLASTP Results for NOV35a
		NOV35a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
S19586	N-methyl-D-	1 . . . 513	380/517 (73%)	0.0
	aspartate receptor	1 . . . 516	403/517 (77%)
	glutamate-binding
	chain—rat,
	516 aa.
Q63863	NMDA receptor	1 . . . 513	379/517 (73%)	0.0
	glutamate-binding	1 . . . 516	402/517 (77%)
	subunit—Rattus
	sp, 516 aa.
Q9ESF4	LAG protein—	22 . . . 341	277/322 (86%)	e−158
	Mus musculus	21 . . . 341	287/322 (89%)
	(Mouse), 345 aa.
O43836	NMDA receptor	197 . . . 399	172/207 (83%)	4e−83
	glutamate-binding	6 . . . 208	178/207 (85%)
	chain—Homo
	sapiens (Human),
	208 aa
	(fragment).
AAM68613	CG3798-PA—	67 . . . 344	134/291 (46%)	3e−65
	Drosophila	25 . . . 312	190/291 (65%)
	melanogaster
	(Fruit fly),
	313 aa.

[0559] PFam analysis predicts that the NOV35a protein contains the domains shown in the Table 35E.

TABLE 35E
Domain Analysis of NOV35a
Pfam	NOV35a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
UPF0005	157 . . . 344	76/208 (37%)	7.9e−79
		180/208 (87%)

Example 36

[0560] The NOV36 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 36A.

TABLE 36A
NOV36 Sequence Analysis
	SED ID NO: 141	1675 bp
NOV36a,	ATGGAGGGCGCAGGGCCCCGGGGGGCCGGGCCGGCGCGGCGCCGGGGAGCCGGGGGGCCGCCGTCAC
CG150189-01
DNA Sequence	CGCTGCTGCCGTCGCTGCTGCTGCTGCTGCTGCTCTGGATGCTGCCGGACACCGTGGCGCCTCAGGA
	ACTGAACCCTCGCGGCCGCAACGTGTGCCGTGCTCCCGGCTCCCAGGTGCCCACGTGCTCCGCTGGC
	TGGAGGCAGCAAGGGGACGAGTGTGGGATTGCGGTGTGCGAAGGCAACTCCACGTGCTCAGAGAACG
	AGGTGTGCGTGAGGCCTGGCGAGTGCCGCTGCCGCCACGGCTACTTCGGTGCCAACTGCGACACCAA
	GTGCCCGCGCCAGTTCTGCGGCCCCGACTGCAAGGAGCTGTGTAGCTGCCACCCACACGGGCAGTGC
	GAGGACGTGACAGGCCGGTGCAAGGGCCAGCAGCCGTGCACGGTGGCCGAGGGCCGCTGCTTGACGT
	GCGAGCCCGGCTGGAACGGAACCAAGTGCGACCAGCCTTGCGCCACCGGTTTCTATGGCGAGGGCTG
	CAGCCACCGCTGTCCGCCATGCCGCGACGGGCATGCCTGTAACCATGTCACCGGCAAGTGTACGCGC
	TGCAACGCGGGCTGGATCGGCGACCGGTGCGAGACCAACTGTAGCAATGCCACTTACGGCGAGGACT
	GCGCCTTCGTGTGCGCCGACTGCGGCAGCGGACACTGCGACTTCCAGTCGGGGCGCTGCCTGTGCAG
	CCCTGGCGTCCACGGGCCCCACTGTAACGTGACGTGCCCGCCCGGACTCCACGGCGCGGACTGTGCT
	CAGGCCTCCAGCTGCCACGAGGACTCGTGCGACCCGGTCACTGGTGCCTGCCACCTAGAAACCAACC
	AGCGCAAGGGCGTGATGGGCGCGGGCGCGCTGCTCGTCCTGCTCGTCTGCCTGCTGCTCTCGCTGCT
	TGGCTGCTGCTGCGCTTGCCGCGGCAAGGACCCTACGCGCCGGGAGCTTTCGCTTGGGAGGAAGAAG
	GCGCCGCACCGACTATGCGGGCGCTTCAGTCGCATCAGCATGAAGCTGCCCCGGATCCCGCTCCGGA
	GGCAGAAACTACCCAAAGTCGTAGTGGCCCACCACGACCTGGATAACACACTCAACTGCAGCTTCCT
	GGAGCCACCCTCAGGGCTGGAGCAGCCCTCACCATCCTGGTCCTCTCGGGCCTCCTTCTCCTCGTTT
	GACACCACTGATGAAGGCCCTGTGTACTGTGTACCCCATGAGGGTAAGTAAGGCCCTACCTGGGCAT
	CACTCCAGCCCAGTGAAATGTTCCCATGGAAAAGCTGTGTTCTGGGTGGGACACAGGAGAAGGGCAG
	GCAGCATGGAGAGGAAGGCCTTGGCCATGCTGGTACCTGAGGGTTGCCCACAGAGCTGAGGCCATAG
	AGCTGGACTCTGCTGCTCAGTACCGGAGACAGGTGTGGGGAGATGGGTAGGCCACAGCCCAGGGTTG
	CTCCTCGGGGAAAGTAGGCAGAGACAAGTTTCTGGGCTTAGGTAGGGGGTGGCAGAGGAGACAGGAG
	GAAGGGATCCACAGAGTATGGGAGTTGGATCCACACACAGCCTTTGATCCACAGATAGCAGAAAGGA
	GCCTGATGGTCTGGCATTCTGCCCCTAGAATTCAGCGGCCGCTTTTTTTTTTTTTTTTTTTTTTTTT
	ORF Start: ATG at 1		ORF Stop: TAA at 1255
	SEQ ID NO: 142	418 aa	MW at 44706.5 kD
NOV36a,	MEGAGPRGAGPARRRGAGGPPSPLLPSLLLLLLLWMLPDTVAPQELNPRGRNVCRAPGSQVPTCCAG
CG150189-01
Protein Sequence	WRQQGDECGIAVCEGNSTCSENEBCBRPGECRCRHGYFGANCDTKCPRQFWGPDCKELCSCHPHGQC
	EDVTGRCKGQQPCTVAEGRCLTCEPGWNGTKCDQPCATCFYGEGCSHRCPPCRDACNHVTGKCTR
	CNAGWIGDRCETKCSNGTYGEDCAFVCADCGSGHCDFQSGRCLCSPGVHGPHCNVTCPPGLHGADCA
	QACSCHEDSCDPVTGACHLETNQRKGVMCAGALLVLLVCLLLSLLGCCCACRGKDPTRRELSLGRKK
	APHRLCGRFSRISMXLPRIPLRRQKLPKVVVAHHDLDNTLNCSFLEPPSGLEQPSPSWSSRASFSSF
	DTTDEGPVYCVPHEGK

[0561] Further analysis of the NOV36a protein yielded the following properties shown in Table 36B.

TABLE 36B
Protein Sequence Properties NOV36a
PSort     0.6000 probability located in plasma membrane; 0.4000
analysis: probability located in Golgi body; 0.3000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in mitochondrial inner membrane
SignalP   Cleavage site between residues 44 and 45
analysis:

[0562] A search of the NOV36a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 36C.

TABLE 36C
Geneseq Results for NOV36a
		NOV36a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAM47668	MOL8b protein	64 . . . 416	298/370 (80%)	0.0
	sequence—Homo	202 . . . 564	308/370 (82%)
	sapiens, 865 aa.
	[WO200181578-
	A2, 1 NOV.
	2001]
AAM47667	MOL8a protein	64 . . . 416	298/370 (80%)	0.0
	sequence—Homo	271 . . . 633	308/370 (82%)
	sapiens, 884 aa.
	[WO200181578-
	A2, 1 NOV.
	2001]
AAB60394	Human nurse cell	64 . . . 416	298/370 (80%)	0.0
	receptor	202 . . . 564	308/370 (82%)
	B6TNC#10a,
	SEQ ID NO:
	24—Homo
	sapiens, 866 aa.
	[JP2000308492-
	A, 7 NOV. 2000]
AAB60393	Human nurse cell	64 . . . 416	298/370 (80%)	0.0
	receptor	202 . . . 564	308/370 (82%)
	B6TNC#10,
	SEQ ID NO:
	21—Homo
	sapiens, 866 aa.
	[JP2000308492-
	A, 7 NOV. 2000]
AAB60395	Human nurse cell	64 . . . 416	298/375 (79%)	0.0
	receptor	202 . . . 569	308/375 (81%)
	B6TNC#10b,
	SEQ ID NO:
	26—Homo
	sapiens, 871 aa.
	[JP2000308492-
	A, 7 NOV. 2000]

[0563] In a BLAST search of public sequence datbases, the NOV36a protein was found to have homology to the proteins shown in the BLASTP data in Table 36D.

TABLE 36D
Public BLASTP Results for NOV36a
		NOV36a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q96GP6	Unknown	113 . . . 416	282/304 (92%)	0.0
	(Protein for	5 . . . 296	286/304 (93%)
	IMAGE:
	4125591)—Homo
	sapiens (Human),
	598 aa
	(fragment).
CAD29035	Sequence 17	1 . . . 205	153/205 (74%)	2e−88
	from Patent	1 . . . 175	158/205 (76%)
	WO0214358—
	Homo sapiens
	(Human), 254 aa.
BAC02696	SREC-5—Homo	28 . . . 414	172/462 (37%)	7e−76
	sapiens (Human),	6 . . . 455	224/462 (48%)
	744 aa.
Q14162	Endothelial cells	35 . . . 414	153/405 (37%)	2e−75
	scavenger	154 . . . 541	195/405 (47%)
	receptor precursor
	(Acetyl LDL
	receptor)—Homo
	sapiens (Human),
	830 aa.
BAC02694	SREC-3—Homo	35 . . . 367	130/355 (36%)	1e−64
	sapiens (Human),	154 . . . 497	168/355 (46%)
	569 aa.

[0564] PFam analysis predicts that the NOV36a protein contains the domains shown in the Table 36E.

TABLE 36E
Domain Analysis of NOV36a
Pfam	NOV36a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
laminin_EGF	80 . . . 122	13/60 (22%)	0.13
		29/60 (48%)
laminin_EGF	126 . . . 183	19/66 (29%)	0.039
		41/66 (62%)
laminin_EGF	186 . . . 228	16/60 (27%)	0.33
		28/60 (47%)
laminin_EGF	231 . . . 271	18/60 (30%)	0.22
		31/60 (52%)

Example 37

[0565] The NOV37 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 37A.

TABLE 37A
NOV37 Sequence Analysis
	SEQ ID NO: 143	1025 bp
NOV37a,	TTGTGTCTCGCGCCGGCCCGCCAGCCCACCGGCGCCTGCGGCGGGGCGCGAAGCCATGGAGCCGCG
CG150267-01
DNA Sequence	GGCCCTCGTCACGGCGCTCAGCCTCGGCCTCAGCCTGTGCTCCCTGGGCCTGCTCGTCACGCCCATC
	TTCACCGACCACTGGTACGAGACCGACCCCCGGCGCCACAAGGAGAGCTGCGAGCGCAGCCGCGCGG
	GCGCCGACCCCCCGGACCAGAAGAACCGCCTGATGCCGCTGTCGCACCTGCCGCTGCGGGACTCGCC
	CCCGCTGGGCCGCCGGCTGCTCCCGGGCGGCCCGGGGCGCGCCGACCCCGAGTCCTGGCGCTCGCTC
	CTGGGCCTCGGCGGGCTGGACGCCGAGTCCGGCCGGCCCCTCTTCGCCACCTACTCGGGCCTCTGGA
	GGAAGTGCTACTTCCTGGGCATCGACCGGGACATCGACACCCTCATCCTGAAAGGTATTGCGCAGCG
	ATGCACGGCCATCAAGTACCACTTTTCTCAGCCCATCCGCTTGCGAAACATTCCTTTTAATTTAACC
	AAGACCATACAGCAAGATGAGTGGCACCTGCTTCCGATATTTTGCACCATTTCCCTCTGTACTTATG
	CCGCCAGTATCTCCTATGATTTGAACCGGCTCCCAAAGCTAATTTATAGCCTGCCTGCTGATGTGGA
	ACATGGTTACAGCTGGTCCATCTTTTGCGCCTGGTGCAGTTTAGGCTTTATTGTGGCAGCTGGAGGT
	CTCTGCATCGCTTATCCGTTTATTAGCCGGACCAAGATTGCACAGCTAAAGTCTGGCAGAGACTCCA
	CGGTAATGACTGTCCTCACTGGGCCTGTCCACAGTGCGAGCGACTCCTGACGGGGACAGCGCGGAGTT
	CAGGAGTCCAAGCACAAAGCGCTCTTTTACATTCCAACCTGTTGCCTGCCAGCCCTTTCTGGATTAC
	TGATAGAAAATCATGCAAAACCTCCCAACCTTTCTAAGGACAAGACTACTGTGGATTCAAGTGCTTT
	AATGACTATTTATGCGTTGA
	ORF Start: ATG at 57		ORF Stop: TGA at 810
	SEQ ID NO: 144	251 aa	MW at 28111.1 kD
NOV37a,	MEPRALVTALSLGLSLCSLGLLVTAIFTDHWYETDPRRHKESCERSRAGADPPDQKNRLMPLSHLPL
CG150267-01
Protein Sequence	RDSPPLGRRLLPGGPGRADPESWRSLLGLGGLDAECGRPLFATYSGLWRKCYFLGIDRDIDTLILKG
	IAQRCTAIKYHFSQPIRLRNIPFNLTKTIQQDEWHLLRIGCTISLCTYAASISYDLNRLPKLIYSLP
	ADVEHGYSWSIFCAWCSLGFIVAAGGLCIAYPFISRTKIAQLKSGRDSTV

[0566] Further analysis of the NOV37a protein yielded the following properties shown in Table 37B.

TABLE 37B
Protein Sequence Properties NOV37a
PSort     0.4600 probability located in plasma membrane; 0.3000
analysis: probability located in lysosome (membrane); 0.2800
          probability located in endoplasmic reticulum (membrane);
          0.2196 probability located in microbody (peroxisome)
SignalP   Cleavage site between residues 26 and 27
analysis:

[0567] A search of the NOV37a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 37C.

TABLE 37C
Geneseq Results for NOV37a
			Identities/
		NOV37a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABG61908	Prostate cancer-	1 . . . 251	250/297	e−142
	associated protein		(84%)
	#109—Mammalia,	1 . . . 297	250/297
	297 na.		(84%)
	[WO200230268-A2,
	18 APR. 2002]
AAB88388	Human membrane	1 . . . 251	250/297	e−142
	or secretory protein		(84%)
	clone PSEC0131—	1 . . . 297	250/297
	Homo sapiens,		(84%)
	297 aa.
	[EP1067182-A2,
	10 JAN. 2001]
AAE21272	Human gene 16	92 . . . 251	159/206	4e−85
	encoded secreted		(77%)
	protein fragment,	2 . . . 207	159/206
	SEQ ID NO: 138—		(77%)
	Homo sapiens,
	207 aa.
	[WO200216390-A1,
	28 FEB. 2002]
ABG64865	Human albumin	173 . . . 251	79/79	4e−41
	fusion protein		(100%)
	#1540—Homo	37 . . . 115	79/79
	sapiens, 115 aa.		(100%)
	[WO200177137-A1,
	18 OCT. 2001]
ABB90241	Human polypeptide	173 . . . 251	79/79	4e−41
	SEQ ID NO 2617—		(100%)
	Homo sapiens,	37 . . . 115	79/79
	115 aa.		(100%)
	[WO200190304-A2,
	29 NOV. 2001]

[0568] In a BLAST search of public sequence datbases, the NOV37a protein was found to have homology to the proteins shown in the BLASTP data in Table 37D.

TABLE 37D
Public BLASTP Results for NOV37a
		NOV37a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
CAC39753	Sequence 143	1 . . . 251	250/297 (84%)	e−142
	from Patent	1 . . . 297	250/297 (84%)
	EP1067182—
	Homo sapiens
	(Human), 297 aa.
AAH29530	Similar to	1 . . . 251	249/297 (83%)	e−142
	RIKEN cDNA	1 . . . 297	250/297 (83%)
	2810417M05
	gene—Homo
	sapiens (Human),
	297 aa.
Q9CZ16	2810417M05Rik	1 . . . 194	188/240 (78%)	e−104
	protein—Mus	1 . . . 240	191/240 (79%)
	musculus
	(Mouse), 241 aa.
BAC11344	CDNA FLJ90516	10 . . . 64	23/60 (38%)	0.43
	fis, clone	323 . . . 376	31/60 (51%)
	NT2RP3004481,
	weakly similar to
	BUTYROPHILIN
	PRECURSOR—
	Homo sapiens
	(Human), 388 aa.
CAC35426	Sequence 1	10 . . .64	23/60 (38%)	0.43
	from Patent	275 . . . 328	31/60 (51%)
	WO0118204—
	Homo sapiens
	(Human), 340 aa.

[0569] PFam analysis predicts that the NOV37a protein contains the domains shown in the Table 37E.

TABLE 37E
Domain Analysis of NOV37a
	Pfam	NOV37a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value

Example 38

[0570] The NOV38 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 38A.

TABLE 38A
NOV38 Sequence Analysis
	SEQ ID NO: 145	6094 bp
NOV38a,	CAGGTGGGCGGGCTGGTGGGCAGAAGGGCAGACGGGCAGAGGAAGTGCCAGTGCCACTGGGACCATG
CG1503662-01
DNA Sequence	GCTCTGACGGTAAGCGTGCACGACTAACAGGGCTGACCGGCACCCACGACCGACAAGTGAAGCTCA
	CCTTTCGAGGCTTTACCCAGAAAACAAGAAAAATTCACTGTGGTCCAGAAGCAGATATCGGTGAGCT
	GTTCCGATGGCCCCACTATGGGGCTCCACTCGCTGGGGAGTGTCTGTCTGTGCAGGTGGTCAACTGC
	AGCCGTGTATTCAGCCTTAGGCCTCTAGCGACCCTGGTGATCTCCCTGCAGCAGCTACAGAATGCTG
	GGCATTTGGTGCTACGGGAAGCCCTAGTGGATGAGAATCTTCAAGTGTCCCCGATCCAGGTGGAGCT
	TGACCTGAAGTACCAGCCCCCAGAGGGCGCTACTGGAGCCTGGTCAGAGGAGGACTTTGGGGCACCC
	ATCCAGGACAGCTTCGAGTTAATCATCCCCAATGTGGGCTTCCAGGAACTGGAGCCTGGGGAGGCCC
	AGCTGGAGCGGCGGGCAGTGGCTCTAGGCCGCAGGCTAGCTCGAAGTCTAGGCCAGCAGGACGATGA
	AGAGAATGAGCTGGAGCTTGAGCTGGAGCAGGACCTGGATGATGAGCCTGACGTGGAACTTTCTGGT
	GTTATGTTCAGCCCCCTCAAGAGCCGCGCCAGGGCCCTGCCCCATGGGGATCCCTTCCAGGTGTCCA
	GAGCTCAAGACTTCCAGGTGGGAGTCACTGTGCTGGAAGCCCAGAAACTGGTGGGAGTCAACATTAA
	CCCCTATGTGGCCGTGCAAGTGGCGGGGCAGCGCCGTGTGACCGCCACACAGCGTGCGACCAGTTGC
	CCCTTCTACAATGAGTACTTCTTGTTCGAATTTCATGACACGCGGCTTCGTCTCCAAGACTTGCTGC
	TGGAGATCACGGTGAGTGGGGTAGGGGTGACCAGTGTCCTTCACAGAAGGGGGGATGAGAAAGCTGC
	AGGACTAACACCACCTTCCCCCAAGGCTTTCCATTCGCAGACCCTCCCCTTTATGGCCACCCGGATA
	GGCACCTTCAGGATGCACCTGGGCATCATCTTGGACCAGCCAGATGGCCAGTTCTACCAAAGATGGG
	TTCCGCTGCATGATCCCCGAGACACCCGCGCCGGGACCAAGGGTTTCATTAAGGTCACCTTGTCCGT
	GAGGGCGCGCGGGGACCTGCCCCCTCCAATGCTACCCCCCGCCCCAGGGCACTGTTCGGACATCGAG
	AAGAACCTGCTCCTGCCGCGCGGGGTGCCCGCCGAGAGGCCATGGCCGCGGCTCCGCGTGCGCCTGT
	ACCGCGCCGAGGGGCTTCCCGCGCTGCGCCTGGGGCTGCTGGGCAGCCTGGTCCGCGCCCTGCACGA
	CCAGCGCGTCCTGGTGGAGCCCTATGTGCGGGTGTCTTTCCTGGGCCAGGAGGGCGAGACGTCGGTG
	AGCCCCGAGGCCGCGGCGCCCGAATGGAACGAGCAGCTGAGCTTCGTCCAGCTCTTCCCGCCGCTGA
	CGCGCAGCCTCCGCCTGCAGCTGCGGGACGACGCGCCCCTGGTCGACGCGGCACTCGCTACGCACGT
	GCCGGACCTGAGGCGGATCTCCCATCCGGGCCGCGCGGCGGGGTTTAACCCTACCTTCGGCCCGGCC
	TGGGTGCCCCTCTATGGCTCGCCCCCCCGCGCGGGGCTCCGGGATACTCTTCAAGGTCTCAACGAAG
	GCGTTGGCCAAGGCATTTGGTTCCGCGGCCGCCTTCTGCTGGCTGTGTCCATGCAGCTGTTGGAAGG
	GAGAGCTGAACCTGAGCCTCCCCAGGCCCAGCAGGGGTCCACGTTGTCCCGGCTCACCCGAAAGAAG
	AAAAAGAAAGCCAGAACGGATCAGACCCCAAAGGCGGTTCCGCACCACTTGGACGCCAGCCCCGGTG
	CCGAGGGGCCTGAGATCCCCCGTGCCATGGAGGTGGAGGTCGAGGACCTGCTGCCCCTGCCAGAGAA
	TGTCCTCGCGCCCTGTGAAGATTTCCTGCTTTTCGGTGTGCTCTTCGAGGCCACCATGATCGACCCC
	ACCGTGGCCTCCCAGCCCATCAGCTTCGAGATCTCCATTGGTCGCGCAGGCCGTCTGGAGGACCAAT
	TGGGCCGAGGGTCCAGGGCTGGGGAGGGAACTGAGGGTGCAGCCGTGGAGGCTCAGCCTCTGCTGGG
	AGCCAGGCCAGAGGAGGAGAAAGAGGAGGAAGAACTGGGGACCCATGCTCAGCGGCCTGAGCCCATG
	GACGGCAGTGGGCCATACTTCTGCTTGCCCCTCTGTCACTGCAAGCCATGCATGCATGTGTGGACTT
	GCTGGGAGGACCACACCTGGCGCCTGCAGAGCAGCAACTGCGTGCGCAAAGTGGCCGAGAGGCTGGA
	CCAGGGGCTGCAGGAGGTTGAGACACTGCAGCGCAAGCCGGGGCCTGGCGCCTGTGCACAGCTCAAG
	CACGCACTGGAAGTACTGGTGGCTGGGAGCAGACAGTTTTGCCACGGTGCCGAGCGCAGGACGATGA
	CCCGGCCCAATGCCCTGGATCGATGCCCGAGGGAACTCCTGGTGCACAGCCTGAACCTTTTGGCTAA
	GCAAGGACTGCGACTTCTACGCAGCCTGAGACCGCGCAATGTGCAAAAGAAGGTGGCACTGGCCAAG
	AAGCTCCTGCCAAAACTGCGCTTTCTGGCTGAGGAGCCCCAGCCACCCCTCCCCGATGTGCTGGTCT
	GGATCCTCAGCGGCCAGCGCCGTGTGGCCTGGGCCCGGATCCCTGCCCACGATGTGCTGTTCTCTGT
	GGTTGAGGAGGAACGGGGCCGAGACTGTGGCAAGATCCAGAGTCTAATGCTCACGGCACCCGGGGCA
	GCCCCTGGTGAGGTCTGTGCCAAGCTGGAGCTCTTCCTGCGGCTGGGCCTGGGCAAGCAAGCCAAGG
	CCTGCACCTCTGAGCTGCCCCCGGATTTGCTGCCCCAGCCCTCAGCCGGGCTGCCCTCCAGCCTACA
	CCGGGACGACTTTAGCTACTTCCAACTCCGCGCTCACTTGTACCAGGCCCGGGGTGTGTTGGCTGCA
	GATGACAGTCGCCTCTCGGACCCCTTTGCTCGAGTCCTCATCTCTACCCAGTGTCAGACCACACGGG
	TCCTGGAGCAGACGCTGAGCCCTCTGTGGGATGAACTCCTGGTATTTCAGCAGTTGATCGTGGATGG
	GAGGAGGGAGCACCTGCAGGAGGAGCCTCCATTAGTGATCATCAATGTATTTGACCACACTAAGTTT
	GGCCCCCCCGTGTTCCTGCGCAGGGCACTGGCCGCCCCAAGGGTAAAGCTCATGGAGGACCCATACC
	AACGCCCAGAGTTGCAGTTCTTCCCCCTGAGGAAGGGACCCTGGGCACCCGGAGAGCTCATTGCCGC
	CTTTCAACTCATTGAACTAGACTACAGTCGCCGACTTGAGCCCTCAGTGCCCAGTGAGGTGGAGCCC
	CAGGATCTGGCACCCCTGGTTGAGCCCCACTCTGGACGCCTGTCCCTTCCACCCAACGTGTGCCCAG
	TGCTCAGGGAGTTCCGTGTTCAGGTGCTGTTCTGGGGTCTTAGGGGACTTGGTCGTGTGCATCTGCT
	CGAGGTGGAGCAGCCCCAGGTTGTACTGGAGGTGGCTGGGCAAGGTGTGGAGTCTGAGGTCCTGGCC
	AGCTACCGTGAGAGCCCCAATTTCACTGAGCTTGTCAGCCATCTCACAGTGGTCTTCAAAGACACAG
	CTCCTCTCTTCCACCCCCAGGACTTGCCGGAGCAGCCTTACTTGCAGCCTCCACTCAGCATCTTGGT
	GATTGAGCGCCGGGCCTTTGGCCACACAGTCCTTGTGGGTTCCCACATTGTCCCCCACATGCTGCGA
	TTCACATTTCGGGGTCATGAGGATCCTCCTGAGGAGGAAGGAGAGATGGAGGAGACAGGGGATATGA
	TGCCCAAGGGACCTCAAGGACAGAAGTCCCTGGATCCCTTCTTGGCTGAAGCGGGTATATCCAGACA
	GCTCCTGAAGCCTCCTCTGAAGAAGCTCCCACTAGGAGGCCTCCTAAATCAAGGCCCTGGGCTGGAG
	GAAGACATCCCAGATCCAGAGGAGCTCGACTGGGGGTCCAAGTACTATGCGTCGCTGCAGGAGCTCC
	AGGGGCAGCACAACTTTGATGAAGATGAAATGGATGATCCTGGAGATTCAGATGGGGTCAACCTCAT
	TTCTATGGTTGGGGAGATCCAAGACCAGGGTGAGGCTGAAGTCAAAGGCACTGTGTCCCCAAAAAAA
	GCAGTTGCCACCCTGAAGATCTACAACAGGTCCCTGAAGGAAGAATTTAACCACTTTGAAGACTGGC
	TGAATGTGTTTCCTCTGTACCGAGGGCAAGGGGGCCAGGATGGAGGTGGAGAAGAGGAAGGATCTGG
	ACACCTTGTGGGCAAGTTCAAGGGCTCCTTCCTCATTTACCCTGAATCAGAGGCAGTGTTGTTCTCT
	GAGCCCCAGATCTCCCGGGGGATCCCACAGAACCGGCCCATCAAGCTCCTGGTCAGAGTGTATGTTG
	TAAAGGCTACCAACCTCGCTCCTGCAGACCCCAATGGCAAAGCAGACCCTTACGTGGTGGTGAGCGC
	TGGCCGGGAGCGGCAGGACACCAAGGAACGCTACATCCCCAAGCAGCTCAACCCCATCTTTGGACAG
	ATCCTGGAGCTAAGCATCTCTCTCCCAGCTGAGACGGAGCTGACGGTCGCCGTATTTGATCATGACC
	TCGTGGGTTCTGACGACCTCATCGGGGAGACCCACATTGATCTGGAAAACCGATTCTATAGCCACCA
	CAGAGCAAACTGTGGGCTGGCCTCCCAGTATGAAGTAGATGGTTACAATGCCTGGCGTGATGCATTC
	TGGCCTTCGCAGATCCTGGCGGGGCTGTGCCAACGCTGTGGCCTCCCTGCCCCTGAATACCGAGCCG
	GTGCTGTCAAGGTGGGCAGCAAAGTCTTCCTGACACCACCGGAGACCCTGCCCCCAGTGGCGAGCGG
	GGACCCTGAACAGGCCCAGGCATTGCTTGTGCTGCGGCGCTGGCAGGAAATGCCGGGTTTTGGGATC
	CAGCTGGTACCCGAGCATGTAGAAACCAGGCCTCTCTACCATCCCCACAGCCCAGGGCTGCTACAGG
	GATCTCTTCACATGTGGATTGACATCTTTCCTCAAGATGTGCCTGCTCCACCCCCAGTTGACATCAA
	GCCTCGGCAGCCAATCAGCTATGAGCTCAGAGTTGTCATCTGGAACACGGAGGATGTGGTTCTGGAT
	GACGAGAATCCACTCACCGCAGAGATGTCGAGTGACATCTATGTGAAGAGCTGAATGAAGGGGTTGG
	AGCATGACAAGCAGGAGACAGACGTTCACTTCAACTCCCTGACTGGGGAGGGGAACTTCAATTGGCG
	CTTTGTGTTCCGCTTTGACTACCTGCCCACGCAGCGGGAGGTCAGCGTCTGGCGCAGGTCTGGACCC
	TTTGCCCTGGAGGAGGCGGAGTTCCGGCAGCCTGCAGTGCTGGTCCTGCAGGTCTGGGACTATGACC
	GCATCTCTCCCAATCACTTCCTTGCATCCCTOCAGTTGCAGCTACCAGACATCGTCCGTGGGGCCCG
	GGGCCCCGAGCTCTGCTCTCTGCAGCTCGCCCGCAATGGGGCCGGGCCGACGTGCAATCTCTTTCGC
	TGCCGCCGCCTGAGGGGCTGGTGGCCGGTAGTGAAGCTGAAGGAGGCAGAGGACGGCAAGGTGGAGG
	CAGAGTTTGAGCTGCTGACTGTGGAGGAGGCCGAGAAACGGCCAGTGGGGAAGGGGCGGAAGCACCC
	ACAGCCTCTGGAGAAACCCAGCCGCCCCAAAACTTCCTTCAACTGCTTTGTGAACCCGCTGAAGACC
	TTTGTCTTCTTCATCTGGCGCCGGTACTGGCGCACCCTGGTGCTGCTGCTACTGGTGCTGCTCACCG
	TCTTCCTCCTCCTGGTCTTCTACACCATCCCTGCCCAGATCAGCCAGGTCATCTTCCGTCCCCTCCA
	CAAGTGACTCTCGCTGACCTTGGACACTCACCCAGGGTGCCAACCCTTCAATGCCTGCTCCTGG
	ORF Start: ATG at 65		ORF Stop: TGA at 6035
	SEQ ID NO: 146	1990 aa	MW at 222395.9 kD
NOV38a,	MALTVSVQRLTGLTGTHDRQVKLTFRGFTQKTRKIHCGPEADIGELGRWPHYGAPLAGECLSVQVVN
CG150362-01
Protein Sequence	CSRVFSLRPLGTVISLQQLQNAGHLVLREALVDENLQVSPIQVELDLKYQPPEGATGAWSEEDFGA
	PIQDSFELIIPNVGFQELEPGEAQLERRAVALGRRLARSLGQQDDEENELELELEQDLDDEPDVELS
	GVMFSPLKSRARALAHGDPFQVSRAQDFQVGVTVLEAQKLVGVNINPYVAVQVGGQRRVTATQRGTS
	CPFYNEYFLFEFHDTRLRLQDLLLEITVSGVGVTSVLQRRGDEKAAGLTPPSPKAFHSQTLPFMATR
	IGTFRMDLGIILDQPDCQFYQRWVPLHDPRDTFAGTKGFIKVTLSVRARGDLPPPMLPPAPGHCSDI
	EKNILLPRGVPAERPWARLRVRLYRAECLPALRLGLLGSLVRALHDQRVLVEPYVRVSFLGQEGETS
	VSAEAAAPEWNEQLSFVELFPPLTRSLRLQLRDDAPLVDAALATHVPDLRRISHPGRAAGFNPTFGP
	AWVPLYGSPPGAGLRDSLQGLNEGVGQGIWFRCRLLLAVSMQVLEGRAEPEPPQAQQGSTLSRLTRK
	KKKKARRDQTPKAVPQHLDASPGAECPEIPRAMEVEVEELLPLPENVLAFCEDFLLFGVLFEATMID
	FTVASQPISFEISIGRAGRLEEQLGRGSRAGEGTEGAAVEAQPLLGARPEEEKEEEELGTHAQRPEP
	MDGSGPYFCLPLCHCKPCMHVWSCWEDHTWRLQSSNCVRKVAERLDQGLQEVERLQRKPGPGACAQL
	KQALEVLVAGSRQFCHGAERRTMTRPNALDRCRGKLLVHSLNLLAKQGLRLLRSLRRRNVQKKVALA
	KKLLAKLRFLAEEPQPPLPDVLVWMLSGQRRVAWARIPAQDVLFSVVEEERGRDCGKIQSLMLTAPG
	APPGEVCAKLELFLRLGLGKQAKACTSELPPDLLPEPSAGLPSSLHRDDFSYFQLRAHLYQARGVLA
	ADDSCLSDPFARVLTSTQCQTTRVLEQTLSPLWDELLVFEQLIVDGRREHLQEEPPLVIINVFDHNK
	FGPPVFLGRALAAPRVKLMEDPYQRPELQFFPLRKGPWAAGELIAAFQLIELDYSGRLEPSVPSEVE
	PQDLAPLVEPHSGRLSLPPNVCPVLREFRVEVLFWGLRGLGRVHLLEVEQPQVVLEVAGQGVESEVL
	ASYRESPNFTELVRHLTVVFKDTAPLFHPQDLPEQPYLQPPLSILVTERRAFGHTVLVGSHIVPHML
	RFTFRGHEDFPEEEGEMEETGDMMPKGPQCQKSLDFFLAEAGTSRQLLKPPLKKLPLGGLLNQGPGL
	EEDIPDPEELDWGSKYYASLQELQGQHNFDEDEMDDPGDSDGVNLISMVGEIQDQGEAEVKGTVSPK
	KAVATLKIYNRSLKEEFNHFEDWLNVFPLYRGQGGQDGGGEEECSGHLVGKFKGSFLIYPESEAVLF
	SEPQISRGIPQNRPIKLLVRVYVVKATNLAPADPNGKADPYVVVSAGRERQDTKERYIPKQLNPIFG
	EILELSISLPAETELTVAVFDHDLVGSDDLIGETHIDLENRFYSHHRANCGLASQYEVDGYNAWRDA
	FWPSQILAGLCQRCGLPAPEYRAGAVKVGSKVFLTPPETLPPVASGDPEEAQALLVLRRWQEMPGFG
	IQLVPEHVETRPLYHPHSPGLLQGSLHMWIDIFPQDVPAPPPVDIKPRQPISYELRVVIWNTEDVVL
	DDENPLTGEMSSDTYXTKSWVKGLEHDKQETDVHFNSLTGEGNFNWRFVFRBDYLPTEREVSVRRSG
	PFALEEAEFRQPAVLVLQVWDYDRISANDFLGSLELQLPDMVRCARGPELCSVQLARNGAGPRCNLF
	RCRRLRGWWPVVKLKEAEDCKVEAEFELLTVEEAEKRPVCKGRKQPEPLEKPSRPKTSFNWFVNPLK
	TFVFFIWRRYWRTLVLLLLVLLTVFLLLVFYTIPGQISQVTFRPLHK

[0571] Further analysis of the NOV38a protein yielded the following properties shown in Table 38B.

TABLE 38B
Protein Sequence Properties NOV38a
PSort     0.8000 probability located in mitochondrial inner membrane;
analysis: 0.7000 probability located in plasma membrane; 0.3793
          probability located in microbody (peroxisome); 0.3500
          probability located in nucleus
SignalP   No Known Signal Sequence Predicted
analysis:

[0572] A search of the NOV38a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 38C.

TABLE 38C
Geneseq Results for NOV38a
			Identities/
		NOV38a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU70673	Human otoferlin	1 . . . 1984	811/2104	0.0
	#2—Homo		(38%)
	sapiens, 1997 aa.	1 . . . 1994	1198/2104
	[WO200170972-		(56%)
	A2, 27 SEP.
	2001]
AAU70669	Murine cochlea	1 . . . 1978	797/2091	0.0
	otoferlin—Mus		(38%)
	sp, 2298 aa.	35 . . . 2017	1188/2091
	[W0200170972-		(56%)
	A2, 27 SEP.
	2001]
AAU70674	Murine otoferlin	1 . . . 1978	797/2091	0.0
	#2—Mus		(38%)
	sp, 1992 aa.	1 . . . 1983	1188/2091
	[W0200170972-		(56%)
	A2, Sep. 27,
	2001]
AAU70675	Human	803 . . . 1984	540/1249	0.0
	otoferlin—Homo		(43%)
	sapiens, 1230 aa.	12 . . . 1227	769/1249
	[WO200170972-		(61%)
	A2, 27 SEP.
	2001]
AAU70672	Human otoferlin	783 . . . 1984	542/1289	0.0
	#1—Homo		(42%)
	sapiens, 1307 aa.	49 . . . 1304	778/1289
	[WO200170972-		(60%)
	A2, 27 SEP.
	2001]

[0573] In a BLAST search of public sequence datbases, the NOV38a protein was found to have homology to the proteins shown in the BLASTP data in Table 38D.

TABLE 38D
Public BLASTP Results for NOV38a
			Identities/
		NOV38a	Similarities
Protein		Residues/	for the
Accession	Protein/	Match	Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9HC10	Otoferlin (Fer-1 like	1 . . . 1984	810/2104	0.0
	protein 2)—Homo		(38%)
	sapiens (Human),	1 . . . 1994	1197/2104
	1997 aa.		(56%)
Q9ESF1	Otoferlin (Fer-1 like	1 . . . 1984	803/2100	0.0
	protein 2)—Mus		(38%)
	musculus (Mouse),	1 . . . 1994	1188/2100
	1997 aa.		(56%)
Q9H4S7	BA563A22B.1	885 . . . 1499	615/615	0.0
	(Contains a novel		(100%)
	protein similar to	1 . . . 615	615/615
	otoferlin (A FER-1-		(100%)
	like protein))—
	Homo sapiens
	(Human), 615 aa
	(fragment).
Q9NTZ8	DJ309K20.1.1	231 . . . 782	552/552	0.0
	(Novel protein		(100%)
	similar to dysferlin,	1 . . . 552	552/552
	isoform 1)—Homo		(100%)
	sapiens (Human),
	552 aa (fragment).
Q9H448	DJ477O4.1.1	1500 . . . 1990	491/531	0.0
	(Novel protein		(92%)
	similar to	1 . . . 531	491/531
	otoferlin and		(92%)
	dysferlin, isoform
	1)—Homo sapiens
	(Human), 531 aa
	(fragment).

[0574] PFam analysis predicts that the NOV38a protein contains the domains shown in the Table 38E.

TABLE 38E
Domain Analysis of NOV38a
	Pfam	NOV38a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value
	C2	231 . . . 303	23/97 (24%)	0.037
			49/97 (51%)
	C2	421 . . . 515	26/107 (24%)	0.0038
			60/107 (56%)
	C2	993 . . . 1083	26/101 (26%)	0.0015
			61/101 (60%)
	C2	1493 . . . 1576	32/97 (33%)	1.8e−11
			57/97 (59%)

Example 39

[0575] The NOV39 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 39A.

TABLE 39A
NOV39 Sequence Analysis
	SEQ ID NO: 147	1293 bp
NOV39a,	ATCAATACCAGCTCTGCCAGTAAGAGTTGCATCTCCCAGTGAATGCTGCTGCTCCCATTTCAAC
CG150637-01
DNA Sequence	TGTTAGCTGTTCTCTTTCCTGGTGGTAACAGTGAACATGCCTTCCAGGGGCCGACCTCCTTTCATGT
	TATCCAGACCTCGTCCTTTACCAATAGTACCTGGGCACAACTCAAGGCTCAGGCTGGTTGGATGAT
	TTGCAGATTCATGGCTGGGATAGCGACTCAGGCACTGCCATATTCCTGAAGCCTTGGTCTAAAGGTA
	ACTTTAGTGATAAGGAGGTTGCTGAGTTAGAGGAGATATTCCGAGTCTACATCTTTGGATTCGCTCG
	AGAAGTACAAGACTTTGCCGGTGATTTCCAGATGAAATACCCCTTTGAGATCCAGGGCATAGCAGGC
	TGTGAGCTACATTCTGGAGGTGCCATAGTAAGCTTCCTCAGGGGAGCTCTAGGAGGATTGGATTTCC
	TGAGTGTCAAGAATGCTTCATGTGTGCCTTCCCCAGAAGGTGGCAGCAGGGCACAGAAATTCTGTGC
	ACTAATCATACAATATCAAGGTATCATGCAAACTGTGAGAATTCTCCTCTATGAAACCTGCCCCCGA
	TATCTCTTGGGCGTCCTCAATGCAGGAAAAGCAGATCTGCAAAGACAAGTGAAGCCTGAGGCCTGGC
	TGTCCAGTGGCCCCAGTCCTGGACCTGGCCGTCTGCAGCTTGTCTGCCATGTCTCAGGATTCTACCC
	AAACCCCGTGTGGGTGATGTGGATGCGGGGTGAGCAGGAGCAGCAGGGCACTCAGCTAGGGGACATC
	CTGCCCAATCCTAACTGCACATGGTATCTCCGAGCAACCCTGGATGTGGCAGATGGGGAGGCGGCTG
	GCCTGTCCTGTCGGGTGAAGCACAGCAGTTTAGAGGGCCAGGACATCATCCTCTACTGGAGAAACCC
	CACCTCCATTGGCTCAATTGTTTTGGCAATAATAGTGCCTTCCTTGCTCCTTTTGCTATGCCTTGCA
	TTATGGTATATGAGGCGCCGGTCATATCAGAATATCCCATGAGCCATCATCATGTCTCCTCTCCCAT
	TCGCAATAAGCTACCAAGAAGCCCAAGATATCAGCCCAAAAATCAATCTTATCATATTTCAAATGAT
	TTTCAAATTTGATGAAATCAGAGTTTTCATGTATTTTTAAAATTATTATTTAAAACATCAGCAAA
	AAAGTACTTAAAACTGTAAATTTATTATGACACTGTACTAACAGTGTGATTCACCCTCATTTTACAC
	ACATTAAAATGTTAGAAAAA
	ORF Start: ATG at 46		ORF Stop: TGA at 1045
	SEQ ID NO: 148	333 aa	MW at 36939.0 kD
NOV39a,	MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDSDSGTAIF
CG150637-01
Protein Sequence	LKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDGQMKYPFEIQGIAGCELHSGGAIVSFLRG
	ALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQGIMETVRILLYETCPRYLLGVLNAGKADLQR
	QVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVMVMWMRGEQEQQGTQLDGILPNANWTWLRATLD
	VADGEAAGLSCRVKHSSLEGQDIILYWRNPTSIGSIVLAIIVPSLLLLLCLALWYMRRRSYQNIP
	SEQ ID NO: 149	880 bp
NOV39b,	CCCTTATGCTGCTGCTGCCATTCAACTGTTAGCTGTTCTCTTTCCTGGTGGTAACAGTGAACATGC
CG150637-02
DNA Sequence	CTTCCAGGGGCCGACCTCCTTTCATGTTATCCAGACCTCGTCCTTTACCAATAGTACCTGGGCACAA
	ACTCAAGGCTCAGGCTGGTTGGATGATTTGCAGATTCATGGCTGGGATAGCGACTCAGCCACTGCCA
	TATTCCTGAAGCCTTGGTCTAAAGCTAACTTTAGTGATAAGGAGGTTGCTGAGTTAGAGGAGATATT
	CCGAGTCTACATCTTTGGATTCGCTCGAGAAGTACAAGACTTTGCCGGTGATTTCCAGATGAAATAC
	CCCTTTGAGATCCAGGGCATAGCAGGCTGTGAGCTACATTCTGGAGGTGCCATAGTAACCTTCCTGA
	GGGGAGCTCTAGGAGGATTGGATTTCCTCAGTGTCAAGAATGCTTCATCTGTGCCTTCCCCAGAAGG
	TGGCAGCAGGGCACAGAAATTCTGTGCACTAATCATACAATATCAAGGTATCATGGAAACTGTGAGA
	ATTCTCCTCTATGAAACCTGCCCCCGATATCTCTTGGGCGTCCTCAATGCAGGAAAAGCAGATCTGC
	AAACACAAGTGAAGCCTGAGGCCTGCCTGTCCAGTGGCCCCAGTCCTGGACCTGGCCGTCTGCAGCT
	TGTGTGCCATGTCTCACGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATCCGGGGAAACCCCACC
	TCCATTGGCTCAATTGTTTTGGCAATAATAGTGCCTTCCTTCCTCCTTTTGCTATGCCTTGCATTAT
	CGTATATGAGGCGCCGGTCATATCAGAATATCCCATGAGCCATCATCATGTCTCCTCTCCCATTCGC
	AATAAGTAC
	ORF Start: ATG at 6		ORF Stop: TGA at 840
	SEQ ID NO: 150	278 aa	MW at 30739.2 kD
NOV39b,	MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDSDSGTAIF
CG150637-02
Protein Sequence	LKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDFDQMKYPFEIQGIAGCELHSGGAIVSFLRG
	ALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQFIMETVRILLYETCPRVYLLGVLNAGKADLQR
	QVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGNPTSIGSIVLAIIVPSLLLLLCLALWY
	MRRRSYQNIP

[0576] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 39B.

TABLE 39B
Comparison of NOV39a against NOV39b.
	Protein	NOV39a Residues/	Identities/Similarities
	Sequence	Match Residues	for the Matched Region
	NOV39b	15 . . . 247	228/233 (97%)
		15 . . . 247	228/233 (97%)

[0577] Further analysis of the NOV39a protein yielded the following properties shown in Table 39C.

TABLE 39C
Protein Sequence Properties NOV39a
PSort     0.4600 probability located in plasma membrane; 0.3000
analysis: probability located in lysosome (membrane); 0.2800
          probability located in endoplasmic reticulum (membrane);
          0.2404 probability located in microbody (peroxisome)
SignalP   Cleavage site between residues 19 and 20
analysis:

[0578] A search of the NOV39a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 39D.

TABLE 39D
Geneseq Results for NOV39a
		NOV39a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABG13799	Novel human	35 . . . 196	93/163 (57%)	5e−49
	diagnostic protein	518 . . . 680	118/163 (72%)
	#13790—Homo
	sapiens, 681 aa.
	[WO200175067-
	A2, 11 OCT.
	2001]
AAY94506	Chicken BFIV21	114 . . . 329	61/221 (27%)	4e−17
	class I MHC	114 . . . 326	107/221 (47%)
	protein—Gallus
	gallus, 355 aa.
	[US6075125-A,
	13 JUN. 2000]
AAY94508	Chicken	114 . . . 329	60/221 (27%)	1e−15
	BFIV19v1 class I	97 . . . 309	105/221 (47%)
	MHC protein—
	Gallus gallus,
	338 aa.
	[US6075125-A,
	13 JUN. 2000]
AAG00593	Human secreted	1 . . . 64	39/64 (60%)	1e−15
	protein, SEQ ID	1 . . . 64	46/64 (70%)
	NO: 4674—
	Homo sapiens,
	64 aa.
	[EP1033401-A2,
	6 SEP. 2000]
ABB08372	B-FIV*12 amino	114 . . . 315	58/211 (27%)	2e−15
	acid sequence—	93 . . . 295	99/211 (46%)
	Gallus
	domesticus,
	334 aa.
	[WO200194615-
	A2, 13 DEC.
	2001]

[0579] In a BLAST search of public sequence datbases, the NOV39a protein was found to have homology to the proteins shown in the BLASTP data in Table 39E.

TABLE 39E
Public BLASTP Results for NOV39a
		NOV39a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
P29016	T-cell surface	1 . . . 333	333/333 (100%)	0.0
	glycoprotein CD1b	1 . . . 333	333/333 (100%)
	precursor (CD1b
	antigen)—Homo
	sapiens (Human),
	333 aa.
Q28565	T-cell surface	1 . . . 332	248/332 (74%)	e−150
	glycoprotein	1 . . . 332	280/332 (83%)
	CD1b-1 precursor
	(CD1b-1 antigen)
	(SCD1A25)—Ovis
	aries (Sheep),
	333 aa.
Q29422	T-cell surface	1 . . . 332	244/332 (73%)	e−147
	glycoprotein CD1b-	1 . . . 332	282/332 (84%)
	2 precursor (CD1b-2
	antigen)
	(SCD1B-42)
	(Antigen IAH-
	CC14)—Ovis
	aries (Sheep),
	333 aa.
Q9GKE4	CD1B—	1 . . . 332	237/332 (71%)	e−140
	Oryctolagus	1 . . . 331	271/332 (81%)
	cuniculus (Rabbit),
	332 aa.
Q9QZZ1	T-cell surface	1 . . . 332	228/332 (68%)	e−134
	glycoprotein	1 . . . 331	267/332 (79%)
	CD1b2 precursor
	(CD1-b2 antigen)—
	Cavia porcellus
	(Guinea pig),
	332 aa.

[0580] PFam analysis predicts that the NOV39a protein contains the domains shown in the Table 39F.

TABLE 39F
Domain Analysis of NOV39a
	Pfam	NOV39a	Identities/Similarities	Expect
	Domain	Match Region	for the Matched Region	Value
	ig	217 . . . 281	15/67 (22%)	0.00019
			45/67 (67%)

Example 40

[0581] The NOV40 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 40A.

TABLE 40A
NOV40 Sequence Analysis
	SEQ ID NO: 151	505 bp
NOV40a,	AATATGTCGCTCTTGGGACCCAAGGTGCTGCTGTTTCTTGCTGCATTCATCATCACCTCTGACTGGA
CG150694-01
DNA Sequence	TACCCCTGGGGGTCAATAGTCAACGAGGAGACGATGTGACTCAAGCGACTCCAGAAACATTCACAGA
	AGATCCTAATCTGCTGAATGATCCCGCTACAGATGAAACAGAGTGCTCGGATGAGAAATTTACCTGC
	ACAAGGCTCTACTCTGTGCATCGGCCGGTTAAACAATGCATTCATCAGTTATGCTTCACCAGTTTAC
	GACGTATGTACATCGTCAACAAGGAGATCTCCTCTCCTCTTGTCTGTAAGGAACACGAAGCTATGAA
	AGATGAGCTTTGCCGTCAGATGGCTGGTCTGCCCCCTAGGAGACTCCGTCGCTCCAATTACTTCCGA
	CTTCCTCCCTGTGAAAATGTGGATTTGCAGAGACCCAATGGTCTGTGATCATTGAAAAACAGGAAAG
	AGAAAAAATGTATGGGTGAGAGGAAGGAGGATCTC
	ORF Start: ATG at 4		ORF Stop: TGA at 448
	SEQ ID NO: 152	48 aa	MW at 17113.5kD
NOV40a,	MSLLGPKVLLFLAAFIITSDWIPLGXTNSQRGDDVTQATPETFTEDPNLVNDPATDETECWDEKFTCT
CG150694-01
Protein Sequence	RLYSVHRPVKQCIHQLCFTSLRRMYIVNKEICSRLVCKEEEAHKDELCRQNAGLPPRRLRRSNYFRL
	PPCENVDLQRPNGL

[0582] Further analysis of the NOV40a protein yielded the following properties shown in Table 40B.

TABLE 40B
Protein Sequence Properties NOV40a
PSort     0.6850 probability located in plasma membrane; 0.6400
analysis: probability located in endoplasmic reticulum (membrane);
          0.3700 probability located in Golgi body; 0.1000
          probability located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 29 and 30
analysis:

[0583] A search of the NOV40a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 40C.

TABLE 40C
Geneseq Results for NOV40a
		NOV40a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB10284	Human fetal placenta protein	1 . . . 148	148/173 (85%)	5e−82
	fragment AC175_2i - Homo	1 . . . 173	148/173 (85%)
	sapiens, 173 aa.
	[WO200037630-A1,
	Jun. 29, 2000]
AAG03464	Human secreted protein, SEQ	1 . . . 76	76/91 (83%)	5e−37
	ID NO: 7545 - Homo	1 . . . 91	76/91 (83%)
	sapiens, 91 aa.
	[EP1033401-A2,
	Sep. 6, 2000]
ABP41833	Human ovarian antigen	58 . . . 116	33/59 (55%)	4e−17
	HOPJF55, SEQ ID NO:2965 -	145 . . . 203	48/59 (80%)
	Homo sapiens, 232 aa.
	[WO200200677-A1,
	Jan. 3, 2002]
AAU30569	Novel human secreted	58 . . . 115	32/58 (55%)	2e−16
	protein #1060 - Homo	114 . . . 171	47/58 (80%)
	sapiens, 203 aa.
	[WO200179449-A2,
	Oct. 25, 2001]
AAY35324	Chlamydia pneumoniae	72 . . . 107	11/41 (26%)	7.8
	transmembrane protein	3 . . . 43	19/41 (45%)
	sequence - Chlamydia
	pneumoniae, 172 aa.
	[WO9927105-A2,
	Jun. 3, 1999]

[0584] In a BLAST search of public sequence datbases, the NOV40a protein was found to have homology to the proteins shown in the BLASTP data in Table 40D.

TABLE 40D
Public BLASTP Results for NOV40a
		NOV40a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q13361	Microfibrillar-associated	1 . . . 148	148/173 (85%)	1e−81
	protein 5 precursor (MFAP-5)	1 . . . 173	148/173 (85%)
	(Microfibril- associated
	glycoprotein 2) (MAGP-2)
	(MP25) - Homo sapiens
	(Human), 173 aa.
Q28022	Microfibrillar-associated	1 . . . 148	118/170 (69%)	2e−64
	protein 5 precursor (MFAP-5)	1 . . . 170	130/170 (76%)
	(Microfibril- associated
	glycoprotein 2) (MAGP-2)
	(MP25) - Bos taurus (Bovine),
	170 aa.
Q9QZJ6	Microfibrillar-associated	1 . . . 148	118/168 (70%)	7e−64
	protein 5 precursor (MFAP-5)	1 . . . 164	130/168 (77%)
	(Microfibril- associated
	glycoprotein 2) (MAGP-2) -
	Mus musculus (Mouse), 164
	aa.
Q99PM0	Microfibril-associated	29 . . . 116	42/93 (45%)	1e−17
	glycoprotein 1 - Mus	64 . . . 156	58/93 (62%)
	musculus (Mouse), 185 aa.
P55002	Microfibrillar-associated	29 . . . 116	42/93 (45%)	1e−17
	protein 2 precursor (MFAP-2)	62 . . . 154	58/93 (62%)
	(Microfibril- associated
	glycoprotein) (MAGP)
	(MAGP-1) - Mus musculus
	(Mouse), 183 aa.

[0585] PFam analysis predicts that the NOV40a protein contains the domains shown in the Table 40E.

TABLE 40E
Domain Analysis of NOV40a
Pfam Domain	NOV40a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 41

[0586] The NOV41 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 41A.

TABLE 41A
1NOV41 Sequence Analysis
	SEQ ID NO: 153	2518 bp
NOV41a,	CAAAAGGGAACTTTATATGGAAAAGCTTCAAGAACATTTAATCAAAGCAAAAGCCTTTACCATAAAG
CG151069-01
DNA Sequence	AAGACGCTGGAGATCTATGTGCCCATCAAACAGTTCTTTTACAACCTCATCCACCCGGAGTATAGCG
	CCGTGACTGACGTGTATGTACTCATGTTCCTGGCTGACACTGTGGACTTCATCATCATTGTCTTCGG
	CTTTTGGGCCTTTGGGAAACACTCAGCAGCTGCAGACATCACCTCTTCACTGTCAGAGGACCAGGTC
	CCGGGGCCGTTTTTGGTGATGGTCCTCATTCAGTTTGGAACCATGGTGGTGGACCGAGCCCTCTACC
	TCAGGAAGACTGTACTGGGAAAGGTCATCTTCCAGGTCATTCTTGTGTTCGGAATTCACTTCTGGAT
	GTTCTTCATCTTACCTGGTGTGACTGAGAGGAAATTCAGCCAGAACCTGGTTGCCCAGCTTTGGTAC
	TTTGTGAAATGTGTTTACTTCGGGTTGTCTGCTTACCAGATCCGTTGTGGCTACCCAACGCGAGTCC
	TGGGGAACTTCCTCACCAAGAGCTACAATTACGTCAACCTCTTCTTATTCCAAGGGTTTCGCCTCGT
	GCCCTTTTTGACTGAGCTGAGGGCAGTGATGGACTGGGTGTGGACGGACACAACTTTGAGCCTGTCC
	AGCTGGATCTGTGTGGAGGACATCTATGCTCACATATTCATCCTGAAGTGTTGGCGGGAGTCGGAGA
	AGAGATACCCTCAGCCACGGGGCCAGAAGAAGAAGAAAGTGGTGAAGTATGGCATGGGAGGAATGAT
	CATCGTCCTGCTCATCTGCATTGTCTGGTTTCCTCTTCTCTTCATGTCTTTGATCAAATCTGTGGCT
	GGGGTCATCAACCAGCCCCTGGACGTCTCCGTCACAATTACCCTGGGAGGGTATCAGCCTATTTTCA
	CAATGAGTGCCCAACAAAGCCAGTTGAAAGTTATGGACCAGCAGAGCTTTAACAAATTTATACAAGC
	TTTTTCTAGGGACACCGGTGCTATGCAATTTCTGGAAAATTATGAAAAAGAAGACATAACAGTAGCA
	GAACTGGAAGGAAACTCAAATTCTTTGTGGACCATCAGCCCACCCAGTAAGCAGAAAATGATACACG
	AACTCCTGGACCCCAATAGTAGCTTCTCTGTTGTTTTTTCATGGAGTATTCAGAGAAACTTAAGTCT
	GGGTGCAAAATCGGAAATAGCAACAGATAAGCTTTCTTTTCCTCTTAAAAATATTACTCGAAAGAAT
	ATCGCTAAAATGATAGCAGGCAACAGCACAGAAAGTTCAAAAACACCAGTGACCATAGAAAAGATTT
	ATCCATATTATGTGAAAGCACCTAGTGATTCTAACTCAAAACCTATAAAGCAACTTTTATCTGAAAA
	TAATTTCATGGATATTACCATCATTTTGTCCAGAGACAATACAACTAAATATAACAGTGAGTGGTGG
	GTTCTCAACCTGACTGGAAACAGAATATACAATCCGAACTCTCAGGCCCTGGAACTGGTGGTCTTCA
	ATGACAAAGTCAGTCCCCCAAGTCTGGGGTTCCTGGCTGGCTATGGTATTATGGGATTATATGCTTC
	AGTTGTCCTTGTGATTGGGAAATTTGTCCGTGAATTCTTCAGTGGGATTTCTCACTCCATCATGTTT
	GAAGAGCTTCCAAATGTGGATCGAATTTTGAAGTTGTGCACAGATATTTTTTTAGTTCGAGAGACAG
	GAGAACTGGAGCTAGAAGAAGATCTCTATGCCAAATTAATATTCCTATATCGCTCACCAGAGACAAT
	GATCAAATGGACTAGAGAAAAAACAAATTGAAACCTTAGAACACAGACTGCAAATAATGTTAACATT
	TGAATTTTTTTTAAAAGCACAATATTCTCATAAGAGCTAAGCATTTCTAGTTCGACGGAAATGGTTT
	GTTTCTCTTCTGATAGGTAGACAAAAGGAGCTGATATCCTTCTGCAGTAAAAGCTACCTGGCAAGTT
	AAGGCACTGTTGAAAATGTTATTTGTAACTCCATTTCTCTGAAATCAGGGCTACTTGCTTTATGTTT
	TAGTCAACAGTGTCTCGCATTCTGATTGATCATGTGAAGGAATCATTTATGGGCCCCGTCCCTAAGA
	GAAACAGAAGAGGAGTCAGAAAGAAAGATGCCTGTGTTTTCCTCTGTGGGGCCCGTGCACTTCCTGG
	AGAGATGCTACAATGCAATATACAGCGCTCCATCCCCACTGGGGAAGCTGCTGTGATGAGACTAGAT
	GAGCCTTCAACACACTCAGAAAATGCAACAGCAATAGGGGGCAGACAGCTCCTACCTGTGTTTCTAG
	GAGCAAAAGAGAGGGAACTAATTGCCCGTGAAGACGCCAGTGGAAGGATCAGCCTCATTCTAAGCAA
	AAACATAGTATTAGTGATACTCTTACTGCCTTATCTTAACCAAGGACTAATAGGATACCTTTCCATT
	AAACACCAGTGACTTCTCAGGAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 17		ORF Stop: TGA at 1838
	SEQ ID NO: 154	607 aa	MW at 69659.7 kD
NOV41a,	MEKLQEHLIKAKAFTIKKTLEIYVPIKQFFYNLIHPEYSAVTDVYVLMFLADTVDFIIIVFGFWAFG
CG151069-01
Protein Sequence	KHSAAADITSSLSEDQVPGPFLVMVLIQFGTMVVDRALYLRKTVLGKVIFQVILVFGIHFWMFFILP
	GVTERKFSQNLVAQLWYFVKCVYFGLSAYQIRCGYPTRVLGNFLTKSYNYVNLFLFQGFRLVPFLTE
	LRAVMDWVWTDTTLSLSSWICVEDIYAHIFILKCWRESEKRYPQPRGQKKKKVVKYGMGGMIIVLLI
	CIVWFPLLFMSLIKSVAGVINQPLDVSVTITLGGYQPIFTMSAQQSQLKVMDQQSFNKFIQAFSRDT
	GAMQFLENYEKEDITVAELEGNSNSLWTISPPSKQKMIHELLDPNSSFSVVFSWSIQRNLSLGAKSE
	IATDKLSFPLKNITRKNIAKMIAGNSTESSKTPVTIEKIYPYYVKAPSDSNSKPIKQLLSENNFMDI
	TIILSRDNTTKYNSEWWVLNLTGNRIYNPNSQALELVVFNDKVSPPSLGFLAGYGIMGLYASVVLVI
	GKFVREFFSGISHSIMFEELPNVDRILKLCTDIFLVRETGELELEEDLYAKLIFLYRSPETMIKWTR
	EKTN

[0587] Further analysis of the NOV41a protein yielded the following properties shown in Table 41B.

TABLE 41B
Protein Sequence Properties NOV41a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);
                  0.3000 probability located in microbody (peroxisome)
SignalP analysis: No Known Signal Sequence Predicted

[0588] A search of the NOV41a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 41C.

TABLE 41C
Geneseq Results for NOV41a
		NOV41a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAY53635	A bone marrow secreted	141 . . . 605	290/471 (61%)	e−169
	protein designated BMS53 -	2 . . . 465	362/471 (76%)
	Homo sapiens, 466 aa.
	[WO9933979-A2,
	Jul. 8, 1999]
ABB89128	Human polypeptide SEQ ID	338 . . . 607	266/270 (98%)	e−150
	NO 1504 - Homo sapiens,	1 . . . 270	266/270 (98%)
	270 aa. [WO200190304-A2,
	Nov. 29, 2001]
ABB63880	Drosophila melanogaster	28 . . . 605	233/607 (38%)	e−125
	polypeptide SEQ ID NO	2140 . . . 2740	366/607 (59%)
	18432 - Drosophila
	melanogaster, 2771 aa.
	[WO200171042-A2,
	Sep. 27, 2001]
AAB56086	Human secreted protein	246 . . . 605	201/366 (54%)	e−109
	sequence encoded by gene 10	20 . . . 378	261/366 (70%)
	SEQ ID NO:180 - Homo
	sapiens, 379 aa.
	[WO200070042-A1,
	Nov. 23, 2000]
ABB89513	Human polypeptide SEQ ID	48 . . . 180	97/133 (72%)	2e−48
	NO 1889 - Homo sapiens,	1 . . . 132	105/133 (78%)
	135 aa. [WO200190304-A2,
	Nov. 29, 2001]

[0589] In a BLAST search of public sequence datbases, the NOV41a protein was found to have homology to the proteins shown in the BLASTP data in Table 41D.

TABLE 41D
Public BLASTP Results for NOV41a
		NOV41a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q9H515	CDNA: FLJ23403 fis, clone	1 . . . 607	533/607 (87%)	0.0
	HEP18857 - Homo sapiens	1 . . . 544	537/607 (87%)
	(Human), 544 aa.
Q92508	Hypothetical protein	10 . . . 605	381/602 (63%)	0.0
	KIAA0233 - Homo sapiens	1440 . . . 2034	467/602 (77%)
	(Human), 2035 aa.
Q9VLS3	CG8486 protein - Drosophila	28 . . . 605	233/607 (38%)	e−124
	melanogaster (Fruit fly), 2771	2140 . . . 2740	366/607 (59%)
	aa.
C88779	protein T20D3.9 [imported] -	25 . . . 603	215/637 (33%)	5e−96
	Caenorhabditis elegans, 1001	371 . . . 994	337/637 (52%)
	aa.
Q9H5R4	CDNA: FLJ23144 fis, clone	423 . . . 572	150/150 (100%)	2e−81
	LNG09262 - Homo sapiens	1 . . . 150	150/150 (100%)
	(Human), 150 aa.

[0590] PFam analysis predicts that the NOV41a protein contains the domains shown in the Table 41E.

TABLE 41E
Domain Analysis of NOV41a
Pfam Domain	NOV41a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 42

[0591] The NOV42 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 42A.

TABLE 42A
NOV42 Sequence Analysis
	SEQ ID NO: 155	2035 bp
NOV42a,	AGCGGGGCAGGTGGTGGCCGCCGGCCGGGCCCCGCCCTGGGGCCGCCTCCCCGCGGGTTCCGTTGGC
CG151189-01
DNA Sequence	TGTGGCGGCAGCTGACGCTTGTGGCGGCGGTGGCTTCGGGGTGGGCGTAAGATGGCGACAGCAGCGC
	AGGGACCCCTAAGCTTGCTGTGGGGCTGGCTGTGGAGCGAGCGCTTCTGGCTACCCGAGAACGTGAG
	CTGGGCTGATCTGGAGGGGCCGGCCGACGGCTACGGTTACCCCCGCGGCCGGCACATCCTCTCGGTG
	TTCCCGCTGGCGGCGGGCATCTTCTTCGTGAGGCTGCTCTTCGAGCGATTTATTGCCAAACCCTGTG
	CACTCCGTATTGGCATCGAGGACAGTGGTCCTTATCAGGCCCAACCCAATGCCATCCTTGAAAAGGT
	GTTCATATCTATTACCAAGTATCCTGATAAGAAAAGGCTGGAGGGCCTGTCAAAGCAGCTGGATTGG
	AATGTCCGAAAAATCCAATGCTGGTTTCGCCATCGGAGGAATCAGGACAAGCCCCCAACGCTTACTA
	AATTCTGTGAAAGCATGTGGAGATTCACATTTTATTTATGTATATTCTGCTATGGAATTAGATTTCT
	CTGGTCGTCACCTTGGTTCTGGGACATCCGACAGTGCTGGCATAACTATCCATTTCAGCCTCTTTCA
	AGTGGGCTTTATCACTATTATATCATGGAATTGGCCTTCTATTGGTCCCTTATGTTTTCTCAGTTTA
	CAGACATTAAAAGAAAGGACTTCCTGATCATGTTTGTGCATCACTTGGTCACCATTGGGCTTATCTC
	CTTCTCCTACATCAACAATATGGTTCGAGTGGGAACTCTGATCATGTGTCTACATGATGTCTCAGAC
	TTCTTGCTGGAGGCAGCCAAACTGGCCAATTATGCCAAGTATCAGCGGCTCTGTGACACCCTTTTTG
	TGATCTTCAGTGCTGTTTTTATGGTTACACGACTAGGAATCTATCCATTCTGGATTCTGAACACGAC
	CCTCTTTGAGAGTTGGGAGATAATCGGGCCTTATGCTTCATGGTGGCTCCTCAATGGCCTGCTGCTG
	ACCCTACAGCTTCTGCATGTCATCTGGTCCTACCTAATTGCACGGATTGCTTTGAAAGCCTTGATCA
	GGGGAAAGGTATCGAAGGATGATCGCAGTGATGTGGAGAGCAGCTCAGAGGAAGAAGATGTGACCAC
	CTGCACAAAAAGTCCCTGTGACAGTAGCTCCAGCAATGGTGCCAATCGGGTGAATGGTCACATGGGA
	GGCAGCTACTGGGCTGAAGAGTAAGGTGGTTGCTATAGGGACTTCAGCACACATGGACTTGTAGGGC
	CACTGGCAACATACTCCTCTTGGCCCTTCCCATATCTACTCTTCTGTGATTGGGAGACTGCAAGGCA
	CTGAGGAGTATCAAAGAAGCAAATATTTTCACTTTGAAAGAAAACTGCCATTTTGTATTTAATAGCC
	TCCAGGTTCTTTCAGTAATGTTATTTGCTCTGTGTGTTTTTGTGTGTTTGTTGATGTGCGTTTGTGC
	ATATGCGTGAGTTTCATTGCCGGGGTTGGGGCACAATTGTGGACTGGGGCCATGAGGCCTTCCCTGG
	TCCCCACTGAACCCACCTTAGTTCCACATTTGGCTGCATCTTGAATTATGCCGACTCCAGACTTCTC
	CTCCTTTTTTGCCCTTGGCTCTTGACACTCTAAACCCCTGGACCATCTGAATGGAGCAGCCAAGTTC
	AGTCCCACATTTCTGTACTGTTCCTCTTTCACAGCTGGAATATGTCACATGATGAAGTTGTATAGAA
	ACAGAACCATGGATGGATGGCCAGGATTGCCGTGGTCCCTAGCTAGATCCCCTTCCTATCAATCACC
	TGATAGCAACAGGGACAGCTGCCAATACCCTGCTCTTTACTCAATGGTACCCAGGGAGGGAGCATGG
	GAAGAGGGTGAGCTGAGGGCTGGAGGAGGGCAACAGCCACTGGGTGAGCTGTTCACGGTCTTATACT
	ATTGTTTGTGATTAAAAGTGCTTCA
	ORF Start: ATG at 119		ORF Stop: TAA at 1295
	SEQ ID NO: 156	392 aa	MW at 45804.6 kD
NOV42a,	MATAAQGPLSLLWGWLWSERFWLPENVSWADLEGPADGYGYPRGRHILSVFPLAAGIFFVRLLFERF
CG151189-01
Protein Sequence	IAKPCALRIGIEDSGPYQAQPNAILEKVFISITKYPDKKRLEGLSKQLDWNVRKIQCWFRHRRNQDK
	PPTLTKFCESMWRFTFYLCIFCYGIRFLWSSPWFWDIRQCWHNYPFQPLSSGLYHYYIMELAFYWSL
	MFSQFTDIKRKDFLIMFVHHLVTIGLISFSYINNMVRVGTLIMCLHDVSDFLLEAAKLANYAKYQRL
	CDTLFVIFSAVFMVTRLGIYPFWILNTTLFESWEIIGPYASWWLLNGLLLTLQLLHVIWSYLIARIA
	LKALIRGKVSKDDRSDVESSSEEEDVTTCTKSPCDSSSSNGANRVNGHHGGSYWAEE

[0592] Further analysis of the NOV42a protein yielded the following properties shown in Table 42B.

TABLE 42B
Protein Sequence Properties NOV42a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3104 probability located in mitochondrial intermembrane space;
                  0.3000 probability located in endoplasmic reticulum (membrane)
SignalP analysis: Cleavage site between residues 31 and 32

[0593] A search of the NOV42a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 42C.

TABLE 42C
Geneseq Results for NOV42a
		NOV42a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU00782	Human apoptosis protein,	100 . . . 392	291/293 (99%)	e−179
	APOP-2 - Homo sapiens, 311	19 . . . 311	293/293 (99%)
	aa. [WO200118042-A2,
	Mar. 15, 2001]
ABB90335	Human polypeptide SEQ ID	15 . . . 293	183/279 (65%)	e−116
	NO 2711 - Homo sapiens,	7 . . . 284	230/279 (81%)
	296 aa. [WO200190304-A2,
	Nov. 29, 2001]
AAB93884	Human protein sequence	15 . . . 361	160/347 (46%)	4e−90
	SEQ ID NO:13813 - Homo	8 . . . 353	218/347 (62%)
	sapiens, 394 aa.
	[EP1074617-A2,
	Feb. 7, 2001]
ABB90167	Human polypeptide SEQ ID	15 . . . 360	159/346 (45%)	1e−89
	NO 2543 - Homo sapiens,	8 . . . 352	217/346 (61%)
	394 aa. [WO200190304-A2,
	Nov. 29, 2001]
AAM78909	Human protein SEQ ID NO	15 . . . 360	159/346 (45%)	1e−89
	1571 - Homo sapiens, 394 aa.	8 . . . 352	217/346 (61%)
	[WO200157190-A2,
	Aug. 9, 2001]

[0594] In a BLAST search of public sequence datbases, the NOV42a protein was found to have homology to the proteins shown in the BLASTP data in Table 42D.

TABLE 42D
Public BLASTP Results for NOV42a
		NOV42a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
AAH32565	Similar to RIKEN cDNA	1 . . . 392	391/392 (99%)	0.0
	2310081H14 gene - Homo	1 . . . 392	391/392 (99%)
	sapiens (Human), 392 aa.
Q924Z3	TRH4 - Mus musculus	1 . . . 392	301/392 (76%)	0.0
	(Mouse), 414 aa.	1 . . . 392	339/392 (85%)
Q9D6K9	2310081H14Rik protein -	1 . . . 392	301/392 (76%)	0.0
	Mus musculus (Mouse), 414	1 . . . 392	339/392 (85%)
	aa.
Q8QGA3	TRH4 - Xenopus laevis	9 . . . 392	288/385 (74%)	e−179
	(African clawed frog), 382	1 . . . 382	326/385 (83%)
	aa.
Q90YY6	Trh1 - Brachydanio rerio	15 . . . 360	166/348 (47%)	4e−92
	(Zebrafish) (Zebra danio),	11 . . . 358	224/348 (63%)
	406 aa.

[0595] PFam analysis predicts that the NOV42a protein contains the domains shown in the Table 42E.

TABLE 42E
Domain Analysis of NOV42a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	Nov42a Match Region	Region	Value
homeobox	92 . . . 135	16/44 (36%)	0.029
		28/44 (64%)

Example 43

[0596] The NOV43 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 43A.

TABLE 43A
NOV43 Sequence Analysis
	SEQ ID NO: 157	1845 bp
NOV43a,	GTGTGAAAATCACAAATGTCAAATGATGGAAGATCCAGGAATCGGGACAGGCGCTACGATGAGGTCC
CG151801-01
DNA Sequence	CAAGCGACCTGCCCTATCAAGATACCACCATAAGAACCCACCCAACTCTTCATGACAGTGAGCGGGC
	AGTGAGCGCTGATCCCTTGCCACCACCCCCTCTCCCATTACAGCCACCATTCGGCCCAGACTTCTAC
	TCAAGTGACACAGAAGAACCAGCTATAGCGCCAGATCTCAAACCAGTAAGGCGCTTTGTCCCTGACT
	CCTGGAAGAACTTTTTCAGAGGGAAGAAAAAGGACCCCGAATGGGATAAGCCGGTGTCTGATATCAG
	GTACATCTCCGATGGAGTGGAGTGTTCACCACCAGCCTCTCCAGCAAGACCAAACCACCGTTCGCCC
	CTCAACTCCTGCAAAGATCCCTACGGCGGGTCAGAAGGAACCTTTAGTTCCCGGAAAGAGGCTGACG
	CAGTGTTTCCCCGGGATCCCTATGGATCTCTAGACCGACACACACAAACAGTTCGAACATACAGTGA
	GAAGGTGGAGGAGTATAACCTGAGATACTCCTACATGAAGTCGTGGGCAGGCCTGCTGAGAATACTG
	GGTGTGGTGGAGCTGCTTTTGGGGGCCGGTGTCTTTGCTTGTGTCACAGCTTACATTCACAAGGACA
	GTGAGTGGTACAACTTGTTTGGATATTCACAACCGTATGGCATGGGAGGCGTTGGTGGATTGGGCAG
	TATGTATGGGGGCTATTACTACACTGGCCCTAAGACCCCTTTTGTACTCGTGGTTGCTGGATTAGCT
	TGGATCACCACCATTATTATTCTGGTTCTTGGCATGTCCATGTATTACCGGACCATTCTTCTGGACT
	CTAATTGGTGGCCCCTAACTGAATTTGGAATTAACGTTGCCTTGTTTATTTTGTATATGGCCGCAGC
	CATAGTCTATGTGAATGATACCAACCGAGGTGGCCTCTGCTACTATCCGTTATTTAATACACCAGTG
	AATGCAGTGTTCTGCCGGGTAGAAGGAGGACAGATAGCTGCAATGATCTTCCTGTTTGTCACCATGA
	TAGTTTATCTCATTAGTGCTTTGGTTTGCCTAAAGTTATGGAGGCATGAGGCAGCTCGGAGACATAG
	AGAATATATGGAACAACAGGAGGTAAGTGATATAAATGAGCCATCATTGTCATCGAAAAGGAAAATG
	TGTGAAATGGCCACCAGTGGTGACAGACAAAGAGACTCAGAAGTTAATTTCAAGGAACTGAGAACAG
	CAAAAATGAAACCTGAACTACTGAGTGGACACATCCCCCCAGGCCACATTCCTAAACCTATCGTGAT
	GCCCGACTATGTGGCGAAATACCCTGTGATTCAGACAGATGATGAGCGAGAACGCTATAAAGCTGTG
	TTCCAAGACCAGTTTTCAGAGTACAAAGAGCTGTCTGCAGAAGTTCAGGCTGTCCTGAGGAAGTTTG
	ATGAGCTGGATGCAGTGATGAGCAGATTGCCACATCATTCGGAAAGCCGACAGGAACATGAGAGAAT
	TTCAAGAATCCATGAAGAGTTTAAGAAAAAAAAGAATGATCCTACATTTCTGGAAAAAAAAGAACGC
	TGTGATTACCTAAAGAATAAACTTTCTCACATAAAGCAAAGAATTCAAGAATATGATAAAGTAATGA
	ATTGGGATGTACAAGGTTATTCTTAACGCTTATTTGAAACCACTTTATTTTTTTATTTTATTTTATT
	TTTTTGAGATGAAGTCTCGCTCTGTTACCCAGGCTGGAATGCAGTGGCACAATCTCGGCTCACTGCA
	ACCTCCACCTCCCGGGTTCAAGCAATTCTCCTGTTC
	ORF Start: ATG at 16		ORF Stop: TAA at 1699
	SEQ ID NO: 158	61 aa	MW at 64468.7 kD
NOV43a,	MSNDGRSRNRDRRYDEVPSDLPYQDTTIRTHPTLHDSERAVSADPLPPPPLPLQPPFGPDFYSSDTE
CG151801-01
Protein Sequence	EPAIAPDLKPVRRFVPDSWKNFFRGKKKDPEWDKPVSDIRYISDGVECSPPASPARPNHRSPLNSCK
	DPYGGSEGTFSSRKEADAVFPRDPYGSLDRHTQTVRTYSEKVEEYNLRYSYMKSWAGLLRILGVVEL
	LLGAGVFACVTAYIHKDSEWYNLFGYSQPYGMGGVGGLGSMYGGYYYTGPKTPFVLVVAGLAWITTI
	IILVLGMSMYYRTILLDSNWWPLTEFGINVALFILYMAAAIVYVNDTNRGGLCYYPLFNTPVNAVFC
	RVEGGQIAAMIFLFVTMIVYLISALVCLKLWRHEAARRHREYMEQQEVSDINEPSLSSKRKMCEMAT
	SGDRQRDSEVNFKELRTAKMKRELLSGHIPPGHIPKPIVMPDYVAKYPVIQTDDERERYKAVFQDQF
	SEYKELSAEVQAVLRKFDELDAVMSRLPHHSESRQEHERISRIHEEFKKKKNDPTFLEKKERCDYLK
	NKLSHIKQRIQEYDKVMNWDVQGYS

[0597] Further analysis of the NOV43a protein yielded the following properties shown in Table 43B.

TABLE 43B
Protein Sequence Properties NOV43a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);
                  0.3000 probability located in microbody (peroxisome)
SignalP analysis: No Known Signal Sequence Predicted

[0598] A search of the NOV43a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 43C.

TABLE 43C
Geneseq Results for NOV43a
		NOV43a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABG14568	Novel human diagnostic	1 . . . 332	325/333 (97%)	0.0
	protein #14559 - Homo	1 . . . 333	326/333 (97%)
	sapiens, 363 aa.
	[WO200175067-A2,
	Oct. 11, 2001]
AAB82940	Human androgen receptor	392 . . . 550	63/161 (39%)	2e−26
	trapped protein 5 (ARTS) -	94 . . . 253	98/161 (60%)
	Homo sapiens, 264 aa.
	[WO200172332-A1,
	Oct. 4, 2001]
AAB56085	Human secreted protein	392 . . . 550	63/161 (39%)	2e−26
	sequence encoded by gene 9	94 . . . 253	98/161 (60%)
	SEQ ID NO:179 - Homo
	sapiens, 264 aa.
	[WO200070042-A1,
	Nov. 23, 2000]
AAW76212	Human ELL2 protein - Homo	371 . . . 551	60/184 (32%)	6e−19
	sapiens, 640 aa.	466 . . . 633	100/184 (53%)
	[WO9837194-A1,
	Aug. 27, 1998]
AAB57048	Human prostate cancer	371 . . . 551	60/184 (32%)	1e−18
	antigen protein sequence	503 . . . 670	99/184 (53%)
	SEQ ID NO: 1626 - Homo
	sapiens, 677 aa.
	[WO200055174-A1,
	Sep. 21, 2000]

[0599] In a BLAST search of public sequence datbases, the NOV43a protein was found to have homology to the proteins shown in the BLASTP data in Table 43D.

TABLE 43D
Public BLASTP Results for NOV43a
		NOV43a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
AAH33689	Similar to hypothetical	1 . . . 561	557/561 (99%)	0.0
	protein FLJ30532 - Homo	1 . . . 558	557/561 (99%)
	sapiens (Human), 558 aa.
Q96NM9	CDNA FLJ30532 fis, clone	1 . . . 433	429/433 (99%)	0.0
	BRAWH2001129, weakly	1 . . . 430	429/433 (99%)
	similar to occludin - Homo
	sapiens (Human), 457 aa.
Q99LE8	Hypothetical 50.4 kDa	121 . . . 560	386/441 (87%)	0.0
	protein - Mus musculus	1 . . . 435	409/441 (92%)
	(Mouse), 436 aa (fragment).
Q9H607	CDNA: FLJ22709 fis, clone	392 . . . 550	63/161 (39%)	5e−26
	HSI13338 - Homo sapiens	94 . . . 253	98/161 (60%)
	(Human), 264 aa.
Q8VCR9	Similar to RIKEN cDNA	437 . . . 550	49/114 (42%)	2e−20
	9430098E02 gene - Mus	94 . . . 206	73/114 (63%)
	musculus (Mouse), 219 aa.

[0600] PFam analysis predicts that the NOV43a protein contains the domains shown in the Table 43E.

TABLE 43E
Domain Analysis of NOV43a
		Identities/
		Similarities
Pfam Domain	NOV43a Match Region	for the Matched Region	Expect Value
Occludin	444 . . . 553	33/110 (30%)	6.2e−09
		56/110 (51%)

Example 44

[0601] The NOV44 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 44A.

TABLE 44A
NOV44 Sequence Analysis
	SEQ ID NO: 159	1112 bp
NOV44a,	TGAGGCGAGTGAAGTGGACTCTGAGGGCTACCGCTACCGCCACTGCTGCGGCAGGGGCGTGGAGGGC
CG165961-01
DNA Sequence	AGAGGGCCGCGGAGGCCGCAGTTGCAAACATGGCTCAGAGCAGAGACGGCGGAAACCCGTTCGCCGA
	GCCCAGCGAGCTTGACAACCCCTTTCAGGACCCAGCTGTGATCCAGCACCGACCCAGCCGGCAGTAT
	GCCACGCTTGACGTCTACAACCCTTTTGAGACCCGGGAGGCCTCAGCTGCAGCAGCCACAGCTGAGC
	TGCTGAAGAAACAGGAGGAGCTCAACCGGAAGGCAGAGGAGTTGGACCGAAGGGAGCGAGAGCTGCA
	GCATGCTGCCCTGGGAGGCACAGCTACTCGACAGAACAATTGGCCCCCTCTACCTTCTTTTTGTCCA
	GTTCAGCCCTGCTTTTTCCAGGACATCTCCATGGAGATCCCCCAAGAATTTCAGAAGACTGTATCCA
	CCATGTACTACCTCTGGATGTGCAGCACGCTGGCTCTTCTCCTGAACTTCCTCGCCTGCCTGGCCAG
	CTTCTGTGTGGAAACCAACAATGGCGCAGGCTTTGGGCTTTCTATCCTCTGGGTCCTCCTTTTCACT
	CCCTGCTCCTTTGTCTGCTGGTACCGCCCCATGTATAAGGCTTTCCGGAGTGACAGTTCATTCAATT
	TCTTCGTTTTCTTCTTCATTTTCTTCGTCCAGGATGTGCTCTTTGTCCTCCAGGCCATTGGTATCCC
	AGGTTGGGGATTCAGTGGCTGGATCTCTGCTCTGGTGGTGCCGAAGGGCAACACAGCAGTATCCGTG
	CTCATGCTGCTGGTCGCCCTGCTCTTCACTGGCATTGCTGTGCTAGGAATTGTCATGCTGAAACGGA
	TCCACTCCTTATACCGCCGCACAGGTGCCAGCTTTCAGAAGGCCCAGCAAGAATTTGCTGCTGGTGT
	CTTCTCCAACCCTGCGGTGCGAACCGCAGCTGCCAATGCAGCCGCTGGGGCTGCTGAAAATGCCTTC
	CGGGCCCCGTGACCCCTGACTGGGATGCCCTGGCCCTGCTACTTGAGGGAGCTGACTTAGCTCCCGT
CCCTAAGGTCTCTGGGACTTGGAGAGACATCACTAACTGA
	ORF Start: ATG at 97		ORF Stop: TGA at 1015
	SEQ ID NO: 160	306 aa	MW at 33990.7 kD
NOV44a,	MAQSRDGGNPFAEPSELDNPFQDPAVIQHRPSRQYATLDVYNPFETREASAAAATAELLKKQEELNR
CG165961-01
Protein Sequence	KAEELDRRERELQHAALGGTATRQNNWPPLPSFCPVQPCFFQDISMEIPQEFQKTVSTMYYLWMCST
	LALLLNFLACLASFCVETNNGAGFGLSILWVLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFV
	QDVLFVLQAIGIPGWGFSGWISALVVPKGNTAVSVLMLLVALLFTGIAVLGIVMLKRIHSLYRRTGA
	SFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP
	SEQ ID NO: 161	1310 bp
NOV44b,	TGAGGCGAGTGAAGTGGACTCTGAGGGCTACCGCTACCGCCACTGCTGCGGCAGGGGCGTGGAGGGC
CG165961-02
DNA Sequence	AGAGGGCCGCGGAGGCCGCAGTTGCAAACATGGCTCAGAGCAGAGACGGCGGAAACCCGTTCGCCGA
	GCCCAGCGAGCTTGACAACCCCTTTCAGGACCCAGCTGTGATCCAGCACCGACCCAGCCGGCAGTAT
	GCCACGCTTGACGTCTACAACCCTTTTGAGACCCGGGAGGCCTCAGCTGCAGCAGCCACAGCTGAGC
	TGCTGAAGAAACAGGAGGAGCTCAACCGGAAGGCAGAGGAGTTGGACCGAAGGGAGCGAGAGCTGCA
	GCATGCTGCCCTGGGAGGCACAGCTACTCGACAGAACAATTGGCCCCCTCTACCTTCTTTTTGTCCA
	GTTCAGCCCTGCTTTTTCCAGGACATCTCCATGGAGATCCCCCAAGAATTTCAGAAGACTGTATCCA
	CCATGTACTACCTCTGGATGTGCAGCACGCTGGCTCTTCTCCTGAACTTCCTCGCCTGCCTGGCCAG
	CTTCTGTGTGGAAACCAACAATGGCGCAGGCTTTGGGCTTTCTATCCTCTGGGTCCTCCTTTTCACT
	CCCTGCTCCTTTGTCTGCTGGTACCGCCCCATGTATAAGGCTTTCCGGAGTGACAGTTCATTCAATT
	TCTTCGTTTTCTTCTTCATTTTCTTCGTCCAGGATGTGCTCTTTGTCCTCCAGGCCATTGGTATCCC
	AGGTTGGGGATTCAGTGGCTGGATCTCTGCTCTGGTGGTGCCGAAGGGCAACACAGCAGTATCCGTG
	CTCATGCTGCTGGTCGCCCTGCTCTTCACTGGCATTGCTGTGCTAGGAATTGTCATGCTGAAACGGA
	TCCACTCCTTATACCGCCGCACAGGTGCCAGCTTTCAGAAGGCCCAGCAAGAATTTGCTGCTGGTGT
	CTTCTCCAACCCTGCGGTGCGAACCGCAGCTGCCAATGCAGCCGCTGGGGCTGCTGAAAATGCCTTC
	CGGGCCCCGTGACCCCTGACTGGGATGCCCTGGCCCTGCTACTTGAGGGAGCTGACTTAGCTCCCGG
	CCCTAAGGTCTCTGGGACTTGGAGAGACATCACTAACTGATGGCTCCTCCGTAGTGCTCCCAATCCT
	ATGGCCATGACTGCTGAACCTGACAGGCGTGTGGGGAGTTCACTGTGACCTAGTCCCCCCATCAGGC
	CACACTGCTGCCACCTCTCACACGCCCCAACCCAGCTTCCCTCTGCTGTGCCACGGCTGTTGCTTCG
	GTTATTTAAATAAAAAGAAAGTGGAACTGGAACTGAC
	ORF Start: ATG at 97		ORF Stop: TGA at 1015
	SEQ ID NO: 162	306 aa	MW at 33990.7 kD
NOV44b,	MAQSRDGGNPFAEPSELDNPFQDPAVIQHRPSRQYATLDVYNPFETREASAAAATAELLKKQEELNR
CG165961-02
Protein Sequence	KAEELDRRERELQHAALGGTATRQNNWPPLPSFCPVQPCFFQDISMEIPQEFQKTVSTMYYLWMCST
	LALLLNFLACLASFCVETNNGAGFGLSILWVLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFV
	QDVLFVLQAIGIPGWGFSGWISALVVPKGNTAVSVLMLLVALLFTGIAVLGIVMLKRIHSLYRRTGA
	SFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP
	SEQ ID NO: 163	135 bp
NOV44c,	TGAGGCGAGTGAAGTGGACTCTGAGGGCTACCGCTACCGCCACTGCTGCGGCAGGGGCGTGGAGGGC
CG 165961-03
DNA Sequence	AGAGGGCCGCGGAGGCCGCAGTTGCGAACATGGCTCAGAGCAGAGACGGCGGAAACCCGTTCGCCGA
	GCCCAGCGAGCTTGACAACCCCTTTCAGGACCCACCTGTGATCCAGCACCGACCCAGCCGGCAGTAT
	GCCACGCTTGACGTCTACAACCCTTTTGAGACCCGGGAGCCACCACCAGCCTATGAGCCTCCAGCCC
	CTGCCCCATTGCCTCCACCCTCAGCTCCCTCCTTGCAGCCCTCGAGAAAGCTCAGCCCCACAGAACC
	TAAGAACTATGGCTCATACAGCACTCAGGCCTCAGCTGCAGCAGCCACAGCTGAGCTGCTGAAGAAA
	CAGGAGGAGCTCAACCGGAAGGCAGAGGAGTTGGACCGAAGGGAGCGAGAGCTGCAGCATGCTGCCC
	TGGGGGGCACAGCTACTCGACAGAACAATTGGCCCCCTCTACCTTCTTTTTGTCCAGTTCAGCCCTG
	CTTTTTCCAGGACATCTCCATGGAGATCCCCCAAGAATTTCAGAAGACTGTATCCACCATGTACTAC
	CTCTGGATGTGCAGCACGCTGGCTCTTCTCCTGAACTTCCTCGCCTGCCTGGCCAGCTTCTGTGTGG
	AAACCAACAATGGCGCAGGCTTTGGGCTTTCTATCCTCTGGGTCCTCCTTTTCACTCCCTGCTCCTT
	TGTCTGCTGGTACCGCCCCATGTATAAGGCTTTCCGGAGTGACAGTTCATTCAATTTCTTCGTTTTC
	TTCTTCATTTTCTTCGTCCAGGATGTGCTCTTTGTCCTCCAGGCCATTGGTATCCCAGGTTGGGGAT
	TCAGTGGCTGGATCTCTGCTCTGGTGGTGCCGAAGGGCAACACAGCAGTATCCGTGCTCATGCTGCT
	GGTCGCCCTGCTCTTCACTGGCATTGCTGTGCTAGGAATTGTCATGCTGAAACGGATCCACTCCTTA
	TACCGCCGCACAGGTGCCAGCTTTCAGAAGGCCCAGCAAGAATTTGCTGCTGGTGTCTTCTCCAACC
	CTGCGGTGCGAACCGCAGCTGCCAATGCAGCCGCTGGGGCTGCTGAAAATGCCTTCCGGGCCCCGTTG
	ACCCCTGACTGGGATGCCCTGGCCCTGCTACTTGAGGGAGCTGACTTAGCTCCCGTCCCTAAGGTCT
	CTGGGACTTGGAGAGACATCACTAACTGA
	ORF Start: ATG at 97		ORF Stop: TGA at 1138
	SEQ ID NO: 164	347 aa	MW at 38312.5 kD
NOV44c,	MAQSRDGGNPFAEPSELDNPFQDPPVIQHRPSRQYATLDVYNFPETREPPPAYEPPAPAPLPPPSAP
CG165961-03
Protein Sequence	SLQPSRKLSPTEPKNYGSYSTQASAAAATAELLKKQEELNRKAEELDRRERELQHAALGGTATRQNN
	WPPLPSFCPVQPCFFQDISMEIPQEFQKTVSTMYYLWMCSTLALLLNFLACLASFCVETNNGAGFGL
	SILWVLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFVQDVLFVLQAIGIPGWGFSGWISALVV
	PKGNTAVSVLMLLVALLFTGIAVLGIVMLKRIHSLYRRTGASFQKAQQEFAAGVFSNPAVRTAAANA
	AAGAAENAFRAP
	SEQ ID NO: 165	1543 bp
NOV44d,	CGGCCGCGTCGACGGACTCTGAGGGCTACCGCTACCGCCACTGCTGCGGCAGGGGCGTGGAGGGCAG
CG165961-04
DNA Sequence	AGGGCCGCGGAGGCCGCAGTTGCAAACATGGCTCAGAGCAGAGACGGCGGAAACCCGTTCGCCGAGC
	CCAGCGAGCTTGACAACCCCTTTCAGCCACCACCAGCCTATGAGCCTCCAGCCCCTGCCCCATTGCC
	TCCACCCTCAGCTCCCTCCTTGCAGCCCTCGAGAAAGCTCAGCCCCACAGAACCTAAGAACTATGGC
	TCATACAGCACTCAGGCCTCAGCTGCAGCAGCCACAGCTCAGCTGCTGAAGAAACAGGAGGAGCTCA
	ACCGGAAGGCAGAGGAGTTGGACCGAAGGGAGCGAGAGCTGCAGCATGCTGCCCTGGGGGGCACAGC
	TACTCGACAGAACAATTGGCCCCCTCTACCTTCTTTTTGTCCAGTTCAGCCCTGCTTTTTCCAGGAC
	ATCTCCATGGAGATCCCCCAAGAATTTCAGAAGACTGTATCCACCATGTACTACCTCTGGATGTGCA
	GCACGCTGGCTCTTCTCCTGAACTTCCTCGCCTGCCTGGCCAGCTTCTGTGTGGAAACCAACAATGG
	CGCAGGCTTTGGGCTTTCTATCCTCTGGGTCCTCCTTTTCACTCCCTGCTCCTTTGTCTGCTGGTAC
	CGCCCCATGTATAAGGCTTTCCGGAGTGACAGTTCATTCAATTTCTTCGTTTTCTTCTTCATTTTCT
	TCGTCCAGGATGTGCTCTTTGTCCTCCAGGCCATTGGTATCCCAGGTTGGGGATTCAGTGGCTGGAT
	CTCTGCTCTGGTGGTGCCGAAGGGCAACACAGCAGTATCCGTGCTCATGCTGCTGGTCGCCCTGCTC
	TTCACTGGCATTGCTGTGCTAGGAATTGTCATGCTGAAACGGATCCACTCCTTATACCGCCGCACAG
	GTGCCAGCTTTCAGAAGGCCCAGCAAGAATTTGCTGCTGGTGTCTTCTCCAACCCTGCGGTGCGAAC
	CGCAGCTGCCAATGCAGCCGCTGGGGCTGCTGAAAATGCCTTCCGGGCCCCGTGACCCCTGACTGGG
	ATGCCCTGGCCCTGCTACTTGAGGGAGCTGACTTAGCTCCCGTCCCTAAGGTCTCTGGGACTTGGAG
	AGACATCACTAACTGATGGCTCCTCCGTAGTGCTCCCAATCCTATGGCCATGACTGCTGAACCTGAC
	AGGCGTGTGGGGAGTTCACTGTGACCTAGTCCCCCCATCAGGCCACACTGCTGCCACCTCTCACACG
	CCCCAACCCAGCTTCCCTCTGCTGTGCCACGGCTGTTGCTTCGGTTATTTAAATAAAAAGAAAGTGG
	AACTGGAACTGAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
	AAAAAAAAAACTATAATTTTTTTTTTTTTTTTTTTTTTTTACCCCCCCCGCTTTTTTTTTTTTTTTT
	TTTTTTTCCCCCCCTTTTTTTTTTTTTTTTTTTTTTTTTTTTTGTGTTTTTTTTTTTTTTTTTTCCC
	CC
	ORF Start: ATG at 95		ORF Stop: TGA at 1058
	SEQ ID NO: 166	321 aa	MW at 35201.1 kD
NOV44d,	MAQSRDGGNPFAEPSELDNPFQPPPAYEPPAPAPLPPPSAPSLQPSRKLSPTEPKNYGSYSTQASAA
CG165961-04
Protein Sequence	AATAELLKKQEELNRKAEELDRRERELQHAALGGTATRQNNWPPLPSFCPVQPCFFQDISMEIPQEF
	QKTVSTMYYLWMCSTLALLLNFLACLASFCVETNNGAGFGLSILWVLLFTPCSFVCWYRPMYKAFRS
	DSSFNFFVFFFIFFVQDVLFVLQAIGIPGWGFSGWISALVVPKGNTAVSVLMLLVALLFTGIAVLGI
	VMLKRIHSLYRRTGASFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP

[0602] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 44B.

TABLE 44B
Comparison of NOV44a against NOV44b through NOV44d.
	NOV44a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV44b	1 . . . 285	223/285 (78%)
	1 . . . 285	223/285 (78%)
NOV44c	1 . . . 285	228/326 (69%)
	1 . . . 326	229/326 (69%)
NOV44d	1 . . . 285	201/300 (67%)
	1 . . . 300	203/300 (67%)

[0603] Further analysis of the NOV44a protein yielded the following properties shown in Table 44C.

TABLE 44C
Protein Sequence Properties NOV44a
PSort analysis:   0.6000 probability located in plasma membrane; 0.4000 probability located in
                  Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);
                  0.0300 probability located in mitochondrial inner membrane
SignalP analysis: No Known Signal Sequence Predicted

[0604] A search of the NOV44a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 44D.

TABLE 44D
Geneseq Results for NOV44a
		NOV44a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB62698	Human membrane recycling	1 . . . 306	306/347 (88%)	e−173
	protein (HMRP)-1 - Homo	1 . . . 347	306/347 (88%)
	sapiens, 347 aa.
	[U.S. Pat. No. 6,235,715-B1,
	May 22, 2001]
AAY30521	A human membrane	1 . . . 306	306/347 (88%)	e−173
	recycling protein designated	1 . . . 347	306/347 (88%)
	HMRP-1 - Homo sapiens,
	347 aa. [U.S. Pat. No. 5,962,263-A,
	Oct. 5, 1999]
AAB62700	Rat SCAMP 37 protein -	9 . . . 304	180/333 (54%)	4e−92
	Rattus sp, 338 aa.	7 . . . 334	217/333 (65%)
	[U.S. Pat. No. 6,235,715-B1,
	May 22, 2001]
ABG61921	Prostate cancer-associated	9 . . . 304	178/333 (53%)	3e−90
	protein #122 - Mammalia,	7 . . . 334	215/333 (64%)
	338 aa. [WO200230268-A2,
	Apr. 18, 2002]
AAB62699	Human membrane recycling	9 . . . 298	164/322 (50%)	1e−87
	protein (HMRP)-2 - Homo	7 . . . 325	220/322 (67%)
	sapiens, 329 aa.
	[U.S. Pat. No. 6,235,715-B1,
	May 22, 2001]

[0605] In a BLAST search of public sequence datbases, the NOV44a protein was found to have homology to the proteins shown in the BLASTP data in Table 44E.

TABLE 44E
Public BLASTP Results for NOV44a
		NOV44a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
O14828	Secretory carrier-associated	1 . . . 306	302/347 (87%)	e−170
	membrane protein 3 - Homo	1 . . . 347	302/347 (87%)
	sapiens (Human), 347 aa.
T08826	secretory carrier membrane	1 . . . 306	301/347 (86%)	e−169
	protein homolog propin1 -	1 . . . 347	301/347 (86%)
	human, 347 aa.
Q99M48	Similar to secretory carrier	1 . . . 306	277/350 (79%)	e−156
	membrane protein 3 - Mus	1 . . . 350	289/350 (82%)
	musculus (Mouse), 350 aa.
Q9ERM9	Secretory carrier membrane	1 . . . 306	276/349 (79%)	e−155
	protein 3 - Mus musculus	1 . . . 349	288/349 (82%)
	(Mouse), 349 aa.
O35609	Secretory carrier-associated	1 . . . 306	274/349 (78%)	e−154
	membrane protein 3 - Mus	1 . . . 349	286/349 (81%)
	musculus (Mouse), 349 aa.

[0606] PFam analysis predicts that the NOV44a protein contains the domains shown in the Table 44F.

TABLE 44F
Domain Analysis of NOV44a
Pfam Domain	NOV44a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 45

[0607] The NOV45 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 45A.

TABLE 45A
NOV45 Sequence Analysis
	SEQ ID NO: 167	1356 bp
NOV45a,	CTGCGCTGCCGAGGCGAGCTAAGCGCCCGCTCGCCATGGGGAGCCCCGCACATCGGCCCGCGCTGCT
CG171681-01
DNA Sequence	GCTGCTGCTGCCGCCTCTGCTGCTGCTGCTGCTGCTGCGCGTCCCGCCCAGCCGCAGCTTCCCAGAT
	ATGGAACCTCCTAGAATCAAGTGCCCAAGTGTGAAGGAACGCATTGCAGAACCCAACAAACTGACAG
	TCCGGGTGTCCTGGGAGACACCCGAAGGAAGAGACACAGCAGATGGAATTCTTACTGATGTCATTCT
	AAAAGGCCTCCCCCCAGGCTCCAACTTTCCAGAAGGAGACCACAAGATCCAGTACACAGTCTATGAC
	AGAGCTGAGAATAAGGGCACTTGCAAATTTCGAGTTAAAGTAAGAGTCAAACGCTGTGGCAAACTCA
	ATGCCCCAGAGAATGGTTACATGAAGTGCTCCAGCGACGGTGATAATTATGGAGCCACCTGTGAGTT
	CTCCTGCATCGGCGGCTATGAGCTCCAGGGTAGCCCTGCCCGAGTATGTCAATCCAACCTGGCTTGG
	TCTGGCACGGAGCCCACCTGTGCAGCCATGAACGTCAATGTGGGTGTCAGAACGGCAGCTGCACTTC
	TGGATCAGTTTTATGAGAAAAGGAGACTCCTCATTGTGTCCACACCCACAGCCCGAAACCTCCTTTA
	CCGGCTCCAGCTAGGAATGCTGCAGCAAGCACAGTGTGGCCTTGATCTTCGACACATCACCGTGGTG
	GAGCTGGTGGGTGTGTTCCCGACTCTCATTGGCAGGATAGGAGCAAAGATTATGCCTCCAGCCCTAG
	CGCTGCAGCTCAGGCTGTTGCTGCGAATCCCACTCTACTCCTTCAGTATGGTGCTAGTGGATAAGCA
	TGGCATGGACAAAGAGCGCTATGTCTCCCTGGTGATGCCTGTGGCCCTGTTCAACCTGATTGACACT
	TTTCCCTTGAGAAAAGAAGAGATGGTCCTACAAGCCGAAATGAGCCAGACCTGTAACACCTGACATG
	ATGGTTCCTCTCTTGGCAATTCCTCTTCATTGTCTACATAGTGACATGCACACGGGAAAGCCTTAAA
	AATATCCTTGATGTACAGATTTTATTTGTAATTTTAAAAGTCTATTTTATTATGAGCTTTCTTTGCA
	CTTAAAAATTAGCATGCTGCTTTTTGTACTTGGAAGTGTTTCAAAAAATTATATGACCATATTTACT
	CTTTCTAACCTTTCTTTACTCCATCATGGCTGGTTGATTTGTAGAGAAATTAGAACCCATAACCATA
	CACAGGCTATCAACATGTTATTCAATGTGACACCTAACTCTTTTCTATTTTGTTTTTTAAGTAAGAC
	TTTTATTAATAAAACG
	ORF Start: ATG at 36		ORF Stop: TGA at 999
	SEQ ID NO: 168	321 aa	MW at 35636.4 kD
NOV45a,	MGSPAHRPALLLLLPPLLLLLLLRVPPSRSFPDMEPPRIKCPSVKERIAEPNKLTVRVSWETPEGRD
CG171681-01
Protein Sequence	TADGILTDVILKGLPPGSNFPEGDHKIQYTVYDRAENKGTCKFRVKVRVKRCGKLNAPENGYMKCSS
	DGDNYGATCEFSCIGGYELQGSPARVCQSNLAWSGTEPTCAAMNVNVGVRTAAALLDQFYEKRRLLI
	VSTPTARNLLYRLQLGMLQQAQCGLDLRHITVVELVGVFPTLIGRIGAKIMPPALALQLRLLLRIPL
	YSFSMVLVDKHGMDKERYVSLVMPVALFNLIDTFPLRKEEMVLQAIMSQTCNT
	SEQ ID NO: 169	1798 bp
NOV45b,	CTTGGTCTCTTCGGTCTCCTGCCGCCCCCGGGAAGCGCGCTGCGCTGCCGAGGCGAGCTAAGCGCCC
CG171681-02
DNA Sequence	GCTCGCCATGGGGAGCCCCGCACATCGGCCCGCGCTGCTGCTGCTGCTGCCGCCTCTGCTGCTGCTG
	CTGCTGCTGCGCGTCCCGCCCAGCCGCAGCTTCCCAGATACCCCGTGGTGCTCCCCCATCAAGGTGA
	AGTATGGGGATGTGTACTGCAGGGCCCCTCAAGGAGGATACTACAAAACAGCCCTGGGAACCAGGTG
	CGACATTCGCTGCCAGAAGGGCTACGAGCTGCATGGCTCTTCCCTACTGATCTGCCAGTCAAACAAA
	CGATGGTCTGACAAGGTCATCTGCAAACAAAAGCGATGTCCTACCCTTGCCATGCCAGCAAATGGAG
	GGTTTAAGTGTGTAGATGGTGCCTACTTTAACTCCCGGTGTGAGTATTATTGTTCACCAGGATACAC
	GTTGAAAGGGGAGCGGACCGTCACATGTATGGACAACAAGGCCTGGAGCGGCCGGCCAGCCTCCTGT
	GTGGATATGGAACCTCCTAGAATCAAGTGCCCAAGTGTGAAGGAACGCATTGCAGAACCCAACAAAC
	TGACAGTCCGGGTGTCCTGGGAGACACCCGAAGGAAGAGACACAGCAGATGGAATTCTTACTGATGT
	CATTCTAAAAGGCCTCCCCCCAGGCTCCAACTTTCCAGAAGGAGACCACAAGATCCAGTACACAGTC
	TATGACAGAGCTGAGAATAAGGGCACTTGCAAATTTCGAGTTAAAGTAAGAGTCAAACGCTGTGGCA
	AACTCAATGCCCCAGAGAATGGTTACATGAAGTGCTCCAGCGACGGTGATAATTATGGAGCCACCTG
	TGAGTTCTCCTGCATCGGCGGCTATGAGCTCCAGGGTAGCCCTGCCCGAGTATGTCAATCCAACCTG
	GCTTGGTCTGGCACGGAGCCCACCTGTGCAGCCATGAACGTCAATGTGGGTGTCAGAACGGCAGCTG
	CACTTCTGGATCAGTTTTATGAGAAAAGGAGACTCCTCATTGTGTCCACACCCACAGCCCGAAACCT
	CCTTTACCGGCTCCAGCTAGGAATGCTGCAGCAAGCACAGTGTGGCCTTGATCTTCGACACATCACC
	GTGGTGGAGCTGGTGGGTGTGTTCCCGACTCTCATTGGCAGGATAGGAGCAAAGATTATGCCTCCAG
	CCCTAGCGCTGCAGCTCAGGCTGTTGCTGCGAATCCCACTCTACTCCTTCAGTATGGTGCTAGTGGA
	TAAGCATGGCATGGACAAAGAGCGCTATGTCTCCCTGGTGATGCCTGTGGCCCTGTTCAACCTGATT
	GACACTTTTCCCTTGAGAAAAGAAGAGATGGTCCTACAAGCCGAAATGAGCCAGACCTGTAACACCT
	GACATGATGGTTCCTCTCTTGGCAATTCCTCTTCATTGTCTACATAGTGACATGCACACGGGAAAGC
	CTTAAAAATATCCTTGATGTACAGATTTTATTTGTAATTTTAAAAGTCTATTTTATTATGAGCTTTC
	TTTGCACTTAAAAATTAGCATGCTGCTTTTTGTACTTGGAAGTGTTTCAAAAAATTATATGACCATA
	TTTACTCTTTCTAACTTTCTTTACTCCATCATGGCTGGTTGATTTTGTAGAGAAATTAGAACCCATA
	ACCATACACAGGCTATCAACATGTTATTCAATGTGACACCTAACTCTTTTCTATTTTGTTTTTTAAG
	TAAGACTTTTATTAATAAAACAAAATGTTTTGGAGCAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 75		ORF Stop: TGA at 1407
	SEQ ID NO: 170	444 aa	MW at 49381.1 kD
NOV45b,	MGSPAHRPALLLLLPPLLLLLLLRVPPSRSFPDTPWCSPIKVKYGDVYCRAPQGGYYKTALGTRCDI
CG171681-02
Protein Sequence	RCQKGYELHGSSLLICQSNKRWSDKVICKQKRCPTLAMPANGGFKCVDGAYFNSRCEYYCSPGYTLK
	GERTVTCMDNKAWSGRPASCVDMEPPRIKCPSVKERIAEPNKLTVRVSWETPEGRDTADGILTDVIL
	KGLPPGSNFPEGDHKIQYTVYDRAENKGTCKFRVKVRVKRCGKLNAPENGYMKCSSDGDNYGATCEF
	SCIGGYELQGSPARVCQSNLAWSGTEPTCAAMNVNVGVRTAAALLDQFYEKRRLLIVSTPTARNLLY
	RLQLGMLQQAQCGLDLRHITVVELVGVFPTLIGRIGAKIMPPALALQLRLLLRIPLYSFSMVLVDKH
	GMDKERYVSLVMPVALFNLIDTFPLRKEEMVLQAEMSQTCNT
	SEQ ID NO: 171	1795 bp
NOV45c,	CTTGGTCTCTTCGGTCTCCTGCCGCCCCCGGGAAGCGCGCTGCGCTGCCGAGGCCGAGCTAAGCGCCC
CG171681-03
DNA Sequence	GCTCGCCATGGGGAGCCCCGCACATCGGCCCGCGCTGCTGCTGCTGCTGCCGCCTCTGCTGCTGCTG
	CTGCTGCGCGTCCCGCCCAGCCGCAGCTTCCCAGATACCCCGTGGTGCTCCCCCATCAAGGTGAAGT
	ATGGGGATGTGTACTGCAGGGCCCCTCAAGGAGGATACTACAAAACAGCCCTGGGAACCAGGTGCGA
	CATTCGCTGCCAGAAGGGCTACGAGCTGCATGGCTCTTCCCTACTGATCTGCCAGTCAAACAAACGA
	TGGTCTGACAAGGTCATCTGCAAACAAAAGCGATGTCCTACCCTTGCCATGCCAGCAAATGGAGGGT
	TTAAGTGTGTAGATGGTGCCTACTTTAACTCCCGGTGTGAGTATTATTGTTCACCAGGATACACGTT
	GAAAGGGGAGCGGACCGTCACATGTATGGACAACAAGGCCTGGAGCGGCCGGCCAGCCTCCTGTGTG
	GATATGGAACCTCCTAGAATCAAGTGCCCAAGTGTGAAGGAACGCATTGCAGAACCCAACAAACTGA
	CAGTCCGGGTGTCCTGGGAGACACCCGAAGGAAGAGACACAGCAGATGGAATTCTTACTGATGTCAT
	TCTAAAAGGCCTCCCCCCAGGCTCCAACTTTCCAGAAGGAGACCACAAGATCCAGTACACAGTCTAT
	GACAGAGCTGAGAATAAGGGCACTTGCAAATTTCGAGTTAAAGTAAGAGTCAAACGCTGTGGCAAAC
	TCAATGCCCCAGAGAATGGTTACATGAAGTGCTCCAGCGACGGTGATAATTATGGAGCCACCTGTGA
	GTTCTCCTGCATCGGCGGCTATGAGCTCCAGGGTAGCCCTGCCCGAGTATGTCAATCCAACCTGGCT
	TGGTCTGGCACGGAGCCCACCTGTGCAGCCATGAACGTCAATGTGGGTGTCAGAACGGCAGCTGCAC
	TTCTGGATCAGTTTTATGAGAAAAGGAGACTCCTCATTGTGTCCACACCCACAGCCCGAAACCTCCT
	TTACCGGCTCCAGCTAGGAATGCTGCAGCAAGCACAGTGTGGCCTTGATCTTCGACACATCACCGTG
	GTGGAGCTGGTGGGTGTGTTCCCGACTCTCATTGGCAGGATAGGAGCAAAGATTATGCCTCCAGCCC
	TAGCGCTGCAGCTCAGGCTGTTGCTGCGAATCCCACTCTACTCCTTCAGTATGGTGCTAGTGGATAA
	GCATGGCATGGACAAAGAGCGCTATGTCTCCCTGGTGATGCCTGTGGCCCTGTTCAACCTGATTGAC
	ACTTTTCCCTTGAGAAAAGAAGAGATGGTCCTACAAGCCGAAATGAGCCAGACCTGTAACACCTGAC
	ATGATGGTTCCTCTCTTGGCAATTCCTCTTCATTGTCTACATAGTGACATGCACACGGGAAAGCCTT
	AAAAATATCCTTGATGTACAGATTTTATTTGTAATTTTAAAAGTCTATTTTATTATGAGCTTTCTTT
	GCACTTAAAAATTAGCATGCTGCTTTTTGTACTTGGAAGTGTTTCAAAAAATTATATGACCATATTT
	ACTCTTTCTAACTTTCTTTACTCCATCATGGCTGGTTGATTTTGTAGAGAAATTAGAACCCATAACC
	ATACACAGGCTATCAACATGTTATTCAATGTGACACCTAACTCTTTTCTATTTTGTTTTTTAAGTAA
	GACTTTTATTAATAAAACAAAATGTTTTGGAGCAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 75		ORF Stop: TGA at 1404
	SEQ ID NO: 172	443 aa	MW at 49267.9 kD
NOV45c,	MGSPAHRPALLLLLPPLLLLLLRVPPSRSFPDTPWCSPIKVKYGDVYCRAPQGGYYKTALGTRCDIR
CG171681-03
Protein Sequence	CQKGYELHGSSLLICQSNKRWSDKVICKQKRCPTLAMPANGGFKCVDGAYFNSRCEYYCSPGYTLKG
	ERTVTCMDNKAWSGRPASCVDMEPPRIKCPSVKERIAEPNKLTVRVSWETPEGRDTADGILTDVILK
	GLPPGSNFPEGDHKIQYTVYDRAENKGTCKFRVKVRVKRCGKLNAPENGYMKCSSDGDNYGATCEFS
	CIGGYELQGSPARVCQSNLAWSGTEPTCAAMNVNVGVRTAAALLDQFYEKRRLLIVSTPTARNLLYR
	LQLGMLQQAQCGLDLRHITVVELVGVFPTLIGRIGAKIMPPALALQLRLLLRIPLYSFSMVLVDKHG
	MDKERYVSLVMPVALFNLIDTFPLRKEEMVLQAEMSQTCNT

[0608] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 45B.

TABLE 45B
Comparison of NOV45a against NOV45b and NOV45c.
	NOV45a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV45b	33 . . . 321	273/289 (94%)
	156 . . . 444	273/289 (94%)
NOV45c	33 . . . 321	273/289 (94%)
	155 . . . 443	273/289 (94%)

[0609] Further analysis of the NOV45a protein yielded the following properties shown in Table 45C.

TABLE 45C
Protein Sequence Properties NOV45a
PSort analysis:   0.8200 probability located in outside; 0.1000 probability located in
                  endoplasmic reticulum (membrane); 0.1000 probability located in
                  endoplasmic reticulum (lumen); 0.1000 probability located in lysosome
                  (lumen)
SignalP analysis: Cleavage site between residues 31 and 32

[0610] A search of the NOV45a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 45D.

TABLE 45D
Geneseq Results for NOV45a
		NOV45a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB07747	A human cancer-associated	33 . . . 319	148/287 (51%)	7e−89
	protein-1 (CAP-1) - Homo	178 . . . 464	205/287 (70%)
	sapiens, 465 aa.
	[WO200043508-A2,
	Jul. 27, 2000]
AAB59009	Breast and ovarian cancer	33 . . . 319	148/287 (51%)	7e−89
	associated antigen protein	144 . . . 430	205/287 (70%)
	sequence SEQ ID 717 -
	Homo sapiens, 431 aa.
	[WO200055173-A1,
	Sep. 21, 2000]
ABB72149	Rat protein isolated from skin	88 . . . 203	71/116 (61%)	3e−38
	cells SEQ ID NO: 188 -	3 . . . 118	89/116 (76%)
	Rattus sp, 118 aa.
	[WO200190357-A1,
	Nov. 29, 2001]
AAB55949	Skin cell protein, SEQ ID	88 . . . 203	71/116 (61%)	3e−38
	NO: 188 - Rattus sp, 118 aa.	3 . . . 118	89/116 (76%)
	[WO200069884-A2,
	Nov. 23, 2000]
AAY76010	Rat DRS protein homologue,	88 . . . 203	71/116 (61%)	3e−38
	SEQ ID NO:188 - Rattus sp,	3 . . . 118	89/116 (76%)
	118 aa. [WO9955865-A1,
	Nov. 4, 1999]

[0611] In a BLAST search of public sequence datbases, the NOV45a protein was found to have homology to the proteins shown in the BLASTP data in Table 45E.

TABLE 45E
Public BLASTP Results for NOV45a
		NOV45a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
P78539	Sushi repeat-containing	33 . . . 321	289/289 (100%)	e−168
	protein SRPX precursor -	176 . . . 464	289/289 (100%)
	Homo sapiens (Human), 464
	aa.
Q63769	Sushi repeat-containing	33 . . . 321	279/289 (96%)	e−164
	protein SRPX precursor	176 . . . 464	286/289 (98%)
	(DRS protein) (Down-
	regulated by V-SRC) -
	Rattus norvegicus (Rat), 464
	aa.
Q9R0M3	Sushi-repeat-containing	33 . . . 320	276/288 (95%)	e−163
	protein - Mus musculus	176 . . . 463	285/288 (98%)
	(Mouse), 464 aa.
Q9R0M2	Sushi-repeat-containing	33 . . . 320	276/288 (95%)	e−163
	protein - Mus musculus	92 . . . 379	285/288 (98%)
	(Mouse), 380 aa.
AAM73691	Sushi-repeat containing	33 . . . 319	152/287 (52%)	2e−89
	protein - Mus musculus	181 . . . 467	203/287 (69%)
	(Mouse), 468 aa.

[0612] PFam analysis predicts that the NOV45a protein contains the domains shown in the Table 45F.

TABLE 45F
Domain Analysis of NOV45a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV45a Match Region	Region	Value
HYR	33 . . . 114	27/86 (31%)	2.2e−34
		78/86 (91%)
sushi	119 . . . 174	19/64 (30%)	2.7e−09
		41/64 (64%)

Example 46

[0613] The NOV46 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 46A.

TABLE 46A
NOV46 Sequence Analysis
	SEQ ID NO: 173	1785 bp
NOV46a,	GTCGCCAGCTGAGGCGGTTTGTAAGTTTTGGGTCGCAGTATGCTAGAATTTTGAGGCTCCCTTCTGA
CG173318-01
DNA Sequence	TGAAAATTGAGCTGTCCATGCAGCCATGGAACCCGGGTTACAGCAGTGAGGGGGCCACGGCTCAAGA
	AACTTACACATGTCCAAAAATGATTGAGATGGAGCAGGCGGAGGCCCAGCTTGCTGAGTTAGACCTG
	CTAGCCAGTATGTTCCCTGGTGAGAATGAGCTCATAGTGAATGACCAGCTGGCTGTAGCAGAACTGA
	AAGATTGTATTGAAAAGAAGACAATGGAGGGGCGATCTTCAAAAGTCTACTTTACTATCAATATGAA
	CCTGGATGTATCTGACGAAAAAATGGTAATTCAGTTTTGCTTTTAGAGGGATTGAAACATGTTGAGA
	CTTAAAACATTGGTTAGTGCACTTTTTCTTCTTCTCTTTAATCAGGCGATGTTTTCTCTGGCCTGTA
	TTCTTCCCTTTAAATACCCGGCAGTTCTGCCTGAAATTACTGTCAGATCAGTATTATTGAGTAGATC
	CCAGCAGACTCAGCTGAACACAGATCTGACTGCATTCCTGCAAAAACATTGTCATGGAGATGTTTGT
	ATACTGAATGCCACAGAGTGGGTTAGAGAACACGCCTCTGGCTATGTCAGCAGAGATACTTCATCTT
	CACCCACCACAGGAAGCACAGTCCAGTCAGTTGACCTCATCTTCACGAGACTCTGGATCTACAGCCA
	TCATATCTATAACAAATGCAAAAGAAAGAATATTCTAGAGTGGGCAAAGGAGCTTTCCCTGTCTGGG
	TTTAGCATGCCTGGAAAACCTGGTGTTGTTTGTGTGGAAGGCCCACAAAGTGCCTGTGAAGAATTCT
	GGTCAAGACTCAGAAAATTAAACTGGAAGAGAATTTTAATTCGCCATCGAGAAGACATTCCTTTTGA
	TGGTACAAATGATGAAACGGAAAGACAAAGGAAATTTTCCATTTTTGAAGAAAAAGTGTTCAGTGTT
	AATGGAGCCAGGGGAAACCACATGGACTTTGGTCAGCTCTATCAGTTCTTAAACACCAAAGGATGTG
	GGGATGTTTTCCAGATGTTCTTTGGTGTAGAAGGACAATGACATCAAGAGTAGTTGAAAGTATCTTG
	CCACTGTTGGCCTTTTGATTTTTTTTTCCCACTTTTTCTTGAAAGATTAAGTAATTTTATTTTAGTT
	CCATTCTAGAATGTTGGGGAGTGGGGCACAAGAAAAAATAGTATAGCTGAAATGCATCTGTTAAAAA
	TGTCATGATTGAAAGCAGAACTGAGTTTCAAATTACAACCTTAAAATTGTTGTTAGATATTTCTTCA
	CATATCAGCTGCCCATTTTGAAAAAGAAATTATCCATAAAGGTAATGTTGGTGCTCCAATTTGCCAG
	CCATTCCCAACCCCCTTCTCCCTTACCTGCCTTCACTAAAGAACCCAGAAAAGCTAATTGCTCCCCT
	TTCAGCCTCTGTTGCAACTAACAACTCTCAGTGGCCTCAGGACACAGCTTTGGCCTTGGGAATTCTG
	GGAAAACTTTTACTTCCTGATTAAAGATACATATGCAGCTAGGCCACCTCCTCCCCCCCTTACTGCC
	ATAAACACCAAAGTGATGACTGGAGCTGGAGGAGTTATTTGAACCACGACGGAAGGGCCAAGAGAAC
	CACGAAGATGCCAGTTGCCACATTGTTGAGCTGCTGACCCAACACCAGCCATTGCCTGTCTCTAAAC
	ATCTTATGAAATAAAACCAATTTTGTTTAAAAAAAAAAAAAAA
	ORF Start: ATG at 394		ORF Stop: TGA at 1111
	SEQ ID NO: 174	239 aa	MW at 27409.3kD
NOV46a,	MLRLKTLVSALFLLLFNQAMFSLACILPFKYPAVLPEITVRSVLLSRSQQTQLNTDLTAFLQKHCHG
CG173318-01
Protein Sequence	DVCILNATEWVREHASGYVSRDTSSSPTTGSTVQSVDLIFTRLWIYSHHIYNKCKRKNILEWAKELS
	LSGFSMPGKPGVVCVEGPQSACEEFWSRLRKLNWKRILIRHREDIPFDGTNDETERQRKFSIFEEKV
	FSVNGARGNHMDFGQLYQFLNTKGCGDVFQMFFGVEGQ

[0614] Further analysis of the NOV46a protein yielded the following properties shown in Table 46B.

TABLE 46B
Protein Sequence Properties NOV46a
PSort analysis:   0.8000 probability located in outside; 0.2726 probability located in microbody
                  (peroxisome); 0.1000 probability located in endoplasmic reticulum
                  (membrane); 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 23 and 24

[0615] A search of the NOV46a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 46C.

TABLE 46C
Geneseq Results for NOV46a
		NOV46a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAE15253	Human RNA metabolism	19 . . . 239	221/221 (100%)	e−131
	protein-16 (RMEP-16) -	99 . . . 319	221/221 (100%)
	Homo sapiens, 319 aa.
	[WO200183524-A2,
	Nov. 8, 2001]
AAM78405	Human protein SEQ ID NO	19 . . . 239	221/221 (100%)	e−131
	1067 - Homo sapiens, 319	99 . . . 319	221/221 (100%)
	aa. [WO200157190-A2,
	Aug. 9, 2001]
AAM79389	Human protein SEQ ID NO	19 . . . 236	215/218 (98%)	e−127
	3035 - Homo sapiens, 354	137 . . . 354	216/218 (98%)
	aa. [WO200157190-A2,
	Aug. 9, 2001]
ABB11888	Human novel protein, SEQ	19 . . . 236	215/218 (98%)	e−127
	ID NO:2258 - Homo sapiens,	137 . . . 354	216/218 (98%)
	354 aa. [WO200157188-A2,
	Aug. 9, 2001]
AAB58229	Lung cancer associated	19 . . . 167	147/149 (98%)	9e−84
	polypeptide sequence SEQ	103 . . . 251	147/149 (98%)
	ID 567 - Homo sapiens, 305
	aa. [WO200055180-A2,
	Sep. 21, 2000]

[0616] In a BLAST search of public sequence datbases, the NOV46a protein was found to have homology to the proteins shown in the BLASTP data in Table 46D.

TABLE 46D
Public BLASTP Results for NOV46a
		NOV46a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
P57060	Protein C21orf6 (GL011) -	19 . . . 239	221/221 (100%)	e−130
	Homo sapiens (Human), 319	99 . . . 319	221/221 (100%)
	aa.
Q99M03	Similar to open reading frame	21 . . . 239	182/219 (83%)	e−105
	5 - Mus musculus (Mouse),	72 . . . 290	192/219 (87%)
	290 aa.
Q9DCJ3	Open reading frame 5 - Mus	21 . . . 239	182/219 (83%)	e−105
	musculus (Mouse), 244 aa.	26 . . . 244	192/219 (87%)
Q9JLH4	Orf5 protein - Mus musculus	21 . . . 239	181/219 (82%)	e−105
	(Mouse), 291 aa.	73 . . . 291	192/219 (87%)
Q9D9S3	1700030C20Rik protein -	23 . . . 239	85/222 (38%)	3e−38
	Mus musculus (Mouse), 292	72 . . . 288	127/222 (56%)
	aa.

[0617] PFam analysis predicts that the NOV46a protein contains the domains shown in the Table 46E.

TABLE 46E
Domain Analysis of NOV46a
Pfam Domain	NOV46a Match Region	Identities/	Expect
		Similarities	Value
		for the Matched
		Region

Example 47

[0618] The NOV47 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 47A.

TABLE 47A
NOV47 Sequence Analysis
	SEQ ID NO: 175	6373 bp
NOV47a,	GACAGAGTGCAGCCTTTTCAGACTCTGTGACACAGTTCCCCTTTTGCAAAAATACTTAGCGAGGATC
CG51595-01
DNA Sequence	ATTACTTTCCAACAGTCGTGTCCAGAGACCTACTTTGTAACACCGCAGGGAAGTTAATGTACTAGGT
	CTTGAAAGGTCTTTCTGGAATGTGCAGTAACTTGTAGTTTTCTTCTAGTAGCACTGCTAATTTTTGT
	GTTATAATTTTTGTAGGTCCATGGGGCCGATGTATGGGAGATGAATGTGGTCCCGGCATCCAAA
	CGAGGGCTGTGTGGTGTGCTCATGTGGAGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGA
	GAGACCCAATAACCAGCAGAATTGTTTCAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGA
	CTGGGACCTTGGAATCAGTGTCAGCCCGTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTA
	AGGGGGAAGAAGGTATTCAGGTGAGGGAGATAGCGTGCATCCAGAAAGACAAAGACATTCCTGCGGA
	GGATATCATCTGTGAGTACTTTGAGCCCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAG
	CAAGATTGCATCGTGTCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCC
	AGCACCGGACGCGTCATGTGGTGGCGCCCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGA
	GTTCCAGGTGTGCCAATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCC
	TGGAGCACCTGCTCAATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAG
	AACGGGAAAAGGACCGCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAG
	AAACAGAAACAGGCAGAACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGACCAGA
	GAGGTTATGTGCATTAACAAGACGGGGAAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTC
	CAATGACCTTCCAGTCCTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGTGGAGCCC
	CTGCTCAAAAACATGCCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGG
	CAGTTTCCCATTGGCAGTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAG
	GAGATGGAGTTGTCCCCTGTGCCACGTATGGCTGGAGAACTACAGAGTGGACTGAGTGCCGTGTGGA
	CCCTTTGCTCAGTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCATCCAG
	ACCCGAGAGGTGTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAAGAACA
	AAGAAGCCTCAAAGCCAATGGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAGCTGTG
	CCACATTCCTTGTCCAACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTTATGAA
	AACTGTAATGATCAGCAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATGAGCCCA
	CTGGAGGCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAGCCTGC
	CTGTTATGACTGGAAAGCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGGAGTGTGGTCCA
	GGCACGCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGACAGCTGTGCA
	GAGATGCCATCTTCCCCATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTGTGCTCAGCAC
	ATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGATACGA
	GCACGATCCATTCTGGCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGCTTTGC
	AAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGGTCCCTGGGGCCA
	GTGCATTGAGGACACCTCAGTATCGTCCTTCAACACAACTACGACTTGGAATGGGGAGGCCTCCTGC
	TCTGTCGGCATGCAGACAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCCAAGTGGGACCCAAAA
	AATGTCCTGAAAGCCTTCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTTGTAAGAAGGACTGTAT
	TGTGACCCCATATAGTGACTGGACATCATGCCCCTCTTCGTGTAAAGAAGGGGACTCCAGTATCAGG
	AAGCAGTCTAGGCATCGGGTCATCATTCAGCTGCCAGCCAACGGGGGCCGAGACTGCACAGATCCCC
	TCTATGAAGAGAAGGCCTGTGAGGCACCTCAAGCGTGCCAAAGCTACAGGTGGAAGACTCACAAATG
	GCGCAGATGCCAATTAGTCCCTTGGAGCGTGCAACAAGACAGCCCTGGAGCACAGGAAGGCTGTGGG
	CCTGGGCGACAGGCAAGAGCCATTACTTGTCGCAAGCAAGATGGAGGACAGGCTGGAATCCATGAGT
	GCCTACAGTATGCAGGCCCTGTGCCAGCCCTTACCCAGGCCTGCCAGATCCCCTGCCAGGATGACTG
	TCAATTGACCAGCTGGTCCAAGTTTTCTTCATGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAG
	CGCACTCTTGTTGGAAAAAGTAAAAAGAAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTG
	AGACTCAGTATTGTCCTTGTGACAAATATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTT
	ACCAGAGGGAAAAGTGGAAGTGTTGCTGGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAA
	GGATATCGTTACCAAGCAATGGCATGCTACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTA
	ACAGCCATGGTTACATTGAGGAGGCCTGCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTG
	GTCCAACTGGTCGCGCTGCAGCAAGTCCTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGT
	GAAAAACCATATAATGGAGGAAGGCCTTGCCCCAAACTGGACCATGTCAACCAGGCACAGGTGTATG
	AGGTTGTCCCATGCCACAGTGACTGCAACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAA
	GGTGACCTTTGTGAATATGCGGGAGAACTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATG
	CAGAATACAGCAGATGGCCCTTCTGAACATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCC
	TGGGCTCTAGAGTGTGCAAATTACCATGCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGAC
	CCAATGTGTTTTGCCTTGCAATCAAAGCAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCA
	GCTGATGAAGGAAGATCTTGCCCTAATGCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCT
	ACCACTATGATTATAATGTAACAGACTGGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAA
	TGGAATAAAAACAAGGATGTTGGATTGTGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGT
	GAAGCGCTTGGCTTGGAGAAGAACTGGCAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACT
	GTCAGCTTTCTGATTGGTCTCCTTGGTCAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGAT
	CCGAAGACGAACAGTGACCCAGCCCTTTCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAG
	TCCAAACCCTGCCCAGTGAAGCCTTGTTATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGC
	AGGAGGCCCAGTGTGGAGAAGGGACCAGAACAAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGC
	TGATGATTTCAGCAAAGTGGTGGATGAGGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAAT
	AAAAATATGGTTCTGGAGGAATCCTGCAGCCAGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGT
	CTTCCTGGAGCCTGTGTCAGCTGACCTGTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGT
	CAGATCCAGACCGGTGATTATACAAGAACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAA
	ACAAAATCATGTTATGATGGACAGTGCTATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTT
	CCCGAACAGTGTGGTGTCAAAGGTCAGATGGTATAAATGTAACAGGGGGCTGCTTGGTGATGAGCCA
	GCCTGATGCCGACAGGTCTTGTAACCCACCGTGTAGTCAACCCCACTCGTACTGTAGCGAGACAAAA
	ACATGCCATTGTGAAGAAGGGTACACTGAAGTCATGTCTTCTAACAGCACCCTTGAGCAATGCACAC
	TTATCCCCGTGGTGGTATTACCCACCATGGAGGACAAAAGAGGAGATGTGAAAACCAGTCGGGCTGT
	ACATCCAACCCAACCCTCCAGTAACCCAGCAGGACGGGGAAGGACCTGGTTTCTACAGCCATTTGGG
	CCAGATGGGAGACTAAAGACCTGGGTTTACGGTGTAGCAGCTGGGGCATTTGTGTTACTCATCTTTA
	TTGTCTCCATGATTTATCTAGCTTGCAAAAAGCCAAAGAAACCCCAAAGAAGGCAAAACAACCGACT
	GAAACCTTTAACCTTAGCCTATGATGGAGATGCCGACATGTAACATATAACTTTTCCTGGCAACAAC
	CAGTTTCGGCTTTCTGACTTCATAGATGTCCAGAGGCCACAACAAATGTATCCAAACTGTGTGGATT
	AAAATATATTTTAATTTTTAAAAATGGCATCATAAAGACAAGAGTGAAAATCATACTGCCACTGGAG
	ATATTTAAGACAGTACCACTTATATACAGACCATCAACCGTGAGAATTATAGGAGATTTAGCTGAAT
	ACATGCTGCATTCTGAAAGTTTTATGTCATCTTTTCTGAAATCTACCGACTGAAAAACCACTTTCAT
	CTCTAAAAAATAATGGTGGAATTGGCCAGTTAGGATGCCTGATACAAGACCGTCTGCAGTGTTAATC
	CATAAAACTTCCTAGCATGAAGAGTTTCTACCAAGATCTCCACAATACTATGGTCAAATTAACATGT
	GTACTCAGTTGAATGACACACATTATGTCAGATTATGTACTTGCTAATAAGCAATTTTAACAATGCA
	TAACAAATAAACTCTAAGCTAAGCAGAAAATCCACTGAATAAATTCAGCATCTTGGTGGTCGATGGT
	AGATTTTATTGACCTGCATTTCAGAGACAAAGCCTCTTTTTTAAGACTTCTTGTCTCTCTCCAAAGT
	AAGAATGCTGGACAAGTACTAGTGTCTTAGAAGAACGAGTCCTCAAGTTCAGTATTTTATAGTGGTA
	ATTGTCTGGAAAACTAATTTACTTGTGTTAATACAATACGTTTCTACTTTCCCTGATTTTCAAACTG
	GTTGCCTGCATCTTTTTTGCTATATGGAAGGCACATTTTTGCACTATATTAGTGCAGCACGATAGGC
	GCTTAACCAGTATTGCCATAGAAACTGCCTCTTTTCATGTGGGATGAAGACATCTGTGCCAAGAGTG
	GCATGAAGACATTTGCAAGTTCTTGTATCCTGAAGAGAGTAAAGTTCAGTTTGGATGGCAGCAAGAT
	GAAATCAGCTATTACACCTGCTGTACACACACTTCCTCATCACTGCAGCCATTGTGAAATTGACAAC
	ATGGCGGTAATTTAAGTGTTGAAGTCCCTAACCCCTTAACCCTCTAAAAGGTGGATTCCTCTAGTTG
	GTTTGTAATTGTTCTTTGAAGGCTGTTTATGACTAGATTTTTATATTTGTTATCTTTGTTAAGAAAA
	AAAAAAGAAAAAGGAACTGGATGTCTTTTTAATTTTGAGCAGATGGAGAAAATAAATAATGTATCAA
	TGACCTTTGTAACTAAAGGAAAAAAAAAAAAAATGTGGATTTTCCTTTCTCTCTGATTTCCCAGTTT
	CAGATTGAATGTCTGTCTTGCAGGCAGTTATTTCAAAATCCATAGTCTTTNGCCTTTCTCACTGGCA
	AAATTTGA
	ORF Start: ATG at 235		ORF Stop: TAA at 4999
	SEQ ID NO: 176	1588 aa	MW at 178042.1 kD
NOV47a,	MGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPVI
CG51595-01
Protein Sequence	SKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAW
	SECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQ
	VRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKA
	ADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECP
	EFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANE
	NLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGF
	KLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCIN
	SDGEEVDROLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKOIRARSILAYAGEE
	GGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVIC
	VRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQL
	PANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCR
	KQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSDDDE
	KCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYQAMACYD
	QNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCP
	KLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENCGEGVQTRKVRCMQNTADGPSEHV
	EDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAV
	EKEPCNLNKNCYHYDYNVTDWSTCQLSEDAVCGNGIKTRMLDCVRSDGKSVDLKYCEALGLEKNWQM
	NTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYR
	WQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEEFCADIELIIDGNKNMVLEESCSQ
	PCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCYDGQCYE
	YKWMASAWKGSSRTVWCQRSDGINVTGGCLVMSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYTEV
	MSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPDGRLKTWVYG
	VAAGAFVLLIFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDGDADM
	SEQ ID NO: 177	1401 bp
NOV47b,	GAGTGGAGCCCCTGCTCAAAAACATGCCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACAC
CG51595-03
DNA Sequence	GAACCATCAGGCAGTTTCCCATTGGCAGTGAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTG
	TTTGTCTCAAGGAGATGGAGTTGTCCCCTGTGCCACGTATGGCTGGAGAACTACAGAGTGGACTGAG
	TGCCGTGTGGACCCTTTGCTCAGTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAG
	GGGGCATCCAGACCCGAGAGGTGTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTAC
	CCACAAGAACAAAGAAGCCTCAAAGCCAATGGACTTAAAATTATGCACTGGACCTATCCCTAATACT
	ACACAGCTGTGCCACATTCCTTGTCCAACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTT
	GTACTTATGAAAACTGTAATGATCAGCAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTAC
	CAATGAGCCCACTGGAGGCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGT
	GAAGAGCCTGCCTGTTATGACTGGAAAGCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGG
	AGTGTGGTCCAGGCACGCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAG
	ACAGCTGTGCAGAGATGCCATCTTCCCCATCCCTGTGGCCTGTGATGCCCCGTCCCCGAAAGACTGT
	GTGCTCAGCACATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGA
	AACAGATACGAGCACGATCCATTCTGGCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAG
	CAGTGCTTTGCAAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGGT
	CCCTGGGGCCAGTGCATTGAGGACACCTCAGTATCGTCCTTCAACACAACTACGACTTGGAATGGGG
	AGGCCTCCTGCTCTGTCGGCATGCAGACAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCCAAGT
	GGGACCCAAAAAATGTCCTGAAAGCCTTCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTTGTAAG
	AAGGAGTGTATTGTGACCCCATATAGTGACTGGACATCATGCCCCTCTTCGTGTAAAGAAGGGGACT
	CCAGTATCAGGAAGCAGTCTAGGCATCGGGTCATCATTCAGCTGCCAGCCAACGGGGGCCGAGACTG
	CACAGATCCCCTCTATGAAGAGAAGGCCTGTGAGGCACCTCAAGCGTGCCAAAGCTACAGG
	ORF Start: at 1		ORF Stop: end of sequence
	SEQ ID NO: 178	467 aa	MW at 51476.5 kD
NOV47b,	EWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECPEFEEKEPCLSQGDGVVPCATYGWRTTEWTE
CG51595-03
Protein Sequence	CRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANENLLSQLSTHKNKEASKPMDLKLCTGPIPNT
	TQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGFKLRKRRITNEPTGGSGVTGNCPHLLEAIPC
	EEPACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCINSDGEEVDRQLCRDAIFPIPVACDAPSPKDC
	VLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEEGGIRCPNSSALQEVRSCNEHPCTVYHWQTG
	PWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVICVRVNVGQVGPKKCPESLRPETVRPCLLPCK
	KECIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQLPANGGRDCTDPLYEEKACEAPQACQSYR
	SEQ ID NO: 179	1713 bp
NOV47c,	TGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAGCGCACTCTTGTTGGAAAAAGTAAAAAGAAGG
CG51595-04
DNA Sequence	AAAAATGTAAAAATTCCCATTTGTATCCCCTGATTGAGACTCAGTATTGTCCTTGTGACAAATATAA
	TGCACAACCTGTGGGGAACTGGTCAGACTGTATTTTACCAGAGGGAAAAGTGGAAGTGTTGCTGGGA
	ATGAAAGTACAAGGAGACATCAAGGAATGCGGACAAGGATATCGTTACCAAGCAATGGCATGCTACG
	ATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTAACAGCCATGGTTACATTGAGGAGGCCTGCAT
	CATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTGGTCCAACTGGTCGCGCTGCAGCAAGTCCTGT
	GGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGTGAAAAACCATATAATGGAGGAAGGCCTTGCC
	CCAAACTGGACCATGTCAACCAGGCACAGGTGTATGAGGTTGTCCCATGCCACAGTGACTGCAACCA
	GTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAAGGTGACCTTTGTGAATATGCGGGAGAACTGT
	GGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATGCAGAATACAGCAGATGGCCCTTCTGAACATG
	TAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCCTGGGCTCTAGAGTGTGCAAATTACCATGCCC
	TGAGGACTGTGTGATATCTGAATGGGGTCCATGGACCCAATGTGTTTTGCCTTGCAATCAAAGCAGT
	TTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCAGCTGATGAAGGAAGATCTTGCCCTAATGCTG
	TTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCTACCACTATGATTATAATGTAACAGACTGGAG
	TACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAATGGAATAAAAACAAGGATGTTGGATTGTGTT
	CGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGTGAAGCGCTTGGCTTGGAGAAGAACTGGCAGA
	TGAACACGTCCTGCATGGTGGAATGCCCTGTGAACTGTCAGCTTTCTGATTGGTCTCCTTGGTCAGA
	ATGTTCTCAAACATGTGGCCTCACAGGAAAAATGATCCGAAGACGAACAGTGACCCAGCCCTTTCAA
	GGTGATGGAAGACCATGCCCTTCCCTGATGGACCAGTCCAAACCCTGCCCAGTGAAGCCTTGTTATC
	GGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGCAGGAGGCCCAGTGTGGAGAAGGGACCAGAAC
	AAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGCTGATGATTTCAGCAAAGTGGTGGATGAGGAA
	TTCTGTGCTGACATTGAACTCATTATAGATGGTAATAAAAATATGGTTCTGGAGGAATCCTGCAGCC
	AGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGTCTTCCTGGAGCCTGTGTCAGCTGACCTGCGT
	GAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGTCAGATCCAGACCGGTGATTATACAAGAACTA
	GAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAAACAAAATCATGTTATGATGGACAGTGCTATG
	AATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTTCC
	ORF Start: at 1		ORF Stop: end of sequence
	SEQ ID NO: 180	571 aa	MW at 64468.4 kD
NOV47c,	CNGDCGAVRTRKRTLVGKSKKKEKCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLG
CG51595-04
Protein Sequence	MKVQGDIKECGQGYRYQAMACYDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSC
	GSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENC
	GEGVQTRKVRCMQNTADGPSEHVEDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSS
	FRQRSADPIRQPADEGRSCPNAVEKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCV
	RSDGKSVDLKYCEALGLEKNWQMNTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQ
	GDGRPCPSLMDQSKPCPVKPCYRWQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEE
	FCADIELIIDGNKNMVLEESCSQPCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQEL
	ENQHLCPEQMLETKSCYDGQCYEYKWMASAWKGSS
	SEQ ID NO: 181	14881 bp
NOV47d,	CGTCCATGGGGCCGATGTATGGGAGATGAATGTGGTCCCGGAGGCATCCAAACGAGGGCTGTGTGGT
CG51595-06
DNA Sequence	GTGCTCATGTGGAGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGAGAGACCCAATAACCA
	GCAGAATTGTTTCAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGACTGGGACCTTGGAAT
	CAGTGTCAGCCCGTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTAAGGGGGAAGAAGGTA
	TTCAGGTGAGGGAGATAGCGTGCATCCAGAAAGACAAAGACATTCCTGCGGAGGATATCATCTGTGA
	GTACTTTGAGCCCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAGCAAGATTGCATCGTG
	TCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCCAGCACCGGACGCGTC
	ATGTGGTGGCGCCCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGAGTTCCAGGTGTGCCA
	ATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCCTGGAGCACCTGCTCA
	ATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAGAACGGGAAAAGGACC
	GCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAGAAACAGAAACAGGCA
	GAACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGACCAGAGAGGTTATGTGCATT
	AACAAGACGGGGAAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTCCAATGACCTTCCAGT
	CCTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGTGGAGCCCCTGCTCAAAAACATG
	CCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGGCAGTTTCCCATTGGC
	AGTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAGGAGATGGAGTTGTCC
	CCTGTGCCACGTATGGCTGGAGAACTACAGAGTGGACTGAGTGCCGTGTGGACCCTTTGCTCAGTCA
	GCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCATCCAGACCCGAGAGGTGTAC
	TGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAAGAACAAAGAAGCCTCAAAGC
	CAATGGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAGCTGTGCCACATTCCTTGTCC
	AACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTTATGAAAACTGTAATGATCAG
	CAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATGAGCCCACTGGAGGCTCTGGGG
	TAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAGCCTGCCTGTTATGACTGGAA
	AGCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGGAGTGTGGTCCAGGCACGCAAGTTCAA
	GAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGACAGCTGTGCAGAGATGCCATCTTCC
	CCATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTGTGCTCAGCACATGGTCTACGTGGTC
	CTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGATACGAGCACGATCCATTCTG
	GCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGCTTTGCAAGAAGTACGAAGCT
	GTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGGTCCCTGGGGCCAGTGCATTGAGGACAC
	CTCAGTATCGTCCTTCAACACAACTACGACTTGGAATGGGGAGGCCTCCTGCTCTGTCGGCATGCAG
	ACAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCCAAGTGGGACCCAAAAAATGTCCTGAAAGCC
	TTCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTTGTAAGAAGGACTGTATTGTGACCCCATATAG
	TGACTGGACATCATGCCCCTCTTCGTGTAAAGAAGGGGACTCCAGTATCAGGAAGCAGTCTAGGCAT
	CGGGTCATCATTCAGCTGCCAGCCAACGGGGGCCGAGACTGCACAGATCCCCTCTATGAAGAGAAGG
	CCTGTGAGGCACCTCAAGCGTGCCAAAGCTACAGGTGGAAGACTCACAAATGGCGCAGATGCCAATT
	AGTCCCTTGGAGCGTGCAACAAGACAGCCCTGGAGCACAGGAAGGCTGTGGGCCTGGGCGACAGGCA
	AGAGCCATTACTTGTCGCAAGCAAGATGGAGGACAGGCTGGAATCCATGAGTGCCTACAGTATGCAG
	GCCCTGTGCCAGCCCTTACCCAGGCCTGCCAGATCCCCTGCCAGGATGACTGTCAATTGACCAGCTG
	GTCCAAGTTTTCTTCATGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAGCGCACTCTTGTTGGA
	AAAAGTAAAAAGAAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTGAGACTCAGTATTGTC
	CTTGTGACAAATATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTTACCAGAGGGAAAAGT
	GGAAGTGTTGCTGGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAAGGATATCGTTACCAA
	GCAATGGCATGCTACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTAACAGCCATGGTTACA
	TTGAGGAGGCCTGCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTGGTCCAACTGGTCGCG
	CTGCAGCAAGTCCTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGTGAAAAACCATATAAT
	GGAGGAAGGCCTTGCCCCAAACTGGACCATGTCAACCAGGCACAGGTGTATGAGGTTGTCCCATGCC
	ACAGTGACTGCAACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAAGGTGACCTTTGTGAA
	TATGCGGGAGAACTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATGCAGAATACAGCAGAT
	GGCCCTTCTGAACATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCCTGGGCTCTAGAGTGT
	GCAAATTACCATGCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGACCCAATGTGTTTTGCC
	TTGCAATCAAAGCAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCAGCTGATGAAGGAAGA
	TCTTGCCCTAATGCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCTACCACTATGATTATA
	ATGTAACAGACTGGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAATGGAATAAAAACAAG
	GATGTTGGATTGTGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGTGAAGCGCTTGGCTTG
	GAGAAGAACTGGCAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACTGTCAGCTTTCTGATT
	GGTCTCCTTGGTCAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGATCCGAAGACGAACAGT
	GACCCAGCCCTTTCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAGTCCAAACCCTGCCCA
	GTGAAGCCTTGTTATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGCAGGAGGCCCAGTGTG
	GAGAAGGGACCAGAACAAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGCTGATGATTTCAGCAA
	AGTGGTGGATGAGGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAATAAAAATATGGTTCTG
	GAGGAATCCTGCAGCCAGCCTTGCCCAGGTCACTGTTATTTGAAGGACTGGTCTTCCTGGAGCCTGT
	GTCAGCTGACCTGTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGTCAGATCCAGACCGGT
	GATTATACAAGAACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAAACAAAATCATGTTAT
	GATGGACAGTGCTATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTTCCCGAACAGTGTGGT
	GTCAAAGGTCAGATGGTATAAATGTAACAGGGGGCTGCTTGGTGATGAGCCAGCCTGATGCCGACAG
	GTCTTGTAACCCACCGTGTAGTCAACCCCACTCGTACTGTAGCGAGACAAAAACATGCCATTGTGAA
	GAAGGGTACACTGAAGTCATGTCTTCTAACAGCACCCTTGAGCAATGCACACTTATCCCCGTGGTGG
	TATTACCCACCATGGAGGACAAAAGAGGAGATGTGAAAACCAGTCGGGCTGTACATCCAACCCAACC
	CTCCAGTAACCCAGCAGGACGGGGAAGGACCTGGTTTCTACAGCCATTTGGGCCAGCAAAAAGCCAA
	AGAAACCCCAAAGAAGGCAAAACAACCGACTGAAACCTTTAACCTTAGCCTATGATGGAGATGCCGA
	CATGTAACATATAACTTTTCCTGGCAACAACCAGTTTCGGCTTTCTGACTTCATAGATGTCCAGAGG
	CCACAACAAATGTATCCAAACTGTGTGGATTAAAATATATTTTAATTTTTAAAAATGGCATCATAAA
	GACAAGAGTGAAAATCATACTGCCACTGGAGATATTTAAGACAGTACCACTTATATA
	ORF Start: ATG at 19		ORF Stop: TGA at 4654
	SEQ ID NO: 182	1545 aa	MW at 173146.2 kD
NOV47d,	MGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPVI
CG15195-06
Protein Sequence	SKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAW
	SECSKTCGSGLQHRTRHVVAPPQFGGSGCPNDTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQ
	VRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKA
	ADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECP
	EFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANE
	NLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGF
	KLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCIN
	SDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEE
	GGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVIC
	VRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQL
	PANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCR
	KQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKKKE
	KCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYQAMACYD
	QNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSDWLREKPYNGGRPCP
	KLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENCGEGVQTRKVRCMQNTADGPSEHV
	EDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAV
	EKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLKYCEALGLEKNWQM
	NTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYR
	WQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEEFCADIELIIDGNKNMVLEESCSQ
	PCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCTDGQCYE
	YKWMASAWKGSSRTVWCQRSDGINVTGGCLVMSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYTEV
	MSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPAKSQRNPKEG
	KKTD
	SEQ ID NO: 183	4679 bp
NOV47e,	GTCCATGGGGCCGATGTATGGGAGATGAATGTGGTCCCGGAGGCATCCAAACGAGGGCTGTGTGGTG
CG51595-07
DNA Sequence	TGCTCATGTGGAGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGAGAGACCCAATAACCAG
	CAGAATTGTTTCAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGACTGGGACCTTGGAATC
	AGTGTCAGCCCGTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTAAGGGGGAAGAAGGTAT
	TCAGGTGAGGGAGATAGCGTGCATCCAGAAAGACAAAGACATTCCTGCGGAGGATATCATCTGTGAG
	TACTTTGAGCCCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAGCAAGATTGCATCGTGT
	CTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCCAGCACCGGACGCGTCA
	TGTGGTGGCGCCCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGAGTTCCAGGTGTGCCAA
	TCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCCTGGAGCACCTGCTCAA
	TGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAGAACGGGAAAAGGACCG
	CAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAGAAACAGAAACAGGCAG
	AACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGACCAGAGAGGTTATGTGCATTA
	ACAAGACGGGGAAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTCCAATGACCTTCCAGTC
	CTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGTGGAGCCCCTGCTCAAAAACATGC
	CATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGGCAGTTTCCCATTGGCA
	GTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAGGAGATGGAGTTGTCCC
	CTGTGCCACGTATGGCTGGAGAACTACAGAGTGGACTGAGTGCCGTGTGGACCCTTTGCTCAGTCAG
	CAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCATCCAGACCCGAGAGGTGTACT
	GCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAAGAACAAAGAAGCCTCAAAGCC
	AATGGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAGCTGTGCCACATTCCTTGTCCA
	ACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTTATGAAAACTGTAATGATCAGC
	AAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATGAGCCCACTGGAGGCTCTGGGGT
	AACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAGCCTGCCTGTTATGACTGGAAA
	GCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGGAGTGTGGTCCAGGCACGCAAGTTCAAG
	AGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGACAGCTGTGCAGAGATGCCATCTTCCC
	CATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTGTGCTCAGCACATGGTCTACGTGGTCC
	TCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGATACGAGCACGATCCATTCTGG
	CCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGCTTTGCAAGAAGTACGAAGCTG
	TAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGGTCCCTGGGGCCAGTGCATTGAGGACACC
	TCAGTATCGTCCTTCAACACAACTACGACTTGGAATGGGGAGGCCTCCTGCTCTGTCGGCATGCAGA
	CAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCCAAGTGGGACCCAAAAAATGTCCTGAAAGCCT
	TCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTTGTAAGAAGGACTGTATTGTGACCCCATATAGT
	GACTGGACATCATGCCCCTCTTCGTGTAAAGAAGGGGACTCCAGTATCAGGAAGCAGTCTAGGCATC
	GGGTCATCATTCAGCTGCCAGCCAACGGGGGCCGAGACTGCACAGATCCCCTCTATGAAGAGAAGGC
	CTGTGAGGCACCTCAAGCGTGCCAAAGCTACAGGTGGAAGACTCACAAATGGCGCAGATGCCAATTA
	GTCCCTTGGAGCGTGCAACAAGACAGCCCTGGAGCACAGGAAGGCTGTGGGCCTGGGCGACAGGCAA
	GAGCCATTACTTGTCGCAAGCAAGATGGAGGACAGGCTGGAATCCATGAGTGCCTACAGTATGCAGG
	CCCTGTGCCAGCCCTTACCCAGGCCTGCCAGATCCCCTGCCAGGATGACTGTCAATTGACCAGCTGG
	TCCAAGTTTTCTTCATGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAGCGCACTCTTGTTGGAA
	AAAGTAAAAAGAAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTGAGACTCAGTATTGTCC
	TTGTGACAAATATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTTACCAGAGGGAAAAGTG
	GAAGTGTTGCTGGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAAGGATATCGTTACCAAG
	CAATGGCATGCTACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTAACAGCCATGGTTACAT
	TGAGGAGGCCTGCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTGGTCCAACTGGTCGCGC
	TGCAGCAAGTCCTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGTGAAAAACCATATAATG
	GAGGAAGGCCTTGCCCCAAACTGGACCATGTCAACCAGGCACAGGTGTATGAGGTTGTCCCATGCCA
	CAGTGACTGCAACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAAGGTGACCTTTGTGAAT
	ATGCGGGAGAACTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATGCAGAATACAGCAGATG
	GCCCTTCTGAACATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCCTGGGCTCTAGAGTGTG
	CAAATTACCATGCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGACCCAATGTGTTTTGCCT
	TGCAATCAAAGCAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCAGCTGATGAAGGAAGAT
	CTTGCCCTAATGCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCTACCACTATGATTATAA
	TGTAACAGACTGGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAATGGAATAAAAACAAGG
	ATGTTGGATTGTGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGTGAAGCGCTTGGCTTGG
	AGAAGAACTGGCAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACTGTCAGCTTTCTGATTG
	GTCTCCTTGGTCAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGATCCGAAGACGAACAGTG
	ACCCAGCCCTTTCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAGTCCAAACCCTGCCCAG
	TGAAGCCTTGTTATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGCAGGAGGCCCAGTGTGG
	AGAAGGGACCAGAACAAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGCTGATGATTTCAGCAAA
	GTGGTGGATGAGGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAATAAAAATATGGTTCTGG
	AGGAATCCTGCAGCCAGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGTCTTCCTGGAGCCTGTG
	TCAGCTGACCTGTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGTCACATCCAGACCGGTG
	ATTATACAAGAACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAAACAAAATCATGTTATG
	ATGGACAGTGCTATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTTCCCGAACAGTGTGGTG
	TCAAAGGTCAGATGGTATAAATGTAACAGATGGGAGACTAAAGACCTGGGTTTACGGTGTAGCAGCT
	GGGGCATTTGTGTTACTCATCTTTATTGTCTCCATGATTTATCTAGCTTGCAAAAAGCCAAAGAAAC
	CCCAAAGAAGGCAAAACAACCGACTGAAACCTTTAACCTTAGCCTATGATGGAGATGCCGACATGTA
	ACATATAACTTTTCCTGGCAACAACCAGTTTCGGCTTTCTGACTTCATAGATGTCCAGAGGCCACAA
	ORF Start: ATG at 18		ORF Stop: TAA at 4488
	SEQ ID NO: 184	1490 aa	MW at 167403.2 kD
NOV47e,	MGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPVI
CG51595-07
Protein Sequence	SKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAW
	SECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCPSSPCEAEELRYSLHVGPWSTCSMPHSRQ
	VRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKA
	ADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECP
	EFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANE
	NLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGF
	KLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCIN
	SDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEE
	GGIRCPNSSALOEVRSCNEHPCTVYHWOTGPWGOCIEDTSVSSFNTTTTWNGEASCSVGMOTRKVIC
	VRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQL
	PANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCR
	KQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKKKE
	KCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYOAMACYD
	QNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCP
	KLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENCGEGVQTRKVRCMQNTADGPSEHV
	EDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAV
	EKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLRYCEALGLEKNWQM
	NTSCMVENPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYR
	WQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEEFCADIELIIDGNKNMVLEESCSQ
	PCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCYDGQCYE
	YKWMASAWKGSSRTVWCQRSDGINVTDGRLKTWVYGVAAGAFVLLIFIVSMIYLACKKPKKPQRRQN
	NRLKPLTLAYDGDADM
	SEQ ID NO: 185	4647 bp
NOV47f,	GGTACCATGGGAGATGAATGTGGTCCCGGAGGCATCCAAACGAGGGCTGTGTGGTGTGCTCATGTGG
306395637 DNA
Sequence	AGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGAGAGACCCAATAACCAGCAGAATTGTTT
	CAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGACTGGGACCTTGGAATCAGTGTCAGCCC
	GTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTAAGGGGGAAGAAGGTATTCAGGTGAGGG
	AGATAGCGTGCATCCAGAAAGACAAAGACATTCCTGCGGAGGATATCATCTGTGAGTACTTTGAGCC
	CAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAGCAAGATTGCATCGTGTCTGAATTTTCT
	GCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCCAGCACCGGACGCGTCATGTGGTGGCGC
	CCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGAGTTCCAGGTGTGCCAATCCAGTCCATG
	CGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCCTGGAGCAGGTGCTCAATGCCCCACTCC
	CGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAGAACGGGAAAAGGACCGCAGCAAAGGAG
	TAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAGAAACAGAAACAGACAGAACAGACAAGA
	GAACAAATATTGGGACATCCAGATTGGATATCAGACCAGAGAGGTTATGTGCATTAACAAGACGGGG
	AAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTCCAATGACCTTCCAGTCCTGTGTGATCA
	CCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGCGGAGCCCCTGCTCAAAAACATGCCATGACATGGT
	GTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGGCAGTTTCCCATTGGCAGTGAAAAGGAG
	TGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAGGAGATGGAGTTGTCCCCTGTGCCACGT
	ATGGCTGGAGAACTACAGAGTGGACTGAGTGCCGTGTGGACCCTTTGCTCAGTCAGCAGGACAAGAG
	GCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCATCCAGACCCGAGAGGTGTACTGCGTGCAGGCC
	AACGAAAACCTCCTCTCACAATTAAGTACCCACAAGAACAAAGAAGCCTCAAAGCCAATGGACTTAA
	AATTATGCACTGGACCTATCCCTAATACTACACAGCTGTGCCACATTCCTTGTCCAACTGAATGTGA
	AGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTTATGAAAACTGTAATGATCAGCAAGGGAAAAAA
	GGCTTCAAACTGAGGAAGCGGCGCATTACCAATGAGCCCACTGGAGGCTCTGGGGTAACCGGAAACT
	GCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAGCCTGCCTGTTATGACTGGAAAGCAGTGAGACT
	GGGAAACTGCGAGCCAGATAACGGAAAGGAGTGTGGTCCAGGCACGCAAGTTCAAGAGGTTGTGTGC
	ATCAACAGTGATGGAGAAGAAGTTGACAGACAGCTGTGCAGAGATGCCATCTTCCCCATCCCTGTGG
	CCTGTGATGCCCCGTGCCCGAAAGACTGTGTGCTCAGCACATGGTCTACGTGGTCCTCCTGCTCACA
	CACCTGCTCAGGGAAAACGACAGAAGGGAAACAGATACGAGCACGATCCATTCTGGCCTATGCGGGT
	GAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGCTTTGCAAGAAGTACGAAGCTGTAATGAGCATC
	CTTGCACAGTGTACCACTGGCAAACTGGTCCCTGGGGCCAGTGCATTGAGGACACCTCAGTATCGTC
	CTTCAACACAACTACGACTTGGAATGGGGAGGCCTCCTGCTCTGTCGGCATGCAGACAAGAAAAGTC
	ATCTGTGTGCGAGTCAATGTGGGCCAAGTGGGACCCAAAAAATGTCCTGAAAGCCTTCGACCTGAAA
	CTGTAAGGCCTTGTCTGCTTCCTTGTAAGAAGGAGTGTATTGTGACCCCATATAGTGACTGGACATC
	ATGCCCCTCTTCGTGTAAAGAAGGGGACTCCAGTATCAGGAAGCAGTCTAGGCATCGGGTCATCATT
	CAGCTGCCAGCCAACGGGGGCCGAGACTGCACAGATCCCCTCTATGAAGAGAAGGCCTGTGAGGCAC
	CTCAAGCGTGCCAAAGCTACAGGTGGAAGACTCACAAATGGCGCAGATGCCAATTAGTCCCTTGGAG
	CGTGCAACAAGACAGCCCTGGAGCACAGGAAGGCTGTGGGCCTGGGCGACAGGCAAGAGCCATTACT
	TGTCGCAAGCAAGATGGAGGACAGGCTGGAATCCATGAGTGCCTACAGTATGCAGGCCCTGTGCCAG
	CCCTTACCCAGGCCTGCCAGATCCCCTGCCAGGATGACTGTCAATTGACCAGCTGGTCCAAGTTTTC
	TTCATGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAGCGCACTCTTGTTGGAAAAAGTAAAAAG
	AAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTGAGACTCAGTATTGTCCTTGTGACAAAT
	ATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTTACCAGAGGGAAAAGTGGAAGTGTTGCT
	GGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAAGGATATCGTTACCAAGCAATGGCATGC
	TACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTAACAGCCATGGTTACATTGAGGAGGCCT
	GCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTGGTCCAACTGGTCGCGCTGCAGCAAGTC
	CTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGTGAAAAACCATATAATGGAGGAAGGCCT
	TGCCCCAAACTGGACCATGTCAACCAGGCACAGGTGTATGAGGTTGTCCCATGCCACAGTGACTGCA
	ACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAAGGTGACCTTTGTGAATATGCGGGAGAA
	CTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATGCAGAATACAGCAGATGGCCCTTCTGAA
	CATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCCTGGGCTCTAGAGTGTGCAAATTACCAT
	GCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGACCCAATGTGTTTTGCCTTGCAATCAAAG
	CAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCAGCTGATGAAGGAAGATCTTGCCCTAAT
	GCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCTACCACTATGATTATAATGTAACAGACT
	GGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAATGGAATAAAAACAAGGATGTTGGATTG
	TGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGTGAAGCGCTTGGCTTGGAGAAGAACTGG
	CAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACTGTCAGCTTTCTGATTGGTCTCCTTGGT
	CAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGATCCGAAGACGAACAGTGACCCAGCCCTT
	TCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAGTCCAAACCCTGCCCAGTGAAGCCTTGT
	TATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGCAGGAGGCCCAGTGTGGAGAAGGGACCA
	GAACAAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGCTGATGATTTCAGCAAAGTGGTGGATGA
	GGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAATAAAAATATGGTTCTGGAGGAATCCTGC
	AGCCAGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGTCTTCCTGGAGCCTGTGTCAGCTGACCT
	GTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGTCAGATCCAGACCGGTGATTATACAAGA
	ACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAAACAAAATCATGTTATGATGGACAGTGC
	TATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTTCCCGAACAGTGTGGTGTCAAAGGTCAG
	ATGGTATAAATGTAACAGGGGGCTGCTTGGTGATGAGCCAGCCTGATGCCGACAGGTCTTGTAACCC
	ACCGTGTAGTCAACCCCACTCGTACTGTAGCGAGACAAAAACATGCCATTGTGAAGAAGGGTACACT
	GAAGTCATGTCTTCTAACAGCACCCTTGAGCAATGCACACTTATCCCCGTGGTGGTATTACCCACCA
	TGGAGGACAAAAGAGGAGATGTGAAAACCAGTCGGGCTGTACATCCAACCCAACCCTCCAGTAACCC
	AGCAGGACGGGGAAGGACCTGGTTTCTACAGCCATTTGGGCCAGCAAAAAGCCAAAGAAACCCCAAA
	GAAGGCAAAACAACCGACGTCGAC
	ORF Start: at 1		ORF Stop: end of sequence
	SEQ ID NO: 186	1549 aa	MW at 173501.6 kD
NOV47f,	GTMGDECGPGGIQTRAVWCAHVEGWTTLGTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQP
306395637
Protein	VISKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFS
Sequence
	AWSECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHS
	RQVRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTG
	KAADLSFCQQELKPMTFQSCVITKECQVSEWSERSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKE
	CPEFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQA
	NENLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKK
	GFKLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGNCEPDNGKECGPGTQVQEVVC
	INSDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAG
	EEGGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKV
	ICVRVNVGQVGPKKCPESLRPETVRPCLLPCKKECIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVII
	QLPANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAIT
	CRKQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKK
	KEKCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYQAMAC
	YDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRP
	CPKLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENCGEGVQTRKVRCMQNTADGPSE
	HVEDYLCDPEEMPLGSRVCKPLCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPN
	AVEKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLKYCEALGLEKNW
	QMNTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPC
	YRWQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEEFCADIELIIDGNKNMVLEESC
	SQPCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETDSCYDGQC
	YEYKWMASAWKGSSRTVWCQRSDGINVYGGCDVMSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYT
	EVMSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPAKSQRNPK
	EGKTTDVD
	SEQ ID NO: 187	16373 bp
NOV47g,	GACAGAGTGCAGCCTTTTCAGACTCTGTGACACAGTTCCCCTTTTGCAAAAATACTTAGCGAGGATC
CG51595-01
DNA Sequence	ATTACTTTCCAACAGTCGTGTCCAGAGACCTACTTTGTAACACCGCAGGGAAGTTAATGTACTAGGT
	CTTGAAAGGTCTTTCTGGAATGTGCAGTAACTTGTAGTTTTCTTCTAGTAGCACTGCTAATTTTTGT
	GTTATAATTTTTGTAGGTCCATGGGGCCGATGTATGGGAGATGAATGTGGTCCCGGAGGCATCCAAA
	CGAGGGCTGTGTGGTGTGCTCATGTGGAGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGA
	GAGACCCAATAACCAGCAGAATTGTTTCAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGA
	CTGGGACCTTGGAATCAGTGTCAGCCCGTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTA
	AGGGGGAAGAAGGTATTCAGGTGAGGGAGATAGCGTGCATCCAGAAAGACAAAGACATTCCTGCGGA
	GGATATCATCTGTGAGTACTTTGAGCCCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAG
	CAAGATTGCATCGTGTCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCC
	AGCACCGGACGCGTCATGTGGTGGCGCCCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGA
	GTTCCAGGTGTGCCAATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCC
	TGGAGCACCTGCTCAATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAG
	AACGGGAAAAGGACCGCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAG
	AAACAGAAACAGGCAGAACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGACCAGA
	GAGGTTATGTGCATTAACAAGACGGGGAAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTC
	CAATGACCTTCCAGTCCTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGTGGAGCCC
	CTGCTCAAAAACATGCCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGG
	CAGTTTCCCATTGGCAGTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAG
	GAGATGGAGTTGTCCCCTGTGCCACGTATGGCTCCAGAACTACAGAGTGGACTGAGTGCCGTGTGGA
	CCCTTTGCTCAGTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCATCCAG
	ACCCGAGAGGTGTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAAGAACA
	AAGAAGCCTCAAAGCCAATGGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAGCTGTG
	CCACATTCCTTGTCCAACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTTATGAA
	AACTGTAATGATCAGCAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATGAGCCCA
	CTGGAGGCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAGCCTGC
	CTGTTATGACTGGAAAGCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGGAGTGTGGTCCA
	GGCACGCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGACAGCTGTGCA
	GAGATGCCATCTTCCCCATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTGTGCTCAGCAC
	ATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGATACGA
	GCACGATCCATTCTGGCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGCTTTGC
	AAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGGTCCCTGGGGCCA
	GTGCATTGAGGACACCTCAGTATCGTCCTTCAACACAACTACGACTTGGAATGGGGAGGCCTCCTGC
	TCTGTCGGCATGCAGACAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCCAAGTGGGACCCAAAA
	AATGTCCTGAAAGCCTTCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTTGTAAGAAGGACTGTAT
	TGTGACCCCATATAGTGACTGGACATCATGCCCCTCTTCGTGTAAAGAAGGGGACTCCAGTATCAGG
	AAGCAGTCTAGGCATCGGGTCATCATTCAGCTGCCAGCCAACGGGGGCCGAGACTGCACAGATCCCC
	TCTATGAAGAGAAGGCCTGTGAGGCACCTCAAGCGTGCCAAAGCTACAGGTGGAAGACTCACAAATG
	GCGCAGATGCCAATTAGTCCCTTGGAGCGTGCAACAAGACAGCCCTGGAGCACAGGAAGGCTGTGGG
	CCTGGGCGACAGGCAAGAGCCATTACTTGTCGCAAGCAAGATGGAGGACAGGCTGGAATCCATGAGT
	GCCTACAGTATGCAGGCCCTGTGCCAGCCCTTACCCAGGCCTGCCAGATCCCCTGCCAGGATGACTG
	TCAATTGACCAGCTGGTCCAAGTTTTCTTCATGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAG
	CGCACTCTTGTTGGAAAAAGTAAAAAGAAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTG
	AGACTCAGTATTGTCCTTGTGACAAATATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTT
	ACCAGAGGGAAAAGTGGAAGTGTTGCTGGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAA
	GGATATCGTTACCAAGCAATGGCATGCTACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTA
	ACAGCCATGGTTACATTGAGGAGGCCTGCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTG
	GTCCAACTGGTCGCGCTGCAGCAAGTCCTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGT
	GAAAAACCATATAATGGAGGAAGGCCTTGCCCCAAACTGGACCATGTCAACCAGGCACAGGTGTATG
	AGGTTGTCCCATGCCACAGTGACTGCAACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAA
	GGTGACCTTTGTGAATATGCGGGAGAACTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATG
	CAGAATACAGCAGATGGCCCTTCTGAACATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCC
	TGGGCTCTAGAGTGTGCAAATTACCATGCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGAC
	CCAATGTGTTTTGCCTTGCAATCAAAGCAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCA
	GCTGATGAAGGAAGATCTTGCCCTAATGCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCT
	ACCACTATGATTATAATGTAACAGACTGGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAA
	TGGAATAAAAACAAGGATGTTGGATTGTGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGT
	GAAGCGCTTGGCTTGGAGAAGAACTGGCAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACT
	GTCAGCTTTCTGATTGGTCTCCTTGGTCAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGAT
	CCGAAGACGAACAGTGACCCAGCCCTTTCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAG
	TCCAAACCCTGCCCAGTGAAGCCTTGTTATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGC
	AGGAGGCCCAGTGTGGAGAAGGGACCAGAACAAGCAACATTTCTTGTGTAGTAAGTGATGGGTCAGC
	TGATGATTTCAGCAAAGTGGTGGATGAGGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAAT
	AAAAATATGGTTCTGGAGGAATCCTGCAGCCAGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGT
	CTTCCTGGAGCCTGTGTCAGCTGACCTGTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGT
	CAGATCCAGACCGGTGATTATACAAGAACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAA
	ACAAAATCATGTTATGATGGACAGTGCTATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTT
	CCCGAACAGTGTGGTGTCAAAGGTCAGATGGTATAAATGTAACAGGGGGCTGCTTGGTGATGAGCCA
	GCCTGATGCCGACAGGTCTTGTAACCCACCGTGTAGTCAACCCCACTCGTACTGTAGCGAGACAAAA
	ACATGCCATTGTGAAGAAGGGTACACTGAAGTCATGTCTTCTAACAGCACCCTTGAGCAATGCACAC
	TTATCCCCGTGGTGGTATTACCCACCATGGAGGACAAAAGAGGAGATGTGAAAACCAGTCGGGCTGT
	ACATCCAACCCAACCCTCCAGTAACCCAGCAGGACGGGGAAGGACCTGGTTTCTACAGCCATTTGGG
	CCAGATGGGAGACTAAAGACCTGGGTTTACGGTGTAGCAGCTCGGGCATTTGTGTTACTCATCTTTA
	TTGTCTCCATGATTTATCTAGCTTGCAAAAAGCCAAAGAAACCCCAAAGAAGGCAAAACAACCGACT
	GAAACCTTTAACCTTAGCCTATGATGGAGATGCCGACATGTAACATATAACTTTTCCTGGCAACAAC
	CAGTTTCGGCTTTCTGACTTCATAGATGTCCAGAGGCCACAACAAATGTATCCAAACTGTGTGGATT
	AAAATATATTTTAATTTTTAAAAATGGCATCATAAACACAAGAGTGAAAATCATACTGCCACTGGAG
	ATATTTAAGACAGTACCACTTATATACAGACCATCAACCGTGAGAATTATAGGAGATTTAGCTGAAT
	ACATGCTGCATTCTGAAAGTTTTATGTCATCTTTTCTGAAATCTACCGACTGAAAAACCACTTTCAT
	CTCTAAAAAATAATGGTGGAATTGGCCAGTTAGGATGCCTGATACAAGACCGTCTGCAGTGTTAATC
	CATAAAACTTCCTAGCATGAAGAGTTTCTACCAAGATCTCCACAATACTATGGTCAAATTAACATGT
	GTACTCAGTTGAATGACACACATTATGTCAGATTATGTACTTGCTAATAAGCAATTTTAACAATGCA
	TAACAAATAAACTCTAAGCTAAGCAGAAAATCCACTGAATAAATTCAGCATCTTGGTGGTCGATGGT
	AGATTTTATTGACCTGCATTTCAGAGACAAAGCCTCTTTTTTAAGACTTCTTGTCTCTCTCCAAAGT
	AAGAATGCTGGACAAGTACTAGTGTCTTAGAAGAACGAGTCCTCAAGTTCAGTATTTTATAGTGGTA
	ATTGTCTGGAAAACTAATTTACTTGTGTTAATACAATACGTTTCTACTTTCCCTGATTTTCAAACTG
	GTTCCCTGCATCTTTTTTGCTATATGCAAGGCACATTTTTGCACTATATTAGTGCACCACGATAGGC
	GCTTAACCAGTATTGCCATAGAAACTGCCTCTTTTCATGTGGGATGAAGACATCTGTGCCAAGAGTG
	GCATGAAGACATTTGCAAGTTCTTGTATCCTGAAGAGAGTAAAGTTCAGTTTGGATGGCAGCAAGAT
	GAAATCAGCTATTACACCTGCTGTACACACACTTCCTCATCACTGCAGCCATTGTGAAATTGACAAC
	ATGGCGGTAATTTAAGTGTTGAAGTCCCTAACCCCTTAACCCTCTAAAAGGTGGATTCCTCTAGTTG
	GTTTGTAATTGTTCTTTGAAGGCTGTTTATGACTAGATTTTTATATTTGTTATCTTTGTTAAGAAAA
	AAAAAAGAAAAAGGAACTGGATGTCTTTTTAATTTTGAGCAGATGGAGAAAATAAATAATGTATCAA
	TGACCTTTGTAACTAAAGGAAAAAAAAAAAAAATGTGGATTTTCCTTTCTCTCTGATTTCCCAGTTT
	CAGATTGAATGTCTGTCTTGCAGGCAGTTATTTCAAAATCCATAGTCTTTNGCCTTTCTCACTGGCA
	AAATTTGA
	ORF Start: ATG at 235		ORF Stop: TAA at 4999
	SEQ ID NO: 188	1588 aa	MW at 178042.1 kD
NOV47g,	MGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQTVI
CG51595-01
Protein Sequence	SKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAW
	SECSKTCCSGLQHRTRHVVAPPQFGGSGCFNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQ
	RQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKA
	ADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECP
	EFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANE
	NLLSQLSTHKNXEASKPNDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGF
	KLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCIN
	SDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSCKTTEGKQIRARSILAYAGEE
	GGIRCPNSSALQEVRSCNEHFCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVIC
	VRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSTRKQSRHRVIIQL
	PANCGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCR
	KQDGGQACIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKKKE
	KCKNSHLYPLIETQYCPCDKYNAQFVGNWSDCILPEGKVEVLLGMKVQCDIKECGQGYRYQAMACYD
	QNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGCRPCP
	KLDHVNQAQVYEVVFCHSDCNQYLWVTEPWSICKVTFVNNRENCGECVQTRKVRCMQNTADGPSEHV
	EDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAV
	EKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRNLDCVRSDGKSVDLKYCEALGLEKNWQM
	NTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYR
	WQYGQWSPCQVQEAQCGEGTRTRNISCVVSDCSADDFSKVVDEEFCADIELIIDGNKNNVLEESCSQ
	PCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCYDGQCYE
	YKWNASAWKGSSRTVWCQRSDGINVTGGCLVNSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYTEV
	MSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPDGRLKTWVYG
	VAAGAEVLLIFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDGDADM
	SEQ ID NO: 189	1605 bp
NOV47h,	GGTACCGATATCATCTGTGAGTACTTTGAGCGCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTT
283842727 DNA
Sequence	GCCAGCAAGATTGCATCGTGTCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGG
	GCTCCAGCACCGGACGCGTCATGTGGTGGCGCCCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTG
	ACGGAGTTCCAGGTGTGCCAATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGG
	GGCCCTGGAGCACCTGCTCAATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAA
	TAAAGAACCGGAAAAGGACCCCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCPTATTAAGAAA
	AACAGAAACAGAAACAGGCAGAACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGA
	CCAGAGAGGTTATGTGCATTAACAAGACGGGGAAAGCTGCTGATTTAACCTTTTGCCAGCAAGAGAA
	GCTTCCAATGACCTTCCAGTCCTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCACACTGG
	AGCCCCTGCTCAAAAACATGCCATGACATGCTGTCCCCTGCAGGCACTCGTOTAAGGACACGAACCA
	TCAGGCAGTTTCCCATTGGCAGTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTC
	TCAAGGAGATCGAGTTCTCCCCTGTGCCACGTATCGCTGGAGAACTACAGACTGGACTGAGTGCCGT
	GTGGACCCTTTGCTCAGTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCA
	TCCAGACCCGAGAGGTCTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAA
	CAACAAAGAAGCCTCAAAGCCAATCGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAG
	CTGTGCCACATTCCTTGTCCAACTGAATCTGAAGTTTCACCTTGGTCAGCTTCGGGACCTTGTACTT
	ATGAAAACTGTAATGATCAGCAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATGA
	GCCCACTGCAGCCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAACAG
	CCTCCCTGTTATGACTCGAAAGCGGTGAGACTGGGAGACTCCGAGCCAGATAACGGAAAGGAGTGTG
	GTCCAGGCACCCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGCAGAAGAAGTTGACAGACAGCT
	CTGCAGACATGCCATCTTCCCCATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTCTGCTC
	AGCACATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGA
	TACGAGCACGATCCATTCTGGCCTATGCGGGTCAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTCC
	TTTGCAAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGTCGAC
	ORF Start: at 1		ORF Stop: end of sequence
	SEQ ID NO: 190	535 aa	MW at 59956.1 kD
NOV47h,	GRDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAWSECSKTCGSGLQHRTRHVVAPPQFGGSGCPNL
283842727
Protein Sequence	TEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQVRQARRRGKNREREKDRSKGVKDFEARELIKK
	KRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKAADLSFCQQEKLPMTFQSCVITKECQVSEWSEW
	SPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECFEEEEKEPCLSQGDGVVPCATYGWRTTEWTECR
	VDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANENLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQ
	LCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGFKLRKRRITNEPTGGSGVTGNCPMLLEAIFCEE
	PACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCINSDGEEVDRQLCRDAIFPIPVACDAPCPKDCVL
	STWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEEGGIRCPNSSALQEVRSCNEHPCTVYHWQTVD
	SEQ ID NO: 191	1605 bp
NOV47i,	GGTACCGATATCATCTGTGAGTACTTTGAGCCCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTT
283842704 DNA
Sequnce	GCCAGCAAGATTGCATCGTGTCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGG
	GCTCCAGCACCGGACGCGTCATGTGGTGGCGCCCCCGCAGTTCCGAGGCTCTGGCTGTCCAAACCTG
	ACGGAGTTCCAGGTGTGCCAATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGC
	GGCCCTGGAGCACCTGCTCAATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAA
	TAAAGAACCGGAAAAGGACCGCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAA
	AAGAGAAACAGAAACAGGCAGAACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGA
	CCACAGAGGTTATGTGCATTAACAAGACGGGGAAAGCTGCTGATTTAACCTTTTGCCAGCAAGAGAA
	GCTTCCAATGACCTTCCAGTCCTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGTGG
	AGCCCCTCCTCAAAAACATGCCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACCAACCA
	TCAGGCAGTTTCCCATTGGCAGTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTCTTTGTC
	TCAAGGAGATGGAGTTGTCCCCTGTGCCACCTATGGCTGGAGAACTACAGAGTGGACTGAGTGCCCT
	GTGGACCCTTTGCTCAOTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGOGGCCA
	TCCAGACCCGAGAGGTGTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAA
	GAACAAAGAAGCCTCAAAGCCAATGCACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAG
	CTGTGCCACATTCQTTGTCCAACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTT
	ATGAAAACTGTAATGATCAGCAAGCGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATGA
	GCCCACTGGAGGCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAG
	CCTGCCTGTTATGACTGGAAAGCAGTGAGACTGGGAAACTGCGAGCCAGATAACGGAAAGGAGTGTG
	GTCCAGGCACGCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGACAGCT
	GTGCAGAGATGCCATCTTCCCCATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTGTGCTC
	AGCACATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGA
	TACGAGCACGATCCATTCTGGCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGC
	TTTGCAAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGTCCAC
	ORF Start: at 1		ORF Stop: end of sequence
	SEQ ID NO: 192	535 aa	MW at 59955.1 kD
NOV47i,	GTDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAWSECSKTCGSGLQHRTRHVVAPPQFGGSGCPNL
283842704
Protein	TEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQVRQARRRGKNKEREKDRSKGVKDPEARELIKK
Sequence
	KRNRNRQNRQENKYWKIQIGYQTREVMCINKTGKAADLSFCQQEKLPMTFQSCVITKECQVSEWSEW
	SPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECPEFEEKEPCLSQGDGVVPCATYGWRTTEWTECR
	VDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANENLLSQLSTHKNKEASKPNDLKLCTGPIPNTTQ
	LCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGFKLRKRRITNEPTGCSGVTGNCPHLLEAIPCEE
	PACYDWKAVRLGNCEPDNGKECCPGTQVQEVVCINSDGEEVDRQLCRDAIFPIPVACDAPCPKDCVL
	STWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEEGGIRCPNSSALQEVRSCNEHPCTVYIIWQTVD
	SEQ ID NO: 193	6373 bp
NOV47J,	GACAGAGTGCAGCCTTTTCAGACTCTGTGACACAGTTCCCCTTTTGCAAAAATACTTAGCGAGGATC
CG51595-01
DNA Sequence	ATTACTTTCCAACAGTCGTCTCCAGAGACCTACTTTGTAACACCGCAGGGAAGTTAATGTACTAGGT
	CTTGAAAGGTCTTTCTGGAATGTGCAGTAACTTGTAGTTTTCTTCTAGTAGCACTGCTAATTTTTGT
	GTTATAATTTTTGTAGGTCCATGGGGCCGATGTATGGGAGATGAATGTGGTCCCGGAGGCATCCAAA
	CGAGGGCTGTGTGGTGTGCTCATGTGGAGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGA
	GAGACCCAATAACCAGCAGAATTGTTTCAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGA
	CTGCGACCTTCGAATCAGTGTCAGCCCGTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTA
	AGGGGGAAGAAGGTATTCACGTGAGGGAGATAGCGTGCATCCAGAAAGACAAAGACATTCCTGCGGA
	GGATATCATCTGTGACTACTTTGAGCCCAAGCCTCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAG
	CAAGATTGCATCGTGTCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCC
	AGCACCGGACGCGTCATCTGGTGGCGCCCCCGCAGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGA
	GTTCCAGGTGTGCCAATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCC
	TGGAGCACCTGCTCAATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAG
	AACGGGAAAAGGACCGCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAG
	AAACAGAAACAGGCAGAACAGACAAGAGAACAAATATTGGGACATCCAGATTGGATATCAGACCAGA
	GAGGTTATGTGCATTAACAAGACGGGGAAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTC
	CAATGACCTTCCAGTCCTGTGTGATCACCAAAGAGTGCCAGGTTTCCGAGTGGTCAGAGTGGAGCCC
	CTGCTCAAAAACATGCCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGG
	CAGTTTCCCATTGGCAGTGAAAAGCAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAG
	GAGATGGAGTTGTCCCCTGTGCCACGTATGGCTGGAGAACTACAGAGTGGACTGAGTGCCGTGTGGA
	CCCTTTGCTCAGTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGCGCATCCAG
	ACCCGAGAGGTGTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAAGAACA
	AAGAAGCCTCAAAGCCAATGGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAGCTGTG
	CCACATTCCTTGTCCAACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTTATGAA
	AACTGTAATGATCAGCAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCCCATTACCAATGACCCCA
	CTGGAGGCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAGAGCCTGC
	CTGTTATGACTGGAAAGCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGGAGTGTGGTCCA
	GGCACCCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGACAGCTGTGCA
	GAGATGCCATCTTCCCCATCCCTGTGGCCTGTGATGCCCCATGCCCGAAAGACTGTGTGCTCAGCAC
	ATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGAAACAGATACGA
	GCACGATCCATTCTGGCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATAGCAGTGCTTTGC
	AAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTGGTCCCTGGGGCCA
	GTGCATTGAGGACACCTCAGTATCGTCCTTCAACACAACTACGACTTGGAATGGGGAGGCCTCCTGC
	TCTGTCGGCATGCAGACAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCCAAGTGGGACCCAAAA
	AATGTCCTGAAAGCCTTCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTTGTAAGAAGGACTGTAT
	TGTGACCCCATATAGTGACTGGACATCATGCCCCTCTTCGTGTAAAGAAGGGGACTCCAGTATCAGG
	AAGCAGTCTAGGCATCGGGTCATCATTCAGCTGCCAGCCAACGGGGGCCGAGACTGCACAGATCCCC
	TCTATGAAGAGAAGGCCTGTGAGGCACCTCAAGCGTGCCAAAGCTACAGGTGGAAGACTCACAAATG
	GCGCAGATGCCAATTAGTCCCTTGGAGCGTGCAACAAGACAGCCCTGGAGCACAGGAAGGCTGTGGG
	CCTGGGCGACAGGCAAGAGCCATTACTTGTCGCAAGCAAGATGGAGGACAGGCTGGAATCCATGAGT
	GCCTACAGTATGCAGGCCCTGTGCCAGCCCTTACCCAGGCCTCCCAGATCCCCTGCCAGGATGACTC
	TCAATTGACCAGCTGGTCCAAGTTTTCTTCATGCAATGGAGACTGTGGTGCAGTTAGGACCAGAAAG
	CGCACTCTTGTTGGAAAAAGTAAAAAGAAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTG
	AGACTCAGTATTGTCCTTGTGACAAATATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTT
	ACCAGAGGGAAAAGTGGAAGTGTTGCTGGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAA
	GGATATCGTTACCAAGCAATGGCATGCTACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTA
	ACAGCCATGGTTACATTGAGGAGGCCTGCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTG
	GTCCAACTGGTCGCGCTGCAGCAAGTCCTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGT
	GAAAAACCATATAATGGAGGAAGGCCTTGCCCCAAACTGGACCATGTCAACCAGGCACAGGTGTATG
	AGGTTGTCCCATGCCACAGTGACTGCAACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAA
	GGTGACCTTTGTGAATATGCGGGAGAACTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATG
	CAGAATACAGCAGATGGCCCTTCTGAACATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCC
	TGGGCTCTAGAGTGTGCAAATTACCATGCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGAC
	CCAATGTGTTTTGCCTTGCAATCAAAGCAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCA
	GCTGATGAAGGAAGATCTTGCCCTAATGCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCT
	ACCACTATGATTATAATGTAACAGACTGGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAA
	TGGAATAAAAACAAGGATGTTGGATTGTGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGT
	GAAGCGCTTGGCTTGGAGAAGAACTGGCAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACT
	GTCAGCTTTCTGATTGGTCTCCTTGGTCAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGAT
	CCGAAGACGAACAGTGACCCAGCCCTTTCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAG
	TCCAAACCCTGCCCAGTGAAGCCTTGTTATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGC
	AGGAGGCCCAGTGTGGAGAAGGGACCAGAACAAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGC
	TGATGATTTCAGCAAAGTGGTGGATGAGGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAAT
	AAAAATATGGTTCTGGAGGAATCCTGCAGCCAGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGT
	CTTCCTGGAGCCTGTGTCAGCTGACCTGTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGT
	CAGATCCAGACCGGTGATTATACAAGAACTAGAGAATCACCATCTGTGCCCAGAGCAGATGTTAGAA
	ACAAAATCATGTTATGATGGACAGTGCTATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTT
	CCCGAACAGTGTGGTGTCAAAGGTCAGATGGTATAAATGTAACAGGGGGCTGCTTGGTGATGAGCCA
	GCCTGATGCCGACAGGTCTTGTAACCCACCGTGTAGTCAACCCCACTCGTACTGTAGCGAGACAAAA
	ACATGCCATTGTGAAGAAGGGTACACTGAAGTCATGTCTTCTAACAGCACCCTTGAGCAATGCACAC
	TTATCCCCGTGGTGGTATTACCCACCATGGAGGACAAAAGAGGAGATGTGAAAACCAGTCGGGCTGT
	ACATCCAACCCAACCCTCCAGTAACCCAGCAGGACGGGGAAGGACCTGGTTTCTACAGCCATTTGGG
	CCAGATGGGAGACTAAAGACCTGGGTTTACGGTGTAGCAGCTGGGGCATTTGTGTTACTCATCTTTA
	TTGTCTCCATGATTTATCTAGCTTGCAAAAAGCCAAAGAAACCCCAAAGAAGGCAAAACAACCGACT
	GAAACCTTTAACCTTAGCCTATGATGGAGATGCCGACATGTAACATATAACTTTTCCTGGCAACAAC
	CAGTTTCGGCTTTCTGACTTCATAGATGTCCAGAGGCCACAACAAATGTATCCAAACTGTGTGGATT
	AAAATATATTTTAATTTTTAAAAATGGCATCATAAAGACAAGAGTGAAAATCATACTGCCACTGGAG
	ATATTTAAGACAGTACCACTTATATACAGACCATCAACCGTGAGAATTATAGGAGATTTAGCTGAAT
	ACATGCTGCATTCTGAAAGTTTTATGTCATCTTTTCTGAAATCTACCGACTGAAAAACCACTTTCAT
	CTCTAAAAAATAATGGTGGAATTGGCCAGTTAGGATGCCTGATACAAGACCGTCTGCAGTGTTAATC
	CATAAAACTTCCTAGCATGAAGAGTTTCTACCAAGATCTCCACAATACTATGGTCAAATTAACATGT
	GTACTCAGTTGAATGACACACATTATGTCAGATTATGTACTTGCTAATAAGCAATTTTAACAATGCA
	TAACAAATAAACTCTAAGCTAAGCAGAAAATCCACTGAATAAATTCAGCATCTTGGTGGTCGATGGT
	AGATTTTATTGACCTGCATTTCAGAGACAAAGCCTCTTTTTTAAGACTTCTTGTCTCTCTCCAAAGT
	AAGAATGCTGGACAAGTACTAGTGTCTTAGAAGAACGAGTCCTCAAGTTCAGTATTTTATAGTGGTA
	ATTGTCTGGAAAACTAATTTACTTGTGTTAATACAATACGTTTCTACTTTCCCTGATTTTCAAACTG
	GTTGCCTGCATCTTTTTTGCTATATGCAAGGCACATTTTTGCACTATATTAGTGCAGCACGATAGGC
	GCTTAACCAGTATTGCCATAGAAACTGCCTCTTTTCATGTGGGATGAAGACATCTGTGCCAAGAGTG
	GCATGAAGACATTTGCAAGTTCTTGTATCCTGAAGAGAGTAAAGTTCAGTTTGGATGGCAGCAAGAT
	GAAATCAGCTATTACACCTGCTGTACACACACTTCCTCATCACTGCAGCCATTGTGAAATTGACAAC
	ATGGCGGTAATTTAAGTGTTGAAGTCCCTAACCCCTTAACCCTCTAAAAGGTGGATTCCTCTAGTTG
	GTTTGTAATTGTTCTTTGAAGGCTGTTTATGACTAGATTTTTATATTTGTTATCTTTGTTAAGAAAA
	AAAAAAAAAAAAGGAACTGGATGTCTTTTTAATTTTGAGCAGATGGAGAAAATAAATAATGTATCAA
	TGACCTTTGTAACTAAAGGAAAAAAAAAAAAAATGTGGATTTTCCTTTCTCTCTGATTTCCCAGTTT
	CAGATTGAATGTCTGTCTTGCAGGCAGTTATTTCAAAATCCATAGTCTTTNGCCTTTCTCACTGGCA
	AAATTTGA
	ORF Start: ATG at 235		ORF Stop: TAA at 4999
	SEQ ID NO: 194	1588 aa	MW at 178042.1 kD
NOV47j,	MGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPVI
CG51595-01
Protein	SKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDITCEYFEPKPLLEQACLIPCQQDCIVSEFSAW
Sequence
	SECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQ
	VRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKA
	ADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECP
	EFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANE
	NLLSOLSTHKNKEASKPMDLKLCTGPIPNTTOLCHIPCPTECEVSPWSAWGPCTYENCNCOOGKKGF
	KLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGDCEPDNGKECGPGTQVQEVVCIN
	SDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEE
	GGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVIC
	VRVNVGQVGPKKCPESLRFETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQL
	PANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCR
	KQDGGQAGIHECLQYAGPVPALTQACQIFCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKKKE
	KCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYQAMACYD
	QNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNCGRPCP
	KLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNNRENCGEGVQTRKVRCMQNTADGPSEHV
	EDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAV
	EKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLKTCEALGLEKNWQM
	NTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYR
	WQYGQWSPCQVQEAQCGEGTRTRNISCVVSDCSADDFSKVVDEEFCADIELIIDGNKNMVLEESCSQ
	PCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCYDGQCYE
	YKWMASAWKGSSRTVWCQRSDGINVTGGCLVMSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYTEV
	MSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPDGRLKTWVYG
	VAAGAFVLLIFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDGDADM
	SEQ ID NO: 195	1732 bp
NOV47k,	CACCTCGCGAGGAGACTGTGGTGCAGTTAGGACCAGAAAGCGCACTCTTGTTGGAAAAAGTAAAAAG
310658551 DNA
Sequence	AAGGAAAAATGTAAAAATTCCCATTTGTATCCCCTGATTGAGACTCAGTATTGTCCTTGTGACAAAT
	ATAATGCACAACCTGTGGGGAACTGGTCAGACTGTATTTTACCAGAGGGAAAAGTGGAAGTGTTGCT
	GGGAATGAAAGTACAAGGAGACATCAAGGAATGCGGACAAGGATATCGTTACCAAGCAATGGCATGC
	TACGATCAAAATGGCAGGCTTGTGGAAACATCTAGATGTAACAGCCATGGTTACATTGAGGAGGCCT
	GCATCATCCCCTGCCCCTCAGACTGCAAGCTCAGTGAGTGGTCCAACTGGTCGCGCTGCAGCAAGTC
	CTGTGGGAGTGGTGTGAAGGTTCGTTCTAAATGGCTGCGTGAAAAACCATATAATGGAGGAAGGCCT
	TGCCCCAAACTGGACCATGTCAACCAGCCACAGGTCTATGAGGTTGTCCCATGCCACAGTGACTGCA
	ACCAGTACCTATGGGTCACAGAGCCCTGGAGCATCTGCAAGGTGACCTTTGTGAATATGCGGGAGAA
	CTGTGGAGAGGGCGTGCAAACCCGAAAAGTGAGATGCATGCAGAATACAGCAGATGGCCCTTCTGAA
	CATGTAGAGGATTACCTCTGTGACCCAGAAGAGATGCCCCTGGGCTCTAGAGTGTGCAAATTACCAT
	GCCCTGAGGACTGTGTGATATCTGAATGGGGTCCATGGACCCAATGTGTTTTGCCTTGCAATCAAAG
	CAGTTTCCGGCAAAGGTCAGCTGATCCCATCAGACAACCAGCTGATGAAGGAAGATCTTGCCCTAAT
	GCTGTTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCTACCACTATGATTATAATGTAACAGACT
	GGAGTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAATGGAATAAAAACAAGGATGTTGGATTG
	TGTTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGTGAAGCGCTTGGCTTGGAGAAGAACTGG
	CAGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACTGTCAGCTTTCTGATTGGTCTCCTTGGT
	CAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGATCCGAAGACGAACAGTGACCCAGCCCTT
	TCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAGTCCAAACCCTGCCCAGTGAAGCCTTGT
	TATCGGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGCAGGAGGCCCAGTGTGGAGAAGGGACCA
	GAACAAGGAACATTTCTTGTCTAGTAAGTCATGGCTCAGCTGATGATTTCAGCAAAGTGGTGGATGA
	GGAATTCTGTGCTGACATTGAACTCATTATAGATGGTAATAAAAATATGGTTCTGGAGGAATCCTGC
	AGCCAGCCTTGCCCAGGTGACTGTTATTTGAAGGACTGGTCTTCCTGGAGCCTGTGTCAGCTGACCT
	GTGTGAATGGTGAGGATCTAGGCTTTGGTGGAATACAGGTCAGATCCAGACCGGTGATTATACAAGA
	ACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAAACAAAATCATGTTATGATGGACAGTGC
	TATGAATATAAATGGATGGCCAGTGCTTCGAAGGGCTCTTCCCGAACAGTCGACGGC
	ORF Start: at 2		ORF Stop: end of sequence
	SEQ ID NO: 196	577 aa	MW at 65124.1 kD
NOV47k,	TSRGDCGAVRTRKRTLVGKSKKKEKCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLL
310658551
Protein Sequence	GMKVQGDIKECGQGYRYQANACYDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKS
	CGSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMREN
	CGEGVQTRKVRCMQNTADGPSEHVEDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQS
	VRSDGKSVDLKYCEALGLEKNWQMNTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPF
	QGDGRPCPSLMDQSKPCPVKPCYRWQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDE
	EFCADIELIIDGNKNMVLEESCSQPCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQE
	LENQHLCPEQMLETKSCYDGQCYEYKWMASAWKGSSRTVDG
	SEQ ID NO: 197	921 bp
N0V47l,	ATGGGAGATGAATGTGGTCCCGGAGGCATCCAAACGAGGGCTGTGTGGTGTGCTCATGTGGAGGGAT
CG 51595-02
DNA Sequence	GGACTACACTGCATACTAACTGTAAGCAGGCCGAGAGACCCAATAACCAGCAGAATTGTTTCAAAGT
	TTGCGATTGGCACAAAGAGTTGTACGACTGGAGACTGGGACCTTGGAATCAGTGTCAGCCCGTGATT
	TCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTAAGGGGGAAGAAGGTATTCAGGTGAGGGAGATAG
	CGTGCATCCAGAAAGACAAAGACATTCCTGCGGAGGATATCATCTGTGAGTACTTTGAGCCCAAGCC
	TCTCCTGGAGCAGGCTTGCCTCATTCCTTGCCAGCAAGATTGCATCGTGTCTGAATTTTCTGCCTGG
	TCCGAATCCTCCAAGACCTGCGGCAGCGGGCTCCAGCACCGGACGCGTCATCTGGTGGCGCCCCCGC
	AGTTCGGAGGCTCTGGCTGTCCAAACCTGACGGAGTTCCAGGTGTGCCAATCCAGTCCATGCGAGGC
	CGAGGAGCTCAGGTACAGCCTGCATGTGGGGCCCTGGAGCACCTGCTCAATGCCCCACTCCCGACAA
	GTAAGACAAGCAAGGAGACGCGGGAAGAATAAAGAACGGGAAAAGGACCGCAGCAAAGGAGTAAAGG
	ATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAGAAACAGAAACAGGCAGAACAGACAAGAGAACAA
	ATATTGGGACATCCAGATTGGATATCAGACCAGAGAGGTTATGTGCATTAACAAGACGGGGAAAGCT
	GCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTCCAATGACCTTCCAGTCCTGTGTGATCACCAAAG
	AGTGCCAGGTTTCCGAGTGGTCAGAGTGGAGCCCCTGCTCAAAAACATGC
	ORF Start: ATG at 1		ORF Stop: end of sequence
	SEQ ID NO: 198	307 aa	MW at 35305.8 kD
NOV47l,	MGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELTDWRLGPWNQCQPVI
CG51595-02
Protein	SKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLTPCQQDCIVSEFSAW
Sequence
	SECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQ
	VRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKA
	ADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTC
	SEQ ID NO: 199	4810 bp
NOV47m,	GTCCATGGGGCCGATGTATGGGAGATGAATGTGGTCCCGGAGGCATCCAAACGAGGGCTGTGTGGT
CG51595-05
DNA Sequence	GTGCTCATGTGGAGGGATGGACTACACTGCATACTAACTGTAAGCAGGCCGAGAGACCCAATAACC
	AGCAGAATTGTTTCAAAGTTTGCGATTGGCACAAAGAGTTGTACGACTGGAGACTGGGACCTTGGA
	ATCAGTGTCAGCCCGTGATTTCAAAAAGCCTAGAGAAACCTCTTGAGTGCATTAAGGGGGAAGAAG
	GTATTCAGGTGAGGGAGATAGCGTGCATCCAGAAAGAGAAAGACATTCCTGCGGAGGATATCATCT
	GTGAGTACTTTGAGCCCAAGCCTCTCCTGGACCACGCTTGCCTCATTCCTTGCCACCAAGATTGCA
	TCGTGTCTGAATTTTCTGCCTGGTCCGAATGCTCCAAGACCTGCGGCAGCGGGCTCCAGCACCGGA
	CGCGTCATGTGGTGGCGCCCCCGCAGTTCGGAGGCTCTCGCTGTCCAAACCTGACGGAGTTCCAGG
	TGTGCCAATCCAGTCCATGCGAGGCCGAGGAGCTCAGGTACAGCCTGCATCTGGGGCCCTGGAGCA
	CCTGCTCAATGCCCCACTCCCGACAAGTAAGACAAGCAAGGAGACGCGGGAAGAATAAAGAACGGG
	AAAAGGACCGCAGCAAAGGAGTAAAGGATCCAGAAGCCCGCGAGCTTATTAAGAAAAAGAGAAACA
	GAAACAGGCAGAACAGACAAGAGAACAAATATTCCGACATCCAGATTGGATATCAGACCAGAGAGG
	TTATGTGCATTAACAAGACGGGGAAAGCTGCTGATTTAAGCTTTTGCCAGCAAGAGAAGCTTCCAA
	TGACCTTCCAGTCCTGTGTGATCACCAAACAGTCCCAGGTTTCCGAGTGGTCAGACTGGACCCCCT
	GCTCAAAAACATGCCATGACATGGTGTCCCCTGCAGGCACTCGTGTAAGGACACGAACCATCAGGC
	AGTTTCCCATTGGCAGTGAAAAGGAGTGTCCAGAATTTGAAGAAAAAGAACCCTGTTTGTCTCAAG
	GAGATGGAGTTGTCCCCTGTGCCACGTATGGCTGGAGAACTACAGAGTGGACTGAGTGCCGTGTGG
	ACCCTTTGCTCAGTCAGCAGGACAAGAGGCGCGGCAACCAGACGGCCCTCTGTGGAGGGGGCATCC
	AGACCCGAGAGGTGTACTGCGTGCAGGCCAACGAAAACCTCCTCTCACAATTAAGTACCCACAAGA
	ACAAAGAAGCCTCAAAGCCAATGGACTTAAAATTATGCACTGGACCTATCCCTAATACTACACAGC
	TGTGCCACATTCCTTGTCCAACTGAATGTGAAGTTTCACCTTGGTCAGCTTGGGGACCTTGTACTT
	ATGAAAACTGTAATGATCAGCAAGGGAAAAAAGGCTTCAAACTGAGGAAGCGGCGCATTACCAATG
	AGCCCACTGGAGGCTCTGGGGTAACCGGAAACTGCCCTCACTTACTGGAAGCCATTCCCTGTGAAG
	AGCCTGCCTGTTATGACTGGAAAGCGGTGAGACTGGGAGACTGCGAGCCAGATAACGGAAAGGAGT
	GTGGTCCAGGCACGCAAGTTCAAGAGGTTGTGTGCATCAACAGTGATGGAGAAGAAGTTGACAGAC
	AGCTGTGCAGAGATGCCATCTTCCCCATCCCTGTGGCCTCTGATGCCCCATGCCCGAAAGACTGTG
	TGCTCAGCACATGGTCTACGTGGTCCTCCTGCTCACACACCTGCTCAGGGAAAACGACAGAAGGGA
	AACAGATACGAGCACGATCCATTCTGGCCTATGCGGGTGAAGAAGGTGGAATTCGCTGTCCAAATA
	GCAGTGCTTTGCAAGAAGTACGAAGCTGTAATGAGCATCCTTGCACAGTGTACCACTGGCAAACTG
	GTCCCTGGGGCCAGTGCATTGAGGACACCTCAGTATCGTCCTTCAACACAACTACGACTTGGAATG
	GGGAGGCCTCCTGCTCTGTCGGCATGCAGACAAGAAAAGTCATCTGTGTGCGAGTCAATGTGGGCC
	AAGTGGGACCCAAAAAATGTCCTGAAAGCCTTCGACCTGAAACTGTAAGGCCTTGTCTGCTTCCTT
	GTAAGAAGGACTGTATTGTGACCCCATATAGTGACTCGACATCATGCCCCTCTTCGTGTAAAGAAG
	GGGACTCCAGTATCAGGAAGCAGTCTAGGCATCGGGTCATCATTCAGCTGCCAGCCAACGGGGGCC
	GAGACTGCACAGATCCCCTCTATGAAGAGAAGGCCTGTGAGGCACCTCAAGCGTGCCAAAGCTACA
	GGTGGAAGACTCACAAATGGCGCAGATGCCAATTAGTCCCTTGGAGCGTGCAACAAGACAGCCCTG
	GAGCACAGGAAGGCTGTGGGCCTGGGCGACAGGCAAGAGCCATTACTTGTCGCAAGCAAGATGGAG
	GACAGGCTGGAATCCATGAGTGCCTACAGTATGCAGGCCCTGTGCCAGCCCTTACCCAGGCCTGCC
	AGATCCCCTGCCAGGATGACTGTCAATTGACCAGCTGGTCCAAGTTTTCTTCATGCAATGGAGACT
	GTGGTGCAGTTAGGACCAGAAAGCGCACTCTTGTTGGAAAAAGTAAAAAGAAGGAAAAATGTAAAA
	ATTCCCATTTGTATCCCCTGATTGAGACTCAGTATTGTCCTTGTGACAAATATAATGCACAACCTG
	TGGGGAACTGGTCAGACTGTATTTTACCAGAGGGAAAAGTGGAAGTGTTGCTGGGAATGAAAGTAC
	AAGGAGACATCAAGGAATGCGGACAAGGATATCGTTACCAAGCAATGGCATGCTACGATCAAAATG
	GCAGGCTTGTGGAAACATCTAGATGTAACAGCCATGGTTACATTGAGGAGGCCTGCATCATCCCCT
	GCCCCTCAGACTGCAAGCTCAGTGAGTGGTCCAACTGGTCGCGCTGCAGCAAGTCCTGTGGGAGTG
	GTGTGAAGGTTCGTTCTAAATGGCTGCGTGAAAAACCATATAATGGAGGAAGGCCTTGCCCCAAAC
	TGCACCATGTCAACCAGGCACAGGTGTATGAGGTTGTCCCATGCCACAGTGACTGCAACCAGTACC
	TATGGGTCACAGAGCCCTGGAGCATCTGCAAGGTGACCTTTGTGAATATGCGGGAGAACTGTGGAG
	AGGGCGTGCAAACCCGAAAAGTGAGATGCATGCAGAATACAGCAGATGGCCCTTCTGAACATGTAG
	AGGATTACCTCTGTGACCCAGAAGAGATGCCCCTGGGCTCTAGAGTGTGCAAATTACCATGCCCTG
	AGGACTGTCTGATATCTGAATGGGGTCCATGGACCCAATGTGTTTTGCCTTGCAATCAAAGCAGTT
	TCCGGCAAAGGTCAGCTGATCCCATCAGACAACCAGCTGATGAAGGAAGATCTTGCCCTAATGCTG
	TTGAGAAAGAACCCTGTAACCTGAACAAAAACTGCTACCACTATGATTATAATGTAACAGACTGGA
	GTACATGTCAGCTGAGTGAGAAGGCAGTTTGTGGAAATGGAATAAAAACAAGGATGTTGGATTGTG
	TTCGAAGTGATGGCAAGTCAGTTGACCTGAAATATTGTGAAGCGCTTGGCTTGGAGAAGAACTCGC
	AGATGAACACGTCCTGCATGGTGGAATGCCCTGTGAACTGTCAGCTTTCTGATTGGTCTCCTTGCT
	CAGAATGTTCTCAAACATGTGGCCTCACAGGAAAAATGATCCGAAGACCAACAGTGACCCAGCCCT
	TTCAAGGTGATGGAAGACCATGCCCTTCCCTGATGGACCAGTCCAAACCCTGCCCAGTGAACCCTT
	GTTATCCGTGGCAATATGGCCAGTGGTCTCCATGCCAAGTGCAGGAGGCCCAGTGTGGAGAAGGGA
	CCAGAACAAGGAACATTTCTTGTGTAGTAAGTGATGGGTCAGCTGATGATTTCAGCAAAGTCGTGG
	ATCACCAATTCTCTGCTGACATTGAACTCATTATAGATGGTAATAAAAATATGGTTCTGGAGGAAT
	CCTGCAGCCAGCCTTGCCCAGCTGACTGTTATTTGAAGGACTGGTCTTCCTGGAGCCTGTGTCAGC
	TGACCTGTGTGAATCGTGAGGATCTAGGCTTTGGTGGAATACAGGTCAGATCCAGACCGGTGATTA
	TACAAGAACTAGAGAATCAGCATCTGTGCCCAGAGCAGATGTTAGAAACAAAATCATGTTATGATG
	CACAGTGCTATGAATATAAATGGATGGCCAGTGCTTGGAAGGGCTCTTCCCGAACAGTGTGCTGTC
	AAAGGTCAGATGGTATAAATGTAACAGGGGGCTGCTTGGTGATGAGCCAGCCTGATGCCGACAGGT
	CTTGTAACCCACCGTGTAGTCAACCCCACTCGTACTCTAGCGAGACAAAAACATGCCATTGTGAAG
	AAGGGTACACTGAAGTCATGTCTTCTAACAGCACCCTTGAGCAATGCACACTTATCCCCGTGGTGG
	TATTACCCACCATGGAGGACAAAAGAGGAGATGTGAAAACCAGTCGGOCTGTACATCCAACCCAAC
	CCTCCAGTAACCCAGCAGGACGGGGAAGGACCTGGTTTCTACAGCCATTTGCGCCAGATCGGAGAC
	TAAAGACCTGGGTTTACGGTGTAGCAGCTGCGGCATTTGTGTTACTCATCTTTATTCTCTCCATGA
	TTTATCTAGCTTGCAAAAAGCCAAAGAAACCCCAAAGAAGGCAAAACAACCGACTGAAACCTTTAA
	CCTTAGCCTATGATGGAGATGCCGACATGTAACATATAACTTTTCCTGGCAACAACCA
	ORF Start: ATG at 18		ORF Stop: TAA at 4782
	SEQ ID NO: 200	11588 aa	MW at 178042.1 kD
NOV47m,	MGDECGPGGIQTRAVWCAHVAGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPV
CG51595-05
Protein Sequence	ISKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFS
	AWSECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPH
	SRQVRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTEEVMCINK
	TGKAADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGS
	EKECPEFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGTQTREVY
	CVQANENLLSQLSTHKNKEASKPHDLKLCTGPTPNTTQLCHIPCPTECEVSPWSAWGPCTYENCND
	QQGKKGFKLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGDCEPDNGKECCPGTQ
	VQEVVCINSDGEEVDRQLCRDAIFPTPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRAR
	SILAYAGEEGGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCS
	VCMQTRKVICVRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCTVTPYSDWTSCPSSCKEGDSSIR
	KQSRHRVIIQLPANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGC
	GPGRQARAITCRKQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRT
	RKRTLVCKSKKKEKCKNSHLYPLIETQYCPCDKYNAQPVCNWSDCILPEGKVEVLLGMKVQGDIKE
	CGQGYRYQAMACYDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRS
	KWLREKPYNGGRPCPKLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNNRENCGEGVQTR
	KVRCMQNTADGPSEHVEDYLCDPEEMPLGSRVCKLPCPEDCVISEGWPWTQCVLPCNQSSFRQRSA
	DPIRQPADEGRSCPNAVEKEPCNLNXNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGK
	SVDLKYCEALGLEKNWQMNTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGR
	PCPSLMDQSKPCPVKPCYRWQYGQWSPCQVQEAQCGEGTRTRNTSCVVSDGSADDFSKVVDEEFCA
	DIELIIDGNKNMVLEESCSQPCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELEN
	QHLCPEQMLETKSCYDGQCYEYKWMASAWKGSSRTVWCQRSDGINVTGGCLVMSQPDADRSCNPPC
	SQPHSYCSETKTCHCEEGYTEVMSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPA
	GRGRTWELQPFGPDGRLKTWVYGVAAGAFVLLIFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDG
	DADM

[0619] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 47B.

TABLE 47B
Comparison of NOV47a against NOV47b through NOV47m.
	NOV47a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV47b	299 . . . 765	438/467 (93%)
	1 . . . 467	439/467 (93%)
NOV47c	849 . . . 1419	562/571 (98%)
	1 . . . 571	562/571 (98%)
NOV47d	1 . . . 1531	1480/1531 (96%)
	1 . . . 1531	1480/1531 (96%)
NOV47e	1 . . . 1437	1384/1437 (96%)
	1 . . . 1437	1384/1437 (96%)
NOV47f	1 . . . 1531	1477/1531 (96%)
	3 . . . 1533	1479/1531 (96%)
NOV47g	1 . . . 1588	1537/1588 (96%)
	1 . . . 1588	1537/1588 (96%)
NOV47h	102 . . . 632	489/531 (92%)
	3 . . . 533	489/531 (92%)
NOV47i	102 . . . 632	488/531 (91%)
	3 . . . 533	489/531 (91%)
NOV47j	1 . . . 1588	1537/1588 (96%)
	1 . . . 1588	1537/1588 (96%)
NOV47k	851 . . . 1422	563/572 (98%)
	4 . . . 575	563/572 (98%)
NOV47l	1 . . . 307	292/307 (95%)
	1 . . . 307	292/307 (95%)
NOV47m	1 . . . 1588	1537/1588 (96%)
	1 . . . 1588	1537/1588 (96%)

[0620] Further analysis of the NOV47a protein yielded the following properties shown in Table 47C.

TABLE 47C
Protein Sequence Properties NOV47a
PSort analysis:   0.7000 probability located in plasma membrane; 0.3500 probability located in
                  nucleus; 0.3000 probability located in microbody (peroxisome); 0.2000
                  probability located in endoplasmic reticulum (membrane)
SignalP analysis: No Known Signal Sequence Predicted

[0621] A search of the NOV47a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 47D.

TABLE 47D
Geneseq Results for NOV47a
		NOV47a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAB20155	Secreted protein SECP1 -	1 . . . 1588	1588/1588 (100%)	0.0
	Homo sapiens, 1588 aa.	1 . . . 1588	1588/1588 (100%)
	[WO200105971-A2,
	Jan. 25, 2001]
AAM39295	Human polypeptide SEQ ID	1 . . . 1588	1587/1588 (99%)	0.0
	NO 2440 - Homo sapiens,	1 . . . 1588	1588/1588 (99%)
	1588 aa.
	[WO200153312-A1,
	Jul. 26, 2001]
AAM41081	Human polypeptide SEQ ID	48 . . . 1588	1540/1541 (99%)	0.0
	NO 6012 - Homo sapiens,	11 . . . 1551	1540/1541 (99%)
	1551 aa.
	[WO200153312-A1,
	Jul. 26, 2001]
AA342496	Human ORFX ORF2260	1 . . . 614	605/614 (98%)	0.0
	polypeptide sequence SEQ	6 . . . 617	607/614 (98%)
	ID NO:4520 - Homo
	sapiens, 617 aa.
	[WO200058473-A2,
	Oct. 5, 2000]
AAM28984	Peptide #3021 encoded by	1 . . . 271	271/271 (100%)	e−169
	probe for measuring	6 . . . 276	271/271 (100%)
	placental gene expression -
	Homo sapiens, 277 aa.
	[WO200157272-A2,
	Aug. 9, 2001]

[0622] In a BLAST search of public sequence datbases, the NOV47a protein was found to have homology to the proteins shown in the BLASTP data in Table 47E.

TABLE 47E
Public BLASTP Results for NOV47a
		NOV47a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
CAC32422	Sequence 1 from Patent	1 . . . 1588	1588/1588 (100%)	0.0
	WO0105971 - Homo	1 . . . 1588	1588/1588 (100%)
	sapiens (Human), 1588 aa.
BAA76804	KIAA0960 protein - Homo	87 . . . 1588	1502/1502 (100%)	0.0
	sapiens (Human), 1502 aa	1 . . . 1502	1502/1502 (100%)
	(fragment).
Q9UPZ6	KIAA0960 protein - Homo	299 . . . 1588	1290/1290 (100%)	0.0
	sapiens (Human), 1290 aa	1 . . . 1290	1290/1290 (100%)
	(fragment).
Q9C0I4	KIAA1679 protein - Homo	22 . . . 1588	790/1574 (50%)	0.0
	sapiens (Human), 1536 aa	1 . . . 1536	1044/1574 (66%)
	(fragment).
O43384	Hypothetical protein	954 . . . 1401	446/448 (99%)	0.0
	GS164B05.1 in	1 . . . 446	446/448 (99%)
	chromosome 7 - Homo
	sapiens (Human), 446 aa
	(fragment).

[0623] PFam analysis predicts that the NOV47a protein contains the domains shown in the Table 47F.

TABLE 47F
Domain Analysis of NOV47a
		Identities/
		Similarities
		for the Matched	Expect
Pfam Domain	NOV47a Match Region	Region	Value
tsp_1	129 . . . 177	20/54 (37%)	1.8e−13
		39/54 (72%)
tsp_1	295 . . . 353	23/63 (37%)	0.0015
		45/63 (71%)
tsp_1	447 . . . 504	21/62 (34%)	0.1
		39/62 (63%)
tsp_1	569 . . . 625	19/60 (32%)	0.0012
		41/60 (68%)
tsp_1	706 . . . 761	17/59 (29%)	0.0014
		40/59 (68%)
tsp_1	841 . . . 889	17/57 (30%)	0.022
		34/57 (60%)
tsp_1	970 . . . 1021	18/55 (33%)	1.1e−05
		40/55 (73%)
tsp_1	1030 . . . 1093	14/69 (20%)	0.79
		46/69 (67%)
tsp_1	1100 . . . 1150	15/55 (27%)	0.039
		36/55 (65%)
tsp_1	1221 . . . 1271	20/55 (36%)	6.9e−11
		39/55 (71%)
tsp_1	1349 . . . 1405	17/62 (27%)	0.29
		34/62 (55%)

Example 48

[0624] The NOV48 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 48A.

TABLE 48A
NOV48 Sequence Analysis
	SEQ ID NO: 201	3149 bp
NOV48a,	CTAAAGTTTTTTTCTTTGAATGACAGAACTACAGCATAATGCGTGGCTTCAACCTGCTCCTCTTCTG
CG57209-01
DNA Sequence	GGGATGTTGTGTTATGCACAGCTGGGAAGGGCACATAAGACCCACACGGAAACCAAACACAAAGGGT
	AATAACTGTAGAGACAGTACCTTGTGCCCAGCTTATGCCACCTGCACCAATACGGTGGACAGTTACT
	ATTGCACTTGCAAACAAGGCTTCCTGTCCAGCAATGGGCAAAATCACTTCAAGGATCCAGGAGTGCG
	ATGCAAAGATATTGATGAATGTTCTCAAAGCCCCCAGCCCTGTGGTCCTAACTCATCCTGCAAAAAC
	CTGTCAGGGAGGTACAAGTGCAGCTGTTTAGATGGTTTCTCTTCTCCCACTGGAAATGACTGGGTCC
	CAGGAAAGCCGGGCAATTTCTCCTGTACTGATATCAATGAGTGCCTCACCAGCAGGGTCTGCCCTGA
	GCATTCTGACTGTGTCAACTCCATGGGAAGCTACAGTTGCAGCTGTCAAGTTGGATTCATCTCTAGA
	AACTCCACCTGTGAAGACGTGAATGAATGTGCAGATCCAAGAGCTTGCCCAGAGCATGCAACTTGTA
	ATAACACTGTTGGAAACTACTCTTGTTTCTGCAACCCAGGATTTGAATCCAGCAGTGGCCACTTGAG
	TTGCCAGGGTCTCAAAGCATCGTGTGAAGATATTGATGAATGCACTGAAATGTGCCCCATCAATTCA
	ACATGCACCAACACTCCTGGGAGCTACTTTTGCACCTGCCACCCTGGCTTTGCACCAAGCAGTGGAC
	AGTTGAATTTCACAGACCAAGGAGTGGAATGTAGAGATATTGATGAGTGCCGCCAAGATCCATCAAC
	CTGTGGTCCTAATTCTATCTGCACCAATGCCCTGGGCTCCTACAGCTGTGGCTGCATTGTAGGCTTT
	CATCCCAATCCAGAAGGCTCCCAGAAAGATGGCAACTTCAGCTGCCAAAGGGTTCTCTTCAAATGTA
	AGGAAGATGTGATACCCGATAATAAGCAGATCCAGCAATGCCAAGAGGGAACCGCAGTGAAACCTGC
	ATATGTCTCCTTTTGTGCACAAATAAATAACATCTTCAGCGTTCTGGACAAAGTGTGTGAAAATAAA
	ACGACCGTAGTTTCTCTGAAGAATACAACTGAGAGCTTTGTCCCTGTGCTTAAACAAATATCCATGT
	GGACTAAATTCACCAAGGAAGAGACGTCCTCCCTGGCCACAGTCTTCCTGGAGAGTGTGGAAAGCAT
	GACACTGGCATCTTTTTGGAAACCCTCAGCAAATGTCACTCCGGCTGTTCGGGCGGAATACTTAGAC
	ATTGAGAGCAAAGTTATCAACAAAGAATGCAGTGAAGAGAATGTGACGTTGGACTTGGTAGCCAAGG
	GGGATAAGATGAAGATCGGGTGTTCCACAATTGAGGAATCTGAATCCACAGAGACCACTGGTGTGGC
	TTTTGTCTCCTTTGTGGGCATGGAATCGGTTTTAAATGAGCGCTTCTTCCAAGACCACCAGGCTCCC
	TTGACCACCTCTGAGATCAAGCTGAAGATGAATTCTCGAGTCGTTGGGGGCATAATGACTGGAGAGA
	AGAAAGACGGCTTCTCAGATCCAATCATCTACACTCTGGAGAACGTTCAGCCAAAGCAGAAGTTTGA
	GAGGCCCATCTGTGTTTCCTGGAGCACTGATGTGAAGGGTGGAAGATGGACATCCTTTGGCTGTGTG
	ATCCTGGAAGCTTCTGAGACATATACCATCTGCAGCTGTAATCAGATGGCAAATCTTGCCGTTATCA
	TGGCGTCTGGGGAGCTCACGATGGACTTTTCCTTGTACATCATTAGCCATGTAGGCATTATCATCTC
	CTTGGTGTGCCTCGTCTTGGCCATCGCCACCTTTCTGCTGTGTCGCTCCATCCGAAATCACAACACC
	TACCTCCACCTGCACCTCTGCGTGTGTCTCCTCTTGGCGAAGACTCTCTTCCTCGCCGGTATACACA
	AGACTGACAACAAGACGGGCTGCGCCATCATCGCGGGCTTCCTGCACTACCTTTTCCTTGCCTGCTT
	CTTCTGGATGCTGGTGGAGGCTGTGATACTGTTCTTGATGGTCAGAAACCTGAAGGTGGTGAATTAC
	TTCAGCTCTCGCAACATCAAGATGCTGCACATCTGTGCCTTTGGTTATGGGCTGCCGATGCTGGTGG
	TGGTGATCTCTGCCAGTGTGCAGCCACAGGGCTATGGAATGCATAATCGCTGCTGGCTGAATACAGA
	GACAGGGTTCATCTGGAGTTTCTTGGGGCCAGTTTGCACAGTTATAGTGATCAACTCCCTTCTCCTG
	ACCTGGACCTTGTGGATCCTGAGGCAGAGGCTTTCCAGTGTTAATGCCGAAGTCTCAACGCTAAAAG
	ACACCAGGTTACTGACCTTCAAGGCCTTTGCCCAGCTCTTCATCCTGGGCTGCTCCTGGGTGCTGGG
	CATTTTTCAGATTGGACCTGTGGCAGGTGTCATGGCTTACCTGTTCACCATCATCAACAGCCTGCAG
	GGGGCCTTCATCTTCCTCATCCACTGTCTGCTCAACGGCCAGGTACGAGAAGAATACAAGAGGTGGA
	TCACTGGGAAGACGAAGCCCAGCTCCCAGTCCCAGACCTCAAGGATCTTGCTGTCCTCCATGCCATC
	CGCTTCCAAGACGGGTTAAAGCCTTTCTTGCTTTCAAATATGCTATGGAGCCACAGTTGAGGACAGT
	AGTTTCCTGCAGGAGCCTACCCTGAAATCTCTTCTCAGCTTAACATGGAAATGAGGATCCCACCAGC
	CCCAGAACCCTCTGGGGAAGAATGTTGGGGGCCGTCTTCCTGTGGTTGTATGCACTGATGAGAAATC
	AGACGTTTCTGCTCCAAACGACCATTTTATCTTCGTGCTCTGCAACTTCTTCAATTCCAGAGTTTCT
	GAGAACAGACCCAAATTCAATGGCATGACCAAGAACACCTGGCTACCATTTTGTTTTCTCCTGCCCT
	TGTTGGTGCATGGTTCTAAGCGTGCCCCTCCAGCGCCTATCATACGCCTGACACAGAGAACCTCTCA
	ATAAATGATTTGTCGCCTGTCTGACTGATTTACCCTAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 39		ORF Stop: TAA at 2697
	SEQ ID NO: 202	886 aa	MW at 97679.1 kD
NOV48a,	MRGFNLLLFWGCCVMHSWEGHIRPTRKPNTKGNNCRDSTLCPAYATCTNTVDSYYCTCKQGFLSSNG
CG57209-01
Protein Sequence	QNHFKDPGVRCKDIDECSQSPQPCGPNSSCKNLSGRYKCSCLDGFSSPTGNDWVPGKPGNFSCTDIN
	ECLTSRVCPEHSDCVNSMGSYSCSCQVGFISRNSTCEDVNECADPRACPEHATCNNTVGNYSCFCNP
	GFESSSGHLSCQGLKASCEDIDECTEMCPINSTCTNTPGSYFCTCHPGFAPSSGQLNFTDQGVECRD
	IDECRQDPSTCGPNSICTNALGSYSCGCIVGFHPNPEGSQKDGNFSCQRVLFKCKEDVIPDNKQIQQ
	CQEGTAVKPAYVSFCAQINNIFSVLDKVCENKTTVVSLKNTTESFVPVLKQISMWTKFTKEETSSLA
	TVFLESVESMTLASFWKPSANVTPAVRAEYLDIESKVINKECSEENVTLDLVAKGDKMKIGCSTIEE
	SESTETTGVAFVSFVGMESVLNERFFQDHQAPLTTSEIKLKMNSRVVGGIMTGEKKDGFSDPIIYTL
	ENVOPKOKFERPICVSWSTDVKGGRWTSFGCVILEASETYTICSCNOMANLAVIMASGELTMDFSLY
	IISHVGIIISLVCLVLAIATFLLCRSIRNHNTYLHLHLCVCLLLAKTLFLAGIHKTDNKTGCAIIAG
	FLHYLFLACFFWMLVEAVILFLMVRNLKVVNYFSSRNIKMLHICAFGYGLPMLVVVISASVQPQGYG
	MHNRCWLNTETGFIWSFLGPVCTVIVINSLLLTWTLWILRQRLSSVNAEVSTLKDTRLLTFKAFAQL
	FILGCSWVLGIFQIGPVAGVMAYLFTIINSLQGAFIFLIHCLLNGQVREEYKRWITGKTKPSSQSQT
	SRILLSSMPSASKTG
	SEQ ID NO: 203	1764 bp
NOV48b,	AGATCTTGGGAAGGGCACATAAGACCCACACGGAAACCAAACACAAAGGGTAATAACTGTAGAGACA
CGA57209-03
DNA Sequence	GTACCTTGTGCCCAGCTTATGCCACCTGCACCAATACAGTGGACAGTTACTATTGCACTTGCAAACA
	AGGCTTCCTGTCCAGCAATGGGCAAAATCACTTCAAGGATCCAGGAGTGCGATGCAAAGATATTGAT
	GAATGTTCTCAAAGCCCCCAGCCCTGTGGTCCTAACTCATCCTGCAAAAACCTGTCAGGGAGGTACA
	AGTGCAGCTGTTTAGATGGTTTCTCTTCTCCCACTGGAAATGACTGGGTCCCAGGAAAGCCGGGCAA
	TTTCTCCTGTACTGATATCAATGAGTGCCTCACCAGCAGGGTCTGCCCTGAGCATTCTGACTGTGTC
	AACTCCATGGGAAGCTACAGTTGCAGCTGTCAAGTTGGATTCATCTCTAGAAACTCCACCTGTGGAG
	ACGTGAATGAATGTGCAGATCCAAGAGCTTGCCCAGAGCATGCAACTTGTAATAACACTGTTGGAAA
	CTACTCTTGTTTCTGCAACCCAGGATTTGAATCCAGCAGTGGCCACTTGAGTTTCCAGGGTCTCAAA
	GCATCGTGTGAAGATATTGATGAATGCACTGAAATGTGCCCCATCAATTCAACATGCACCAACACTC
	CTGGGAGCTACTTTTGCACCTGCCACCCTGGCTTTGCACCAAGCAATGGACAGTTGAATTTCACAGA
	CCAAGGAGTGGAATGTAGAGATATTGATGAGTGCCGCCAAGATCCATCAACCTGTGGTCCTAATTCT
	ATCTGCACCAATGCCCTGGGCTCCTACAGCTGTGGCTGCATTGTAGGCTTTCATCCCAATCCAGAAG
	GCTCCCAGAAAGATGGCAACTTCAGCTGTCAAAGGGTTCTCTTCAAATGTAAGGAAGATGTGATACC
	CGATAATAAGCAGATCCAGCAATGCCAAGAGGGAACCGCAGTGAAACCTGCATATGTCTCCTTTTGT
	GCACAAATAAATAACATCTTCAGCGTTCTGGACAAAGTGTGTGAAAATAAAACGACCGTAGTTTCTC
	TGAAGAATACAACTGAGAGCTTTGTCCCTGTGCTTAAACAAATATCCACGTGGACTAAATTCACCAA
	GGAAGAGACGTCCTCCCTGGCCACAGTCTTCCTGGAGAGTGTGGAAAGCATGACACTGGCATCTTTT
	TGGAAACCCTCAGCAAATGTCACTCCGGCTGTTCGGACGGAATACTTAGACATTGAGAGCAAAGTTA
	TCAACAAAGAATGCAGTGAAGAGAATGTGACGTTGGACTTGGTAGCCAAGGGGGATAAGATGAAGAT
	CGGGTGTTCCACAATTGAGGAATCTGAATCCACAGAGACCACTGGTGTGGCTTTTGTCTCCTTTGTG
	GGCATGGAATCGGTTTTAAATGAGCGCTTCTTCCAAGACCACCAGGCTCCCTTGACCACCTCTGAGA
	TCAAGCTGAAGATGAATTCTCGAGTCGTTGGGGGCATAATGACTGGAGAGAAGAAAGACGGCTTCTC
	AGATCCAATCATCTACACTCTGGAGAACGTTCAGCCAAAGCAGAAGTTTGAGAGGCCCATCTGTGTT
	TCCTGGAGCACTGATGTGAAGGGTGGAAGATGGACATCCTTTGGCTGTGTGATCCTGGAAGCTTCTG
	AGACATATACCATCTGCAGCTGTAATCAGATGGCAAATCTTGCCGTTATCATGGCGTCTGGGGAGCT
	CACGGTCGACAAGGGCGAATTT
	ORF Start: at 7		ORF Stop: at 1747
	SEQ ID NO: 204	580 aa	MW at 63248.2 kD
NOV48b,	WEGHIRPTRKPNTKGNNCRDSTLCPAYATCTNTVDSYYCTCKQGFLSSNGQNHFKDPGVRCKDIDEC
CG57209-03
Protein Sequence	SQSPQPCGPNSSCKNLSGRYKCSCLDGFSSPTGNDWVPGKPGNFSCTDINECLTSRVCPEHSDCVNS
	MGSYSCSCQVGFISRNSTCGDVNECADPRACPEHATCNNTVGNYSCFCNPGFESSSGHLSFQGLKAS
	CEDIDECTEMCPINSTCTNTPGSYFCTCHPGFAPSNGQLNFTDQGVECRDIDECRQDPSTCGPNSIC
	TNALGSYSCGCIVGFHPNPEGSQKDGNFSCQRVLFKCKEDVIPDNKQIQQCQEGTAVKPAYVSFCAQ
	INNIFSVLDKVCENKTTVVSLKNTTESFVPVLKQISTWTKFTKEETSSLATVFLESVESMTLASFWK
	PSANVTPAVRTEYLDIESKVINKECSEENVTLDLVAKGDKMKIGCSTIEESESTETTGVAFVSFVGM
	ESVLNERFFQDHQAPLTTSEIKLKMNSRVVGGIMTGEKKDGFSDPIIYTLENVQPKQKFERPICVSW
	STDVKGGRWTSFGCVILEASETYTICSCNQMANLAVIMASGELT
	SEQ ID NO: 205	1740 bp
NOV48c,	TGGGAAGGGCACATAAGACCCACACGGAAACCAAACACAAAGGGTAATAACTGTAGAGACAGTACCT
CG57209-02
DNA Sequence	TGTGCCCAGCTTATGCCACCTGCACCAATACAGTGGACAGTTACTATTGCACTTGCAAACAAGGCTT
	CCTGTCCAGCAATGGGCAAAATCACTTCAAGGATCCAGGAGTGCGATGCAAAGATATTGATGAATGT
	TCTCAAAGCCCCCAGCCCTGTGGTCCTAACTCATCCTGCAAAAACCTGTCAGGGAGGTACAAGTGCA
	GCTGTTTAGATGGTTTCTCTTCTCCCACTGGAAATGACTGGGTCCCAGGAAAGCCGGGCAATTTCTC
	CTGTACTGATATCAATGAGTGCCTCACCAGCAGGGTCTGCCCTGAGCATTCTGACTGTGTCAACTCC
	ATGGGAAGCTACAGTTGCAGCTGTCAAGTTGGATTCATCTCTAGAAACTCCACCTGTGGAGACGTGA
	ATGAATGTGCAGATCCAAGAGCTTGCCCAGAGCATGCAACTTGTAATAACACTGTTGGAAACTACTC
	TTGTTTCTGCAACCCAGGATTTGAATCCAGCAGTGGCCACTTGAGTTTCCAGGGTCTCAAAGCATCG
	TGTGAAGATATTGATGAATGCACTGAAATGTGCCCCATCAATTCAACATGCACCAACACTCCTGGGA
	GCTACTTTTGCACCTGCCACCCTGGCTTTGCACCAAGCAATGGACAGTTGAATTTCACAGACCAAGG
	AGTGGAATGTAGAGATATTGATGAGTGCCGCCAAGATCCATCAACCTGTGGTCCTAATTCTATCTGC
	ACCAATGCCCTGGGCTCCTACAGCTGTGGCTGCATTGTAGGCTTTCATCCCAATCCAGAAGGCTCCC
	AGAAAGATGGCAACTTCAGCTGTCAAAGGGTTCTCTTCAAATGTAAGGAAGATGTGATACCCGATAA
	TAAGCAGATCCAGCAATGCCAAGAGGGAACCGCAGTGAAACCTGCATATGTCTCCTTTTGTGCACAA
	ATAAATAACATCTTCAGCGTTCTGGACAAAGTGTGTGAAAATAAAACGACCGTAGTTTCTCTGAAGA
	ATACAACTGAGAGCTTTGTCCCTGTGCTTAAACAAATATCCACGTGGACTAAATTCACCAAGGAAGA
	GACGTCCTCCCTGGCCACAGTCTTCCTGGAGAGTGTGGAAAGCATGACACTGGCATCTTTTTGGAAA
	CCCTCAGCAAATGTCACTCCGGCTGTTCGGACGGAATACTTAGACATTGAGAGCAAAGTTATCAACA
	AAGAATGCAGTGAAGAGAATGTGACGTTGGACTTGGTAGCCAAGGGGGATAAGATGAAGATCGGGTG
	TTCCACAATTGAGGAATCTGAATCCACAGAGACCACTGGTGTGGCTTTTGTCTCCTTTGTGGGCATG
	GAATCGGTTTTAAATGAGCGCTTCTTCCAAGACCACCAGGCTCCCTTGACCACCTCTGAGATCAAGC
	TGAAGATGAATTCTCGAGTCGTTGGGGGCATAATGACTGGAGAGAAGAAAGACGGCTTCTCAGATCC
	AATCATCTACACTCTGGAGAACGTTCAGCCAAAGCAGAAGTTTGAGAGGCCCATCTGTGTTTCCTGG
	AGCACTGATGTGAAGGGTGGAAGATGGACATCCTTTGGCTGTGTGATCCTGGAAGCTTCTGAGACAT
	ATACCATCTGCAGCTGTAATCAGATGGCAAATCTTGCCGTTATCATGGCGTCTGGGGAGCTCACG
	ORF Start: at 1		ORF Stop: end of sequence
	SEQ ID NO: 206	580 aa	MW at 63248.2kD
NOV48c,	WEGHIRPTRKPNTKGNNCRDSTLCPAYATCTNTVDSYYCTCKQGFLSSNGQNHFKDPGVRCKDIDEC
CG57209-02
Protein Sequence	SQSPQPCGPNSSCKNLSGRYKCSCLDGFSSPTGNDWVPGKPGNFSCTDINECLTSRVCPEHSDCVNS
	MGSYSCSCQVGFISRNSTCGDVNECADPRACPEHATCNNTVGNYSCFCNPGFESSSGHLSFQGLKAS
	CEDIDECTEMCPINSTCTNTPGSYFCTCHPGFAPSNGQLNFTDQGVECRDIDECRQDPSTCGPNSIC
	TNALGSYSCGCIVGFHPNPEGSQKDGNFSCQRVLFKCKEDVIPDNKQIQQCQEGTAVKPAYVSFCAQ
	INNIFSVLDKVCENKTTVVSLKNTTESFVPVLKQISTWTKFTKEETSSLATVFLESVESMTLASFWK
	PSANVTPAVRTEYLDIESKVINKECSEENVTLDLVAKGDKMKIGCSTIEESESTETTGVAFVSFVGM
	ESVLNERFFQDHQAPLTTSEIKLKMNSRVVGGIMTGEKKDGFSDPIIYTLENVQPKQKFERPICVSW
	STDVKGGRWTSFGCVILEASETYTICSCNQMANLAVIMASGELT
	SEQ ID NO: 207		2851 bp
NOV48d,	GCTCCTCTTCTGGGGTGTTGTGTTATGCACAGCTGGGAAGGGCACATAAGACCCACACGGAAACCAA
CG57209-04
DNA Sequence	ACACAAAGGGTAATAACTGTAGAGACAGTACCTTGTGCCCAGCTTATGCCACCTGCACCAATACAGT
	GGACAGTTACTATTGCGCTTGCAAACAAGGCTTCCTGTCCAGCAATGGGCAAAATCACTTCAAGGAT
	CCAGGAGTGCGATGCAAAGATATTGATGAATGTTCTCAAAGCCCCCAGCCCTGTGGTCCTAACTCAT
	CCTGCAAAAACCTGTCAGGGAGGTACAAGTGCAGCTGTTTAGATGGTTTCTCTTCTCCCACTGGAAA
	TGACTGGGTCCCAGGAAAGCCGGGCAATTTCTCCTGTACTGATATCAATGAGTGCCTCACCAGCAGC
	GTCTGCCCTGAGCATTCTGACTGTGTCAACTCCATGGGAAGCTACAGTTGTAGCTGTCAAGTTGGAT
	TCATCTCTAGAAACTCCACCTGTGAAGACGTGGATGAATGTGCAGATCCAAGAGCTTGCCCAGAGCA
	TGCAACTTGTAATAACACTGTTGGAAACTACTCTTGTTTCTGCAACCCAGGATTTGAATCCAGCAGT
	GGCCACTTGAGTTTCCAGGGTCTCAAAGCATCGTGTGAAGATATTGATGAATGCACTGAAATGTGCC
	CCATCAATTCAACATGCACCAACACTCCTGGGAGCTACTTTTGCACCTGCCACCCTGGCTTTGCACC
	AAGCAATGGACAGTTGAATTTCACAGACCAAGGAGTGGAATGTAGAGATATTGATGAGTGCCGCCAA
	GATCCATCAACCTGTGGTCCTAATTCTATCTGCACCAATGCCCTGGGCTCCTGCAGCTGTGGCTGCA
	TTGCAGGCTTTCATCCCAATCCAGAAGGCTCCCAGAAAGATGGCAACTTCAGCTGCCAAAGGGTTCT
	CTTCAAATGTAAGGAAGATGTGATACCCGATAATAAGCAGATCCAGCAATGCCAAGAGGGAACCGCA
	GTGAAACCTGCATATGTCTCCTTTTGTGCACAAATAAATAACATCTTCAGCGTTCTGGACAAAGTGT
	GTGAAAATAAAACGACCGTAGTTTCTCTGAAGAATACAACTGAGAGCTTTGTCCCTGTGCTTAAACA
	AATATCCACGTGGACTAAATTCACCAAGGAAGAGACGTCCTCCCTGGCCACAGTCTTCCTGGAGAGT
	GTGGAAAGCATGACACTGGCATCTTTTTGGAAACCCTCAGCAAATGTCACTCCGGCTGTTCGGACGG
	AATACTTAGACATTGAGAGCAAAGTTATCAACAAAGAATGCAGTGAAGAGAATGTGACGTTGGACTT
	GGTAGCCAAGGGGGATAAGATGAAGATCGGGTGTTCCACAATTGAGGAATCTGAATCCACAGAGACC
	ACTGGTGTGGCTTTTGTCTCCTTTGTGGGCATGGAATCGGTTTTAAATGAGCGCTTCTTCCAAGACC
	ACCAGGCTCCCTTGACCACCTCTGAGATCAAGCTGAAGATGAATTCTCGAGTCGTTGGGGGCATAAT
	GACTGGAGAGAAGAAAGACGGCTTCTCAGATCCAATTATCTACACTCTGGAGAACGTTCAGCCAAAG
	CAGAAGTTTGAGAGGCCCATCTGTGTTTCCTGGAGCACTGATGTGAAGGGTGGAAGATGGACATCCT
	TTGGCTGTGTGATCCTGGAAGCTTCTGAGACATATACCATCTGCAGCTGTAATCAGATGGCAAATCT
	TGCCGTTATCATCGCGTCTGGGGAGCTCACGATGGGCTGCGCCATCATCGCGGGCTTCCTGCACTAC
	CTTTTCCTTGCCTGCTTCTTCTGGATGCTGGTGGAGGCTGTGATACTGTTCTTGATGGTCAGAAACC
	TGAAGGTGGTGAATTACTTCAGCTCTCGCAACATCAAGATGCTGCACATCTGTGCCTTTGGTTATGG
	GCTGCCGATGCTGGTGGTGGTGATCTCTGCCAGTGTGCAGCCACAGGGCTATGGAATGCATAATCGC
	TGCTGGCTGAATACAGAGACAGGGTTCATCTGGAGTTTCTTGGGGCCAGTTTGCACAGTTATAGTGA
	TCAACTCCCTTCTCCTGACCTGGACCTTGTGGATCCTGAGGCAGAGGCTTTCCAGTGTTAATGCCGA
	AGTCTCAACGCTAAAAGACACCAGGTTACTGACCTTCAAGGCCTTTGCCCAGCTCTTCATCCTGGGC
	TGCTCCTGGGTGCTGGGCATTTTTCAGATTGGACCTGTGGCAGGTGTCATGGCTTACCTGTTCACCA
	TCATCAACAGCCTGCAGGGGGCCTTCATCTTCCTCATCCACTGTCTGCTCAACGGCCAGGTACGAGA
	AGAATACAAGAGGTGGATCACTGGGAAGACGAAGCCCAGCTCCCAGTCCCAGACCTCAAGGATCTTG
	CTGTCCTCCATGCCATCCGCTTCCAAGACGGGTTAAAGTCCTTTCTTGCTTTCAAATATGCTATGGA
	GCCACAGTTGAGGACAGTAGTTTCCTGCAGGAGCCTACCCTGAAATCTCTTCTCAGCTTAACATGGA
	AATGAGGATCCCACCAGCCCCAGAACCCTCTGGGGAAGAATGTTGGGGGCCGTCTTCCTGTGGTTGT
	ATGCACTGATGAGAAATCAGGCGTTTCTGCTCCAAACGACCATTTTATCTTCGTGCTCTGCAACTTC
	TTCAATTCCAGAGTTTCTGAGAACAGACCCAAATTCAATGGCATGACCAAGAACACCTGGCTACCAT
	TTTGTTTTCTCCTGCCCTTGTTGGTGCATGGTTCTAAGCGTGCCCCTCCAGCGCCTATCATACGCCT
	GACACAGAGAACCTCTCAATAAATGATTTGTCGCCTG
	ORF Start: at 13		ORF Stop: TAA at 2446
	SEQ ID NO: 208	811 aa	MW at 89011.6 kD
NOV48d,	GCCVMHSWEGHIRPTRKPNTKGNNCRDSTLCPAYATCTNTVDSYYCACKQGFLSSNGQNHFKDPGVR
CG57209-04
Protein Sequence	CKDIDECSQSPQPCGPNSSCKNLSGRYKCSCLDGFSSPTGNDWVPGKPGNFSCTDINECLTSSVCPE
	HSDCVNSMGSYSCSCQVGFISRNSTCEDVDECADPRACPEHATCNNTVGNYSCFCNPGFESSSGHLS
	FQGLKASCEDIDECTEMCPINSTCTNTPGSYFCTCHPGFAPSNGQLNFTDQGVECRDIDECRQDPST
	CGPNSICTNALGSCSCGCIAGFHPNPEGSQKDGNFSCQRVLFKCKEDVIPDNKQIQQCQEGTAVKPA
	YVSFCAQINNIFSVLDKVCENKTTVVSLKNTTESFVPVLKQISTWTKFTKEETSSLATVFLESVESM
	TLASFWKPSANVTPAVRTEYLDIESKVINKECSEENVTLDLVAKGDKMKIGCSTIEESESTETTGVA
	FVSFVGMESVLNERFFQDHQAPLTTSEIKLKMNSRVVGGIMTGEKKDGFSDPIIYTLENVQPKQKFE
	RPICVSWSTDVKGGRWTSFGCVILEASETYTICSCNQMANLAVIMASGELTMGCAIIAGFLHYLFLA
	CFFWMLVEAVILFLMVRNLKVVNYFSSRNIKMLHICAFGYGLPMLVVVISASVQPQGYGMHNRCWLN
	TETGFIWSFLGPVCTVIVINSLLLTWTLWILRQRLSSVNAEVSTLKDTRLLTFKAFAQLFILGCSWV
	LGIFQIGPVAGVMAYLFTIINSLQGAFIFLIHCLLNGQVREEYKRWITGKTKPSSQSQTSRILLSSM
	PSASKTG

[0625] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 48B.

TABLE 48B
Comparison of NOV48a against NOV48b through NOV48d.
	NOV48a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV48b	18 . . . 597	563/580 (97%)
	1 . . . 580	564/580 (97%)
NOV48c	18 . . . 597	563/580 (97%)
	1 . . . 580	564/580 (97%)
NOV48d	11 . . . 886	783/876 (89%)
	1 . . . 811	788/876 (89%)

[0626] Further analysis of the NOV48a protein yielded the following properties shown in Table 48C.

TABLE 48C
Protein Sequence Properties NOV48a
PSort analysis:   0.6850 probability located in endoplasmic reticulum (membrane); 0.6400
                  probability located in plasma membrane; 0.4600 probability located in Golgi
                  body; 0.1000 probability located in endoplasmic reticulum (lumen)
SignalP analysis: Cleavage site between residues 18 and 19

[0627] A search of the NOV48 a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 48D.

TABLE 48D
Geneseq Results for NOV48a
		NOV48a
		Residues/	Identities/
Geneseq	Protein/Organism/Length	Match	Similarities for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
AAB71869	Human EMR1 seven	1 . . . 886	886/886 (100%)	0.0
	transmembrane domain -	1 . . . 886	886/886 (100%)
	Homo sapiens, 886 aa.
	[WO200109328-A1,
	Feb. 8, 2001]
AAB01249	Human EMR1 hormone	1 . . . 886	880/886 (99%)	0.0
	receptor - Homo sapiens, 880	1 . . . 880	880/886 (99%)
	aa. [WO200034473-A2,
	Jun. 15, 2000]
AAE17043	Human CD 97 protein -	74 . . . 872	272/853 (31%)	e−122
	Homo sapiens, 835 aa.	16 . . . 817	422/853 (48%)
	[WO200202602-A2,
	Jan. 10, 2002]
AAB15728	Human CD97 protein -	74 . . . 872	272/853 (31%)	e−122
	Homo sapiens, 835 aa.	16 . . . 817	422/853 (48%)
	[WO200052039-A2,
	Sep. 8, 2000]
AAY41090	Human CD97 protein -	74 . . . 872	272/853 (31%)	e−122
	Homo sapiens, 835 aa.	16 . . . 817	422/853 (48%)
	[WO9945111-A1,
	Sep. 10, 1999]

[0628] In a BLAST search of public sequence datbases, the NOV48a protein was found to have homology to the proteins shown in the BLASTP data in Table 48E.

TABLE 48E
Public BLASTP Results for NOV48a
		NOV48a
Protein		Residues/	Identities/
Accession		Match	Similarities for the	Expect
Number	Protein/Organism/Length	Residues	Matched Portion	Value
Q14246	Cell surface glycoprotein	1 . . . 886	886/886 (100%)	0.0
	EMR1 precursor (EMR1	1 . . . 886	886/886 (100%)
	hormone receptor) - Homo
	sapiens (Human), 886 aa.
BAC06133	Seven transmembrane helix	11 . . . 885	866/877 (98%)	0.0
	receptor - Homo sapiens	29 . . . 905	868/877 (98%)
	(Human), 929 aa.
Q61549	Cell surface glycoprotein	1 . . . 886	606/937 (64%)	0.0
	EMR1 precursor (EMR1	1 . . . 931	709/937 (74%)
	hormone receptor) (Cell
	surface glycoprotein F4/80) -
	Mus musculus (Mouse), 931
	aa.
BAC06178	Seven transmembrane helix	74 . . . 872	272/853 (31%)	e−121
	receptor - Homo sapiens	18 . . . 819	422/853 (48%)
	(Human), 837 aa.
O00718	CD97 - Homo sapiens	74 . . . 872	272/853 (31%)	e−121
	(Human), 835 aa.	16 . . . 817	422/853 (48%)

[0629] PFam analysis predicts that the NOV48a protein contains the domains shown in the Table 48F.

TABLE 48F
Domain Analysis of NOV48a
		Identities/
		Similarities
Pfam Domain	NOV48a Match Region	for the Matched Region	Expect Value
EGF	35 . . . 70	13/47 (28%)	0.29
		26/47 (55%)
TILa	34 . . . 89	16/58 (28%)	0.42
		36/58 (62%)
EGF	176 . . . 212	15/47 (32%)	0.0038
		25/47 (53%)
EGF	225 . . . 255	13/47 (28%)	0.29
		23/47 (49%)
GPS	546 . . . 596	19/54 (35%)	1.5e−18
		46/54 (85%)
7tm_2	599 . . . 851	96/276 (35%)	9.2e−104
		228/276 (83%)

Example 49

[0630] The NOV49 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 49A.

TABLE 49A
NOV49 Sequence Analysis
	SEQ ID NO: 209	5184 bp
NOV49a,	CCCCGCAGGGGAAGGCGGGTCCTGGCGGCCAGCGCGCGGTCCGCGCCCACCCTAGCCGACGGGGCCG
CG57292-01
DNA Sequence	GCAGAGCGCGCGGCGTCGGTGCCCTTGACCATGGCGGCGGCTGCGCTTCTGCTGGGGCTGGCGCTGC
	TGGCACCGCGGGCGGCCGGCGCGGGCATGGGCGCGTGCTATGACGGCGCAGGGCGCCCGCAGCGCTG
	CCTGCCGGTGTTCGAGAACGCGGCGTTTGGGCGGCTCGCCCAGGCCTCGCACACGTGCGGCAGCCCG
	CCCGAGGACTTCTGTCCCCACGTGGGCGCCGCGGGCGCGGGGGCTCATTGCCAGCGCTGCGACGCCG
	CCGACCCCCAGCGCCACCACAACGCCTCCTACCTCACCGACTTCCACAGCCAGGACGAGAGCACCTG
	GTGGCAGAGCCCGTCCATGGCCTTCGGCGTGCAGTACCCCACCTCGGTCAACATCACCCTCCGCCTA
	GGGAAGGCTTATGAGATCACGTATGTGAGGCTGAAGTTCCACACCAGTCGCCCTGAGAGCTTTGCCA
	TCTACAAGCGCAGCCGCGCCGACGGCCCATGGGAGCCCTACCAGTTCTACAGCGCCTCCTGCCAGAA
	GACCTACGGCCGGCCCGAGGGCCAGTACCTGCGCCCCGGCGAGGACGAGCGCGTGGCCTTCTGCACC
	TCTGAGTTCAGCGACATCTCCCCGCTGAGTGGCGGCAACGTGGCCTTCTCCACCCTGGAGGGCCGGC
	CCAGCGCCTACAACTTCGAGGAGAGCCCTGGGCTGCAGGAGTGGGTCACCAGCACCGAACTCCTCAT
	CTCTCTAGACCGGCTCAACACGTTTGGGGACGACATCTTCAAGGACCCCAAGGTGCTCCAGTCCTAC
	TATTATGCCGTGTCCGACTTCTCTGTGGGCGGCAGGTGCAAGTGCAACGGGCATGCCAGCGAGTGCG
	GCCCCGACGTGGCAGGCCAGTTGGCCTGCCGGTGCCAGCACAACACCACCGGCACAGACTGTGAGCG
	CTGCCTGCCCTTCTTCCAGGACCGCCCGTGGGCCCGGGGCACCGCCGAGGCTGCCCACGAGTGTCTG
	CCCTGCAACTGCAGTGGCCGCTCCGAGGAATGCACGTTTGATCGGGAGCTCTTCCGCAGCACAGGCC
	ACGGCGGGCGCTGTCACCACTGCCGTGACCACACAGCTGGGCCACACTGTGAGCGCTGTCAGGAGAA
	TTTCTATCACTGGGACCCGCGGATGCCATGCCAGCCCTGTGACTGCCAGTCGGCAGGCTCCCTACAC
	CTCCAGTGCGATGACACAGGCACCTGCGCCTGCAAGCCCACAGTGACTGGCTGGAAGTGTGACCGCT
	GTCTGCCCGGGTTCCACTCGCTCAGTGAGGGAGGCTGCAGACCCTGCACTTGCAATCCCGCTGGCAG
	CCTGGACACCTGTGACCCCCGCAGTGGGCGCTGCCCCTGCAAAGAGAATGTGGAAGGCAACCTATGT
	GACAGATGTCGCCCGGGGACCTTTAACCTGCAGCCCCACAATCCAGCTGGCTGCAGCAGCTGTTTCT
	GCTATGGCCACTCCAAGGTGTGCGCGTCCACTGCCCAGTTCCAGGTGCATCACATCCTCAGCGATTT
	CCACCAGGGAGCCGAAGGCTGGTGGGCCAGAAGTGTGGGGGGCTCTGAGCACTCCCCACAATGGAGC
	CCAAATGGGGTCCTCCTGAGCCCAGAAGACGAGGAGGAGCTCACAGCACCAGGGAAGTTCCTGGGAG
	ACCAGCGGTTCAGCTATGGGCAGCCCCTCATACTGACCTTCCGGGTGCCCCCCGGGGACTCCCCACT
	CCCTGTACAGCTGAGGCTGGAAGGGACAGGCTTGGCCCTGTCCCTGAGGCACTCTAGCCTGTCTGGC
	CCCCAGGATGCCAGGGCATCCCAGGGAGGTAGAGCTCAGGTTCCACTGCAGGAGACCTCCGAGGACG
	TGGCCCCTCCACTGCCCCCCTTCCACTTCCAGCGGCTCCTCGCCAACCTGACCAGCCTCCGCCTCCG
	CGTCAGTCCCGGCCCCAGCCCTGCCGGTCCAGTGTTCCTGACTGAGGTCCGGCTCACATCCGCCCGG
	CCAGGGCTTTCCCCGCCAGCCTCCTGGGTGGAGATTTGTTCATGTCCCACTGGCTACACGGGCCAGT
	TCTGTGAATCCTGTGCTCCGGGATACAAGAGGGAGATGCCACAGGGGGGTCCCTATGCCAGCTGTGT
	CCCCTGCACCTGTAACCAGCATGGCACCTGTGACCCCAACACAGGGATCTGTGTCTGCAGCCACCAT
	ACCGAGGGCCCATCCTGTGAACGCTGTTTGCCAGGTTTCTATGGCAACCCTTTCGCGGGCCAAGCCG
	ACGACTGCCAGCCCTGTCCCTGCCCTGGCCAGTCGGCCTGTACGACCATCCCAGAGAGCGGGGAGGT
	GGTGTGTACCCACTGCCCCCCGGGCCAGAGAGGGCGGCGCTGTGAGGTCTGTGATGATGGCTTTTTT
	GGGGACCCGCTGGGGCTCTTTGGGCACCCCCAGCCCTGCCACCAGTGCCAGTGTAGCGGGAACGTGG
	ACCCCAATGCCGTGGGCAACTGTGACCCCCTGTCTGGCCACTGCCTGCGCTGCCTGCACAACACCAC
	GGGTGACCACTGTGAGCACTGTCAGGAAGGCTTCTACGGGAGCGCCCTGGCCCCTCGACCCGCAGAC
	AAATGCATGCCTTGCAGCTGTCACCCACAGGGCTCGGTCAGTGAGCAGATGCCCTGCGACCCAGTGA
	CAGGCCAATGCTCCTGCCTGCCTCATGTGACTGCACGGGACTGCAGCCGCTGCTACCCTGGCTTCTT
	CGACCTCCAGCCTGGGAGGGGCTGCCGGAGCTGCAAGTGTCACCCACTGGGCTCCCAGGAGGACCAG
	TGCCATCCCAAGACTGGACAGTGCACCTGCCGCCCAGGTGTCACAGGCCAGGCCTGTGACAGGTGCC
	AGCTGGGTTTCTTCGGCTCCTCAATCAAGGGCTGCCGGGCCTGCAGGTGCTCCCCACTGGGCGCTGC
	CTCGGCCCAGTGCCACTATAACGGCACATGCGTGTGCAGGCCTGGCTTCGAGGGCTACAAATGTGAC
	CGCTGCCACTACAACTTCTTCCTCACGGCAGACGGCACACACTGCCAGCAATGTCCGTCCTGCTACG
	CCCTGGTGAAGGAGGAGACAGCCAAGCTGAAGGCCAGACTGACTTTGACGGAGGGGTGGCTCCAAGG
	GTCCGACTGTGGCAGTCCCTGGGGACCACTAGACATTCTGCTGGGAGAGGCCCCAAGGGGGGACGTC
	TACCAGGGCCATCACCTGCTTCCAGGGGCTCGGGAAGCCTTCCTGGAGCAGATGATGGGCCTCGAGG
	GTGCTGTCAAGGCCGCCCGGGAGCAGCTGCAGAGGCTGAACAAGGGTGCCCGCTGTGCCCAGGCCGG
	ATCCCAGAAGACCTGCACCCAGCTGGCAGACCTGGAGGCAGTGCTGGAGTCCTCGGAAGAGGAGATT
	CTGCATGCAGCTGCCATTCTCGCGTCTCTGGAGATTCCTCAGGAAGGTCCCAGTCAGCCGACCAAAT
	GGAGCCACCTGGCCATAGAGGCCCGTGCCCTCGCCAGGAGCCACAGAGACACCGCCACCAAGATCGC
	AGCCACTGCTTGGAGGGCCCTGCTCGCCTCCAACACCAGCTACGCGCTTCTCTGGAATCTGCTGGAG
	GGAAGGGTGGCCCTAGAGACCCAGCGGGACCTGGAGGACAGGTACCAGGAGGTCCAGGCGGCCCAGA
	AAGCACTGAGGACGGCTGTGGCAGAGGTGCTGCCTGAAGCGGAAAGCGTGTTGGCCACCGTGCAGCA
	AGTTGGCGCAGATACAGCCCCGTACCTGGCCTTGCTGGCTTCCCCGGGAGCTCTGCCTCAGAAGTCC
	CGGGCTGAAGACCTGGGCCTGAAGGCGAAGGCCCTGGAGAAGACAGTTGCATCATGGCAGCACATGG
	CCACTGAGGCTGCCCGAACCCTCCAGACTGCTGCCCAGGCGACGCTACGGCAAACAGAACCCCTCAC
	AATGGCGCGATCTCGGCTCACTGCAACCTTTGCCTCCCAGCTGCACCAGGGGGCCAGAGCCGCCCTG
	ACCCAGGCTTCCTCATCTGTCCAGGCTGCGACAGTGACTGTCATGGGAGCCAGGACTCTGCTGGCTG
	ATCTGGAAGGAATGAAGCTGCAGTTTCCCCGGCCCAAGGACCAGGCGGCATTGCAGAGGAAGGCAGA
	CTCCGTCAGTGACAGACTCCTTGCAGACACGAGAAAGAAGACCAAGCAGGCGGAGAGGATGCTGGGA
	AACGCGGCCCCTCTTTCCTCCAGTGCCAAGAAGAAGGGCAGAGAAGCAGAGGTGTTGGCCAAGGACA
	GTGCCAAGCTTGCCAAGGCCTTGCTGAGGGAGCGGAAACAGGCGCACCGCCGTGCCAGCAGGCTCAC
	CAGCCAGACGCAAGCCACGCTCCAACAGGCGTCCCAGCAGGTGCTGGCGTCTGAAGCACGCAGACAG
	GAGCTGGAGGAAGCTGAGCGGGTGGGTGCTGGGCTGAGCGAGATGGAGCAGCAGATCCGGGAATCGC
	GTATCTCACTGGAGAAGGACATCGAGACCTTGTCAGAGCTGCTTGCCAGGCTGGGGTCGCTGGACAC
	CCATCAAGCCCCAGCCCAGGCCCTGAACGAGACTCAGTGGGCACTAGAACGCCTGAGGCTGCAGCTG
	GGCTCCCCGGGGTCCTTGCAGAGGAAACTCAGTCTGCTGGAGCAGGAATCCCAGCAGCAGGAGCTGC
	AGATCCAGGGCTTCGAGAGTGACCTCGCCGAGATCCGCGCCGACAAACAGAACCTGGAGGCCATTCT
	GCACAGCCTGCCCGAGAACTGTGCCAGCTGGCAGTGAGGGCTGCCCAGATCCCCGGCACACACTCCC
	CCACCTGCTGTTTACATGACCCAGGGGGTGCACACTACCCCACAGGTGTGCCCATACAGACATTCCC
	CGGAGCCGGCTGCTGTGAACTCGACCCCGTGTGGATAGTCACACTCCCTGCCGATTCTGTCTGTGGC
	TTCTTCCCTGCCAGCAGGACTGAGTGTGCGTACCCAGTTCACCTGGACATGAGTGCACACTCTCACC
	CCTGCACATGCATAAACGGGCACACCCCAGTGTCAATAACATACACACGTGAGGGTGCATGTCTGTG
	TGTATGACCCAAATAAAAAAAAAAA
	ORF Start: ATG at 98		ORF Stop: TGA at 4859
	SEQ ID NO: 210	1587 aa	MW at 172049.3 kD
NOV49a,	MAAAALLLGLALLAPRAAGAGMGACYDGAGRPQRCLPVFENAAFGRLAQASHTCGSPPEDFCPHVGA
CG57292-01
Protein Sequence	AGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAFGVQYPTSVNITLRLGKAYEITYVR
	LKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDERVAFCTSEFSDISPLS
	GGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKDPKVLQSYYYAVSDFSVG
	GRCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGTAEAAHECLPCNCSGRSEE
	CTFDRELFRSTGHGGRCHHCRDHTAGPHCERCQENFYHWDPRMPCQPCDCQSAGSLHLQCDDTGTCA
	CKPTVTGWKCDRCLPGFHSLSEGGCRPCTCNPAGSLDTCDPRSGRCPCKENVEGNLCDRCRPGTFNL
	QPHNPAGCSSCFCYGHSKVCASTAQFQVHHILSDFHQGAEGWWARSVGGSEHSPQWSPNGVLLSPED
	EEELTAPGKFLGDQRFSYGQPLILTFRVPPGDSPLPVQLRLEGTGLALSLRHSSLSGPQDARASQGG
	RAQVPLQETSEDVAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGPVFLTEVRLTSARPGLSPPASWV
	EICSCPTGYTGQFCESCAPGYKREMPQGGPYASCVPCTCNQHGTCDPNTGICVCSHHTEGPSCERCL
	PGFYGNPFAGQADDCQPCPCPGQSACTTIPESGEVVCTHCPPGQRGRRCEVCDDGFFGDPLGLFGHP
	QPCHQCQCSGNVDPNAVGNCDPLSGHCLRCLHNTTGDHCEHCQEGFYGSALAPRPADKCMPCSCHPQ
	GSVSEQMPCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGRGCRSCKCHPLGSQEDQCHPKTGQCTC
	RPGVTGQACDRCQLGFFGSSIKGCRACRCSPLGAASAQCHYNGTCVCRPGFEGYKCDRCHYNFFLTA
	DGTHCQQCPSCYALVKEETAKLKARLTLTEGWLQGSDCGSPWGPLDILLGEAPRGDVYQGHHLLPGA
	REAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASL
	EIPQEGPSQPTKWSHLAIEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRD
	LEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAK
	ALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQASSSVQAA
	TVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAK
	KKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGA
	GLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQRKL
	SLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPENCASWQ
	SEQ ID NO: 211	5148 bp
NOV49b,	CCCCGCAGGGGAAGGCGGGTCCTGGCGGCCAGCGCGCGGTCCGCGCCCACCCTAGCCGACGGGGCCG
CG57292-02
DNA Sequence	GCAGAGCGCGCGGCGTCGGTGCCCTTGACCATGGCGGCGGCTGCGCTTCTGCTGGGGCTGGCGCTGC
	TGGCACCGCGGGCGGCCGGCGCGGGCATGGGCGCGTGCTATGACGGCGCAGGGCGCCCGCAGCGCTG
	CCTGCCGGTGTTCGAGAACGCGGCGTTTGGGCGGCTCGCCCAGGCCTCGCACACGTGCGGCAGCCCG
	CCCGAGGACTTCTGTCCCCACGTGGGCGCCGCGGGCGCGGGGGCTCATTGCCAGCGCTGCGACGCCG
	CCGACCCCCAGCGCCACCACAACGCCTCCTACCTCACCGACTTCCACAGCCAGGACGAGAGCACCTG
	GTCGCAGAGCCCGTCCATGGCCTTCGGCGTGCAGTACCCCACCTCGGTCAACATCACCCTCCGCCTA
	GGGAAGGCTTATGAGATCACGTATGTGAGGCTGAAGTTCCACACCAGTCGCCCTGAGAGCTTTGCCA
	TCTACAAGCGCAGCCGCGCCGACGGCCCATGGGAGCCCTACCAGTTCTACAGCGCCTCCTGCCAGAA
	GACCTACGGCCGGCCCGAGGGCCAGTACCTGCGCCCCGGCGAGGACGAGCGCGTGGCCTTCTGCACC
	TCTGAGTTCAGCGACATCTCCCCGCTGAGTGGCGGCAACGTGGCCTTCTCCACCCTGGAGGGCCGGC
	CCAGCGCCTACAACTTCGAGGAGAGCCCTGGGCTGCAGGAGTGGGTCACCAGCACCGAACTCCTCAT
	CTCTCTAGACCGGCTCAACACGTTTGGGGACGACATCTTCAAGGACCCCAAGGTGCTCCAGTCCTAC
	TATTATGCCGTGTCCGACTTCTCTGTGGGCGGCAGGTGCAAGTGCAACGGGCATGCCAGCGAGTGCG
	GCCCCGACGTGGCAGGCCAGTTGGCCTGCCGGTGCCAGCACAACACCACCGGCACAGACTGTGAGCG
	CTGCCTGCCCTTCTTCCAGGACCGCCCGTGGGCCCGGGGCACCGCCGAGGCTGCCCACGAGTGTCTG
	CCCTGCAACTGCAGTGGCCGCTCCGAGGAATGCACGTTTGATCGGGAGCTCTTCCGCAGCACAGGCC
	ACGGCGGGCGCTGTCACCACTGCCGTGACCACACAGCTGGGCCACACTGTGAGCGCTGTCAGGAGAA
	TTTCTATCACTGGGACCCGCGGATGCCATGCCAGCCCTGTGACTGCCAGTCGGCAGGCTCCCTACAC
	CTCCAGTGCGATGACACAGGCACCTGCGCCTGCAAGCCCACAGTGACTGGCTGGAAGTGTGACCGCT
	GTCTGCCCGGGTTCCACTCGCTCAGTGAGGGAGGCTGCAGACCCTGCACTTGCAATCCCGCTGGCAG
	CCTGGACACCTGTGACCCCCGCAGTGGGCGCTGCCCCTGCAAAGAGAATGTGGAAGGCAACCTATGT
	GACAGATGTCGCCCGGGGACCTTTAACCTGCAGCCCCACAATCCAGCTGGCTGCAGCAGCTGTTTCT
	GCTATGGCCACTCCAAGGTGTGCGCGTCCACTGCCCAGTTCCAGGTGCATCACATCCTCAGCGATTT
	CCACCAGGGAGCCGAAGGCTGGTGGGCCAGAAGTGTGGGGGGCTCTGAGCACTCCCCACAATGGAGC
	CCAAATGGGGTCCTCCTGAGCCCAGAAGACGAGGAGGAGCTCACAGCACCAGGGAAGTTCCTGGGAG
	ACCAGCGGTTCAGCTATGGGCAGCCCCTCATACTGACCTTCCGGGTGCCCCCCGGGGACTCCCCACT
	CCCTGTACAGCTGAGGCTGGAAGGGACAGGCTTGGCCCTGTCCCTGAGGCACTCTAGCCTGTCTGGC
	CCCCAGGATGCCAGGGCATCCCAGGGAGGTAGAGCTCAGGTTCCACTGCAGGAGACCTCCGAGGACG
	TGGCCCCTCCACTGCCCCCCTTCCACTTCCAGCGGCTCCTCGCCAACCTGACCAGCCTCCGCCTCCG
	CGTCAGTCCCGGCCCCAGCCCTGCCGGTCCAGTGTTCCTGACTGAGGTCCGGCTCACATCCGCCCGG
	CCAGGGCTTTCCCCGCCAGCCTCCTGGGTGGAGATTTGTTCATGTCCCACTGGCTACACGGGCCAGT
	TCTGTGAATCCTGTGCTCCGGGATACAAGAGGGAGATGCCACAGGGGGGTCCCTATGCCAGCTGTGT
	CCCCTGCACCTGTAACCAGCATGGCACCTGTGACCCCAACACAGGGATCTGTGTCTGCAGCCACCAT
	ACCGAGGGCCCATCCTGTGAACGCTGTTTGCCAGGTTTCTATGGCAACCCTTTCGCGGGCCAAGCCG
	ACGACTGCCAGCCCTGTCCCTGCCCTGGCCAGTCGGCCTGTACGACCATCCCAGAGAGCGGGGAGGT
	GGTGTGTACCCACTGCCCCCCGGGCCAGAGAGGGCGGCGCTGTGAGGTCTGTGATGATGGCTTTTTT
	GGGGACCCGCTGGGGCTCTTTGGGCACCCCCAGCCCTGCCACCAGTGCCAGTGTAGCGGGAACGTGG
	ACCCCAATGCCGTGGGCAACTGTGACCCCCTGTCTGGCCACTGCCTGCGCTGCCTGCACAACACCAC
	GGGTGACCACTGTGAGCACTGTCAGGAAGGCTTCTACGGGAGCGCCCTGGCCCCTCGACCCGCAGAC
	AAATGCATGCCTTGCAGCTGTCACCCACAGGGCTCGGTCAGTGAGCAGATGCCCTGCGACCCAGTGA
	CAGGCCAATGCTCCTGCCTGCCTCATGTGACTGCACGGGACTGCAGCCGCTGCTACCCTGGCTTCTT
	CGACCTCCAGCCTGGGAGGGGCTGCCGGAGCTGCAAGTGTCACCCACTGGGCTCCCAGGAGGACCAG
	TGCCATCCCAAGACTGGACAGTGCACCTGCCGCCCAGGTGTCACAGGCCAGGCCTGTGACAGGTGCC
	AGCTGGGTTTCTTCGGCTCCTCAATCAAGGGCTGCCGGGCCTGCAGGTGCTCCCCACTGGGCGCTGC
	CTCGGCCCAGTGCCACTATAACGGCACATGCGTGTGCAGGCCTGGCTTCGAGGGCTACAAATGTGAC
	CGCTGCCACTACAACTTCTTCCTCACGGCAGACGGCACACACTGCCAGCAATGTCCGTCCTGCTACG
	CCCTGGTGAAGGAGGAGACAGCCAAGCTGAAGGCCAGACTGACTTTGACGGAGGGGTGGCTCCAAGG
	GTCCGACTGTGGCAGTCCCTGGGGACCACTAGACATTCTGCTGGGAGAGGCCCCAAGGGGGGACGTC
	TACCAGGGCCATCACCTGCTTCCAGGGGCTCGGGAAGCCTTCCTGGAGCAGATGATGGGCCTCGAGG
	GTGCTGTCAAGGCCGCCCGGGAGCAGCTGCAGAGGCTGAACAAGGGTGCCCGCTGTGCCCAGGCCGG
	ATCCCAGAAGACCTGCACCCAGCTGGCAGACCTGGAGGCAGTGCTGGAGTCCTCGGAAGAGGAGATT
	CTGCATGCAGCTGCCATTCTCGCGTCTCTGGAGATTCCTCAGGAAGGTCCCAGTCAGCCGACCAAAT
	GGAGCCACCTGGCCATAGAGGCCCGTGCCCTCGCCAGGAGCCACAGAGACACCGCCACCAAGATCGC
	AGCCACTGCTTGGAGGGCCCTGCTCGCCTCCAACACCAGCTACGCGCTTCTCTGGAATCTGCTGGAG
	GGAAGGGTGGCCCTAGAGACCCAGCGGGACCTGGAGGACAGGTACCAGGAGGTCCAGGCGGCCCAGA
	AAGCACTGAGGACGGCTGTGGCAGAGGTGCTGCCTGAAGCGGAAAGCGTGTTGGCCACCGTGCAGCA
	AGTTGGCGCAGATACAGCCCCGTACCTGGCCTTGCTGGCTTCCCCGGGAGCTCTGCCTCAGAAGTCC
	CGGGCTGAAGACCTGGGCCTGAAGGCGAAGGCCCTGGAGAAGACAGTTGCATCATGGCAGCACATGG
	CCACTGAGGCTGCCCGAACCCTCCAGACTGCTGCCCAGGCGACGCTACGGCAAACAGAACCCCTCAC
	AAAGCTGCACCAGGAGGCCAGAGCCGCCCTGACCCAGGCTTCCTCATCTGTCCAGGCTGCGACAGTG
	ACTGTCATGGGAGCCAGGACTCTGCTGGCTGATCTGGAAGGAATGAAGCTGCAGTTTCCCCGGCCCA
	AGGACCAGGCGGCATTGCAGAGGAAGGCAGACTCCGTCAGTGACAGACTCCTTGCAGACACGAGAAA
	GAAGACCAAGCAGGCGGAGAGGATGCTGGGAAACGCGGCCCCTCTTTCCTCCAGTGCCAAGAAGAAG
	GGCAGAGAAGCAGAGGTGTTGGCCAAGGACAGTGCCAAGCTTGCCAAGGCCTTGCTGAGGGAGCGGA
	AACAGGCGCACCGCCGTGCCAGCAGGCTCACCAGCCAGACGCAAGCCACGCTCCAACAGGCGTCCCA
	GCAGGTGCTGGCGTCTGAAGCACGCAGACAGGAGCTGGAGGAAGCTGAGCGGGTGGGTGCTGGGCTG
	AGCGAGATGGAGCAGCAGATCCGGGAATCGCGTATCTCACTGGAGAAGGACATCGAGACCTTGTCAG
	AGCTGCTTGCCAGGCTGGGGTCGCTGGACACCCATCAAGCCCCAGCCCAGGCCCTGAACGAGACTCA
	GTGGGCACTAGAACGCCTGAGGCTGCAGCTGGGCTCCCCGGGGTCCTTGCAGAGGAAACTCAGTCTG
	CTGGAGCAGGAATCCCAGCAGCAGGAGCTGCAGATCCAGGGCTTCGAGAGTGACCTCGCCGAGATCC
	GCGCCGACAAACAGAACCTGGAGGCCATTCTGCACAGCCTGCCCGAGAACTGTGCCAGCTGGCAGTG
	AGGGCTGCCCAGATCCCCGGCACACACTCCCCCACCTGCTGTTTACATGACCCAGGGGGTGCACACT
	ACCCCACAGGTGTGCCCATACAGACATTCCCCGGAGCCGGCTGCTGTGAACTCGACCCCGTGTGGAT
	AGTCACACTCCCTGCCGATTCTGTCTGTGGCTTCTTCCCTGCCAGCAGGACTGAGTGTGCGTACCCA
	GTTCACCTGGACATGAGTGCACACTCTCACCCCTGCACATGCATAAACGGGCACACCCCAGTGTCAA
	TAACATACACACGTGAGGGTGCATGTCTGTGTGTATGACCCAAATAAAAAAAAAAA
	ORF Start: ATG at 98		ORF Stop: TGA at 4823
	SEQ ID NO: 212	1575 aa	MW at 170827.9 kD
NOV49b,	MAAAALLLGLALLAPRAAGAGMGACYDGAGRPQRCLPVFENAAFGRLAQASHTCGSPPEDFCPHVGA
CG57292-02
Protein Sequence	AGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAFGVQYPTSVNITLRLGKAYEITYVR
	LKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDERVAFCTSEFSDISPLS
	GGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKDPKVLQSYYYAVSDFSVG
	GRCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGTAEAAHECLPCNCSGRSEE
	CTFDRELFRSTGHGGRCHHCRDHTAGPHCERCQENFYHWDPRMPCQPCDCQSAGSLHLQCDDTGTCA
	CKPTVTGWKCDRCLPGFHSLSEGGCRPCTCNPAGSLDTCDPRSGRCPCKENVEGNLCDRCRPGTFNL
	QPHNPAGCSSCFCYGHSKVCASTAQFQVHHILSDFHQGAEGWWARSVGGSEHSPQWSPNGVLLSPED
	EEELTAPGKFLGDQRFSYGQPLILTFRVPPGDSPLPVQLRLEGTGLALSLRHSSLSGPQDARASQGG
	RAQVPLQETSEDVAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGPVFLTEVRLTSARPGLSPPASWV
	EICSCPTGYTGQFCESCAPGYKREMPQGGPYASCVPCTCNQHGTCDPNTGICVCSHHTEGPSCERCL
	PGFYGNPFAGQADDCQPCPCPGQSACTTIPESGEVVCTHCPPGQRGRRCEVCDDGFFGDPLGLFGHP
	QPCHQCQCSGNVDPNAVGNCDPLSGHCLRCLHNTTGDHCEHCQEGFYGSALAPRPADKCMPCSCHPQ
	GSVSEQMPCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGRGCRSCKCHPLGSQEDQCHPKTGQCTC
	RPGVTGQACDRCQLGFFGSSIKGCRACRCSPLGAASAQCHYNGTCVCRPGFEGYKCDRCHYNFFLTA
	DGTHCQQCPSCYALVKEETAKLKARLTLTEGWLQGSDCGSPWGPLDILLGEAPRGDVYQGHHLLPGA
	REAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASL
	EIPQEGPSQPTKWSHLAIEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRD
	LEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAK
	ALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLA
	DLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKD
	SAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRES
	RISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQRKLSLLEQESQQQEL
	QIQGFESDLAEIRADKQNLEAILHSLPENCASWQ

[0631] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 49B.

TABLE 49B
Comparison of NOV49a against NOV49b.
	NOV49a Residues/	Identities/Similarities
Protein Sequence	Match Residues	for the Matched Region
NOV49b	25 . . . 1587	1417/1563 (90%)
	25 . . . 1575	1418/1563 (90%)

[0632] Further analysis of the NOV49a protein yielded the following properties shown in Table 49C.

TABLE 49C
Protein Sequence Properties NOV49a
PSort     0.5517 probability located in outside; 0.1900 probability
analysis: located in lysosome (lumen); 0.1080 probability located in
          nucleus; 0.1000 probability located in endoplasmic reticulum
          (membrane)
SignalP   Cleavage site between residues 20 and 21
analysis:

[0633] A search of the NOV49a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 49D.

TABLE 49D
Geneseq Results for NOV49a
			Identities/
		NOV49a	Similarities
	Protein/	Residues/	for the
Geneseq	Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAM50361	Mouse laminin-15	1 . . . 1587	1587/1587	0.0
	gamma 3 chain—		(100%)
	Mus musculus,	1 . . . 1587	1587/1587
	1587 aa.		(100%)
	[WO200183516-A1,
	8 NOV. 2001]
AAB40917	Human ORFX	1 . . . 1587	1585/1587	0.0
	ORF681 poly-		(99%)
	peptide sequence	1 . . . 1587	1586/1587
	SEQ ID NO:		(99%)
	1362—Homo
	sapiens, 1587 aa.
	[WO200058473-A2,
	5 OCT. 2000]
AAY15458	Human laminin	67 . . . 1587	1493/1524	0.0
	gamma 3 subunit—		(97%)
	Homo sapiens,	1 . . . 1524	1496/1524
	1524 aa.		(97%)
	[WO9919348-A1,
	22 APR. 1999]
AAB19803	Human laminin 2	10 . . . 1583	698/1599	0.0
	gamma-1 chain with		(43%)
	C-terminal FLAG	21 . . . 1600	964/1599
	epitope—Homo		(59%)
	sapiens, 1617 aa.
	[WO200066730-A2,
	9 NOV. 2000]
AAB19801	Human laminin 2	10 . . . 1583	698/1599	0.0
	gamma-1 chain—		(43%)
	Homo sapiens,	21 . . . 1600	964/1599
	1609 aa.		(59%)
	[WO200066730-A2,
	9 NOV. 2000]

[0634] In a BLAST search of public sequence datbases, the NOV49a protein was found to have homology to the proteins shown in the BLASTP data in Table 49E.

TABLE 49E
Public BLASTP Results for NOV49a
			Identities/
		NOV49a	Similarities
Protein/		Residues/	for the
Accession	Protein/	Match	Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9Y6N6	Laminin gamma-3	1 . . . 1587	1587/1587	0.0
	chain precursor		(100%)
	(Laminin 12 gamma	1 . . . 1587	1587/1587
	3)—Homo sapiens		(100%)
	(Human), 1587 aa.
Q9R0B6	Laminin gamma-3	17 . . . 1585	1169/1572	0.0
	chain precursor		(74%)
	(Laminin 12 gamma	26 . . . 1581	1296/1572
	3)—Mus musculus		(82%)
	(Mouse), 1581 aa.
CAC17325	Sequence 25 from	10 . . . 1583	698/1599	0.0
	Patent WO0066730		(43%)
	precursor—Homo	21 . . . 1600	964/1599
	sapiens (Human),		(59%)
	1617 aa.
CAC17323	Sequence 21 from	10 . . . 1583	698/1599	0.0
	Patent WO0066730		(43%)
	precursor—Homo	21 . . . 1600	964/1599
	sapiens (Human),		(59%)
	1609 aa.
P11047	Laminin gamma-1	10 . . . 1583	697/1599	0.0
	chain precursor		(43%)
	(Laminin B2	21 . . . 1600	963/1599
	chain)—Homo		(59%)
	sapiens (Human),
	1609 aa.

[0635] PFam analysis predicts that the NOV49a protein contains the domains shown in the Table 49F.

TABLE 49F
Domain Analysis of NOV49a
Pfam	NOV49a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
laminin_Nterm	35 . . . 269	108/264 (41%)	2.3e−110
		182/264 (69%)
laminin_EGF	271 . . . 324	17/63 (27%)	3.4e−10
		43/63 (68%)
laminin_EGF	327 . . . 380	18/61 (30%)	2e−13
		49/61 (80%)
laminin_EGF	383 . . . 427	27/59 (46%)	5e−11
		35/59 (59%)
laminin_EGF	430 . . . 477	28/61 (46%)	1.8e−14
		46/61 (75%)
laminin_B	541 . . . 671	44/152 (29%)	1.6e−09
		86/152 (57%)
laminin_EGF	707 . . . 752	22/60 (37%)	2.3e−12
		39/60 (65%)
laminin_EGF	755 . . . 807	17/61 (28%)	0.0069
		32/61 (52%)
laminin_EGF	810 . . . 863	18/61 (30%)	2.2e−15
		45/61 (74%)
laminin_EGF	866 . . . 914	27/60 (45%)	1.3e−16
		43/60 (72%)
laminin_EGF	917 . . . 962	24/59 (41%)	2e−15
		39/59 (66%)
laminin_EGF	965 . . . 1013	18/59 (31%)	2e−07
		37/59 (63%)

Example 50

[0636] The NOV50 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 50A.

TABLE 50A
NOV50 Sequence Analysis
	SEQ ID NO: 213	942 bp
NOV50a,	CCCCGGCTGCTTCTGCTCTTTCTGGTTCCGCTGCTGTGGGCCCCGGCTGCGGTCCGGGCCGGCCCAG
CG97715-01
DNA Sequence	ATGAAGACCTTAGCCACCGGAACAAAGAACCGCCGGCGCCGGCCCAGCAGCTGCAGCCGCAGCCTGT
	GGCTGTGCAGGGCCCCGAGCCGGCCCGGGTCGAGAAAATATTTACACCAGCAGCTCCAGTTCATACC
	AATAAAGAAGATCCTGCTACCCAAACTAATTTGGGATTTATCCATGCATTTGTCGCTGCCATATCAG
	TTATTATTGTATCTGAATTGGGTGATAAGACATTTTTTATAGCAGCCATCATGGCAATGCGCTATAA
	CCGCCTGACCGTGCTGGCTGGTGCAATGCTTGCCTTGGGACTAATGACATGCTTGTCAGTTTTGTTT
	GGCTATGCCACCACAGTCATCCCCAGGGTCTATACATACTATGTTTCAACTGTATTATTTGCCATTT
	TTGGCATTAGAATGCTTCGGGAAGGCTTAAAGATGAGCCCTGATGAGGGTCAAGAGGAACTGGAAGA
	AGTTCAAGCTGAATTAAAGAAGAAAGATGAAGAATTTCAACGAACCAAACTTTTAAATGGACCGGGA
	GATGTTGAAACGGGTACAAGCATAACAGTACCTCAGAAAAAGTGGTTGCATTTTATTTCACCCATTT
	TTGTTCAAGCTCTTACATTAACATTCTTAGCAGAATGGGGTGATCGCTCTCAACTAACTACAATTGT
	ATTGGCAGCTAGAGAGGACCCCTATGGTGTAGCCGTGGGTGGAACTGTGGGGCACTGCCTGTGCACG
	GGATTGGCAGTAATTGGAGGAAGAATGATAGCACAGAAAATCTCTGTCAGAACTGTGACAATCATAG
	GAGGCATCGTTTTTTTGGCGTTTGCATTTTCTGCACTATTTATAAGGCCTGATTCTGGTTTTTAACA
	AGCT
	ORF Start: at 1		ORF Stop: TAA at 934
	SEQ ID NO: 214	311 aa	MW at 33848.2 kD
NOV50a,	PRLLLLFLVPLLWAPAAVRAGPDEDLSHRNKEPPAPAQQLQPQPVAVQGPEPARVEKIFTPAAPVHT
CG97715-01
Protein Sequence	NKEDPATQTNLGFIHAFVAAISVIIVSELGDKTFFIAAIMAMRYNRLTVLAGAMLALGLMTCLSVLF
	GYATTVIPRVYTYYVSTVLFAIFGIRMLREGLKMSPDEGQEELEEVQAELKKKDEEFQRTKLLNGPG
	DVETGTSITVPQKKWLHFISPIFVQALTLTFLAEWGDRSQLTTIVLAAREDPYGVAVGGTVGHCLCT
	GLAVIGGRMIAQKISVRTVTIIGGIVFLAFAFSALFIRPDSGF

[0637] Further analysis of the NOV50a protein yielded the following properties shown in Table 50B.

TABLE 50B
Protein Sequence Properties NOV50a
PSort     0.6400 probability located in plasma membrane; 0.4600
analysis: probability located in Golgi body; 0.3700 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 21 and 22
analysis:

[0638] A search of the NOV50a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 50C.

TABLE 50C
Geneseq Results for NOV50a
		NOV50a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB90211	Human poly-	1 . . . 311	310/311 (99%)	e−176
	peptide SEQ ID	14 . . . 324	310/311 (99%)
	NO 2587—Homo
	sapiens, 324 aa.
	[WO200190304-
	A2, 29 NOV.
	2001]
AAB51239	Human hTMPT27	1 . . . 311	310/311 (99%)	e−176
	protein sequence	14 . . . 324	310/311 (99%)
	SEQ ID NO: 7—
	Homo sapiens,
	324 aa.
	[CN1268567-A,
	4 OCT. 2000]
AAB20092	Human hydro-	1 . . . 311	310/311 (99%)	e−176
	phobic domain-	14 . . . 324	310/311 (99%)
	containing protein
	HP03373—Homo
	sapiens, 324 aa.
	[WO200100824-
	A2, 4 JAN. 2001]
AAB41971	Human ORFX	1 . . . 311	310/311 (99%)	e−176
	ORF1735 poly-	12 . . . 322	310/311 (99%)
	peptide sequence
	SEQ ID NO:
	3470—Homo
	sapiens, 322 aa.
	[WO200058473-
	A2, 5 OCT.
	2000]
ABB57033	Mouse ischaemic	2 . . . 311	282/310 (90%)	e−158
	condition related	15 . . . 323	288/310 (91%)
	protein sequence
	SEQ ID NO:
	39—Mus
	musculus, 323 aa.
	[WO200188188-
	A2, 22 NOV.
	2001]

[0639] In a BLAST search of public sequence datbases, the NOV50a protein was found to have homology to the proteins shown in the BLASTP data in Table 50D.

TABLE 50D
Public BLASTP Results for NOV50a
		NOV50a	Identities/
Protein/		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
Q9HC07	Transmembrane	1 . . . 311	310/311 (99%)	e−176
	protein PT27—	14 . . . 324	310/311 (99%)
	Homo sapiens
	(Human), 324 aa.
Q9NZ34	Uncharacterized	1 . . . 311	310/311 (99%)	e−176
	hypothalamus	14 . . . 324	310/311 (99%)
	protein HTMP—
	Homo sapiens
	(Human), 324 aa.
Q9R292	TPARDL—	12 . . . 311	287/310 (92%)	e−161
	Mus musculus	15 . . . 323	293/310 (93%)
	(Mouse), 323 aa.
P52875	Transmembrane	2 . . . 311	282/310 (90%)	e−158
	protein PFT27	15 . . . 323	288/310 (91%)
	(TPA regulated
	locus protein)—
	Mus musculus
	(Mouse), 323 aa.
AAM21311	Transmembrane	41 . . . 311	216/272 (79%)	e−118
	protein HTP-1—	34 . . . 305	236/272 (86%)
	Brachydanio
	rerio (Zebrafish)
	(Danio rerio),
	305 aa.

[0640] PFam analysis predicts that the NOV50a protein contains the domains shown in the Table 50E.

TABLE 50E
Domain Analysis of NOV50a
Pfam	NOV50a	Identities/Similarities	Expect
Domain	Match Region	for the Matched Region	Value
UPF0016	84 . . . 158	36/76 (47%)	9.9e−39
		74/76 (97%)
UPF0016	224 . . . 299	42/76 (55%)	8.1e−44
		76/76 (100%)

Example B

Sequencing Methodology and Identification of NOVX Clones

[0641] 1. GeneCalling™ Technology: This is a proprietary method of performing differential gene expression profiling between two or more samples developed at CuraGen and described by Shimkets, et al., “Gene expression analysis by transcript profiling coupled to a gene database query” Nature Biotechnology 17:198-803 (1999). cDNA was derived from various human samples representing multiple tissue types, normal and diseased states, physiological states, and developmental states from different donors. Samples were obtained as whole tissue, primary cells or tissue cultured primary cells or cell lines. Cells and cell lines may have been treated with biological or chemical agents that regulate gene expression, for example, growth factors, chemokines or steroids. The cDNA thus derived was then digested with up to as many as 120 pairs of restriction enzymes and pairs of linker-adaptors specific for each pair of restriction enzymes were ligated to the appropriate end. The restriction digestion generates a mixture of unique cDNA gene fragments. Limited PCR amplification is performed with primers homologous to the linker adapter sequence where one primer is biotinylated and the other is fluorescently labeled. The doubly labeled material is isolated and the fluorescently labeled single strand is resolved by capillary gel electrophoresis. A computer algorithm compares the electropherograms from an experimental and control group for each of the restriction digestions. This and additional sequence-derived information is used to predict the identity of each differentially expressed gene fragment using a variety of genetic databases. The identity of the gene fragment is confirmed by additional, gene-specific competitive PCR or by isolation and sequencing of the gene fragment.

[0642] 2. SeqCalling™ Technology: cDNA was derived from various human samples representing multiple tissue types, normal and diseased states, physiological states, and developmental states from different donors. Samples were obtained as whole tissue, primary cells or tissue cultured primary cells or cell lines. Cells and cell lines may have been treated with biological or chemical agents that regulate gene expression, for example, growth factors, chemokines or steroids. The cDNA thus derived was then sequenced using CuraGen's proprietary SeqCalling technology. Sequence traces were evaluated manually and edited for corrections if appropriate. cDNA sequences from all samples were assembled together, sometimes including public human sequences, using bioinformatic programs to produce a consensus sequence for each assembly. Each assembly is included in CuraGen Corporation's database. Sequences were included as components for assembly when the extent of identity with another component was at least 95% over 50 bp. Each assembly represents a gene or portion thereof and includes information on variants, such as splice forms single nucleotide polymorphisms (SNPs), insertions, deletions and other sequence variations.

[0643] 3. PathCalling™ Technology: The NOVX nucleic acid sequences are derived by laboratory screening of cDNA library by the two-hybrid approach. cDNA fragments covering either the full length of the DNA sequence, or part of the sequence, or both, are sequenced. In silico prediction was based on sequences available in CuraGen Corporation's proprietary sequence databases or in the public human sequence databases, and provided either the full length DNA sequence, or some portion thereof.

[0644] The laboratory screening was performed using the methods summarized below:

[0645] cDNA libraries were derived from various human samples representing multiple tissue types, normal and diseased states, physiological states, and developmental states from different donors. Samples were obtained as whole tissue, primary cells or tissue cultured primary cells or cell lines. Cells and cell lines may have been treated with biological or chemical agents that regulate gene expression, for example, growth factors, chemokines or steroids. The cDNA thus derived was then directionally cloned into the appropriate two-hybrid vector (Gal4-activation domain (Gal4-AD) fusion). Such cDNA libraries as well as commercially available cDNA libraries from Clontech (Palo Alto, Calif.) were then transferred from E. coli into a CuraGen Corporation proprietary yeast strain (disclosed in U.S. Pat. Nos. 6,057,101 and 6,083,693, incorporated herein by reference in their entireties).

[0646] Gal4-binding domain (Gal4-BD) fusions of a CuraGen Corportion proprietary library of human sequences was used to screen multiple Gal4-AD fusion cDNA libraries resulting in the selection of yeast hybrid diploids in each of which the Gal4-AD fusion contains an individual cDNA. Each sample was amplified using the polymerase chain reaction (PCR) using non-specific primers at the cDNA insert boundaries. Such PCR product was sequenced; sequence traces were evaluated manually and edited for corrections if appropriate. cDNA sequences from all samples were assembled together, sometimes including public human sequences, using bioinformatic programs to produce a consensus sequence for each assembly. Each assembly is included in CuraGen Corporation's database. Sequences were included as components for assembly when the extent of identity with another component was at least 95% over 50 bp. Each assembly represents a gene or portion thereof and includes information on variants, such as splice forms single nucleotide polymorphisms (SNPs), insertions, deletions and other sequence variations.

[0647] Physical clone: the cDNA fragment derived by the screening procedure, covering the entire open reading frame is, as a recombinant DNA, cloned into pACT2 plasmid (Clontech) used to make the cDNA library. The recombinant plasmid is inserted into the host and selected by the yeast hybrid diploid generated during the screening procedure by the mating of both CuraGen Corporation proprietary yeast strains N106′ and YULH (U.S. Pat. Nos. 6,057,101 and 6,083,693).

[0648] 4. RACE: Techniques based on the polymerase chain reaction such as rapid amplification of cDNA ends (RACE), were used to isolate or complete the predicted sequence of the cDNA of the invention. Usually multiple clones were sequenced from one or more human samples to derive the sequences for fragments. Various human tissue samples from different donors were used for the RACE reaction. The sequences derived from these procedures were included in the SeqCalling Assembly process described in preceding paragraphs.

[0649] 5. Exon Linking: The NOVX target sequences identified in the present invention were subjected to the exon linking process to confirm the sequence. PCR primers were designed by starting at the most upstream sequence available, for the forward primer, and at the most downstream sequence available for the reverse primer. In each case, the sequence was examined, walking inward from the respective termini toward the coding sequence, until a suitable sequence that is either unique or highly selective was encountered, or, in the case of the reverse primer, until the stop codon was reached. Such primers were designed based on in silico predictions for the full length cDNA, part (one or more exons) of the DNA or protein sequence of the target sequence, or by translated homology of the predicted exons to closely related human sequences from other species. These primers were then employed in PCR amplification based on the following pool of human cDNAs: adrenal gland, bone marrow, brain—amygdala, brain—cerebellum, brain—hippocampus, brain—substantia nigra, brain—thalamus, brain—whole, fetal brain, fetal kidney, fetal liver, fetal lung, heart, kidney, lymphoma—Raji, mammary gland, pancreas, pituitary gland, placenta, prostate, salivary gland, skeletal muscle, small intestine, spinal cord, spleen, stomach, testis, thyroid, trachea, uterus. Usually the resulting amplicons were gel purified, cloned and sequenced to high redundancy. The PCR product derived from exon linking was cloned into the pCR2.1 vector from Invitrogen. The resulting bacterial clone has an insert covering the entire open reading frame cloned into the pCR2.1 vector. The resulting sequences from all clones were assembled with themselves, with other fragments in CuraGen Corporation's database and with public ESTs. Fragments and ESTs were included as components for an assembly when the extent of their identity with another component of the assembly was at least 95% over 50 bp. In addition, sequence traces were evaluated manually and edited for corrections if appropriate. These procedures provide the sequence reported herein.

[0650] 6. Physical Clone: Exons were predicted by homology and the intron/exon boundaries were determined using standard genetic rules. Exons were further selected and refined by means of similarity determination using multiple BLAST (for example, tBlastN, BlastX, and BlastN) searches, and, in some instances, GeneScan and Grail. Expressed sequences from both public and proprietary databases were also added when available to further define and complete the gene sequence. The DNA sequence was then manually corrected for apparent inconsistencies thereby obtaining the sequences encoding the full-length protein.

[0651] The PCR product derived by exon linking, covering the entire open reading frame, was cloned into the pCR2.1 vector from Invitrogen to provide clones used for expression and screening purposes.

Example C

Quantitative Expression Analysis of Clones in Various cells and Tissues

[0652] The quantitative expression of various clones was assessed using microtiter plates containing RNA samples from a variety of normal and pathology-derived cells, cell lines and tissues using real time quantitative PCR (RTQ PCR). RTQ PCR was performed on an Applied Biosystems ABI PRISM® 7700 or an ABI PRISM® 7900 HT Sequence Detection System. Various collections of samples are assembled on the plates, and referred to as Panel 1 (containing normal tissues and cancer cell lines), Panel 2 (containing samples derived from tissues from normal and cancer sources), Panel 3 (containing cancer cell lines), Panel 4 (containing cells and cell lines from normal tissues and cells related to inflammatory conditions), Panel 5D/51 (containing human tissues and cell lines with an emphasis on metabolic diseases), AI_comprehensive_panel (containing normal tissue and samples from autoinflammatory diseases), Panel CNSD.01 (containing samples from normal and diseased brains) and CNS_neurodegeneration_panel (containing samples from normal and Alzheimer's diseased brains).

[0653] RNA integrity from all samples is controlled for quality by visual assessment of agarose gel electropherograms using 28S and 18S ribosomal RNA staining intensity ratio as a guide (2:1 to 2.5:1 28s:18s) and the absence of low molecular weight RNAs that would be indicative of degradation products. Samples are controlled against genomic DNA contamination by RTQ PCR reactions run in the absence of reverse transcriptase using probe and primer sets designed to amplify across the span of a single exon.

[0654] First, the RNA samples were normalized to reference nucleic acids such as constitutively expressed genes (for example, β-actin and GAPDH). Normalized RNA (5 ul) was converted to cDNA and analyzed by RTQ-PCR using One Step RT-PCR Master Mix Reagents (Applied Biosystems; Catalog No. 4309169) and gene-specific primers according to the manufacturer's instructions.

[0655] In other cases, non-normalized RNA samples were converted to single strand cDNA (sscDNA) using Superscript II (Invitrogen Corporation; Catalog No. 18064-147) and random hexamers according to the manufacturer's instructions. Reactions containing up to 10 μg of total RNA were performed in a volume of 20 μl and incubated for 60 minutes at 42° C. This reaction can be scaled up to 50 μg of total RNA in a final volume of 100 μl. sscDNA samples are then normalized to reference nucleic acids as described previously, using 1×TaqMan® Universal Master mix (Applied Biosystems; catalog No. 4324020), following the manufacturer's instructions.

[0656] Probes and primers were designed for each assay according to Applied Biosystems Primer Express Software package (version I for Apple Computer's Macintosh Power PC) or a similar algorithm using the target sequence as input. Default settings were used for reaction conditions and the following parameters were set before selecting primers: primer concentration=250 nM, primer melting temperature (Tm) range=58°-60° C., primer optimal Tm=59° C., maximum primer difference=2° C., probe does not have 5′G, probe Tm must be 10° C. greater than primer Tm, amplicon size 75 bp to 100 bp. The probes and primers selected (see below) were synthesized by Synthegen (Houston, Tex., USA). Probes were double purified by HPLC to remove uncoupled dye and evaluated by mass spectroscopy to verify coupling of reporter and quencher dyes to the 5′ and 3′ ends of the probe, respectively. Their final concentrations were: forward and reverse primers, 900 nM each, and probe, 200 nM.

[0657] PCR conditions: When working with RNA samples, normalized RNA from each tissue and each cell line was spotted in each well of either a 96 well or a 384-well PCR plate (Applied Biosystems). PCR cocktails included either a single gene specific probe and primers set, or two multiplexed probe and primers sets (a set specific for the target clone and another gene-specific set multiplexed with the target probe). PCR reactions were set up using TaqMan® One-Step RT-PCR Master Mix (Applied Biosystems, Catalog No. 4313803) following manufacturer's instructions. Reverse transcription was performed at 48° C. for 30 minutes followed by amplification/PCR cycles as follows: 95° C. 10 min, then 40 cycles of 95° C. for 15 seconds, 60° C. for 1 minute. Results were recorded as CT values (cycle at which a given sample crosses a threshold level of fluorescence) using a log scale, with the difference in RNA concentration between a given sample and the sample with the lowest CT value being represented as 2 to the power of delta CT. The percent relative expression is then obtained by taking the reciprocal of this RNA difference and multiplying by 100.

[0658] When working with sscDNA samples, normalized sscDNA was used as described previously for RNA samples. PCR reactions containing one or two sets of probe and primers were set up as described previously, using 1×TaqMan® Universal Master mix (Applied Biosystems; catalog No. 4324020), following the manufacturer's instructions. PCR amplification was performed as follows: 95° C. 10 min, then 40 cycles of 95° C. for 15 seconds, 60° C. for 1 minute. Results were analyzed and processed as described previously.

[0659] Panels 1, 1.1, 1.2, and 1.3D

[0660] The plates for Panels 1, 1.1, 1.2 and 1.3D include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in these panels are broken into 2 classes: samples derived from cultured cell lines and samples derived from primary normal tissues. The cell lines are derived from cancers of the following types: lung cancer, breast cancer, melanoma, colon cancer, prostate cancer, CNS cancer, squamous cell carcinoma, ovarian cancer, liver cancer, renal cancer, gastric cancer and pancreatic cancer. Cell lines used in these panels are widely available through the American Type Culture Collection (ATCC), a repository for cultured cell lines, and were cultured using the conditions recommended by the ATCC. The normal tissues found on these panels are comprised of samples derived from all major organ systems from single adult individuals or fetuses. These samples are derived from the following organs: adult skeletal muscle, fetal skeletal muscle, adult heart, fetal heart, adult kidney, fetal kidney, adult liver, fetal liver, adult lung, fetal lung, various regions of the brain, the spleen, bone marrow, lymph node, pancreas, salivary gland, pituitary gland, adrenal gland, spinal cord, thymus, stomach, small intestine, colon, bladder, trachea, breast, ovary, uterus, placenta, prostate, testis and adipose.

[0661] In the results for Panels 1, 1.1, 1.2 and 1.3D, the following abbreviations are used:

[0662] ca.=carcinoma,

[0663] *=established from metastasis,

[0664] met=metastasis,

[0665] s cell var=small cell variant,

[0666] non-s=non-sm=non-small,

[0667] squam=squamous,

[0668] pl.eff=pl effusion=pleural effusion,

[0669] glio=glioma,

[0670] astro=astrocytoma, and

[0671] neuro=neuroblastoma.

[0672] General_screening_panel_v1.4, v1.5 and v1.6

[0673] The plates for Panels 1.4, 1.5, and 1.6 include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in Panels 1.4, 1.5, and 1.6 are broken into 2 classes: samples derived from cultured cell lines and samples derived from primary normal tissues. The cell lines are derived from cancers of the following types: lung cancer, breast cancer, melanoma, colon cancer, prostate cancer, CNS cancer, squamous cell carcinoma, ovarian cancer, liver cancer, renal cancer, gastric cancer and pancreatic cancer. Cell lines used in Panels 1.4, 1.5, and 1.6 are widely available through the American Type Culture Collection (ATCC), a repository for cultured cell lines, and were cultured using the conditions recommended by the ATCC. The normal tissues found on Panels 1.4, 1.5, and 1.6 are comprised of pools of samples derived from all major organ systems from 2 to 5 different adult individuals or fetuses. These samples are derived from the following organs: adult skeletal muscle, fetal skeletal muscle, adult heart, fetal heart, adult kidney, fetal kidney, adult liver, fetal liver, adult lung, fetal lung, various regions of the brain, the spleen, bone marrow, lymph node, pancreas, salivary gland, pituitary gland, adrenal gland, spinal cord, thymus, stomach, small intestine, colon, bladder, trachea, breast, ovary, uterus, placenta, prostate, testis and adipose. Abbreviations are as described for Panels 1, 1.1, 1.2, and 1.3D.

[0674] Panels 2D, 2.2, 2.3 and 2.4

[0675] The plates for Panels 2D, 2.2, 2.3 and 2.4 generally include 2 control wells and 94 test samples composed of RNA or cDNA isolated from human tissue procured by surgeons working in close cooperation with the National Cancer Institute's Cooperative Human Tissue Network (CHTN) or the National Disease Research Initiative (NDRI) or from Ardais or Clinomics). The tissues are derived from human malignancies and in cases where indicated many malignant tissues have “matched margins” obtained from noncancerous tissue just adjacent to the tumor. These are termed normal adjacent tissues and are denoted “NAT” in the results below. The tumor tissue and the “matched margins” are evaluated by two independent pathologists (the surgical pathologists and again by a pathologist at NDRI/CHTN/Ardais/Clinomics). Unmatched RNA samples from tissues without malignancy (normal tissues) were also obtained from Ardais or Clinomics. This analysis provides a gross histopathological assessment of tumor differentiation grade. Moreover, most samples include the original surgical pathology report that provides information regarding the clinical stage of the patient. These matched margins are taken from the tissue surrounding (i.e. immediately proximal) to the zone of surgery (designated “NAT”, for normal adjacent tissue, in Table RR). In addition, RNA and cDNA samples were obtained from various human tissues derived from autopsies performed on elderly people or sudden death victims (accidents, etc.). These tissues were ascertained to be free of disease and were purchased from various commercial sources such as Clontech (Palo Alto, Calif.), Research Genetics, and Invitrogen.

[0676] HASS Panel v 1.0

[0677] The HASS panel v 1.0 plates are comprised of 93 cDNA samples and two controls. Specifically, 81 of these samples are derived from cultured human cancer cell lines that had been subjected to serum starvation, acidosis and anoxia for different time periods as well as controls for these treatments, 3 samples of human primary cells, 9 samples of malignant brain cancer (4 medulloblastomas and 5 glioblastomas) and 2 controls. The human cancer cell lines are obtained from ATCC (American Type Culture Collection) and fall into the following tissue groups: breast cancer, prostate cancer, bladder carcinomas, pancreatic cancers and CNS cancer cell lines. These cancer cells are all cultured under standard recommended conditions. The treatments used (serum starvation, acidosis and anoxia) have been previously published in the scientific literature. The primary human cells were obtained from Clonetics (Walkersville, Md.) and were grown in the media and conditions recommended by Clonetics. The malignant brain cancer samples are obtained as part of a collaboration (Henry Ford Cancer Center) and are evaluated by a pathologist prior to CuraGen receiving the samples. RNA was prepared from these samples using the standard procedures. The genomic and chemistry control wells have been described previously.

[0678] ARDAIS Panel v 1.0

[0679] The plates for ARDAIS panel v 1.0 generally include 2 control wells and 22 test samples composed of RNA isolated from human tissue procured by surgeons working in close cooperation with Ardais Corporation. The tissues are derived from human lung malignancies (lung adenocarcinoma or lung squamous cell carcinoma) and in cases where indicated many malignant samples have “matched margins” obtained from noncancerous lung tissue just adjacent to the tumor. These matched margins are taken from the tissue surrounding (i.e. immediately proximal) to the zone of surgery (designated “NAT”, for normal adjacent tissue) in the results below. The tumor tissue and the “matched margins” are evaluated by independent pathologists (the surgical pathologists and again by a pathologist at Ardais). Unmatched malignant and non-malignant RNA samples from lungs were also obtained from Ardais. Additional information from Ardais provides a gross histopathological assessment of tumor differentiation grade and stage. Moreover, most samples include the original surgical pathology report that provides information regarding the clinical state of the patient.

[0680] Panel 3D, 3.1 and 3.2

[0681] The plates of Panel 3D, 3.1, and 3.2 are comprised of 94 cDNA samples and two control samples. Specifically, 92 of these samples are derived from cultured human cancer cell lines, 2 samples of human primary cerebellar tissue and 2 controls. The human cell lines are generally obtained from ATCC (American Type Culture Collection), NCI or the German tumor cell bank and fall into the following tissue groups: Squamous cell carcinoma of the tongue, breast cancer, prostate cancer, melanoma, epidermoid carcinoma, sarcomas, bladder carcinomas, pancreatic cancers, kidney cancers, leukemias/lymphomas, ovarian/uterine/cervical, gastric, colon, lung and CNS cancer cell lines. In addition, there are two independent samples of cerebellum. These cells are all cultured under standard recommended conditions and RNA extracted using the standard procedures. The cell lines in panel 3D, 3.1, 3.2, 1, 1.1., 1.2, 1.3D, 1.4, 1.5, and 1.6 are of the most common cell lines used in the scientific literature.

[0682] Panels 4D, 4R, and 4.1D

[0683] Panel 4 includes samples on a 96 well plate (2 control wells, 94 test samples) composed of RNA (Panel 4R) or cDNA (Panels 4D/4.1D) isolated from various human cell lines or tissues related to inflammatory conditions. Total RNA from control normal tissues such as colon and lung (Stratagene, La Jolla, Calif.) and thymus and kidney (Clontech) was employed. Total RNA from liver tissue from cirrhosis patients and kidney from lupus patients was obtained from BioChain (Biochain Institute, Inc., Hayward, Calif.). Intestinal tissue for RNA preparation from patients diagnosed as having Crohn's disease and ulcerative colitis was obtained from the National Disease Research Interchange (NDRI) (Philadelphia, Pa.).

[0684] Astrocytes, lung fibroblasts, dermal fibroblasts, coronary artery smooth muscle cells, small airway epithelium, bronchial epithelium, microvascular dermal endothelial cells, microvascular lung endothelial cells, human pulmonary aortic endothelial cells, human umbilical vein endothelial cells were all purchased from Clonetics (Walkersville, Md.) and grown in the media supplied for these cell types by Clonetics. These primary cell types were activated with various cytokines or combinations of cytokines for 6 and/or 12-14 hours, as indicated. The following cytokines were used; IL-1 beta at approximately 1-5 ng/ml, TNF alpha at approximately 5-10 ng/ml, WN gamma at approximately 20-50 ng/ml, IL-4 at approximately 5-10 ng/ml, IL-9 at approximately 5-10 ng/ml, IL-13 at approximately 5-10 ng/ml. Endothelial cells were sometimes starved for various times by culture in the basal media from Clonetics with 0.1% serum.

[0685] Mononuclear cells were prepared from blood of employees at CuraGen Corporation, using Ficoll. LAK cells were prepared from these cells by culture in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco/Life Technologies, Rockville, Md.), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco) and Interleukin 2 for 4-6 days. Cells were then either activated with 10-20 ng/ml PMA and 1-21 g/ml ionomycin, IL-12 at 5-10 ng/ml, IFN gamma at 20-50 ng/ml and IL-18 at 5-10 ng/ml for 6 hours. In some cases, mononuclear cells were cultured for 4-5 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco) with PHA (phytohemagglutinin) or PWM (pokeweed mitogen) at approximately 5 μg/ml. Samples were taken at 24, 48 and 72 hours for RNA preparation. MLR (mixed lymphocyte reaction) samples were obtained by taking blood from two donors, isolating the mononuclear cells using Ficoll and mixing the isolated mononuclear cells 1:1 at a final concentration of approximately 2×106cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol (5.5×10−5M) (Gibco), and 10 mM Hepes (Gibco). The MLR was cultured and samples taken at various time points ranging from 1-7 days for RNA preparation.

[0686] Monocytes were isolated from mononuclear cells using CD14 Miltenyi Beads, +ve VS selection columns and a Vario Magnet according to the manufacturer's instructions. Monocytes were differentiated into dendritic cells by culture in DMEM 5% fetal calf serum (FCS) (Hyclone, Logan, Utah), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco), 50 ng/ml GMCSF and 5 ng/ml IL-4 for 5-7 days. Macrophages were prepared by culture of monocytes for 5-7 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), 10 mM Hepes (Gibco) and 10% AB Human Serum or MCSF at approximately 50 ng/ml. Monocytes, macrophages and dendritic cells were stimulated for 6 and 12-14 hours with lipopolysaccharide (LPS) at 1O0 ng/ml. Dendritic cells were also stimulated with anti-CD40 monoclonal antibody (Pharmingen) at 10 μg/ml for 6 and 12-14 hours.

[0687] CD4 lymphocytes, CD8 lymphocytes and NK cells were also isolated from mononuclear cells using CD4, CD8 and CD56 Miltenyi beads, positive VS selection columns and a Vario Magnet according to the manufacturer's instructions. CD45RA and CD45RO CD4 lymphocytes were isolated by depleting mononuclear cells of CD8, CD56, CD14 and CD19 cells using CD8, CD56, CD14 and CD19 Miltenyi beads and positive selection. CD45RO beads were then used to isolate the CD45RO CD4 lymphocytes with the remaining cells being CD45RA CD4 lymphocytes. CD45RA CD4, CD45RO CD4 and CD8 lymphocytes were placed in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco) and plated at 106cells/ml onto Falcon 6 well tissue culture plates that had been coated overnight with 0.5 μg/ml anti-CD28 (Pharmingen) and 3 ug/ml anti-CD3 (OKT3, ATCC) in PBS. After 6 and 24 hours, the cells were harvested for RNA preparation. To prepare chronically activated CD8 lymphocytes, we activated the isolated CD8 lymphocytes for 4 days on anti-CD28 and anti-CD3 coated plates and then harvested the cells and expanded them in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10M (Gibco), and 10 mM Hepes (Gibco) and IL-2. The expanded CD8 cells were then activated again with plate bound anti-CD3 and anti-CD28 for 4 days and expanded as before. RNA was isolated 6 and 24 hours after the second activation and after 4 days of the second expansion culture. The isolated NK cells were cultured in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco) and IL-2 for 4-6 days before RNA was prepared.

[0688] To obtain B cells, tonsils were procured from NDRI. The tonsil was cut up with sterile dissecting scissors and then passed through a sieve. Tonsil cells were then spun down and resupended at 106cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco). To activate the cells, we used PWM at 5 μg/ml or anti-CD40 (Pharmingen) at approximately 10 μg/ml and IL-4 at 5-10 ng/ml. Cells were harvested for RNA preparation at 24, 48 and 72 hours.

[0689] To prepare the primary and secondary Th1/Th2 and Tr1 cells, six-well Falcon plates were coated overnight with 10 μg/ml anti-CD28 (Pharmingen) and 2 μg/ml OKT3 (ATCC), and then washed twice with PBS. Umbilical cord blood CD4 lymphocytes (Poietic Systems, German Town, Md.) were cultured at 105-106cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), 10 mM Hepes (Gibco) and IL-2 (4 ng/ml). IL-12 (5 ng/ml) and anti-IL4 (1 μg/ml) were used to direct to Th1, while IL-4 (5 ng/ml) and anti-IFN gamma (lug/ml) were used to direct to Th2 and IL-10 at 5 ng/ml was used to direct to Tr1. After 4-5 days, the activated Th1, Th2 and Tr1 lymphocytes were washed once in DMEM and expanded for 4-7 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×105M (Gibco), 10 mM Hepes (Gibco) and IL-2 (1 ng/ml). Following this, the activated Th1, Th2 and Tr1 lymphocytes were re-stimulated for 5 days with anti-CD28/OKT3 and cytokines as described above, but with the addition of anti-CD95L (1 μg/ml) to prevent apoptosis. After 4-5 days, the Th1, Th2 and Tr1 lymphocytes were washed and then expanded again with IL-2 for 4-7 days. Activated Th1 and Th2 lymphocytes were maintained in this way for a maximum of three cycles. RNA was prepared from primary and secondary Th1, Th2 and Tr1 after 6 and 24 hours following the second and third activations with plate bound anti-CD3 and anti-CD28 mAbs and 4 days into the second and third expansion cultures in Interleukin 2.

[0690] The following leukocyte cells lines were obtained from the ATCC: Ramos, EOL-1, KU-812. EOL cells were further differentiated by culture in 0.1 mM dbcAMP at 5×105cells/ml for 8 days, changing the media every 3 days and adjusting the cell concentration to 5×105 cells/ml. For the culture of these cells, we used DMEM or RPMI (as recommended by the ATCC), with the addition of 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), 10 mM Hepes (Gibco). RNA was either prepared from resting cells or cells activated with PMA at 10 ng/ml and ionomycin at 1 μg/ml for 6 and 14 hours. Keratinocyte line CCD106 and an airway epithelial tumor line NCI-H292 were also obtained from the ATCC. Both were cultured in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco). CCD1106 cells were activated for 6 and 14 hours with approximately 5 ng/ml TNF alpha and 1 ng/ml IL-1 beta, while NCI-H292 cells were activated for 6 and 14 hours with the following cytokines: 5 ng/ml IL-4, 5 ng/ml IL-9, 5 ng/ml IL-13 and 25 ng/ml IFN gamma.

[0691] For these cell lines and blood cells, RNA was prepared by lysing approximately 107cells/ml using Trizol (Gibco BRL). Briefly, {fraction (1/10)} volume of bromochloropropane (Molecular Research Corporation) was added to the RNA sample, vortexed and after 10 minutes at room temperature, the tubes were spun at 14,000 rpm in a Sorvall SS34 rotor. The aqueous phase was removed and placed in a 15 ml Falcon Tube. An equal volume of isopropanol was added and left at −20° C. overnight. The precipitated RNA was spun down at 9,000 rpm for 15 min in a Sorvall SS34 rotor and washed in 70% ethanol. The pellet was redissolved in 300 μl of RNAse-free water and 35 μl buffer (Promega) 5 μl DTT, 7 μl RNAsin and 8 μl DNAse were added. The tube was incubated at 37° C. for 30 minutes to remove contaminating genomic DNA, extracted once with phenol chloroform and re-precipitated with {fraction (1/10)} volume of 3M sodium acetate and 2 volumes of 100% ethanol. The RNA was spun down and placed in RNAse free water. RNA was stored at −80° C.

[0692] AI_comprehensive panel_v1.0

[0693] The plates for AI_comprehensive panel_v1.0 include two control wells and 89 test samples comprised of cDNA isolated from surgical and postmortem human tissues obtained from the Backus Hospital and Clinomics (Frederick, Md.). Total RNA was extracted from tissue samples from the Backus Hospital in the Facility at CuraGen. Total RNA from other tissues was obtained from Clinomics.

[0694] Joint tissues including synovial fluid, synovium, bone and cartilage were obtained from patients undergoing total knee or hip replacement surgery at the Backus Hospital. Tissue samples were immediately snap frozen in liquid nitrogen to ensure that isolated RNA was of optimal quality and not degraded. Additional samples of osteoarthritis and rheumatoid arthritis joint tissues were obtained from Clinomics. Normal control tissues were supplied by Clinomics and were obtained during autopsy of trauma victims.

[0695] Surgical specimens of psoriatic tissues and adjacent matched tissues were provided as total RNA by Clinomics. Two male and two female patients were selected between the ages of 25 and 47. None of the patients were taking prescription drugs at the time samples were isolated.

[0696] Surgical specimens of diseased colon from patients with ulcerative colitis and Crohns disease and adjacent matched tissues were obtained from Clinomics. Bowel tissue from three female and three male Crohn's patients between the ages of 41-69 were used. Two patients were not on prescription medication while the others were taking dexamethasone, phenobarbital, or tylenol. Ulcerative colitis tissue was from three male and four female patients. Four of the patients were taking lebvid and two were on phenobarbital.

[0697] Total RNA from post mortem lung tissue from trauma victims with no disease or with emphysema, asthma or COPD was purchased from Clinomics. Emphysema patients ranged in age from 40-70 and all were smokers, this age range was chosen to focus on patients with cigarette-linked emphysema and to avoid those patients with alpha-i anti-trypsin deficiencies. Asthma patients ranged in age from 36-75, and excluded smokers to prevent those patients that could also have COPD. COPD patients ranged in age from 35-80 and included both smokers and non-smokers. Most patients were taking corticosteroids, and bronchodilators.

[0698] In the labels employed to identify tissues in the AI_comprehensive panel_v1.0 panel, the following abbreviations are used:

[0699] AI=Autoimmunity

[0700] Syn=Synovial

[0701] Normal=No apparent disease

[0702] Rep22 IRep20=individual patients

[0703] RA=Rheumatoid arthritis

[0704] Backus=From Backus Hospital

[0705] OA=Osteoarthritis

[0706] (SS) (BA) (MF)=Individual patients

[0707] Adj=Adjacent tissue

[0708] Match control=adjacent tissues

[0709] -M=Male

[0710] -F=Female

[0711] COPD=Chronic obstructive pulmonary disease

[0712] Panels 5D and 5I

[0713] The plates for Panel 5D and 5I include two control wells and a variety of cDNAs isolated from human tissues and cell lines with an emphasis on metabolic diseases. Metabolic tissues were obtained from patients enrolled in the Gestational Diabetes study. Cells were obtained during different stages in the differentiation of adipocytes from human mesenchymal stem cells. Human pancreatic islets were also obtained.

[0714] In the Gestational Diabetes study subjects are young (18-40 years), otherwise healthy women with and without gestational diabetes undergoing routine (elective) Caesarean section. After delivery of the infant, when the surgical incisions were being repaired/closed, the obstetrician removed a small sample (<1 cc) of the exposed metabolic tissues during the closure of each surgical level. The biopsy material was rinsed in sterile saline, blotted and fast frozen within 5 minutes from the time of removal. The tissue was then flash frozen in liquid nitrogen and stored, individually, in sterile screw-top tubes and kept on dry ice for shipment to or to be picked up by CuraGen. The metabolic tissues of interest include uterine wall (smooth muscle), visceral adipose, skeletal muscle (rectus) and subcutaneous adipose. Patient descriptions are as follows:

[0715] Patient 2: Diabetic Hispanic, overweight, not on insulin

[0716] Patient 7-9: Nondiabetic Caucasian and obese (BMI>30)

[0717] Patient 10: Diabetic Hispanic, overweight, on insulin

[0718] Patient 11: Nondiabetic African American and overweight

[0719] Patient 12: Diabetic Hispanic on insulin

[0720] Adiocyte differentiation was induced in donor progenitor cells obtained from Osirus (a division of Clonetics/BioWhittaker) in triplicate, except for Donor 3U which had only two replicates. Scientists at Clonetics isolated, grew and differentiated human mesenchymal stem cells (HuMSCs) for CuraGen based on the published protocol found in Mark F. Pittenger, et al., Multilineage Potential of Adult Human Mesenchymal Stem Cells Science Apr. 2, 1999: 143-147. Clonetics provided Trizol lysates or frozen pellets suitable for mRNA isolation and ds cDNA production. A general description of each donor is as follows:

[0721] Donor 2 and 3 U: Mesenchymal Stem cells, Undifferentiated Adipose

[0722] Donor 2 and 3 AM: Adipose, AdiposeMidway Differentiated

[0723] Donor 2 and 3 AD: Adipose, Adipose Differentiated

[0724] Human cell lines were generally obtained from ATCC (American Type Culture Collection), NCI or the German tumor cell bank and fall into the following tissue groups: kidney proximal convoluted tubule, uterine smooth muscle cells, small intestine, liver HepG2 cancer cells, heart primary stromal cells, and adrenal cortical adenoma cells. These cells are all cultured under standard recommended conditions and RNA extracted using the standard procedures. All samples were processed at CuraGen to produce single stranded cDNA.

[0725] Panel 5I contains all samples previously described with the addition of pancreatic islets from a 58 year old female patient obtained from the Diabetes Research Institute at the University of Miami School of Medicine. Islet tissue was processed to total RNA at an outside source and delivered to CuraGen for addition to panel 5I.

[0726] In the labels employed to identify tissues in the 5D and 5I panels, the following abbreviations are used:

[0727] GO Adipose=Greater Omentum Adipose

[0728] SK=Skeletal Muscle

[0729] UT=Uterus

[0730] PL=Placenta

[0731] AD=Adipose Differentiated

[0732] AM=Adipose Midway Differentiated

[0733] U=Undifferentiated Stem Cells

[0734] Panel CNSD.01

[0735] The plates for Panel CNSD.01 include two control wells and 94 test samples comprised of cDNA isolated from postmortem human brain tissue obtained from the Harvard Brain Tissue Resource Center. Brains are removed from calvaria of donors between 4 and 24 hours after death, sectioned by neuroanatomists, and frozen at −80° C. in liquid nitrogen vapor. All brains are sectioned and examined by neuropathologists to confirm diagnoses with clear associated neuropathology.

[0736] Disease diagnoses are taken from patient records. The panel contains two brains from each of the following diagnoses: Alzheimer's disease, Parkinson's disease, Huntington's disease, Progressive Supernuclear Palsy, Depression, and “Normal controls”. Within each of these brains, the following regions are represented: cingulate gyrus, temporal pole, globus palladus, substantia nigra, Brodman Area 4 (primary motor strip), Brodman Area 7 (parietal cortex), Brodman Area 9 (prefrontal cortex), and Brodman area 17 (occipital cortex). Not all brain regions are represented in all cases; e.g., Huntington's disease is characterized in part by neurodegeneration in the globus palladus, thus this region is impossible to obtain from confirmed Huntington's cases. Likewise Parkinson's disease is characterized by degeneration of the substantia nigra making this region more difficult to obtain. Normal control brains were examined for neuropathology and found to be free of any pathology consistent with neurodegeneration.

[0737] In the labels employed to identify tissues in the CNS panel, the following abbreviations are used:

[0738] PSP=Progressive supranuclear palsy

[0739] Sub Nigra=Substantia nigra

[0740] Glob Palladus=Globus palladus

[0741] Temp Pole=Temporal pole

[0742] Cing Gyr=Cingulate gyrus

[0743] BA 4=Brodman Area 4

[0744] Panel CNS_Neurodegeneration_V1.0

[0745] The plates for Panel CNS_Neurodegeneration_V1.0 include two control wells and 47 test samples comprised of cDNA isolated from postmortem human brain tissue obtained from the Harvard Brain Tissue Resource Center (McLean Hospital) and the Human Brain and Spinal Fluid Resource Center (VA Greater Los Angeles Healthcare System). Brains are removed from calvaria of donors between 4 and 24 hours after death, sectioned by neuroanatomists, and frozen at −80° C. in liquid nitrogen vapor. All brains are sectioned and examined by neuropathologists to confirm diagnoses with clear associated neuropathology.

[0746] Disease diagnoses are taken from patient records. The panel contains six brains from Alzheimer's disease (AD) patients, and eight brains from “Normal controls” who showed no evidence of dementia prior to death. The eight normal control brains are divided into two categories: Controls with no dementia and no Alzheimer's like pathology (Controls) and controls with no dementia but evidence of severe Alzheimer's like pathology, (specifically senile plaque load rated as level 3 on a scale of 0-3; 0=no evidence of plaques, 3=severe AD senile plaque load). Within each of these brains, the following regions are represented: hippocampus, temporal cortex (Brodman Area 21), parietal cortex (Brodman area 7), and occipital cortex (Brodman area 17). These regions were chosen to encompass all levels of neurodegeneration in AD. The hippocampus is a region of early and severe neuronal loss in AD; the temporal cortex is known to show neurodegeneration in AD after the hippocampus; the parietal cortex shows moderate neuronal death in the late stages of the disease; the occipital cortex is spared in AD and therefore acts as a “control” region within AD patients. Not all brain regions are represented in all cases.

[0747] In the labels employed to identify tissues in the CNS_Neurodegeneration_V1.0 panel, the following abbreviations are used:

[0748] AD=Alzheimer's disease brain; patient was demented and showed AD-like pathology upon autopsy

[0749] Control=Control brains; patient not demented, showing no neuropathology

[0750] Control (Path)=Control brains; pateint not demented but showing sever AD-like pathology

[0751] SupTemporal Ctx=Superior Temporal Cortex

[0752] Inf Temporal Ctx=Inferior Temporal Cortex

[0753] A. CG105472-01: KIAA0575/Greb1

[0754] Expression of gene CG105472-01 was assessed using the primer-probe sets Ag3041, Ag3042, Ag4301 and Ag4300, described in Tables AA, AB, AC and AD. Results of the RTQ-PCR runs are shown in Tables AE, AF, AG, AH, AI, AJ and AK.

TABLE AA
Probe Name Ag3041
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gtattacctggtccgtaatgca-3′	22	870	215
Probe	TET-5′-caagggactctaaccaaaggaccttt-3′-TAMRA	26	892	216
Reverse	5′-ggcttctaaactctgagccttt-3′	22	928	217

[0755]

TABLE AB
Probe Name Ag3042
			Start	SEQ ID
Primers	Sequence	Length	Position	No
Forward	5′-gtattacctggtccgtaatgca-3′	22	870	218
Probe	TET-5′-caagggactctaaccaaaqgaccttt-3′-TAMRA	26	892	219
Reverse	5′-ggcttctaaactctgagccttt-3′	22	928	220

[0756]

TABLE AC
Probe Name Ag4301
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-ctgtggaaagaaaggcttctg-3′	21	777	221
Probe	TET-5′-tcacggaattctccaatcatataaatctg-3′-TAMRA	29	803	222
Reverse	5′-cttgggttgagtggtcagttt-3′	21	832	223

[0757]

TABLE AD
Probe Name Ag4300
			Start	SEQ ID
Primers	Sequence	Length	Position	No
Forward	5′-gccaagtaggttcccctgta-3′	20	6545	224
Probe	TET-5′-cctcctacaaagcaatattccaaagga-3′-TAMRA	27	6566	225
Reverse	5′-ttcttgtctccagcctttacag-3′	22	6602	226

[0758]

TABLE AE
CNS neurodegeneration v1.0
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag4300,	Ag4301,		Ag4300,	Ag4301,
	Run	Run		Run	Run
Tissue Name	224063041	224064603	issue Name	224063041	224064603
AD 1 Hippo	32.8	15.4	Control (Path) 3	30.1	10.8
			Temporal Ctx
AD 2 Hippo	59.0	28.9	Control (Path) 4	48.0	42.0
			Temporal Ctx
AD 3 Hippo	20.6	10.0	AD 1 Occipital Ctx	31.6	24.3
AD 4 Hippo	22.4	9.2	Ad 2 Occipital Ctx	0.0	0.0
			(Missing)
AD 5 Hippo	100.0	100.0	AD 3 Occipital Ctx	21.6	6.6
AD 6 Hippo	79.6	35.1	AD 4 Occipital Ctx	40.3	26.1
Control 2 Hippo	43.8	21.3	AD 5 Occipital Ctx	72.7	25.9
Control 4 Hippo	25.2	12.3	AD 6 Occipital Ctx	40.6	47.0
Control (Path) 3	18.8	7.7	Control 1 Occipital	5.6	5.5
Hippo			Ctx
AD 1 Temporal Ctx	52.9	17.1	Control 2 Occipital	73.2	62.9
			Ctx
AD 2 Temporal Ctx	90.1	34.6	Control 3 Occipital	34.6	2.0
			Ctx
AD 3 Temporal Ctx	20.6	8.9	Control 4 Occipital	22.1	8.1
			Ctx
AD 4 Temporal Ctx	45.7	31.0	Control (Path) 1	87.7	65.1
			Occipital Ctx
AD 5 Inf Temporal	89.5	71.7	Control (Path) 2	28.5	27.0
Ctx			Occipital Ctx
AD 5 Sup Temporal	58.6	31.9	Control (Path) 3	8.2	3.4
Ctx			Occipital Ctx
AD 6 Inf Temporal	59.0	29.7	Control (Path) 4	31.6	33.0
Ctx			Occipital Ctx
AD 6 Sup Temporal	65.5	43.8	Control 1 Parietal	27.4	12.1
Ctx			Ctx
Control 1 Temporal	18.9	8.5	Control 2 Parietal	66.0	31.2
Ctx			Ctx
Control 2 Temporal	43.5	30.4	Control 3 Parietal	31.6	28.5
Ctx			Ctx
Control 3 Temporal	37.6	24.1	Control (Path) 1	81.2	62.0
Ctx			Parietal Ctx
Control 3 Temporal	22.4	13.0	Control (Path) 2	45.4	35.1
Ctx			Parietal Ctx
Control (Path) 1	67.4	48.6	Control (Path) 3	13.4	7.9
Temporal Ctx			Parietal Ctx
Control (Path) 2	48.0	38.4	Control (Path) 4	58.6	57.8
Temporal Ctx			Parietal Ctx

[0759]

TABLE AF
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag4300,		(%) Ag4300,
	Run		Run
Tissue Name	221998703	issue Name	221998703
Adipose	0.8	Renal ca. TK-10	9.3
Melanoma*	0.1	Bladder	1.1
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.3
Hs688(B).T		NCI-N87
Melanoma* M14	3.8	Gastric ca. KATO III	0.0
Melanoma*	3.9	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	45.7	Colon ca. SW480	0.5
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.4
carcinoma SCC-4		met) SW620
Testis Pool	7.4	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	2.2
met) PC-3
Prostate Pool	14.9	Colon ca. CaCo-2	1.4
Placenta	0.8	Colon cancer tissue	0.3
Uterus Pool	8.6	Colon ca. SW1116	0.0
Ovarian ca.	2.5	Colon ca. Colo-205	0.3
OVCAR-3
Ovarian ca.	1.9	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	36.3
OVCAR-4
Ovarian ca.	16.7	Small Intestine Pool	11.4
OVCAR-5
Ovarian ca.	1.5	Stomach Pool	12.3
IGROV-1
Ovarian ca.	1.6	Bone Marrow Pool	22.8
OVCAR-8
Ovary	24.8	Fetal Heart	1.6
Breast ca. MCF-7	100.0	Heart Pool	6.7
Breast ca.	0.2	Lymph Node Pool	48.3
MDA-MB-231
Breast ca. BT 549	0.2	Fetal Skeletal Muscle	3.3
Breast ca. T47D	44.8	Skeletal Muscle Pool	1.3
Breast ca. MDA-N	11.9	Spleen Pool	0.5
Breast Pool	39.8	Thymus Pool	14.6
Trachea	0.9	CNS cancer (glio/	5.8
		astro) U87-MG
Lung	39.2	CNS cancer (glio/	0.2
		astro) U-118-MG
Fetal Lung	1.4	CNS cancer (neuro;	3.1
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.5
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	1.6
		SNB-75
Lung ca. NCI-H146	1.0	CNS cancer (glio)	1.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	2.2
		SF-295
Lung ca. A549	1.3	Brain (Amygdala)	2.4
		Pool
Lung ca. NCI-H526	0.6	Brain (cerebellum)	2.9
Lung ca. NCI-H23	0.6	Brain (fetal)	2.4
Lung ca. NCI-H460	1.6	Brain (Hippocampus)	3.4
		Pool
Lung ca. HOP-62	1.6	Cerebral Cortex Pool	5.8
Lung ca. NCI-H522	3.3	Brain (Substantia	2.8
		nigra) Pool
Liver	0.1	Brain (Thalamus) Pool	5.6
Fetal Liver	4.6	Brain (whole)	3.7
Liver ca. HepG2	20.9	Spinal Cord Pool	4.3
Kidney Pool	21.5	Adrenal Gland	3.4
Fetal Kidney	3.6	Pituitary gland Pool	1.1
Renal ca. 786-0	0.0	Salivary Gland	0.1
Renal ca. A498	3.0	Thyroid (female)	0.0
Renal ca. ACHN	1.3	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	1.3	Pancreas Pool	25.2

[0760]

TABLE AG
Panel 1.3D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	g3041,	Ag3042,		Ag3041,	Ag3042,
	Run	Run		Run	Run
Tissue Name	167964342	167964481	Tissue Name	167964342	167964481
Liver	0.1	0.1	Kidney (fetal)	2.1	1.6
adenocarcinoma
Pancreas	0.1	0.3	Renal ca. 786-0	0.0	0.0
Pancreatic ca.	0.0	0.0	Renal ca. A498	0.0	0.1
CAPAN 2
Adrenal gland	0.6	0.5	Renal ca. RXF 393	0.0	0.0
Thyroid	0.0	0.0	Renal ca. ACHN	0.0	0.0
Salivary gland	0.0	0.0	Renal ca. UO-31	0.0	0.0
Pituitary gland	0.6	1.0	Renal ca. TK-10	0.0	0.0
Brain (fetal)	0.5	0.3	Liver	0.1	0.0
Brain (whole)	1.1	0.4	Liver (fetal)	0.3	0.5
Brain (amygdala)	0.6	0.6	Liver ca.	32.3	27.5
			(hepatoblast) HepG2
Brain (cerebellum)	1.4	1.0	Lung	0.1	0.0
Brain (hippocampus)	0.6	1.0	Lung (fetal)	0.1	0.2
Brain (substantia	0.7	0.6	Lung ca. (small cell)	0.0	0.0
nigra)			LX-1
Brain (thalamus)	0.2	0.1	Lung ca. (small cell)	0.5	0.3
			NCI-H69
Cerebral Cortex	4.4	4.4	Lung ca. (s.cell var.)	0.5	0.3
			SHP-77
Spinal cord	0.5	0.9	Lung ca. (large	0.1	0.1
			cell)NCI-H460
glio/astro U87-MG	0.0	0.0	Lung ca. (non-sm.	0.3	0.1
			cell) A549
glio/astro U-118-MG	0.0	0.0	Lung ca. (non-s.cell)	0.3	0.5
			NCI-H23
astrocytoma	0.0	0.0	Lung ca. (non-s.cell)	0.1	0.1
SW1783			HOP-62
neuro*; met	1.3	0.9	Lung ca. (non-s.cl)	1.8	1.6
SK-N-AS			NCI-H522
astrocytoma SF-539	0.1	0.0	Lung ca. (squam.)	0.5	0.2
astrocytoma				SW 900
astrocytoma SNB-75	0.2	0.2	Lung ca. (squam.)	3.2	2.7
			NCI-H596
glioma SNB-19	0.0	0.0	Mammary gland	0.7	0.5
glioma U251	0.0	0.0	Breast ca.* (pl.ef)	100.0	100.0
			MCF-7
glioma SF-295	0.0	0.0	Breast ca.* (pl.ef)	0.0	0.0
			MDA-MB-231
Heart (fetal)	2.2	1.0	Breast ca.* (pl.ef)	91.4	90.8
			T47D
Heart	0.3	0.3	Breast ca. BT-549	0.0	0.0
Skeletal muscle	2.5	2.5	Breast ca. MDA-N	0.0	0.0
(fetal)
Skeletal muscle	0.8	0.5	Ovary	46.0	46.7
Bone marrow	0.0	0.0	Ovarian ca.	0.9	0.6
			OVCAR-3
Thymus	0.0	0.0	Ovarian ca.	0.1	0.1
			OVCAR-4
Spleen	0.0	0.0	Ovarian ca.	0.1	0.0
			OVCAR-5
Lymph node	0.0	0.0	Ovarian ca.	0.1	0.1
			OVCAR-8
Colorectal	0.1	0.1	Ovarian ca.	0.9	0.6
			IGROV-1
Stomach	0.1	0.1	Ovarian ca.*	2.2	1.3
			(ascites) SK-OV-3
Small intestine	0.2	0.1	Uterus	7.1	6.2
Colon ca. SW480	0.1	0.1	Placenta	0.1	0.1
Colon ca.*	0.7	0.6	Prostate	7.6	7.7
SW620(SW480 met)
Colon ca. HT29	0.0	0.0	Prostate ca.* (bone	0.0	0.0
			met)PC-3
Colon ca. HCT-116	0.5	0.5	Testis	1.0	0.8
Colon ca. CaCo-2	0.9	0.7	Melanoma	0.0	0.0
			Hs688(A).T
Colon ca.	0.1	0.1	Melanoma* (met)	0.0	0.0
tissue(ODO3866)			Hs688(B).T
Colon ca. HCC-2998	0.6	0.3	Melanoma	0.0	0.1
			UACC-62
Gastric ca.* (liver	0.0	0.0	Melanoma M14	0.0	0.0
met) NCI-N87
Bladder	0.5	0.4	Melanoma LOX	0.0	0.0
			IMVI
Trachea	0.0	0.0	Melanoma* (met)	0.0	0.0
			SK-MEL-5
Kidney	0.7	0.7	Adipose	0.4	0.3

[0761]

TABLE AH
Panel 2.2
	Rel. Ex.		Rel. Exp.
	(%) Ag3041,		(%) Ag3041,
	Run		Run
Tissue Name	174441332	Tissue Name	174441332
Normal Colon	6.3	Kidney Margin	5.2
		(OD04348)
Colon cancer	0.4	Kidney malignant	0.5
(OD06064)		cancer (OD06204B)
Colon Margin	0.3	Kidney normal	0.6
(OD06064)		adjacent tissue
		(OD06204E)
Colon cancer	0.0	Kidney Cancer	2.5
(OD06159)		(OD04450-01)
Colon Margin	0.3	Kidney Margin	1.0
(OD06159)		(OD04450-03)
Colon cancer	0.0	Kidney Cancer	0.0
(OD06297-04)		8120613
Colon Margin	0.0	Kidney Margin	5.4
(OD06297-05)		8120614
CC Gr.2 ascend	0.0	Kidney Cancer	0.4
colon (ODO3921)		9010320
CC Margin	0.4	Kidney Margin	1.0
(ODO3921)		9010321
Colon cancer	0.0	Kidney Cancer	0.0
metastasis		8120607
(OD06104)
Lung Margin	0.3	Kidney Margin	1.2
(OD06104)		8120608
Colon mets to lung	0.0	Normal Uterus	54.0
(OD04451-01)
Lung Margin	0.0	Uterine Cancer	7.1
(OD04451-02)		064011
Normal Prostate	22.4	Normal Thyroid	0.0
Prostate Cancer	16.6	Thyroid Cancer	0.0
(OD04410)		064010
Prostate Margin	24.1	Thyroid Cancer	0.0
(OD04410)		A302152
Normal Ovary	100.0	Thyroid Margin	0.0
		A302153
Ovarian cancer	1.3	Normal Breast	10.3
(OD06283-03)
Ovarian Margin	0.0	Breast Cancer	1.2
(OD06283-07)		(OD04566)
Ovarian Cancer	1.4	Breast Cancer 1024	17.1
064008
Ovarian cancer	0.7	Breast Cancer	62.0
(OD06145)		(OD04590-01)
Ovarian Margin	17.9	Breast Cancer Mets	40.6
(OD06145)		(OD04590-03)
Ovarian cancer	3.8	Breast Cancer	53.2
(OD06455-03)		Metastasis
		(OD04655-05)
Ovarian Margin	10.4	Breast Cancer 064006	7.9
(OD06455-07)
Normal Lung	0.1	Breast Cancer	87.7
		9100266
Invasive poor diff.	0.6	Breast Margin	43.2
lung adeno		9100265
(ODO4945-01
Lung Margin	0.3	Breast Cancer	2.1
(ODO4945-03)		A209073
Lung Malignant	0.0	Breast Margin	17.0
Cancer (OD03126)		A2090734
Lung Margin	0.0	Breast cancer	52.1
(OD03126)		(OD06083)
Lung Cancer	0.0	Breast cancer node	40.9
(OD05014A)		metastasis (OD06083)
Lung Margin	0.3	Normal Liver	1.1
(OD05014B)
Lung cancer	0.4	Liver Cancer 1026	0.5
(OD06081)
Lung Margin	0.1	Liver Cancer 1025	3.0
(OD06081)
Lung Cancer	0.0	Liver Cancer 6004-T	0.0
(OD04237-01)
Lung Margin	0.2	Liver Tissue 6004-N	0.0
(OD04237-02)
Ocular Melanoma	2.0	Liver Cancer 6005-T	1.6
Metastasis
Ocular Melanoma	0.9	Liver Tissue 6005-N	1.3
Margin (Liver)
Melanoma	0.1	Liver Cancer 064003	4.0
Metastasis
Melanoma Margin	0.2	Normal Bladder	0.6
(Lung)
Normal Kidney	1.5	Bladder Cancer 1023	2.7
Kidney Ca, Nuclear	1.4	Bladder Cancer	0.0
grade 2 (OD04338)		A302173
Kidney Margin	1.7	Normal stomach	1.2
(OD04338)
Kidney Ca Nuclear	0.0	Gastric Cancer	0.0
grade ½		9060397
(OD04339)
Kidney Margin	1.7	Stomach Margin	0.5
(OD04339)		9060396
Kidney Ca, Clear	0.0	Gastric Cancer	0.5
cell type (OD04340)		9060395
Kidney Margin	1.1	Stomach Margin	1.5
(OD04340)		9060394
Kidney Ca, Nuclear	0.0	Gastric Cancer	0.2
grade 3 (OD04348)		064005

[0762]

TABLE AI
Panel 3D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag3041,	Ag4300,		Ag3041,	Ag4300,
	Run	Run		Run	Run
Tissue Name	182098857	182114559	Tissue Name	182098857	182114559
Daoy-	11.9	0.0	Ca Ski- Cervical	2.7	0.0
Medulloblastoma			epidermoid carcinoma
			(metastasis)
TE671-	0.8	0.0	ES-2- Ovarian clear	0.0	0.0
Medulloblastoma			cell carcinoma
D283 Med-	9.4	0.0	Ramos- Stimulated	0.0	0.0
Medulloblastoma			with PMA/ionomycin
			6h
PFSK-1- Primitive	27.4	0.0	Ramos- Stimulated	0.0	0.0
Neuroectodermal			with PMA/ionomycin
			14h
XF-498-CNS	0.0	10.3	MEG-01- Chronic	21.0	0.0
			myelogenous leukemia
			(megokaryoblast)
SNB-78-Glioma	0.0	0.0	Raji- Burkitt's	0.9	0.0
			lymphoma
SF-268- Glioblastoma	1.0	0.0	Daudi- Burkitt's	2.0	0.0
			lymphoma
T98G- Glioblastoma	0.0	0.0	U266- B-cell	75.8	2.5
			plasmacytoma
SK-N-SH-	100.0	7.9	CA46- Burkitt's	5.6	0.0
Neuroblastoma			lymphoma
(metastasis)
SF-295- Glioblastoma	0.0	0.0	RL- non-Hodgkin's	2.2	0.0
			B-cell lymphoma
Cerebellum	22.4	00	JM1- pre-B-cell	0.0	0.0
			lymphoma
Cerebellum	19.8	0.0	Jurkat- T cell leukemia	1.0	0.0
NCI-H292-	0.0	0.0	TF-1- Erythroleukemia	0.0	0.0
Mucoepidermoid lung
carcinoma
DMS-114- Small cell	1.8	0.0	HUT 78- T-cell	40.6	0.0
lung cancer			lymphoma
DMS-79- Small cell	32.1	100.0	U937- Histiocytic	14.7	0.0
lung cancer			lymphoma
NCI-H146- Small cell	24.1	0.0	KU-812- Myelogenous	0.9	0.0
lung cancer
NCI-H526- Small cell	57.4	0.0	769-P- Clear cell renal	2.9	0.0
lung cancer			carcinoma
NCI-N417- Small cell	0.9	0.0	Caki-2- Clear cell	0.0	0.0
lung cancer			renal carcinoma
NCI-H82- Small cell	69.7	5.5	SW 839- Clear cell	0.0	0.0
lung cancer			renal carcinoma
NCI-H157- Squamous	1.7	0.0	G401- Wilms'tumor	36.1	0.0
cell lung cancer
(metastasis)
NCI-H1155- Large	8.5	0.0	Hs766T- Pancreatic	0.0	0.0
cell lung cancer			carcinoma (LN
			metastasis)
NCI-H1299- Large	4.5	0.0	CAPAC-1- Pancreatic	2.1	0.0
cell lung cancer			adenocarcinoma (liver
			metastasis)
NCI-H727- Lung	1.9	0.0	SU86.86- Pancreatic	6.8	0.0
carcinoid			carcinoma (liver
			metastasis)
NCI-UMC-11-Lung	2.2	0.0	BxPC-3- Pancreatic	0.0	0.0
carcinoid			adenocarcinoma
LX-1- Small cell lung	0.0	0.0	HPAC- Pancreatic	0.0	0.0
cancer			adenocarcinoma
Colo-205- Colon	9.2	0.0	MIA PaCa-2-	0.0	0.0
cancer			Pancreatic carcinoma
KM12- Colon cancer	2.0	0.0	CFPAC-1- Pancreatic	3.3	0.0
			ductal adenocarcinoma
KM20L2- Colon	0.0	0.0	PANC-1- Pancreatic	0.0	0.0
cancer			epithelioid ductal
			carcinoma
NCI-H716- Colon	0.9	0.0	T24- Bladder carcinma	0.0	0.0
cancer			(transitional cell)
SW-48- Colon	0.0	0.0	5637- Bladder	0.0	0.0
adenocarcinoma			carcinoma
SW1116- Colon	0.0	0.0	HT-1197- Bladder	0.0	0.0
adenocarcinoma			carcinoma
LS 174T- Colon	0.0	0.0	UM-UC-3- Bladder	0.0	0.0
adenocarcinoma			carcinma (transitional
			cell)
SW-948- Colon	1.1	0.0	A204-	6.7	0.0
adenocarcinoma			Rhabdomyosarcoma
SW-480- Colon	0.0	0.0	HT-1080-	0.0	5.4
adenocarcinoma			Fibrosarcoma
NCI-SNU-5- Gastric	3.9	0.0	MG-63- Osteosarcoma	7.7	0.0
carcinoma
KATO III- Gastric	1.0	0.0	SK-LMS-1-	0.0	0.0
carcinoma			Leiomyosarcoma
			(vulva)
NCI-SNU-16- Gastric	0.0	0.0	SJRH30-	0.0	0.0
carcinoma			Rhabdomyosarcoma
			(met to bone marrow)
NCI-SNU-1 - Gastric	0.0	0.0	A431- Epidermoid	0.0	0.0
carcinoma			carcinoma
RF-1- Gastric	1.9	0.0	WM266-4- Melanoma	0.0	94.6
adenocarcinoma
RF-48- Gastric	0.0	0.0	DE 145- Prostate	0.0	0.0
adenocarcinoma			carcinoma (brain
			metastasis)
MKN-45- Gastric	0.0	0.0	MDA-MB-468- Breast	0.0	0.0
carcinoma			adenocarcinoma
NCI-N87- Gastric	0.0	0.0	SCC-4- Squamous cell	0.0	0.0
carcinoma			carcinoma of tongue
OVCAR-5- Ovarian	1.8	0.0	SCC-9- Squamous cell	0.0	0.0
carcinoma			carcinoma of tongue
RL95-2- Uterine	0.0	0.0	SCC-15- Squamous	0.0	0.0
carcinoma			cell carcinoma of
			tongue
HelaS3- Cervical	8.0	0.0	CAL 27- Squamous	0.0	0.0
adenocarcinoma			cell carcinoma of
			tongue

[0763]

TABLE AJ
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	() Ag4301,		(%) Ag4301,
	Run		Run
Tissue Name	181981970	Tissue Name	181981970
Secondary Th1 act	0.2	HUVEC IL-1beta	0.0
Secondary Th2 act	1.0	HUVEC IFN gamma	0.1
Secondary Tr1 act	1.3	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.5	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.6	HUVEC IL-11	0.0
Secondary Tr1 rest	0.7	Lung Microvascular	0.0
		EC none
Primary Th1 act	0.0	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.9	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	0.5	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	1.8	Small airway	0.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.0	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	0.8	Coronery artery SMC	0.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	4.6	Astrocytes rest	1.8
Secondary CD8	0.4	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	2.1	KU-812 (Basophil)	0.4
lymphocyte act		rest
CD4 lymphocyte	0.6	KU-812 (Basophil)	0.6
none		PMA/ionomycin
2ry Th1/Th2/	1.9	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	0.6
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	3.1	Liver cirrhosis	1.5
LAK cells IL-2 +	2.1	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	0.9	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	0.0	NCI-H292 IL-13	0.6
ionomycin
NK Cells IL-2 rest	2.0	NCI-H292 IFN gamma	0.3
Two Way MLR 3	0.6	HPAEC none	0.0
day
Two Way MLR 5	0.8	HPAEC TNF alpha +	0.4
day		IL-1 beta
Two Way MLR 7	1.3	Lung fibroblast	0.0
day		none
PBMC rest	0.0	Lung fibroblast TNF	0.0
		alpha + IL-1 beta
PBMC PWM	1.0	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.7	Lung fibroblast IL-9	0.0
Ramos (B cell) none	1.3	Lung fibroblast IL-13	1.3
Ramos (B cell)	3.8	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	0.6	Dermal fibroblast	0.6
PWM		CCD1070 rest
B lymphocytes	0.0	Dermal fibroblast	1.4
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	100.0	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.3	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	0.3	Dermal fibroblast IL-4	0.0
Dendritic cells LPS	0.0	Dermal Fibroblasts	0.0
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.7
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.4	Colon	0.9
Macrophages rest	0.0	Lung	5.1
Macrophages LPS	0.0	Thymus	5.8
HUVEC none	0.0	Kidney	54.3
HUVEC starved	0.0

[0764]

TABLE AK
AK general oncology screening panel v 2.4
	Rel.	Rel.	Rel.		Rel.	Rel.	Rel.
	Exp. (%)	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)	Exp. (%)
	Ag3042,	Ag4300,	Ag4301,		Ag3042,	Ag4300,	Ag4301,
	Run	Run	Run		Run	Run	Run
Tissue Name	268695244	260280468	268665966	issue Name	268695244	260280468	268665966
Colon cancer 1	0.1	0.0	0.1	Bladder NAT	0.0	0.0	0.0
				2
Colon NAT 1	0.1	0.0	0.0	Bladder NAT	0.0	0.0	0.0
				3
Colon cancer 2	0.2	0.0	0.1	Bladder NAT	0.1	0.0	0.0
				4
Colon NAT 2	0.0	0.0	0.0	Prostate	1.7	5.6	1.1
				adenocarcinoma
				1
Colon cancer 3	0.1	0.0	0.1	Prostate	2.6	0.8	1.1
				adenocarcinoma
				2
Colon NAT 3	0.1	0.0	0.1	Prostate	20.0	31.9	13.4
				adenocarcinoma
				3
Colon	0.1	0.0	0.1	Prostate	0.7	0.0	0.7
malignant				adenocarcinoma
cancer 4				4
Colon NAT 4	0.0	0.0	0.0	Prostate NAT	4.3	6.5	2.5
				5
Lung cancer 1	0.0	0.0	0.0	Prostate	11.1	14.5	9.2
				adenocarcinoma
				6
Lung NAT 1	0.0	0.0	0.0	Prostate	7.0	9.9	3.3
				adenocarcinoma
				7
Lung cancer 2	6.9	14.7	5.8	Prostate	2.9	4.0	1.6
				adenocarcinoma
				8
Lung NAT 2	0.0	0.0	0.0	Prostate	7.9	12.5	5.8
				adenocarcinoma
				9
Squamous cell	0.3	0.0	0.2	Prostate NAT	2.7	4.7	2.0
carcinoma 3				10
Lung NAT 3	0.0	0.0	0.0	Kidney	0.0	0.0	0.0
				cancer 1
Metastatic	15.8	24.1	15.2	Kidney NAT	0.1	0.0	0.1
melanoma 1				1
Melanoma 2	0.1	0.0	0.0	Kidney	3.3	8.8	2.1
				cancer 2
Melanoma 3	0.0	0.0	0.0	Kidney NAT	0.3	0.0	0.5
				2
Metastatic	100.0	100.0	100.0	Kidney	0.3	0.0	0.2
melanoma 4				cancer 3
Metastatic	34.9	63.3	24.0	Kidney NAT	0.1	0.0	0.1
melanoma 5				3
Bladder cancer	0.0	0.0	0.0	Kidney	0.5	0.3	0.5
1				cancer 4
Bladder NAT 1	0.0	0.0	0.0	Kidney NAT	0.2	0.0	0.3
				4
Bladder cancer	0.1	0.0	0.1
2

[0765] CNS_neurodegeneration_v1.0 Summary: Ag4300/Ag4301 This panel confirms the expression of this gene at low levels in the brains of an independent group of individuals. However, no differential expression of this gene was detected between Alzheimer's diseased postmortem brains and those of non-demented controls in this experiment. Please see Panel 1.4 for a discussion of the potential utility of this gene in treatment of central nervous system disorders.

[0766] General_screening_panel_v1.4 Summary: Ag4300 Highest expression of this gene is detected in a breast cancer MCF-7 cell line (CT=25). This gene codes for Greb 1 protein. High expression of this gene is upregulated in response to estrogen in MCF-7 (Ghosh et al., 2000, Cancer Res 60(22):6367-75, PMID: 11103799). In addition, high to moderate levels of expression of this gene is also seen in number of cell lines derived from melanoma, ovarian, breast, lung, liver, renal, colon and brain cancers. Therefore, expression of this gene may be used as diagnostic marker for detection of these cancers. Furthermore, therapeutic modulation of this gene may be useful in the treatment of these cancers.

[0767] Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adipose, adrenal gland, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[0768] Interestingly, this gene is expressed at much higher levels in fetal (CT=29.6) when compared to adult liver (CT=35.9). This observation suggests that expression of this gene can be used to distinguish fetal from adult liver. In addition, the relative overexpression of this gene in fetal tissue suggests that the protein product may enhance liver growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver related diseases.

[0769] High expression of this gene is also detected in adult lung (CT=26). Expression of this gene is higher in adult as compared to fetal lung (CT=31). Therefore, expression of this gene may be used to distinguish between adult and fetal lung.

[0770] In addition, this gene is expressed at moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer's disease, Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[0771] Panel 1.3D Summary: Ag3041/Ag3042 Two experiments with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in a breast cancer MCF-7 cell line (CTs=26.9). Moderate to low levels of expression of this gene is also seen in ovarian, breast, lung, liver, and brain cancer cell lines, brain and tissues with metabolic and endocrine function such as adipose, skeletal muscle, fetal heart, adrenal and pituatary glands. Please see panel 1.4 for further discussion on the utility of this gene.

[0772] Panel 2.2 Summary: Ag3041 Highest expression of this gene is detected in normal uterus (CT=30.9). Moderate to low levels of expression of this gene are also seen in both cancer and normal prostate, breast, and uterus. Therefore, therapeutic modulation of this gene may be useful in the treatment of these cancers.

[0773] Panel 3D Summary: Ag3041 Highest expression of this gene is detected in a neuroblastoma SK-N-SH cell line (CT=32.9). In addition, moderate to low levels of expression of this gene is also seen in cancer cell line derived from small lung cancer, B and T cell lymphoma, and Wilm's tumor. Ag4300 Highest expression of this gene is seen in small lung cancer and melanoma cell line (CT=31.7).

[0774] Therefore, therapeutic modulation of this gene may be useful in the treatment of neuroblastoma, small lung cancer, B and T cell lymphoma and Wilm's tumor.

[0775] Panel 4.1D Summary: Ag4301 Highest expression of this gene is detected in eosinophils (CT=30.7). Differential gene expression is observed in the eosinophil cell line EOL-1 under resting conditions over that in EOL-1 cells stimulated by phorbol ester and ionomycin (CT=39). Thus, this gene may be involved in eosinophil function. Antibodies raised against this protein that stimulate its activity may be useful in the reduction of eosinophil activation and in the treatment of asthma and allergy and T cell-mediated autoimmune and inflammatory diseases.

[0776] Moderate levels of expression of this gene are also detected in kidney. Therefore, therapeutic modulation of this gene may be useful in kidney related diseases including lupus and glomerulonephritis.

[0777] Ag4300 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0778] Panel 4D Summary: Ag3041/Ag3042 Results from two experiments with this gene are not included. The amp plot indicates that there were experimental difficulties with this run. (Data not shown).

[0779] general oncology screening panel_v—2.4 Summary: Ag3042/Ag4300/Ag4301 Three experiments with different probe and primer sets are in excellent agreement. Highest expression of this gene is detected in metastatic melanoma (CTs=25-25.9). In addition, moderate to high expression of this gene is also detected in lung, prostate and kidney cancers. Thus, expression of this gene may be used as diagnostic marker for the detection of metastic melanoma, lung, prostate and kidney cancers.

[0780] B. CG106417-01: von Willebrand Factor Like Protein

[0781] Expression of gene CG106417-01 was assessed using the primer-probe set Ag4470, described in Table BA. Results of the RTQ-PCR runs are shown in Tables BB, BC, BD, BE and BF.

TABLE BA
Probe Name Ag4470
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gcatcaggtgtacagacattga-3′	22	441	227
Probe	TET-5′-cgaatgtgtaacctcctcctgcgag-3′-TAMRA	25	463	228
Reverse	5′-acaaacccaccttctgtgttc-3′	21	499	229

[0782]

TABLE BB
AI_comprehensive panel_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag4470,		(%) Ag4470,
	Run		Run
Tissue Name	249008358	issue Name	249008358
110967 COPD-F	3.0	112427 Match Control	25.7
		Psoriasis-F
110980 COPD-F	8.7	112418 Psoriasis-M	4.3
110968 COPD-M	3.4	112723 Match Control	27.5
		Psoriasis-M
110977 COPD-M	38.2	112419 Psoriasis-M	2.6
110989	31.4	112424 Match Control	4.0
Emphysema-F		Psoriasis-M
110992	3.3	112420 Psoriasis-M	13.7
Emphysema-F
110993	5.5	112425 Match Control	25.7
Emphysema-F		Psoriasis-M
110994	2.1	104689 (MF) OA	7.3
Emphysema-F		Bone-Backus
110995	15.4	104690 (MF) Adj	1.2
Emphysema-F		“Normal” Bone-
		Backus
110996	2.0	104691 (MF) OA	11.3
Emphysema-F		Synovium-Backus
110997 Asthma-M	0.8	104692 (BA) OA	7.4
		Cartilage-Backus
111001 Asthma-F	7.7	104694 (BA) OA	2.0
		Bone-Backus
111002 Asthma-F	5.5	104695 (BA) Adj	5.3
		“Normal” Bone-
		Backus
111003 Atopic	6.0	104696 (BA) OA	6.3
Asthma-F		Synovium-Backus
111004 Atopic	12.4	104700 (SS) OA	5.6
Asthma-F		Bone-Backus
111005 Atopic	5.6	104701 (SS) Adj	5.8
Asthma-F		“Normal” Bone-
		Backus
111006 Atopic	1.4	104702 (SS) OA	15.1
Asthma-F		Synovium-Backus
111417 Allergy-M	3.5	117093 OA Cartilage	12.2
		Rep7
112347 Allergy-M	5.8	112672 OA Bone5	97.3
112349 Normal	6.1	112673 OA	46.0
Lung-F		Synovium5
112357 Normal	100.0	112674 OA Synovial	32.5
Lung-F		Fluid cells5
112354 Normal	69.3	117100 OA Cartilage	0.0
Lung-M		Rep14
112374 Crohns-F	9.4	112756 OA Bone9	14.8
112389 Match	7.1	112757 OA	17.4
Control Crohns-F		Synovium9
112375 Crohns-F	7.4	112758 OA Synovial	5.2
		Fluid Cells9
112732 Match	6.7	117125 RA Cartilage	7.9
Control Crohns-F		Rep2
112725 Crohns-M	5.8	113492 Bone2 RA	1.5
112387 Match	0.0	113493 Synovium2	0.0
Control Crohns-M		RA
112378 Crohns-M	4.7	113494 Syn Fluid	0.0
		Cells RA
112390 Match	52.5	113499 Cartilage4 RA	2.0
Control Crohns-M
112726 Crohns-M	7.9	113500 Bone4 RA	1.7
112731 Match	13.1	113501 Synovium4	2.3
Control Crohns-M		RA
112380 Ulcer Col-F	13.2	113502 Syn Fluid	0.7
		Cells4 RA
112734 Match	8.4	113495 Cartilage3 RA	1.2
Control Ulcer Col-F
112384 Ulcer Col-F	2.8	113496 Bone3 RA	2.3
112737 Match	2.8	113497 Synovium3	0.0
Control Ulcer Col-F		RA
112386 Ulcer Col-F	0.0	113498 Syn Fluid	0.8
		Cells3 RA
112738 Match	1.6	117106 Normal	5.7
Control Ulcer Col-F		Cartilage Rep20
112381 Ulcer	9.4	113663 Bone3 Normal	0.9
Col-M
112735 Match	25.2	113664 Synovium3	1.6
Control Ulcer		Normal
Col-M
112382 Ulcer	7.6	113665 Syn Fluid	3.3
Col-M		Cells3 Normal
112394 Match	0.0	117107 Normal	3.5
Control Ulcer		Cartilage Rep22
Col-M
112383 Ulcer	6.6	113667 Bone4 Normal	8.7
Col-M
112736 Match	2.4	113668 Synovium4	12.8
Control Ulcer		Normal
Col-M
112423 Psoriasis-F	4.5	113669 Syn Fluid	24.3
		Cells4 Normal

[0783]

TABLE BC
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag4470,		(%) Ag4470,
	Run		Run
Tissue Name	224535165	issue Name	224535165
AD 1 Hippo	13.7	Control (Path) 3	2.8
		Temporal Ctx
AD 2 Hippo	22.2	Control (Path) 4	31.6
		Temporal Ctx
AD 3 Hippo	6.3	AD 1 Occipital Ctx	17.8
AD 4 Hippo	10.7	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	35.1	AD 3 Occipital Ctx	7.9
AD 6 Hippo	95.9	AD 4 Occipital Ctx	11.3
Control 2 Hippo	15.8	AD 5 Occipital Ctx	9.3
Control 4 Hippo	23.7	AD 6 Occipital Ctx	20.3
Control (Path) 3	0.0	Control 1 Occipital	5.8
Hippo		Ctx
AD 1 Temporal Ctx	15.0	Control 2 Occipital	36.3
		Ctx
AD 2 Temporal Ctx	14.8	Control 3 Occipital	9.4
		Ctx
AD 3 Temporal Ctx	2.6	Control 4 Occipital	10.7
		Ctx
AD 4 Temporal Ctx	23.7	Control (Path) 1	54.7
		Occipital Ctx
AD 5 Inf Temporal	38.4	Control (Path) 2	10.0
Ctx		Occipital Ctx
AD 5 SupTemporal	29.7	Control (Path) 3	0.0
Ctx		Occipital Ctx
AD 6 Inf Temporal	85.3	Control (Path) 4	18.3
Ctx		Occipital Ctx
AD 6 Sup Temporal	100.0	Control 1 Parietal Ctx	7.4
Ctx
Control 1 Temporal	7.7	Control 2 Parietal Ctx	33.2
Ctx
Control 2 Temporal	28.5	Control 3 Parietal Ctx	9.6
Ctx
Control 3 Temporal	16.7	Control (Path) 1	22.4
Ctx		Parietal Ctx
Control 4 Temporal	14.5	Control (Path) 2	28.1
Ctx		Parietal Ctx
Control (Path) 1	32.3	Control (Path) 3	2.2
Temporal Ctx		Parietal Ctx
Control (Path) 2	34.9	Control (Path) 4	44.1
Temporal Ctx		Parietal Ctx

[0784]

TABLE BD
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag4470,		(%) Ag4470,
	Run		Run
Tissue Name	222655825	issue Name	222655825
Adipose	4.8	Renal ca. TK-10	54.0
Melanoma*	3.3	Bladder	2.9
Hs688(A).T
Melanoma*	3.1	Gastric ca. (liver met.)	2.3
Hs688(B).T		NCI-N87
Melanoma* M14	2.8	Gastric ca. KATO III	0.8
Melanoma*	0.2	Colon ca. SW-948	0.5
LOXIMVI
Melanoma*	0.8	Colon ca. SW480	3.3
SK-MEL-5
Squamous cell	0.6	Colon ca.* (SW480	16.2
carcinoma SCC-4		met) SW620
Testis Pool	5.5	Colon ca. HT29	0.0
Prostate ca.* (bone	3.0	Colon ca. HCT-116	4.4
met) PC-3
Prostate Pool	1.1	Colon ca. CaCo-2	94.0
Placenta	10.0	Colon cancer tissue	16.5
Uterus Pool	2.3	Colon ca. SW1116	0.6
Ovarian ca.	0.8	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.4	Colon ca. SW-48	0.2
SK-OV-3
Ovarian ca.	0.3	Colon Pool	2.6
OVCAR-4
Ovarian ca.	1.6	Small Intestine Pool	10.8
OVCAR-5
Ovarian ca.	0.5	Stomach Pool	2.4
IGROV-1
Ovarian ca.	0.9	Bone Marrow Pool	1.0
OVCAR-8
Ovary	7.7	Fetal Heart	2.6
Breast ca. MCF-7	0.9	Heart Pool	1.7
Breast ca.	1.2	Lymph Node Pool	2.7
MDA-MB-231
Breast ca. BT 549	1.8	Fetal Skeletal Muscle	2.3
Breast ca. T47D	4.9	Skeletal Muscle Pool	0.8
Breast ca. MDA-N	0.3	Spleen Pool	0.6
Breast Pool	2.4	Thymus Pool	16.3
Trachea	4.5	CNS cancer (glio/	5.7
		astro) U87-MG
Lung	7.9	CNS cancer (glio/	2.7
		astro) U-118-MG
Fetal Lung	3.8	CNS cancer (neuro;	4.8
		met) SK-N-AS
Lung ca. NCI-N417	3.9	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.9	CNS cancer (astro)	5.2
		SNB-75
Lung ca. NCI-H146	0.8	CNS cancer (glio)	0.5
		SNB-19
Lung ca. SHP-77	2.3	CNS cancer (glio)	8.3
		SF-295
Lung ca. A549	0.9	Brain (Amygdala)	2.9
		Pool
Lung ca. NCI-H526	2.9	Brain (cerebellum)	5.9
Lung ca. NCI-H23	1.4	Brain (fetal)	25.3
Lung ca. NCI-H460	2.2	Brain (Hippocampus)	3.7
		Pool
Lung ca. HOP-62	2.0	Cerebral Cortex Pool	4.6
Lung ca. NCI-H522	31.6	Brain (Substantia	4.7
		nigra) Pool
Liver	20.7	Brain (Thalamus) Pool	3.8
Fetal Liver	63.7	Brain (whole)	9.2
Liver ca. HepG2	100.0	Spinal Cord Pool	3.6
Kidney Pool	11.2	Adrenal Gland	4.2
Fetal Kidney	5.3	Pituitary gland Pool	0.8
Renal ca. 786-0	1.6	Salivary Gland	1.0
Renal ca. A498	0.8	Thyroid (female)	2.0
Renal ca. ACHN	2.2	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	12.9	Pancreas Pool	3.0

[0785]

TABLE BE
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(%) Ag4470,		(%) Ag4470,
	Run		Run
Tissue Name	191882058	Tissue Name	191882058
Secondary Th1 act	21.8	HUVEC IL-1beta	11.1
Secondary Th2 act	14.9	HUVEC IFN gamma	29.9
Secondary Tr1 act	11.3	HUVEC TNF alpha +	4.5
		IFN gamma
Secondary Th1 rest	5.3	HUVEC TNF alpha +	45.7
		IL4
Secondary Th2 rest	1.8	HUVEC IL-11	28.3
Secondary Tr1 rest	2.3	Lung Microvascular	71.2
		EC none
Primary Th1 act	42.0	Lung Microvascular	27.7
		EC TNFalpha +
		IL-1beta
Primary Th2 act	37.6	Microvascular Dermal	38.4
		EC none
Primary Tr1 act	42.3	Microsvasular Dermal	24.1
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	1.1	Bronchial epithelium	5.0
		TNFalpha + IL-1beta
Primary Th2 rest	1.3	Small airway	6.6
		epithelium none
Primary Tr1 rest	0.0	Small airway	1.3
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	5.9	Coronery artery SMC	10.3
lymphocyte act		rest
CD45RO CD4	9.9	Coronery artery SMC	1.8
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	19.2	Astrocytes rest	1.4
Secondary CD8	10.4	Astrocytes	3.1
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	4.5	KU-812 (Basophil)	29.5
lymphocyte act		rest
CD4 lymphocyte	0.6	KU-812 (Basophil)	18.9
none		PMA/ionomycin
2ry Th1/Th2/	4.9	CCD1106	2.3
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	1.1	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	3.5	Liver cirrhosis	10.2
LAK cells IL-2 +	1.4	NCI-H292 none	16.6
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	9.0
IFN gamma
LAK cells IL-2 +	2.3	NCI-H292 IL-9	32.5
IL-18
LAK cells PMA/	3.3	NCI-H292 IL-13	5.3
ionomycin
NK Cells IL-2 rest	3.9	NCI-H292 IFN gamma	15.5
Two Way MLR 3	4.8	HPAEC none	37.9
day
Two Way MLR 5	9.3	HPAEC TNF alpha +	17.4
day		IL-1 beta
Two Way MLR 7	9.4	Lung fibroblast	22.7
day		none
PBMC rest	0.0	Lung fibroblast TNF	11.7
		alpha + IL-1 beta
PBMC PWM	20.6	Lung fibroblast IL-4	17.7
PBMC PHA-L	18.3	Lung fibroblast IL-9	36.1
Ramos (B cell) none	4.5	Lung fibroblast IL-13	36.1
Ramos (B cell)	9.2	Lung fibroblast IFN	11.7
ionomycin		gamma
B lymphocytes	20.3	Dermal fibroblast	1.3
PWM		CCD1070 rest
B lymphocytes	10.4	Dermal fibroblast	0.8
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	1.9	Dermal fibroblast	1.6
		CCD1070 IL-1 beta
EOL-1 dbcAMP	2.7	Dermal fibroblast IFN	5.4
PMA/ionomycin		gamma
Dendritic cells none	5.1	Dermal fibroblast IL-4	100.0
Dendritic cells LPS	6.7	Dermal Fibroblasts	39.5
		rest
Dendritic cells	7.9	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	1.0	Neutrophils rest	0.5
Monocytes LPS	1.6	Colon	0.5
Macrophages rest	13.0	Lung	0.7
Macrophages LPS	0.0	Thymus	59.9
HUVEC none	18.3	Kidney	0.7
HUVEC starved	13.5

[0786]

TABLE BF
general oncology screening panel_v_2.4
	Rel. Exp.		Rel. Exp.
	(%) Ag4470,		(%) Ag4470,
	Run		Run
Tissue Name	260280484	Tissue ame	260280484
Colon cancer 1	1.0	Bladder NAT 2	0.1
Colon NAT 1	3.0	Bladder NAT 3	0.0
Colon cancer 2	0.0	Bladder NAT 4	1.1
Colon NAT 2	0.3	Prostate	4.3
		adenocarcinoma 1
Colon cancer 3	1.1	Prostate	1.5
		adenocarcinoma 2
Colon NAT 3	0.0	Prostate	1.8
		adenocarcinoma 3
Colon malignant	2.2	Prostate	4.4
cancer 4		adenocarcinoma 4
Colon NAT 4	0.0	Prostate NAT 5	1.0
Lung cancer 1	0.4	Prostate	0.5
		adenocarcinoma 6
Lung NAT 1	0.2	Prostate	0.2
		adenocarcinoma 7
Lung cancer 2	58.2	Prostate	0.7
		adenocarcinoma 8
Lung NAT 2	0.0	Prostate	1.7
		adenocarcinoma 9
Squamous cell	1.3	Prostate NAT 10	0.6
carcinoma 3
Lung NAT 3	46.3	Kidney cancer 1	9.5
Metastatic melanoma 1	28.9	Kidney NAT 1	3.7
Melanoma 2	1.4	Kidney cancer 2	100.0
Melanoma 3	0.3	Kidney NAT 2	2.2
Metastatic melanoma 4	26.2	Kidney cancer 3	71.7
Metastatic melanoma 5	16.3	Kidney NAT 3	1.9
Bladder cancer 1	0.3	Kidney cancer 4	75.8
Bladder NAT 1	0.0	Kidney NAT 4	0.9
Bladder cancer 2	1.0

[0787] AI_comprehensive panel_v1.0 Summary: Ag4470 These results confirm expression of this gene in cells involved in the immune response. Highest expression of this gene is seen in normal lung (CT=30.5). Please see Panel 4D for discussion of utility of this gene in inflammation.

[0788] CNS_neurodegeneration_v1.0 Summary: Ag4470 This panel does not show differential expression of this gene in Alzheimer's disease. However, this profile confirms the expression of this gene at low but significant levels in the brain. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurologic disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, multiple sclerosis, stroke and epilepsy.

[0789] General_screening_panel_v1.4 Summary: Ag4470 Highest expression of this gene is seen in a liver cancer cell line (CT=30), with moderate levels of expression seen in fetal and adult liver, and cell lines derived from colon, renal and lung cancers. Thus, expression of this gene could be used to differentiate liver derived tissue from other samples on this panel.

[0790] Panel 4.1D Summary: Ag4470 Highest expression of this gene in this experiment is detected in IL-4 treated dermal fibroblasts (CTs=30). In addition, this experiment shows low but significant levels of expresion in resting neutrophils (CT=33.2). In addition, this gene is expressed at moderate levels in IFN gamma stimulated dermal fibroblasts, activated lung fibroblasts, BPAECs, lung and dermal microvasculature, activated small airway and bronchial epithelium, activated NCI-H292 cells, acutely activated T cells, and activated B cells. Based on these levels of expression in T cells, activated B cells and cells in lung and skin, therapeutics that block the function of this gene product may be useful as therapeutics that reduce or eliminate the symptoms in patients with autoimmune and inflammatory diseases in which activated B cells present antigens in the generation of the aberrant immune response and in treating T-cell mediated diseases, including Crohn's disease, ulcerative colitis, multiple sclerosis, chronic obstructive pulmonary disease, asthma, allergy, emphysema, rheumatoid arthritis, or psoriasis.

[0791] general oncology screening panel_v—2.4 Summary: Ag4470 Highest expression of this gene is seen in kidney cancer (CT=30). In addition, this gene is more highly expressed in lung and kidney cancer than in the corresponding normal adjacent tissue. Thus, expression of this gene could be used as a marker of these cancers. Furthemore, therapeutic modulation of the expression or function of this gene product may be useful in the treatment of lung and kidney cancer.

[0792] C. CG106417-04: von Willebrand Factor like Protein

[0793] Expression of gene CG106417-04 was assessed using the primer-probe sets Ag1294b, Ag746, Ag905 and Ag4726, described in Tables CA, CB, CC and CD. Results of the RTQ-PCR runs are shown in Tables CE, CF, CG, CH, CI, CJ and CK.

TABLE CA
Probe Name Ag1294b
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-cattggcagctacaagtgttc-3′	21	408	230
Probe	TET-5′-ctgtcgaactggcttccaccttcat-3′-TAMRA	25	429	231
Reverse	5′-cctccgacactcgtttacatc-3′	21	475	232

[0794]

TABLE CB
Probe Name Ag746
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gcattggcagctacaagtgt-3′	20	407	233
Probe	TET-5′-ctgtcgaactggcttccaccttcat-3′-TAMRA	25	429	234
Reverse	5′-cctccgacactcgtttacatc-3′	21	475	235

[0795]

TABLE CC
Probe Name Ag905
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-cattggcagctacaagtgttc-3′	21	408	236
Probe	TET-5′-ctgtcgaactggcttccaccttcat-	25	429	237
	3′-TAMRA
Reverse	5′-cctccgacactcgtttacatc-3′	21	475	238

[0796]

TABLE CD
Probe Name Ag4726
Primers	Length	Start Position	SEQ ID No
Forward	5′-gtgtctgtctggctggaaac-3′	20	1226	239
Probe	TET-5′-tgcatctctcctgagtgtccttctgg	26	1252	240
	-3′-TAMRA
Reverse	5′-acaagtacagcaatccgtctgt-3′	22	1296	241

[0797]

TABLE CE
AI_comprehensive panel_v1.0
	Rel. Exp.		Rel. Exp.
	(%)		(%)
	Ag1294b,		Ag1294b,
	Run		Run
Tissue Name	249007981	issue Name	249007981
110967 COPD-F	6.6	112427 Match Control	30.8
		Psoriasis-F
110980 COPD-F	16.6	112418 Psoriasis-M	4.6
110968 COPD-M	3.9	112723 Match Control	23.8
		Psoriasis-M
110977 COPD-M	31.6	112419 Psoriasis-M	2.7
110989	45.1	112424 Match Control	1.9
Emphysema-F		Psoriasis-M
110992	7.2	112420 Psoriasis-M	4.9
Emphysema-F
110993	5.8	112425 Match Control	25.9
Emphysema-F		Psoriasis-M
110994	3.3	104689 (MF) OA	12.9
Emphysema-F		Bone-Backus
110995	2.0	104690 (MF) Adj	3.7
Emphysema-F		“Normal” Bone-
		Backus
110996	3.1	104691 (MF) OA	6.9
Emphysema-F		Synovium-Backus
110997 Asthma-M	3.7	104692 (BA) OA	21.3
		Cartilage-Backus
111001 Asthma-F	2.8	104694 (BA) OA	6.6
		Bone-Backus
111002 Asthma-F	5.3	104695 (BA) Adj	2.3
		“Normal” Bone-
		Backus
111003 Atopic	6.1	104696 (BA) OA	5.7
Asthma-F		Synovium-Backus
111004 Atopic	3.4	104700 (SS) OA	6.2
Asthma-F		Bone-Backus
111005 Atopic	3.9	104701 (SS) Adj	3.8
Asthma-F		“Normal” Bone-
		Backus
111006 Atopic	2.4	104702 (SS) OA	15.4
Asthma-F		Synovium-Backus
111417 Allergy-M	6.6	117093 OA Cartilage	18.0
		Rep7
112347 Allergy-M	3.3	112672 OA Bone5	90.1
112349 Normal	3.2	112673 OA	63.7
Lung-F		Synovium5
112357 Normal	100.0	112674 OA Synovial	32.3
Lung-F		Fluid cells5
112354 Normal	58.6	117100 OA Cartilage	3.3
Lung-M		Rep14
112374 Crohns-F	7.5	112756 OA Bone9	7.0
112389 Match	3.5	112757 OA	12.2
Control Crohns-F		Synovium9
112375 Crohns-F	5.1	112758 OA Synovial	3.9
		Fluid Cells9
112732 Match	0.5	117125 RA Cartilage	4.6
Control Crohns-F		Rep2
112725 Crohns-M	10.6	113492 Bone2 RA	2.4
112387 Match	3.5	113493 Synovium2	1.1
Control Crohns-M		RA
112378 Crohns-M	1.7	113494 Syn Fluid	1.4
		Cells RA
112390 Match	55.5	113499 Cartilage4 RA	1.4
Control Crohns-M
112726 Crohns-M	3.6	113500 Bone4 RA	0.5
112731 Match	13.9	113501 Synovium4	1.7
Control Crohns-M		RA
112380 Ulcer Col-F	13.7	113502 Syn Fluid	1.8
		Cells4 RA
112734 Match	5.6	113495 Cartilage3 RA	1.6
Control Ulcer Col-F
112384 Ulcer Col-F	3.9	113496 Bone3 RA	1.1
112737 Match	3.3	113497 Synovium3	0.0
Control Ulcer Col-F		RA
112386 Ulcer Col-F	0.0	113498 Syn Fluid	0.6
		Cells3 RA
112738 Match	0.0	117106 Normal	4.5
Control Ulcer Col-F		Cartilage Rep20
112381 Ulcer	4.2	113663 Bone3 Normal	6.7
Col-M
112735 Match	18.2	113664 Synovium3	1.2
Control Ulcer		Normal
Col-M
112382 Ulcer	4.2	113665 Syn Fluid	0.9
Col-M		Cells3 Normal
112394 Match	0.0	117107 Normal	1.3
Control Ulcer		Cartilage Rep22
Col-M
112383 Ulcer	12.2	113667 Bone4 Normal	11.8
Col-M
112736 Match	2.0	113668 Synovium4	12.0
Control Ulcer		Normal
Col-M
112423 Psoriasis-F	3.9	113669 Syn Fluid	10.7
		Cells4 Normal

[0798]

TABLE CF
CNS neurodegeneration v1.0
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag1274b,	Ag4726,		Ag1294b,	Ag4726,
	Run	Run		Run	Run
Tissue Name	206231468	224706360	issue Name	206231468	224706360
AD 1 Hippo	11.2	11.6	Control (Path) 3	1.5	11.4
			Temporal Ctx
AD 2 Hippo	22.5	23.5	Control (Path) 4	19.2	20.3
			Temporal Ctx
AD 3 Hippo	4.7	0.0	AD 1 Occipital Ctx	15.8	17.4
AD 4 Hippo	8.7	15.2	AD 2 Occipital Ctx	0.0	0.0
			(Missing)
AD 5 hippo	37.6	35.6	AD 3 Occipital Ctx	1.2	3.6
AD 6 Hippo	100.0	100.0	AD 4 Occipital Ctx	17.8	7.9
Control 2 Hippo	28.7	21.9	AD 5 Occipital Ctx	8.7	17.6
Control 4 Hippo	30.4	40.3	AD 6 Occipital Ctx	12.3	30.8
Control (Path) 3	6.9	3.6	Control 1 Occipital	0.0	3.0
Hippo			Ctx
AD 1 Temporal Ctx	16.3	26.1	Control 2 Occipital	27.4	34.6
			Ctx
AD 2 Temporal Ctx	31.6	25.2	Control 3 Occipital	5.4	2.8
			Ctx
Ad 3 Temporal Ctx	3.8	5.6	Control 4 Occipital	6.7	15.4
			Ctx
AD 4 Temporal Ctx	10.9	36.1	Control (Path) 1	56.3	85.3
			Occipital Ctx
AD 5 Inf Temporal	34.6	35.8	Control (Path) 2	10.4	21.8
Ctx			Occipital Ctx
AD 5 SupTemporal	19.6	55.9	Control (Path) 3	1.2	0.0
Ctx			Occipital Ctx
AD 6 Inf Temporal	73.7	76.8	Control (Path) 4	6.3	5.0
Ctx			Occipital Ctx
AD 6 Sup Temporal	81.2	97.9	Control 1 Parietal	6.4	9.7
Ctx			Ctx
Control 1 Temporal	1.2	5.1	Control 2 Parietal	39.5	55.9
Ctx			Ctx
Control 2 Temporal	15.5	42.9	Control 3 Parietal	4.4	11.2
Ctx			Ctx
Control 3 Temporal	5.9	18.4	Control (Path) 1	17.6	45.4
Ctx			Parietal Ctx
Control 4 Temporal	7.9	17.2	Control (Path) 2	17.6	12.1
Ctx			Parietal Ctx
Control (Path) 1	41.8	43.5	Control (Path) 3	0.0	4.2
Temporal Ctx			Parietal Ctx
Control (Path) 2	26.2	36.6	Control (Path) 4	26.4	30.1
Temporal Ctx			Parietal Ctx

[0799]

TABLE CG
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag4726,		(%) Ag4726,
	Run		Run
Tissue Name	222842378	issue Name	222842378
Adipose	3.3	Renal ca. TK-10	41.8
Melanoma*	2.7	Bladder	1.8
Hs688(A).T
Melanoma*	2.7	Gastric ca. (liver met.)	2.0
Hs688(B).T		NCI-N87
Melanoma* M14	4.8	Gastric ca. KATO III	0.6
Melanoma*	0.1	Colon ca. SW-948	0.6
LOXIMVI
Melanoma*	0.4	Colon ca. SW480	0.7
SK-MEL-5
Squamous cell	0.2	Colon ca.* (SW480	12.8
carcinoma SCC-4		met) SW620
Testis Pool	4.3	Colon ca. HT29	0.1
Prostate ca.* (bone	1.6	Colon ca. HCT-116	3.7
met) PC-3
Prostate Pool	0.5	Colon ca. CaCo-2	31.9
Placenta	7.7	Colon cancer tissue	7.9
Uterus Pool	0.1	Colon ca. SW1116	1.0
Ovarian ca.	0.7	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.6	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.3	Colon Pool	1.0
OVCAR-4
Ovarian ca.	1.1	Small Intestine Pool	4.9
OVCAR-5
Ovarian ca.	1.4	Stomach Pool	3.4
IGROV-1
Ovarian ca.	0.7	Bone Marrow Pool	0.0
OVCAR-8
Ovary	5.0	Fetal Heart	0.7
Breast ca. MCF-7	0.4	Heart Pool	0.7
Breast ca.	0.5	Lymph Node Pool	2.6
MDA-MB-231
Breast ca. BT 549	0.7	Fetal Skeletal Muscle	1.6
Breast ca. T47D	4.2	Skeletal Muscle Pool	1.0
Breast ca. MDA-N	0.2	Spleen Pool	0.4
Breast Pool	0.8	Thymus Pool	7.9
Trachea	1.3	CNS cancer (glio/	6.4
		astro) U87-MG
Lung	5.5	CNS cancer (glio/	1.6
		astro) U-118-MG
Fetal Lung	1.8	CNS cancer (neuro;	4.4
		met) SK-N-AS
Lung ca. NCI-N417	3.6	CNS cancer (astro)	0.2
		SF-539
Lung ca. LX-1	0.7	CNS cancer (astro)	4.4
		SNB-75
Lung ca. NCI-H146	0.8	CNS cancer (glio)	1.1
		SNB-19
Lung ca. SHP-77	0.3	CNS cancer (glio)	5.1
		SF-295
Lung ca. A549	0.8	Brain (Amygdala)	2.5
		Pool
Lung ca. NCI-H526	2.1	Brain (cerebellum)	7.3
Lung ca. NCI-H23	0.8	Brain (fetal)	12.2
Lung ca. NCI-H460	1.2	Brain (Hippocampus)	1.9
		Pool
Lung ca. HOP-62	0.5	Cerebral Cortex Pool	2.6
Lung ca. NCI-H522	20.2	Brain (Substantia	2.1
		nigra) Pool
Liver	11.6	Brain (Thalamus) Pool	3.9
Fetal Liver	61.1	Brain (whole)	8.5
Liver ca. HepG2	100.0	Spinal Cord Pool	1.9
Kidney Pool	6.7	Adrenal Gland	2.6
Fetal Kidney	2.0	Pituitary gland Pool	0.6
Renal ca. 786-0	1.7	Salivary Gland	0.9
Renal ca. A498	1.3	Thyroid (female)	1.8
Renal ca. ACHN	2.5	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	10.6	Pancreas Pool	1.1

[0800]

TABLE CH
Panel 1.2
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag746,	Ag746,		Ag746,	Ag746,
	Run	Run		Run	Run
Tissue Name	115163442	119442272	Tissue Name	115163442	119442272
Endothelial cells	12.3	5.9	Renal ca. 786-0	0.0	0.0
Heart (Fetal)	0.0	0.0	Renal ca. A498	0.0	0.0
Pancreas	0.0	0.0	Renal ca. RXF 393	0.0	0.0
Pancreatic ca.	0.0	0.0	Renal ca. ACHN	0.0	0.0
CAPAN 2
Adrenal Gland	0.0	0.2	Renal ca. UO-31	0.0	0.0
Thyroid	0.1	0.0	Renal ca. TK-10	0.0	0.0
Salivary gland	0.0	0.0	Liver	32.8	53.2
Pituitary gland	0.2	0.1	Liver (fetal)	72.7	100.0
Brain (fetal)	2.4	16.0	Liver ca.	100.0	94.0
			(hepatoblast) HepG2
Brain (whole)	0.0	0.3	Lung	0.0	0.0
Brain (amygdala)	0.0	0.0	Lung (fetal)	0.0	0.0
Brain (cerebellum)	0.0	0.0	Lung ca. (small cell)	0.0	0.0
			LX-1
Brain (hippocampus)	0.0	0.0	Lung ca. (small cell)	0.0	0.0
			NCI-H69
Brain (thalamus)	0.0	0.0	Lung ca. (s.cell var.)	0.0	0.0
			SHP-77
Cerebral Cortex	0.0	0.0	Lung ca. (large	0.0	0.0
			cell)NCI-H460
Spinal cord	0.0	0.0	Lung ca. (non-sm.	0.0	0.0
			cell) A549
glio/astro U87-MG	0.0	0.0	Lung ca. (non-s.cell)	0.0	0.0
			NCI-H23
glio/astro U-118-MG	0.0	0.0	Lung ca. (non-s.cell)	0.0	0.0
			HOP-62
astrocytoma	0.0	0.0	Lung ca. (non-s.cl)	63.7	90.1
SW1783			NCI-H522
neuro*; met	0.0	0.2	Lung ca. (squam.)	0.0	0.0
SK-N-AS			SW 900
astrocytoma SF-539	0.0	0.0	Lung sa. (squam.)	0.0	0.0
			NCI-H596
astrocytoma SNB-75	0.0	0.0	Mammary gland	0.7	3.6
glioma SNB-19	0.0	0.0	Breast ca.* (pl.ef)	0.0	0.0
			MCF-7
glioma U251	0.0	0.0	Breast ca.* (pl.ef)	0.0	0.0
			MDA-MB-231
glioma SF-295	0.0	0.0	Breast ca.* (pl. ef)	0.0	0.0
			T47D
Heart	0.0	0.0	Breast ca. BT-549	0.0	0.0
Skeletal Muscle	0.0	0.0	Breast ca. MDA-N	0.0	0.0
Bone marrow	0.0	0.0	Ovary	0.5	11.7
Thymus	1.2	2.8	Ovarian ca.	0.0	0.0
			OVCAR-3
Spleen	0.0	0.0	Ovarian ca.	0.0	0.0
			OVCAR-4
Lymph node	0.0	0.0	Ovarian ca.	0.0	0.0
			OVCAR-5
Colorectal Tissue	0.0	0.0	Ovarian ca.	0.0	0.0
			OVCAR-8
Stomach	0.0	0.0	Ovarian ca.	0.0	0.0
			IGROV-1
Small intestine	0.0	0.0	Ovarian ca. (ascites)	0.0	0.0
			SK-OV-3
Colon ca. SW480	0.0	0.0	Uterus	0.0	0.0
Colon ca.* SW620	1.1	1.9	Placenta	34.4	39.5
(SW480 met)
Colon ca. HT29	0.0	0.0	Prostate	0.0	0.0
Colon ca. HCT-116	0.0	0.0	Prostate ca.* (bone	0.0	0.0
			met) PC-3
Colon ca. CaCo-2	46.3	56.6	Testis	1.0	3.5
Colon ca. Tissue	0.0	0.0	Melanoma	0.0	0.0
(ODO3866)			Hs688(A).T
Colon ca. HCC-2998	0.0	0.0	Melanoma* (met)	0.0	0.0
			Hs688(B).T
Gastric ca.* (liver	0.0	0.0	Melanoma	0.0	0.0
met) NCI-N87			UACC-62
Bladder	0.0	0.0	Melanoma M14	0.0	0.0
Trachea	0.0	0.0	Melanoma LOX	0.0	0.0
			IMVI
Kidney	0.0	0.0	Melanoma* (met)	0.0	0.0
			SK-MEL-5
Kidney (fetal)	0.1	0.9

[0801]

TABLE CI
Panel 2D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag746,	Ag746,		Ag746,	Ag746,
	Run	Run		Run	Run
Tissue Name	147127131	148019631	Tissue Name	147127131	148019631
Normal Colon	18.3	21.8	Kidney Margin	6.5	6.4
			8120608
CC Well to Mod Diff	16.5	23.7	Kidney Cancer	2.2	0.7
(ODO3866)			8120613
CC Margin	3.1	0.0	Kidney Margin	6.3	3.0
(ODO3866)			8120614
CC Gr.2 rectosigmoid	0.0	0.8	Kidney Cancer	10.9	16.5
(ODO3868)			9010320
CC Margin	0.5	2.0	Kidney Margin	9.0	11.3
(ODO3868)			9010321
CC Mod Diff	1.2	2.3	Normal Uterus	4.3	6.3
(ODO3920)
CC Margin	1.3	2.3	Uterus Cancer	13.4	17.7
(ODO3920)			064011
CC Gr.2 ascend colon	3.4	4.4	Normal Thyroid	9.1	14.9
(ODO3921)
CC Margin	1.3	0.0	Thyroid Cancer	6.4	5.9
(ODO3921)
CC from Partial	8.4	1.9	Thyroid Cancer	4.4	5.1
Hepatectomy			A302152
(ODO4309) Mets
Liver Margin	49.7	41.5	Thyroid Margin	12.0	22.1
(ODO4309)			A302153
Colon mets to lung	0.3	5.3	Normal Breast	9.9	14.3
(ODO4451-01)
Lung Margin	0.0	1.8	Breast Cancer	0.4	0.2
(ODO4451-02)			(ODO4566)
Normal Prostate	9.1	12.1	Breast Cancer	5.3	3.9
6546-1			(ODO4590-01)
Prostate Cancer	2.0	9.7	Breast Cancer Mets	4.0	10.4
(ODO4410)			(ODO4590-03)
Prostate Margin	16.8	20.3	Breast Cancer	7.2	4.4
(ODO4410)			Metastasis
			(ODO4655-05)
Prostate Cancer	13.5	14.4	Breast Cancer	5.2	3.3
(ODO4720-01)			064006
Prostate Margin	14.0	22.4	Breast Cancer 1024	12.1	18.6
(ODO4720-02)
Normal Lung 061010	6.8	11.7	Breast Cancer	2.7	5.3
			9100266
Lung Met to Muscle	1.8	0.7	Breast Margin	5.0	5.8
(ODO4286)			9100265
Muscle Margin	11.5	13.1	Breast Cancer	0.5	1.8
(ODO4286)			A209073
Lung Malignant	1.5	6.0	Breast Margin	1.7	0.4
Cancer (ODO3126)			A209073
Lung Margin	4.8	2.4	Normal Liver	39.5	47.0
(ODO3126)
Lung Cancer	4.2	2.3	Liver Cancer	4.2	0.6
(ODO4404)			064003
Lung Margin	9.0	10.4	Liver Cancer 1025	66.4	74.2
(ODO4404)
Lung Cancer	0.3	0.0	Liver Cancer 1026	36.1	42.6
(ODO4565)
Lung Margin	0.4	0.3	Liver Cancer	100.0	100.0
(ODO4565)			6004-T
Lung Cancer	10.7	11.1	Liver Tissue	22.8	34.4
(ODO4237-01)			6004-N
Lung Margin	4.9	5.4	Liver Cancer	39.2	35.4
(ODO4237-02)			6005-T
Ocular Mel Met to	10.5	11.9	Liver Tissue	33.2	38.2
Liver (ODO4310)			6005-N
Liver Margin	22.4	32.8	Normal Bladder	6.6	4.9
(ODO4310)
Melanoma Mets to	0.0	0.0	Bladder Cancer	1.0	4.8
Lung (ODO4321)			1023
Lung Margin	0.6	0.0	Bladder Cancer	2.6	0.7
(ODO4321)			A302173
Normal Kidney	5.3	5.3	Bladder Cancer	0.0	0.7
			(ODO4718-01)
Kidney Ca. Nuclear	39.8	43.8	Bladder Normal	3.5	14.4
grade 2 (ODO4338)			Adjacent
			(ODO4718-30)
Kidney Margin	4.8	6.4	Normal Ovary	50.7	47.3
(ODO4338)
Kidney Ca Nuclear	3.0	0.3	Ovarian Cancer	10.2	7.4
grade ½ (ODO4339)			064008
Kidney Margin	5.4	10.0	Ovarian Cancer	73.7	80.7
(ODO4339)			(ODO4768-07)
Kidney Ca, Clear cell	18.2	19.2	Ovary Margin	2.6	0.8
type (ODO4340)			(ODO4768-08)
Kidney Margin	9.0	10.4	Normal Stomach	2.9	2.9
(ODO4340)
Kidney Ca, Nuclear	5.2	8.3	Gastric Cancer	0.0	1.1
grade 3 (ODO4348)			9060358
Kidney Margin	6.9	4.7	Stomach Margin	2.4	0.3
(ODO4348)			9060359
Kidney Cancer	41.8	45.4	Gastric Cancer	0.5	1.1
(ODO4622-01)			9060395
Kidney Margin	1.9	1.4	Stomach Margin	5.2	2.0
(ODO4622-03)		9060394
Kidney Cancer	9.2	6.2	Gastric Cancer	3.4	7.0
(ODO4450-01)			9060397
Kidney Margin	10.2	9.0	Stomach Margin	1.4	0.0
(ODO4450-03)			9060396
Kidney Cancer	2.2	1.7	Gastric Cancer	1.3	6.0
8120607			064005

[0802]

TABLE CJ.
Panel 4.1D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag1294b,	Ag4726,		Ag1294b,	Ag4726,
	Run	Run		Run	Run
Tissue Name	200065765	204150067	Tissue Name	200065765	204150067
Secondary Th1 act	15.3	8.4	HUVEC IL-1beta	5.6	10.2
Secondary Th2 act	7.2	0.4	HUVEC IFN gamma	21.9	13.3
Secondary Tr1 act	5.5	3.1	HUVEC TNF alpha +	3.5	1.1
			IFN gamma
Secondary Th1 rest	6.7	0.5	HUVEC TNF alpha +	31.2	19.1
			IL4
Secondary Th2 rest	1.0	2.6	HUVEC IL-11	17.7	20.7
Secondary Tr1 rest	1.3	0.5	Lung Microvascular	65.1	61.6
			EC none
Primary Th1 act	26.6	24.8	Lung Microvascular	34.4	30.4
			EC TNFalpha +
			IL-1beta
Primary Th2 act	34.2	19.8	Microvascular	42.3	29.9
			Dermal EC none
Primary Tr1 act	40.3	27.9	Microvascular	16.7	7.6
			Dermal EC
			TNFalpha + IL-1beta
Primary Th1 rest	0.3	0.0	Bronchial epithelium	2.4	4.4
			TNFalpha + IL1beta
Primary Th2 rest	0.5	0.0	Small airway	1.7	4.2
			epithelium none
Primary Tr1 rest	0.0	1.1	Small airway	2.5	2.4
			epithelium TNFalpha +
			IL-1beta
CD45RA CD4	7.7	2.2	Coronery artery SMC	9.0	2.1
lymphocyte act			rest
CD45RO CD4	10.9	16.5	Coronery artery SMC	5.2	4.1
lymphocyte act			TNFalpha + IL-1beta
CD8 lymphocyte act	11.0	9.9	Astrocytes rest	2.1	0.8
Secondary CD8	11.8	8.9	Astrocytes TNFalpha +	2.2	1.2
lymphocyte rest			IL-1beta
Secondary CD8	4.7	1.9	KU-812 (Basophil)	10.2	14.9
lymphocyte act			rest
CD4 lymphocyte none	0.0	0.0	KU-812 (Basophil)	11.1	8.6
			PMA/ionomycin
2ry	1.7	2.5	CCD1106	0.0	0.9
Th1/Th2/Tr1_anti-CD95			(Keratinocytes) none
CH11
LAK cells rest	0.0	1.4	CCD1106	0.6	0.0
			(Keratinocytes)
			TNFalpha + IL-1beta
LAK cells IL-2	3.1	1.7	Liver cirrhosis	6.8	6.0
LAK cells IL-2 + IL-12	2.9	1.1	NCI-H292 none	21.3	10.3
LAK cells IL-2 + IFN	0.5	1.3	NCI-H292 IL-4	11.5	7.3
gamma
LAK cells IL-2 + IL-18	0.5	1.1	NCI-H292 IL-9	13.8	17.4
LAK cells	1.0	4.2	NCI-H292 IL-13	19.9	6.7
PMA/ionomycin
NK Cells IL-2 rest	1.4	2.0	NCI-H292 IFN	7.3	13.8
			gamma
Two Way MLR 3 day	3.1	1.8	HPAEC none	20.4	28.9
Two Way MLR 5 day	5.0	4.2	HPAEC TNF alpha +	21.5	15.4
			IL-1 beta
Two Way MLR 7 day	4.7	4.0	Lung fibroblast none	23.5	15.7
PBMC rest	0.6	0.0	Lung fibroblast TNF	8.8	9.2
			alpha + IL-1 beta
PBMC PWM	11.5	9.9	Lung fibroblast IL-4	21.2	24.7
PBMC PHA-L	7.2	14.1	Lung fibroblast IL-9	16.8	18.2
Ramos (B cell) none	1.8	2.0	Lung fibroblast IL-13	33.2	19.8
Ramos (B cell)	3.4	2.7	Lung fibroblast IFN	19.1	7.8
ionomycin			gamma
			CCD1070 rest
B lymphocytes CD40L	12.2	11.0	Dermal fibroblast	0.0	0.2
and IL-4			CCD1070 TNF alpha
EOL-1 dbcAMP	1.5	3.2	Dermal fibroblast	1.5	4.5
			CCD1070 IL-1 beta
EOL-1 dbcAMP	1.1	0.5	Dermal fibroblast	45.1	32.8
PMA/ionomycin			IFN gamma
Dendritic cells none	8.5	4.0	Dermal fibroblast	100.0	100.0
			IL-4
Dendritic cell LPS	6.4	5.9	Dermal Fibroblasts	53.6	39.2
			rest
Dendritic cells	8.7	4.7	Neutrophils	1.5	0.6
anti-CD40			TNFa + LPS
Monocytes rest	0.0	0.0	Neutrophils rest	10.2	0.1
Monocytes LPS	1.1	2.2	Colon	1.5	1.6
Macrophages rest	8.8	4.8	Lung	1.7	1.3
Macrophages LPS	0.0	0.0	Thymus	40.1	25.0
HUVEC none	10.1	8.5	Kidney	1.5	0.0
HUVEC starved	7.6	11.4

[0803]

TABLE CK
Panel 4D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag1294b,	Ag1294b,		Ag1294b,	Ag1294b,
	Run	Run		Run	Run
Tissue Name	138944262	139408252	Tissue Name	138944262	139408252
Secondary Th1 act	10.9	7.7	HUVEC IL-1beta	4.1	1.7
Secondary Th2 act	6.4	8.0	HUVEC IFN gamma	21.0	13.7
Secondary Tr1 act	11.3	9.3	HUVEC TNF alpha +	2.8	0.6
			IFN gamma
Secondary Th1 rest	3.4	2.7	HUVEC TNF alpha +	30.8	25.7
			IL4
Secondary Th2 rest	1.5	2.5	HUVEC IL-11	11.6	7.3
Secondary Tr1 rest	1.4	2.0	Lung Microvascular	24.1	20.0
			EC none
Primary Th1 act	48.0	46.0	Lung Microvascular	8.0	12.2
			EC TNFalpha +
			IL-1beta
Primary Th2 act	38.7	27.7	Microvascular	64.6	45.7
			Dermal EC none
Primary Tr1 act	72.2	55.5	Microsvasular	18.4	11.7
			Dermal EC
			TNFalpha + IL-1beta
Primary Th1 rest	3.1	2.3	Bronchial epithelium	5.2	5.4
			TNFalpha + IL1beta
Primary Th2 rest	1.0	0.8	Small airway	4.0	3.2
			epithelium none
Primary Tr1 rest	1.1	0.5	Small airway	8.2	4.5
			epithelium TNFalpha +
			IL-1beta
CD45RA CD4	2.9	1.8	Coronery artery SMC	5.8	6.3
lymphocyte act			rest
CD45RO CD4	18.6	12.2	Coronery artery SMC	4.5	5.1
lymphocyte act			TNFalpha + IL-1beta
CD8 lymphocyte act	17.8	6.8	Astrocytes rest	0.8	0.5
Secondary CD8	6.8	6.0	Astrocytes TNFalpha +	3.6	1.9
lymphocyte rest			IL-1beta
Secondary CD8	5.5	4.1	KU-812 (Basophil)	16.0	11.1
lymphocyte act			rest
CD4 lymphocyte none	0.0	0.2	KU-812 (Basophil)	12.3	9.5
			PMA/ionomycin
2ry	2.9	3.1	CCD1106	0.0	0.5
Th1/Th2/Tr1_anti-CD95			(Keratinocytes) none
CH11
LAK cells rest	1.4	0.3	CCD1106	0.7	0.4
			(Keratinocytes)
			TNFalpha + IL-1beta
LAK cells IL-2	3.8	2.2	Liver cirrhosis	8.4	3.8
LAK cells IL-2 + IL-12	3.0	0.8	Lupus kidney	2.0	3.2
LAK cells IL-2 + IFN	2.0	1.7	NCI-H292 none	21.9	25.7
gamma
LAK cells IL-2 + IL-18	0.5	0.2	NCI-H292 IL-4	15.7	12.3
LAK cells	0.7	1.3	NCI-H292 IL-9	20.6	14.7
PMA/ionomycin
NK Cells IL-2 rest	0.7	0.7	NCI-H292 IL-13	8.3	5.7
Two Way MLR 3 day	1.1	2.5	NCI-H292 IFN	5.1	8.2
			gamma
Two Way MLR 5 day	2.5	2.8	HPAEC none	18.7	23.8
Two Way MLR 7 day	4.5	5.0	HPAEC TNF alpha +	11.9	12.9
			IL-1 beta
PBMC rest	0.0	0.0	Lung fibroblast none	15.7	13.5
PBMC PWM	41.8	29.1	Lung fibroblast TNF	6.9	4.7
			alpha + IL-1 beta
PBMC PHA-L	34.4	21.8	Lung fibroblast IL-4	25.0	16.6
Ramos (B cell) none	4.7	2.4	Lung fibroblast IL-9	14.7	15.8
Ramos (B cell)	9.2	5.8	Lung fibroblast IL-13	40.3	32.5
ionomycin
B lymphocytes PWM	51.8	51.4	Lung fibroblast IFN	15.4	17.4
			gamma
B lymphocytes CD40L	10.2	12.3	Dermal fibroblast	0.5	0.9
and IL-4			CCD1070 rest
EOL-1 dbcAMP	0.3	0.2	Dermal fibroblast	0.9	0.8
			CCD1070 TNF alpha
EOL-1 dbcAMP	0.4	1.8	Dermal fibroblast	0.6	0.6
PMA/ionomycin			CCD1070 IL-1 beta
Dendritic cells none	6.7	3.8	Dermal fibroblast	32.1	18.4
			IFN gamma
Dendritic cells LPS	4.7	3.1	Dermal fibroblast	100.0	100.0
			IL-4
Dendritic cells	6.0	5.6	IBD Colitis 2	0.0	0.0
anti-CD40
Monocytes rest	0.0	0.0	IBD Crohn's	0.3	0.8
Monocytes LPS	0.7	0.8	Colon	1.4	0.5
Macrophages rest	19.8	9.9	Lung	0.5	0.8
Macrophages LPS	0.7	0.5	Thymus	2.9	4.3
HUVEC none	9.3	10.2	Kidney	65.5	47.3
HUVEC starved	19.2	13.1

[0804] AI_comprehensive panel_v1.0 Summary: Ag1294b Expression of this gene in this panel confirms expression of this gene in cells involved in the immune response. Highest expression of this gene is seen in normal lung (CT=30.5). Please see Panel 4D for discussion of utility of this gene in inflammation.

[0805] CNS_neurodegeneration_v1.0 Summary: Ag1294b/Ag4726 Two experiments with different probe and primer sets produce results that are in reasonable agreement. This panel does not show differential expression of this gene in Alzheimer's disease. However, this profile confirms the expression of this gene at low but significant levels in the brain. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurologic disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, multiple sclerosis, stroke and epilepsy.

[0806] General_screening_panel_v1.4 Summary: Ag4726 Highest expression of this gene is seen in a liver cancer cell line (CTs=30), with moderate levels of expression seen in fetal and adult liver, and cell lines derived from colon, renal and lung cancers. Thus, expression of this gene could be used to differentiate liver derived tissue from other samples on this panel.

[0807] Panel 1.2 Summary: Ag746 Two experiments with the same probe and primer set produce results that are in excellent agreement, with highest expression of this gene in a liver cancer cell line (CTs=27). High levels of expression are also seen in fetal and adult liver tissue, a colon cancer cell line and a lung cancer cell line. Thus, expression of this gene could be used to differentiate liver derived samples, the colon cancer cell line and the lung cancer cell line from other samples on this panel. Expression of this gene could also be used as a diagnostic marker to detect the presence of colon and lung cancers.

[0808] Moderate expression is also seen in the fetal brain, placenta, and endothelial cells.

[0809] Panel 2D Summary: Ag746 Two experiments with the same probe and primer set produce results that are in excellent agreement, with highest expression of this gene in liver cancer (CTs=31). The prominent expression in liver derived tissue is consistent with the results in Panel 1.2. Moderate levels of expression are also evident in samples from ovarian cancer and kidney cancer. Furthermore, expression of this gene is higher in these cancers than in the normal adjacent tissue. Thus, expression of this gene could be used to differentiate between liver derived samples and other samples on this panel and as a marker to detect the presence of liver, kidney, and ovarian cancer. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of liver, kidney, and ovarian cancers.

[0810] Panel 4.1D Summary: Ag1294b/Ag4726 Results from three experiments with three different probe and primer sets are in agreement with the expression profile in Panel 4D, with highest expression of this gene in this experiment in IL-4 treated dermal fibroblasts (CTs=30). In addition, this experiment shows low but significant levels of expresion in resting neutrophils (CT=33.2), a sample absent in Panel 4D. Please see Panel 4D for discussion of utility of this gene in inflammation.

[0811] Panel 4D Summary: Ag1294b Two experiments with the same probe and primer set produce results that are in excellent agreement, with highest expression of this gene in IL-4 treated dermal fibroblasts (CTs=30). In addition, this gene is expressed at moderate levels in IFN gamma stimulated dermal fibroblasts, activated lung fibroblasts, HPAECs, lung and dermal microvasculature, activated small airway and bronchial epithelium, activated NCI-H292 cells, acutely activated T cells, and activated B cells.

[0812] Based on these levels of expression in T cells, activated B cells and cells in lung and skin, therapeutics that block the function of this gene product may be useful as therapeutics that reduce or eliminate the symptoms in patients with autoimmune and inflammatory diseases in which activated B cells present antigens in the generation of the aberrant immune response and in treating T-cell mediated diseases, including Crohn's disease, ulcerative colitis, multiple sclerosis, chronic obstructive pulmonary disease, asthma, allergy, emphysema, rheumatoid arthritis, or psoriasis.

[0813] D. CG108901-03: Cytokine Receptor

[0814] Expression of full length physical clone CG108901-03 was assessed using the primer-probe set Ag6889, described in Table DA. Results of the RTQ-PCR runs are shown in Table DB.

TABLE DA
Probe Name Ag6889
Primers	Length	Start Position	SEQ ID No
Forward	5′-aaggaaagggccctgcct-3′	18	61	242
Probe	TET-5′-caacgtccaccagctgcaccatcac-	25	90	243
Reverse	5′-gaaccatggagaacagctgga-3′	21	120	244

[0815]

TABLE DB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag6889,		(%) Ag6889,
	Run		Run
Tissue Name	278388254	issue Name	278388254
Adipose	0.1	Renal ca. TK-10	1.0
Melanoma*	0.0	Bladder	0.6
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.0
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.0
Melanoma*	0.4	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	0.0	Colon ca. SW480	0.3
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	0.0	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	0.1
met) PC-3
Prostate Pool	0.1	Colon ca. CaCo-2	0.2
Placenta	100.0	Colon cancer tissue	0.2
Uterus Pool	0.0	Colon ca. SW1116	0.0
Ovarian ca.	0.0	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.1	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.1	Colon Pool	0.1
OVCAR-4
Ovarian ca.	0.1	Small Intestine Pool	0.1
OVCAR-5
Ovarian ca.	0.4	Stomach Pool	0.0
IGROV-1
Ovarian ca.	0.3	Bone Marrow Pool	0.0
OVCAR-8
Ovary	0.0	Fetal Heart	0.0
Breast ca. MCF-7	0.0	Heart Pool	0.0
Breast ca.	0.1	Lymph Node Pool	0.0
MDA-MB-231
Breast ca. BT 549	0.0	Fetal Skeletal Muscle	0.0
Breast ca. T47D	0.0	Skeletal Muscle Pool	0.0
Breast ca. MDA-N	0.0	Spleen Pool	0.4
Breast Pool	0.1	Thymus Pool	0.2
Trachea	0.1	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	0.0	CNS cancer (glio/	0.0
		astro) U-118-MG
Fetal Lung	0.1	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.2
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.0
		SF-295
Lung ca. A549	0.0	Brain (Amygdala)	0.1
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	0.3
Lung ca. NCI-H23	0.8	Brain (fetal)	0.2
Lung ca. NCI-H460	0.0	Brain (Hippocampus)	0.1
		Pool
Lung ca. HOP-62	0.0	Cerebral Cortex Pool	0.1
Lung ca. NCI-H522	0.4	Brain (Substantia	0.1
		nigra) Pool
Liver	0.1	Brain (Thalamus) Pool	0.1
Fetal Liver	0.3	Brain (whole)	0.1
Liver ca. HepG2	0.3	Spinal Cord Pool	0.2
Kidney Pool	0.1	Adrenal Gland	0.3
Fetal Kidney	0.0	Pituitary gland Pool	0.0
Renal ca. 786-0	0.3	Salivary Gland	0.1
Renal ca. A498	0.2	Thyroid (female)	0.0
Renal ca. ACHN	0.1	Pancreatic ca.	0.1
		CAPAN2
Renal ca. UO-31	0.5	Pancreas Pool	0.0

[0816] General_screening_panel_v1.6 Summary: Ag6889 High expression of this gene is restricted to placenta. Thus, expression of this gene may be used as a marker to distinguish placenta from other samples. This gene codes for a splice variant of EBV-induced gene 3 (EBI3), encodes a 34-kDa glycoprotein which lacks a membrane-anchoring motif and is secreted. EBI3 is shown to be expressed in vivo by scattered cells in interfollicular zones of tonsil tissue, by cells associated with sinusoids in perifollicular areas of spleen tissue, and at very high levels by placental syncytiotrophoblasts (Devergne et al., 1996, J. Virol. 70: 1143-1153, PMID:8551575). In addition, EBI3 levels are strongly up-regulated in sera from pregnant women and gradually increased with gestational age. EBI3 is an important immunomodulator in the fetal-maternal relationship, possibly involved in NK cell regulation (Devergne et al., 2001, Am J Pathol November 2001;159(5):1763-76, PMID: 11696437). Thus, therapeutic modulation of this gene or EBI3 protein encoded by this gene may be useful in the treatment of placenta or pregnancy related diseases.

[0817] E. CG108901-04: Cytokine Receptor

[0818] Expression of full length physical clone CG108901-04 was assessed using the primer-probe set Ag7033, described in Table EA. Results of the RTQ-PCR runs are shown in Tables EB and EC.

TABLE EA
Probe Name Ag7033
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-ctcccactgcacctgtagct-3′	20	254	245
Probe	TET-5′-taacagaccacatcatcaagcccgac	27	313	246
	c-3′-TAMRA
Reverse	5′-accagccccgtgccttt-3′	17	342	247

[0819]

TABLE EB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag7033,		(%) Ag7033,
	Run		Run
Tissue Name	282263480	issue Name	282263480
Adipose	0.0	Renal ca. TK-10	0.0
Melanoma*	0.0	Bladder	0.0
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.0
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.0
Melanoma*	0.0	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	0.0	Colon ca. SW480	0.0
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	0.0	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	0.0
met) PC-3
Prostate Pool	0.0	Colon ca. CaCo-2	0.0
Placenta	100.0	Colon cancer tissue	0.0
Uterus Pool	0.0	Colon ca. SW1116	0.0
Ovarian ca.	0.0	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.0	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	0.0
OVCAR-4
Ovarian ca.	0.0	Small Intestine Pool	0.0
OVCAR-5
Ovarian ca.	0.0	Stomach Pool	0.0
IGROV-1
Ovarian ca.	0.0	Bone Marrow Pool	0.0
OVCAR-8
Ovary	0.0	Fetal Heart	0.0
Breast ca. MCF-7	0.0	Heart Pool	0.0
Breast ca.	0.0	Lymph Node Pool	0.0
MDA-MB-231
Breast ca. BT 549	0.0	Fetal Skeletal Muscle	0.0
Breast ca. T47D	0.0	Skeletal Muscle Pool	0.0
Breast ca. MDA-N	0.0	Spleen Pool	0.0
Breast Pool	0.0	Thymus Pool	0.0
Trachea	0.0	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	0.0	CNS cancer (glio/	0.0
		astro) U-118-MG
Fetal Lung	0.0	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.0
		SF-295
Lung ca. A549	0.0	Brain (Amygdala)	0.0
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	0.0
Lung ca. NCI-H23	0.0	Brain (fetal)	0.0
Lung ca. NCI-H460	0.0	Brain (Hippocampus)	0.0
		Pool
Lung ca. HOP-62	0.0	Cerebral Cortex Pool	0.0
Lung ca. NCI-H522	0.0	Brain (Substantia	0.0
		nigra) Pool
Liver	0.0	Brain (Thalamus) Pool	0.0
Fetal Liver	0.0	Brain (whole)	0.0
Liver ca. HepG2	0.0	Spinal Cord Pool	0.0
Kidney Pool	0.0	Adrenal Gland	0.0
Fetal Kidney	0.0	Pituitary gland Pool	0.0
Renal ca. 786-0	0.0	Salivary Gland	0.0
Renal ca. A498	0.0	Thyroid (female)	0.0
Renal ca. ACHN	0.0	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	0.0	Pancreas Pool	0.0

[0820]

TABLE EC
Panel 4.1D
	Rel. Ep.		Rel. Exp.
	(%) Ag7033,		(%) Ag7033,
	Run		Run
Tissue Name	312115300	Tissue Name	312115300
Secondary Th1 act	0.0	HUVEC IL-1beta	0.0
Secondary Th2 act	0.0	HUVEC IFN gamma	0.0
Secondary Tr1 act	0.0	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	0.0
Secondary Tr1 rest	0.0	Lung Microvascular	0.0
		EC none
Primary Th1 act	0.0	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.0	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	0.0	Microsvasular Dermal	0.1
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	0.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.0	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	0.0	Coronery artery SMC	0.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.0	Astrocytes rest	0.0
Secondary CD8	0.0	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.0	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	100.0
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.0	Liver cirrhosis	0.0
LAK cells IL-2 +	0.0	NCI-H292 none	0.1
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	0.3	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	0.0
Two Way MLR 3	0.0	HPAEC none	0.0
day
Two Way MLR 5	0.0	HPAEC TNF alpha +	0.1
day		IL-1 beta
Two Way MLR 7	0.0	Lung fibroblast	0.0
day		none
PBMC rest	0.0	Lung fibroblast TNF	0.0
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.0	Lung fibroblast IL-9	0.0
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	0.0	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	0.2	Dermal fibroblast	0.0
PWM		CCD1070 rest
B lymphocytes	0.0	Dermal fibroblast	0.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	0.0	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	0.3	Dermal fibroblast IL-4	0.0
Dendritic cells LPS	0.1	Dermal Fibroblasts	0.0
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.3	Colon	0.0
Macrophages rest	0.6	Lung	0.0
Macrophages LPS	0.1	Thymus	0.0
HUVEC none	0.0	Kidney	0.0
HUVEC starved	0.0

[0821] General_screening_panely1.6 Summary: Ag7033 Low expression of this gene is restricted to placenta. Thus, expression of this gene may be used as a marker to distinguish placenta from other samples. This gene codes for a splice variant of EBV-induced gene 3 (EBI3), a 34-kDa glycoprotein that lacks a membrane-anchoring motif and is secreted. EBI3 is shown to be expressed in vivo by scattered cells in interfollicular zones of tonsil tissue, by cells associated with sinusoids in perifollicular areas of spleen tissue, and at very high levels by placental syncytiotrophoblasts (Devergne et al., 1996, J. Virol. 70: 1143-1153, PMID:8551575). In addition, EBI3 levels are strongly up-regulated in sera from pregnant women and gradually increased with gestational age. EBI3 is an important immunomodulator in the fetal-maternal relationship, possibly involved in NK cell regulation (Devergne et al., 2001, Am J Pathol November 2001;159(5):1763-76, PMID: 11696437). Thus, therapeutic modulation of this gene or EBI3 protein encoded by this gene may be useful in the treatment of placenta or pregnancy related diseases.

[0822] Panel 4.1D Summary: Ag7033 High expression of this gene is restricted to PMA/ionomycin activated basophils (CT=27.9). Basophils release histamines and other biological modifiers in reponse to allergens and play an important role in the pathology of asthma and hypersensitivity reactions. Therefore, therapeutics designed against the putative protein encoded by this gene may reduce or inhibit inflammation by blocking basophil function in these diseases. In addition, these cells are a reasonable model for the inflammatory cells that take part in various inflammatory lung and bowel diseases, such as asthma, Crohn's disease, and ulcerative colitis. Therefore, therapeutics that modulate the function of this gene product may reduce or eliminate the symptoms of patients suffering from asthma, Crohn's disease, and ulcerative colitis.

[0823] F. CG126129-02: Epithelium Differentiation Factor (PEDF) (Similar to Serine or Cysteine Proteinase Inhibitor)

[0824] Expression of full length physical clone CG126129-02 was assessed using the primer-probe set Ag7039, described in Table FA.

TABLE FA
Probe Name Ag7039
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-ggtggaggaggaggatcct-3′	19	169	248
Probe	TET-5′-cttcaaagtccccgtgaacaagctgg	26	190	249
Reverse	5′-tggattctgttcgctggat-3′	19	259	250

[0825] General_screening_panel_v1.6 Summary: Ag7039 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0826] G. CG142202-03: CRL-2

[0827] Expression of full length physical clone CG142202-03 was assessed using the primer-probe set Ag4530, described in Table GA. Results of the RTQ-PCR runs are shown in Tables GB and GC.

TABLE GA
Probe Name Ag4530
Primers	Length	Start Position	SEQ ID No
Forward	5′-acatggaatgccagcaaatac-3′	21	994	251
Probe	TET-5′-tccaggaccaacctgactttccacta	26	968	252
	-3′-TAMRA
Reverse	5′-actggtcataggcctcatcac-3′	21	936	253

[0828]

TABLE GB
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag4530,		(%) Ag4530,
	Run		Run
Tissue Name	222735181	issue Name	222735181
Adipose	2.3	Renal ca. TK-10	19.1
Melanoma*	0.0	Bladder	0.6
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	3.1
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.5
Melanoma*	0.0	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	6.3	Colon ca. SW480	1.3
SK-MEL-5
Squamous cell	0.3	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	0.5	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	1.2
met) PC-3
Prostate Pool	0.5	Colon ca. CaCo-2	0.0
Placenta	0.2	Colon cancer tissue	1.5
Uterus Pool	0.0	Colon ca. SW1116	0.0
Ovarian ca.	0.0	Colon ca. Colo-205	0.1
OVCAR-3
Ovarian ca.	0.0	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	1.6	Colon Pool	3.1
OVCAR-4
Ovarian ca.	1.4	Small Intestine Pool	0.7
OVCAR-5
Ovarian ca.	0.3	Stomach Pool	0.5
IGROV-1
Ovarian ca.	0.8	Bone Marrow Pool	2.3
OVCAR-8
Ovary	0.6	Fetal Heart	0.0
Breast ca. MCF-7	0.1	Heart Pool	0.7
Breast ca.	66.0	Lymph Node Pool	2.9
MDA-MB-231
Breast ca. BT 549	13.2	Fetal Skeletal Muscle	0.3
Breast ca. T47D	1.7	Skeletal Muscle Pool	0.5
Breast ca. MDA-N	0.9	Spleen Pool	1.1
Breast Pool	2.0	Thymus Pool	2.5
Trachea	4.2	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	0.0	CNS cancer (glio/	1.9
		astro) U-118-MG
Fetal Lung	0.4	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.3
		SF-539
Lung ca. LX-1	0.3	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.2
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.0
		SF-295
Lung ca. A549	2.2	Brain (Amygdala)	0.0
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	0.0
Lung ca. NCI-H23	0.5	Brain (fetal)	0.0
Lung ca. NCI-H460	100.0	Brain (Hippocampus)	0.0
		Pool
Lung ca. HOP-62	1.3	Cerebral Cortex Pool	0.0
Lung ca. NCI-H522	0.0	Brain (Substantia	0.0
		nigra) Pool
Liver	0.0	Brain (Thalamus) Pool	0.0
Fetal Liver	0.8	Brain (whole)	0.0
Liver ca. HepG2	0.0	Spinal Cord Pool	0.0
Kidney Pool	1.9	Adrenal Gland	0.0
Fetal Kidney	0.2	Pituitary gland Pool	0.0
Renal ca. 786-0	0.0	Salivary Gland	0.0
Renal ca. A498	0.0	Thyroid (female)	0.7
Renal ca. ACHN	1.0	Pancreatic ca.	5.1
		CAPAN2
Renal ca. UO-31	0.0	Pancreas Pool	1.1

[0829]

TABLE GC
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(%) Ag4530,		(%) Ag4530,
	Run		Run
Tissue Name	198383582	Tissue Name	198383582
Secondary Th1 act	1.8	HUVEC IL-1beta	0.0
Secondary Th2 act	20.9	HUVEC IFN gamma	0.0
Secondary Tr1 act	15.5	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	1.3	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	3.0	HUVEC IL-11	0.1
Secondary Tr1 rest	5.2	Lung Microvascular	0.0
		EC none
Primary Th1 act	0.5	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	4.0	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	0.8	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	3.4	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	3.7	Small airway	0.0
		epithelium none
Primary Tr1 rest	4.2	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.5	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	0.7	Coronery artery SMC	0.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.8	Astrocytes rest	0.0
Secondary CD8	0.5	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	1.7	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	0.5	KU-812 (Basophil)	0.5
none		PMA/ionomycin
2ry Th1/Th2/	19.1	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.5	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.7	Liver cirrhosis	0.0
LAK cells IL-2 +	0.2	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	0.5	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	0.3	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	6.2	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	0.9	NCI-H292 IFN gamma	0.0
Two Way MLR 3	1.3	HPAEC none	0.0
day
Two Way MLR 5	0.4	HPAEC TNF alpha +	0.1
day		IL-1 beta
Two Way MLR 7	0.5	Lung fibroblast	0.0
day		none
PBMC rest	0.1	Lung fibroblast TNF	0.1
		alpha + IL-1 beta
PBMC PWM	0.2	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.5	Lung fibroblast IL-9	0.0
Ramos (B cell) none	7.6	Lung fibroblast IL-13	0.0
Ramos (B cell)	3.8	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	0.2	Dermal fibroblast	0.1
PWM		CCD1070 rest
B lymphocytes	0.6	Dermal fibroblast	1.4
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	0.4	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	100.0	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	0.1	Dermal fibroblast IL-4	0.0
Dendritic cells LPS	3.9	Dermal Fibroblasts	0.1
		rest
Dendritic cells	0.6	Neutrophils TNFa +	0.8
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	9.0	Colon	0.1
Macrophages rest	0.2	Lung	0.0
Macrophages LPS	2.4	Thymus	0.4
HUVEC none	0.0	Kidney	0.0
HUVEC starved	0.0

[0830] CNS_neurodegeneration_v1.0 Summary: Ag4530 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0831] General_screening_panel_v1.4 Summary: Ag4530 Highest expression of this gene is detected in a lung cancer NCI-H460 cell line (CT=27.7). In addition, moderate levels of expression of this gene is also seen in cancer cell lines derived from melanoma, breast, pancreatic, lung, renal, brain and colon cancers. Thus, expression of this gene may be used as diagnostic marker to detect the presence of these cancers. Furthermore, therapeutic modulation of this gene may be useful in the treatment of melanoma, lung, breast, colon, renal, pancreatic and brain cancers.

[0832] Among the tissues with metabolic or endocrine function, this gene is expressed at moderate to low levels in pancreas, adipose, thyroid, heart, fetal liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[0833] Interestingly, this gene is expressed at much higher levels in fetal (CT=34.7) when compared to adult liver (CT=40). This observation suggests that expression of this gene can be used to distinguish fetal from adult liver. In addition, the relative overexpression of this gene in fetal tissue suggests that the protein product may enhance liver growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver related diseases.

[0834] Panel 4.1D Summary: Ag4530 Highest expression of this gene is detected in PMA/ionomycin treated eosinophils (CT=26.4). Expression of this gene is higher in activated as compared to resting eosinophil (CT=34.3). Thus, expression of this gene may be used to distinguish between resting and activated eosinophils and also from other samples used in this panel. In addition, expression of this gene in activated eosinophil suggests a role for this gene in eosinophil functions. Therefore, therapeutic modulation of this gene through the use of antibodies or small molecule drug may be useful in the treatment of T cell-mediated autoimmune and inflammatory diseases including asthma and allergy and also hematopoietic disorders involving eosinphils, parasitic infections.

[0835] In addition, low to moderate levels of expression of this gene is also detected in T lymphocytes prepared under a number of conditions, as well as, in different activated cell types involved in inflammatory and autoimmune disorders such as dendritic cells, monocytes, macrophages, neutrophils and dermal fibroblasts. Dendritic cells and macrophages are powerful antigen-presenting cells (APC) whose function is pivotal in the initiation and maintenance of normal immune responses. Autoimmunity and inflammation may also be reduced by suppression of this function. Therefore, small molecule drugs and antibodies that antagonzie the function of this gene product may reduce or eliminate the symptoms in patients with several types of autoimmune and inflammatory diseases, such as lupus erythematosus, Crohn's disease, ulcerative colitis, multiple sclerosis, chronic obstructive pulmonary disease, asthma, emphysema, rheumatoid arthritis, or psoriasis.

[0836] H. CG142621-01: Hypothetical Membrane Protein

[0837] Expression of gene CGI42621-01 was assessed using the primer-probe set Ag7570, described in Table HA.

TABLE HA
Probe Name Ag7570
Primers	Sequences	Length	Start Position	SEQ ID No
Forward	5′-gccagcatccaactcagattat-3′	22	234	254
Probe	TET-5′-cacaatctccttacattgacagttttg	30	260	255
Reverse	5′-ggattccaagttcttctagcaaa-3′	23	300	256

[0838] CNS_neurodegeneration_v1.0 Summary: Ag7570 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0839] Panel 4.1D Summary: Ag7570 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0840] I. CG142761-01: Similar to histocompatibility 13

[0841] Expression of gene CG142761-01 was assessed using the primer-probe set Ag7623, described in Table IA. Results of the RTQ-PCR runs are shown in Tables IB and IC.

TABLE IA
Probe Name Ag7623
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-cccagcgccatgtaatg-3′	17	1293	257
Probe	TET-5′-atttgactcctcataacttgggcccc	26	1350	258
	-3′-TAMRA
Reverse	5′-gccgctggatccttagg-3′	17	1376	259

[0842]

TABLE IB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7623,		(%) Ag7623,
	Run		Run
Tissue Name	311288617	issue Name	311288617
AD 1 Hippo	8.1	Control (Path) 3	7.7
		Temporal Ctx
AD 2 Hippo	28.9	Control (Path) 4	41.8
		Temporal Ctx
AD 3 Hippo	18.7	AD 1 Occipital Ctx	24.1
AD 4 Hippo	16.8	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	57.8	AD 3 Occipital Ctx	9.8
AD 6 Hippo	31.6	AD 4 Occipital Ctx	63.7
Control 2 Hippo	61.6	AD 5 Occipital Ctx	93.3
Control 4 Hippo	6.0	AD 6 Occipital Ctx	12.8
Control (Path) 3	9.2	Control 1 Occipital	6.9
Hippo		Ctx
AD 1 Temporal Ctx	23.7	Control 2 Occipital	86.5
		Ctx
AD 2 Temporal Ctx	37.1	Control 3 Occipital	37.4
		Ctx
AD 3 Temporal Ctx	18.3	Control 4 Occipital	11.7
		Ctx
AD 4 Temporal Ctx	36.1	Control (Path) 1	66.9
		Occipital Ctx
AD 5 Inf Temporal	72.2	Control (Path) 2	21.6
Ctx		Occipital Ctx
AD 5 Sup Temporal	25.9	Control (Path) 3	15.3
Ctx		Occipital Ctx
AD 6 Inf Temporal	16.7	Control (Path) 4	17.7
Ctx		Occipital Ctx
AD 6 Sup Temporal	31.4	Control 1 Parietal Ctx	21.2
Ctx
Control 1 Temporal	23.2	Control 2 Parietal Ctx	25.9
Ctx
Control 2 Temporal	76.8	Control 3 Parietal Ctx	23.5
Ctx
Control 3 Temporal	43.5	Control (Path) 1	94.0
Ctx		Parietal Ctx
Control 3 Temporal	13.9	Control (Path) 2	37.9
Ctx		Parietal Ctx
Control (Path) 1	100.0	Control (Path) 3	4.9
Temporal Ctx		Parietal Ctx
Control (Path) 2	37.1	Control (Path) 4	52.9
Temporal Ctx		Parietal Ctx

[0843]

TABLE IC
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	%) Ag7623,		(%) Ag7623,
	Run		Run
Tissue Name	311288446	Tissue Name	311288446
Secondary Th1 act	9.3	HUVEC IL-1beta	9.9
Secondary Th2 act	2.4	HUVEC IFN gamma	3.7
Secondary Tr1 act	6.9	HUVEC TNF alpha +	9.9
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	8.2
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	2.5
Secondary Tr1 rest	1.8	Lung Microvascular	15.0
		EC none
Primary Th1 act	2.6	Lung Microvascular	6.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	6.2	Microvascular Dermal	6.6
		EC none
Primary Tr1 act	8.9	Microsvasular Dermal	20.3
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	2.0	Bronchial epithelium	10.6
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	9.6
		epithelium none
Primary Tr1 rest	0.0	Small airway	11.5
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	9.5	Coronery artery SMC	23.2
lymphocyte act		rest
CD45RO CD4	2.5	Coronery artery SMC	12.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	4.0	Astrocytes rest	5.3
Secondary CD8	0.9	Astrocytes	6.4
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	1.5	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	4.1	KU-812 (Basophil)	0.0
none		PMA/ionomycin
2ry Th1/Th2/	1.4	CCD1106	4.8
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	15.7	CCD1106	11.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	6.9	Liver cirrhosis	3.8
LAK cells IL-2 +	4.9	NCI-H292 none	19.3
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	11.2
IFN gamma
LAK cells IL-2 +	2.5	NCI-H292 IL-9	20.7
IL-18
LAK cells PMA/	14.4	NCI-H292 IL-13	7.3
ionomycin
NK Cells IL-2 rest	2.2	NCI-H292 IFN gamma	5.7
Two Way MLR 3	1.5	HPAEC none	2.7
day
Two Way MLR 5	7.0	HPAEC TNF alpha +	6.7
day		IL-1 beta
Two Way MLR 7	1.9	Lung fibroblast	12.7
day		none
PBMC rest	0.0	Lung fibroblast TNF	10.3
		alpha + IL-1 beta
PBMC PWM	3.2	Lung fibroblast IL-4	11.1
PBMC PHA-L	7.6	Lung fibroblast IL-9	48.3
Ramos (B cell) none	5.8	Lung fibroblast IL-13	10.0
Ramos (B cell)	7.4	Lung fibroblast IFN	14.9
ionomycin		gamma
B lymphocytes	3.2	Dermal fibroblast	20.6
PWM		CCD1070 rest
B lymphocytes	3.7	Dermal fibroblast	11.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	2.5	Dermal fibroblast	14.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	4.9	Dermal fibroblast IFN	5.3
PMA/ionomycin		gamma
Dendritic cells none	12.2	Dermal fibroblast IL-4	7.4
Dendritic cells LPS	1.6	Dermal Fibroblasts	11.2
		rest
Dendritic cells	6.0	Neutrophils TNFa +	6.2
anti-CD40		LPS
Monocytes rest	1.2	Neutrophils rest	4.8
Monocytes LPS	100.0	Colon	0.0
Macrophages rest	7.9	Lung	0.0
Macrophages LPS	22.4	Thymus	0.0
HUVEC none	3.1	Kidney	5.1
HUVEC starved	5.7

[0844] CNS_neurodegeneration_v1.0 Summary: Ag7623 This panel confirms the expression of this gene at low levels in the brain in an independent group of individuals. This gene is found to be slightly down-regulated in the temporal cortex of Alzheimer's disease patients. Therefore, up-regulation of this gene or its protein product, or treatment with specific agonists for this receptor may be of use in reversing the dementia, memory loss, and neuronal death associated with this disease.

[0845] Panel 4.1D Summary: Ag7623 Highest expression of this gene is detected in LPS treated monocytes (CT=32.3). Expression of this gene is higher in the stimulted as compared to resting monocytes (CT=38). Thus, expression of this gene may be used to distinguish between activated and resting monocytes. In addition, upon activation with pathogens such as LPS, monocytes contribute to the innate and specific immunity by migrating to the site of tissue injury and releasing inflammatory cytokines. This release contributes to the inflammation process. Therefore, therapeutic modulation of the expression of this gene or the protein encoded by this gene may prevent the recruitment of monocytes and the initiation of the inflammatory process, and reduce the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, or rheumatoid arthritis.

[0846] In addition, low levels of expression of this gene are also seen in NCI-H292, coronery artery SMC, activated macrophage and lung fibroblasts. Therefore, therapeutic modulation of this gene or its protein product may be useful in the treatment of asthma, psoriasis, arthritis, allergy, chronic obstructive pulmonary disease, and emphysema.

[0847] J. CG144193-01: Secreted Phosphoprotein 24 Precursor

[0848] Expression of full length physical clone CG144193-01 was assessed using the primer-probe set Ag7040, described in Table JA. Results of the RTQ-PCR runs are shown in Table JB.

TABLE JA
Probe Name Ag7040
Primers	Sequencs	Length	Start Position	SEQ ID No
Forward	5′-actatgtgtccacgtctgagtctt-3′	24	326	260
Probe	TET-5′-atttatgagatcccaacatgtccccaa	28	370	261
	a-3′-TAMRA
Reverse	5′-tgagaccaaatagataattgcttctc-3′	26	399	262

[0849]

TABLE JB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag7040,		(%) Ag7040,
	Run		Run
Tissue Name	282273676	issue Name	282273676
Adipose	0.0	Renal ca. TK-10	0.0
Melanoma*	0.0	Bladder	0.0
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.0
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.0
Melanoma*	0.0	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	0.0	Colon ca. SW480	0.0
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	0.0	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	0.0
met) PC-3
Prostate Pool	0.0	Colon ca. CaCo-2	0.0
Placenta	0.0	Colon cancer tissue	0.0
Uterus Pool	0.0	Colon ca. SW1116	0.0
Ovarian ca.	0.0	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.0	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	0.0
OVCAR-4
Ovarian ca.	0.0	Small Intestine Pool	0.0
OVCAR-5
Ovarian ca.	0.0	Stomach Pool	0.0
IGROV-1
Ovarian ca.	0.0	Bone Marrow Pool	0.0
OVCAR-8
Ovary	0.0	Fetal Heart	0.0
Breast ca. MCF-7	0.0	Heart Pool	0.0
Breast ca.	0.0	Lymph Node Pool	0.0
MDA-MB-231
Breast ca. BT 549	0.0	Fetal Skeletal Muscle	0.0
Breast ca. T47D	0.0	Skeletal Muscle Pool	0.0
Breast ca. MDA-N	0.0	Spleen Pool	0.0
Breast Pool	0.0	Thymus Pool	0.0
Trachea	0.0	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	0.0	CNS cancer (glio/	0.0
		astro) U-118-MG
Fetal Lung	0.0	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.0
		SF-295
Lung ca. A549	0.0	Brain (Amygdala)	0.0
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	0.0
Lung ca. NCI-H23	0.0	Brain (fetal)	0.0
Lung ca. NCI-H460	0.0	Brain (Hippocampus)	0.0
		Pool
Lung ca. HOP-62	0.0	Cerebral Cortex Pool	0.0
Lung ca. NCI-H522	0.0	Brain (Substantia	0.0
		nigra) Pool
Liver	20.6	Brain (Thalamus) Pool	0.0
Fetal Liver	100.0	Brain (whole)	0.0
Liver ca. HepG2	0.0	Spinal Cord Pool	0.0
Kidney Pool	0.0	Adrenal Gland	0.0
Fetal Kidney	0.0	Pituitary gland Pool	0.0
Renal ca. 786-0	0.0	Salivary Gland	0.0
Renal ca. A498	0.0	Thyroid (female)	0.0
Renal ca. ACHN	0.0	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	0.0	Pancreas Pool	0.0

[0850] General_screening_panel_v1.6 Summary: Ag7040 Significant expression is detected only in fetal liver (CT=33.8). Interestingly, this gene is expressed at much higher levels in fetal when compared to adult liver tissue (CT=40). This observation suggests that expression of this gene can be used to differentiate between the fetal and adult sources of this tissue. In addition, the relative overexpression of this gene in fetal liver suggests that the protein product may enhance liver growth or development in the fetus and thus may also act in a regenerative capacity in the adult to restore liver mass and/or function. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver related diseases, including cirrhosis and fibrosis.

[0851] K. CG144884-02: B-Lymphocyte Activation Marker Blast-1 Precursor

[0852] Expression of full-length physical clone CG144884-02 was assessed using the primer-probe set Ag4390, described in Table KA. Results of the RTQ-PCR runs are shown in Tables KB and KC.

TABLE KA
Probe Name Ag4390
Primers	Length	Start Position	SEQ ID No
Forward	5′-gtctggctctggaattgctact-3′	22	45	263
Probe	TET-5′-ctctgtcactcctggtgaccagcatt	26	72	264
	-3′-TAMRA
Reverse	5′-agaccacggtcatatgtaccaa-3′	22	107	265

[0853]

TABLE KB
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag4390,		(%) Ag4390,
	Run		Run
Tissue Name	222641236	issue Name	222641236
Adipose	38.7	Renal ca. TK-10	0.0
Melanoma*	0.0	Bladder	31.9
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.1
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.0
Melanoma*	0.0	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	0.0	Colon ca. SW480	0.0
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	1.7	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	0.0
met) PC-3
Prostate Pool	8.6	Colon ca. CaCo-2	0.0
Placenta	4.8	Colon cancer tissue	40.6
Uterus Pool	5.8	Colon ca. SW1116	0.0
Ovarian ca.	0.0	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.0	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	24.8
OVCAR-4
Ovarian ca.	0.0	Small Intestine Pool	9.4
OVCAR-5
Ovarian ca.	0.0	Stomach Pool	13.0
IGROV-1
Ovarian ca.	0.0	Bone Marrow Pool	19.6
OVCAR-8
Ovary	10.4	Fetal Heart	1.3
Breast ca. MCF-7	0.0	Heart Pool	5.6
Breast ca.	0.0	Lymph Node Pool	21.9
MDA-MB-231
Breast ca. BT 549	0.0	Fetal Skeletal Muscle	1.8
Breast ca. T47D	0.0	Skeletal Muscle Pool	2.9
Breast ca. MDA-N	0.0	Spleen Pool	69.7
Breast Pool	14.2	Thymus Pool	100.0
Trachea	49.0	CNS cancer (glio/	0.4
		astro) U87-MG
Lung	0.9	CNS cancer (glio/	0.0
		astro) U-118-MG
Fetal Lung	31.9	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.1
		SF-295
Lung ca. A549	0.0	Brain (Amygdala)	0.4
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	0.3
Lung ca. NCI-H23	0.0	Brain (fetal)	0.8
Lung ca. NCI-H460	0.0	Brain (Hippocampus)	1.4
		Pool
Lung ca. HOP-62	0.0	Cerebral Cortex Pool	0.9
Lung ca. NCI-H522	0.0	Brain (Substantia	0.8
		nigra) Pool
Liver	5.7	Brain (Thalamus) Pool	1.0
Fetal Liver	14.0	Brain (whole)	1.5
Liver ca. HepG2	0.0	Spinal Cord Pool	6.4
Kidney Pool	17.7	Adrenal Gland	7.0
Fetal Kidney	3.2	Pituitary gland Pool	1.2
Renal ca. 786-0	0.0	Salivary Gland	14.7
Renal ca. A498	0.0	Thyroid (female)	14.1
Renal ca. ACHN	0.0	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	0.0	Pancreas Pool	21.2

[0854]

TABLE KC
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	() Ag4390,		(%) Ag4390,
	Run		Run
Tissue Name	186502193	Tissue Name	186502193
Secondary Th1 act	40.3	HUVEC IL-1beta	0.0
Secondary Th2 act	33.0	HUVEC IFN gamma	0.0
Secondary Tr1 act	22.7	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	19.1	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	18.8	HUVEC IL-11	2.0
Secondary Tr1 rest	24.0	Lung Microvascular	0.2
		EC none
Primary Th1 act	31.9	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	18.2	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	22.4	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	19.3	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	17.1	Small airway	0.0
		epithelium none
Primary Tr1 rest	31.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	22.1	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	41.2	Coronery artery SMC	0.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	32.5	Astrocytes rest	0.0
Secondary CD8	20.4	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	24.3	KU-812 (Basophil)	0.7
lymphocyte act		rest
CD4 lymphocyte	22.4	KU-812 (Basophil)	0.3
none		PMA/ionomycin
2ry Th1/Th2/	27.0	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	23.7	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	37.4	Liver cirrhosis	0.5
LAK cells IL-2 +	38.2	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	35.1	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	30.4	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	22.8	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	44.8	NCI-H292 IFN gamma	0.0
Two Way MLR 3	28.3	HPAEC none	0.3
day
Two Way MLR 5	19.6	HPAEC TNF alpha +	0.3
day		IL-1 beta
Two Way MLR 7	10.3	Lung fibroblast	0.2
day		none
PBMC rest	23.3	Lung fibroblast TNF	0.2
		alpha + IL-1 beta
PBMC PWM	27.0	Lung fibroblast IL-4	0.1
PBMC PHA-L	12.8	Lung fibroblast IL-9	0.0
Ramos (B cell) none	16.5	Lung fibroblast IL-13	0.0
Ramos (B cell)	31.4	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	21.2	Dermal fibroblast	1.3
PWM		CCD1070 rest
B lymphocytes	25.0	Dermal fibroblast	27.4
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	1.1	Dermal fibroblast	0.2
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.3	Dermal fibroblast IFN	0.3
PMA/ionomycin		gamma
Dendritic cells none	14.6	Dermal fibroblast IL-4	0.7
Dendritic cells LPS	16.6	Dermal Fibroblasts	0.7
		rest
Dendritic cells	6.3	Neutrophils TNFa +	18.9
anti-CD40		LPS
Monocytes rest	39.5	Neutrophils rest	6.0
Monocytes LPS	100.0	Colon	2.3
Macrophages rest	12.2	Lung	1.7
Macrophages LPS	40.1	Thymus	9.5
HUVEC none	0.0	Kidney	1.2
HUVEC starved	0.0

[0855] CNS_neurodegeneration_v1.0 Summary: Ag4390 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0856] General_screening_panel_v1.4 Summary: Ag4390 Highest expression of this gene is detected in thymus (CT=29.4). The protein encoded for by this gene could therefore may play an important role in T cell development. Small molecule therapeutics, or antibody therapeutics designed against the protein encoded for by this gene could be utilized to modulate immune function (T cell development) and be important for organ transplant, AIDS treatment or post chemotherapy immune reconstitution.

[0857] Moderate to low levels of expression of this gene is also seen in tissues with metabolic/endocrine functions including pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[0858] Interestingly, this gene is expressed at much higher levels in fetal (CT=31) when compared to adult lung (CT=36). This observation suggests that expression of this gene can be used to distinguish fetal from adult lung. In addition, the relative overexpression of this gene in fetal tissue suggests that the protein product may enhance lung growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of lung related diseases.

[0859] Panel 4.1D Summary: Ag4390 This gene appears to be expressed mainly in hematopoietic cells, including T cells, B cells, LAK cells, dendritic cells, monocytes and macrophages. This gene encodes a protein with homology to BLAST1, an activation-associated cell surface glycoprotein expressed primarily in mitogen-stimulated human lymphocytes. The expression of this gene in hematopoietic cells and thymus on Panel 1.4 is consistent with this characterization. Highest expression of this gene is seen in LPS treated monocytes (CT=26). Upon activation with pathogens such as LPS, monocytes contribute to the innate and specific immunity by migrating to the site of tissue injury and releasing inflammatory cytokines. This release contributes to the inflammation process. Therefore, modulation of the expression of the protein encoded by this transcript may prevent the recruitment of monocytes and the iniltation of the inflammatory process, and reduce the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, or rheumatoid arthritis.

[0860] L. CG145198-01: Novel Secreted Protein

[0861] Expression of full-length physical clone CG145198-01 was assessed using the primer-probe set Ag6943, described in Table LA. Results of the RTQ-PCR runs are shown in Table LB.

TABLE LA
Probe Name Ag6943
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-cccagaccagatgacctatctt-3′	22	299	266
Probe	TET-5′-ccttccagctctgagtcacttcccat	26	321	267
	-3′-TAMRA
Reverse	5′-aatggtctcagtgacttcgattaac-3′	25	358	268

[0862]

TABLE LB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag6943,		(%) Ag6943,
	Run		Run
Tissue Name	278388849	issue Name	278388849
Adipose	9.9	Renal ca. TK-10	31.4
Melanoma*	19.9	Bladder	37.1
Hs688(A).T
Melanoma*	17.4	Gastric ca. (liver met.)	36.9
Hs688(B).T		NCI-N87
Melanoma* M14	87.1	Gastric ca. KATO III	75.3
Melanoma*	55.1	Colon ca. SW-948	7.4
LOXIMVI
Melanoma*	42.0	Colon ca. SW480	61.1
SK-MEL-5
Squamous cell	21.6	Colon ca.* (SW480	23.3
carcinoma SCC-4		met) SW620
Testis Pool	17.8	Colon ca. HT29	19.3
Prostate ca.* (bone	63.7	Colon ca. HCT-116	33.2
met) PC-3
Prostate Pool	13.6	Colon ca. CaCo-2	29.1
Placenta	6.6	Colon cancer tissue	15.4
Uterus Pool	4.6	Colon ca. SW1116	7.7
Ovarian ca.	18.6	Colon ca. Colo-205	4.0
OVCAR-3
Ovarian ca.	32.1	Colon ca. SW-48	10.7
SK-OV-3
Ovarian ca.	19.8	Colon Pool	17.6
OVCAR-4
Ovarian ca.	27.9	Small Intestine Pool	12.4
OVCAR-5
Ovarian ca.	14.9	Stomach Pool	6.9
IGROV-1
Ovarian ca.	19.8	Bone Marrow Pool	9.6
OVCAR-8
Ovary	6.3	Fetal Heart	5.2
Breast ca. MCF-7	19.9	Heart Pool	4.4
Breast ca.	97.3	Lymph Node Pool	12.5
MDA-MB-231
Breast ca. BT 549	100.0	Fetal Skeletal Muscle	3.5
Breast ca. T47D	9.6	Skeletal Muscle Pool	0.4
Breast ca. MDA-N	23.7	Spleen Pool	11.9
Breast Pool	11.4	Thymus Pool	73.7
Trachea	15.8	CNS cancer (glio/	22.7
		astro) U87-MG
Lung	2.1	CNS cancer (glio/	63.3
		astro) U-118-MG
Fetal Lung	16.2	CNS cancer (neuro;	44.4
		met) SK-N-AS
Lung ca. NCI-N417	8.0	CNS cancer (astro)	31.0
		SF-539
Lung ca. LX-1	13.1	CNS cancer (astro)	59.5
		SNB-75
Lung ca. NCI-H146	19.1	CNS cancer (glio)	19.1
		SNB-19
Lung ca. SHP-77	65.1	CNS cancer (glio)	59.5
		SF-295
Lung ca. A549	39.2	Brain (Amygdala)	13.7
		Pool
Lung ca. NCI-H526	5.4	Brain (cerebellum)	26.8
Lung ca. NCI-H23	33.2	Brain (fetal)	15.8
Lung ca. NCI-H460	11.3	Brain (Hippocampus)	10.0
		Pool
Lung ca. HOP-62	28.1	Cerebral Cortex Pool	14.2
Lung ca. NCI-H522	70.7	Brain (Substantia	7.5
		nigra) Pool
Liver	6.8	Brain (Thalamus) Pool	12.2
Fetal Liver	11.5	Brain (whole)	8.6
Liver ca. HepG2	21.3	Spinal Cord Pool	12.0
Kidney Pool	24.5	Adrenal Gland	12.9
Fetal Kidney	11.3	Pituitary gland Pool	3.2
Renal ca. 786-0	23.2	Salivary Gland	9.5
Renal ca. A498	8.5	Thyroid (female)	4.2
Renal ca. ACHN	11.0	Pancreatic ca.	15.1
		CAPAN2
Renal ca. UO-31	21.0	Pancreas Pool	11.1

[0863] General_screening_panel_v1.6 Summary: Ag6943 Highest expression of this gene Is seen in a breast cancer cell line (CT=27.8). This gene is ubiquitously expressed in this panel, with moderate expression seen in brain, colon, gastric, lung, breast, ovarian, and melanoma cancer cell lines. This expression profile suggests a role for this gene product in cell survival and proliferation. Modulation of this gene product may be useful in the treatment of cancer.

[0864] In addition, this gene is expressed at much higher levels in fetal lung tissue (CT=30) when compared to expression in the adult counterpart (CT=33). Thus, expression of this gene may be used to differentiate between the fetal and adult source of this tissue.

[0865] Among tissues with metabolic function, this gene is expressed at moderate to low levels in pituitary, adipose, adrenal gland, pancreas, thyroid, and adult and fetal skeletal muscle, heart, and liver. This widespread expression among these tissues suggests that this gene product may play a role in normal neuroendocrine and metabolic function and that disregulated expression of this gene may contribute to neuroendocrine disorders or metabolic diseases, such as obesity and diabetes.

[0866] This gene is also expressed at moderate levels in the CNS, including the hippocampus, thalamus, substantia nigra, amygdala, cerebellum and cerebral cortex. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurologic disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, multiple sclerosis, stroke and epilepsy.

[0867] M. CG145650-01 and CG145650-02: Lectin C-type Domain Protein

[0868] Expression of full-length physical clones CG145650-01 and CG145650-02 was assessed using the primer-probe sets Ag6531, AG7094, Ag7397, and Ag7478, described in Tables MA, MB, MC, and MD. Results of the RTQ-PCR runs are shown in Tables ME, MF, and MG. Please note that Ag7094 is specific to CG145650-02 and Ag6531 and Ag7397 are specific to CG145650-01.

TABLE MA
Probe Name Ag6531
Primers	Sequencs	Length	Start Position	SEQ ID No
Forward	5′-agtagaaataaagtagcagttggaactaaa	30	401	269
	-3′
Probe	TET-5′-acttccaattctttgggcaacagctc	26	433	270
	-3′-TAMRA
Reverse	5′-cagcctcttctgcagagaca-3′	20	464	271

[0869]

TABLE MB
Probe Name Ag7094
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-agacaccatacaatgatgttaattgtc-3′	27	636	272
Probe	TET-5′-tctcacaaactgacctttgaggacca	26	664	273	1664	273
	-3′-TAMRA
Reverse	5′-agaatgttcagttcataagtggatctt-3′	27	695	274

[0870]

TABLE MC
Probe Name Ag7397
Primers	Sequencs	Length	Start Position	SEQ ID No
Forward	5′-cttgccaagatgctgattca-3′	20	382	275
Probe	TET-5′-cagttggaactaaatgacttccaattc	30	417	276
Reverse	5′-tctgcagagacagcctgga-3′	19	457	277

[0871]

TABLE MD
Probe Name A27478
Primers	Sequencs	Length	Start Position	SEQ ID No
Forward	5′-ggaagtcatttagttccaactgcta-3′	25	414	278
Probe	TET-5′-atttctactgaatcagcatcttggcaa	30	380	279
	gac-3′-TAMRA
Reverse	5′-aggtgagcctccattctagc-3′	20	345	280

[0872]

TABLE MD
AI comprehensive panel v1.0
	Rel.	Rel.	Rel.		Rel.	Rel.	Rel.
	Exp. (%)	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)	Exp. (%)
	Ag7094,	Ag7397,	g7478,		Ag7094,	Ag7397,	Ag7478,
Tissue	Run	Run	Run	Tissue	Run	Run	Run
Name	306266972	306266974	306518766	Name	306266972	306266974	306518766
110967	0.0	4.6	8.1	112427	14.2	65.1	75.3
COPD-F				Match
				Control
				Psoriasis-F
110980	2.3	3.9	11.3	112418	0.0	7.6	13.5
COPD-F				Psoriasis-M
110968	1.6	10.0	11.7	112723	2.2	21.6	13.6
COPD-M				Match
				Control
				Psoriasis-M
110977	6.0	47.0	39.2	112419	0.0	10.6	20.9
COPD-M				Psoriasis-M
110989	5.1	46.3	26.1	112424	3.1	10.5	24.1
Emphysema-				Match
F				Control
				Psoriasis-M
110992	0.0	6.8	6.3	112420	2.0	35.8	43.2
Emphysema-				Psoriasis-M
F
110993	0.0	10.2	12.8	112425	5.4	38.4	44.8
Emphysema-				Match
F				Control
				Psoriasis-M
110994	0.0	3.7	6.8	104689 (MF)	24.5	84.7	91.4
Emphysema-				OA
F				Bone-Backus
110995	0.0	2.5	19.9	104690 (MF)	5.0	22.5	26.2
Emphysema-				Adj
F				“Normal”
				Bone-Backus
110996	0.0	3.0	2.4	104691 (MF)	11.6	37.1	39.8
Emphysema-				OA
F				Synovium-
				Backus
110997	0.0	2.2	7.7	104692 (BA)	0.0	0.0	0.0
Asthma-M				OA
				Cartilage-
				Backus
111001	3.7	9.3	13.0	104694 (BA)	28.3	100.0	100.0
Asthma-F				OA
				Bone-Backus
111002	2.5	14.6	25.2	104695 (BA)	7.6	33.9	33.2
Asthma-F				Adj
				“Normal”
				Bone-Backus
111003	3.9	16.4	23.0	104696 (BA)	6.6	27.9	33.4
Atopic				OA
Asthma-F				Synovium-
				Backus
111004	2.6	23.3	20.2	104700 (SS)	15.6	38.2	35.4
Atopic				OA
Asthma-F				Bone-Backus
111005	3.8	13.1	12.5	104701 (SS)	8.6	37.6	39.2
Atopic				Adj
Asthma-F				“Normal”
				Bone-Backus
111006	0.0	4.5	0.6	104702 (SS)	9.2	46.3	40.9
Atopic				OA
Asthma-F				Synovium-
				Backus
111417	1.5	6.3	7.3	117093 OA	2.3	9.5	13.6
Allergy-M				Cartilage
				Rep7
112347	0.0	0.0	0.5	112672 OA	1.6	11.3	23.8
Allergy-M				Bone5
112349	0.0	0.0	0.1	112673 OA	2.0	6.8	16.4
Normal				Synovium5
Lung-F
112357	4.0	41.8	37.6	112674 OA	0.0	15.1	19.3
Normal				Synovial
Lung-F				Fluid cells5
112354	5.4	17.9	21.2	117100 OA	0.0	3.1	5.6
Normal				Cartilage
Lung-M				Rep14
112374	3.4	22.7	19.1	112756 OA	0.0	11.2	12.6
Crohns-F				Bone9
112389	2.4	6.1	7.4	112757 OA	0.0	7.0	9.8
Match				Synovium9
Control
Crohns-F
112375	2.0	13.5	13.8	112758 OA	0.0	7.2	16.0
Crohns-F				Synovial
				Fluid Cells9
112732	6.2	31.9	32.5	117125 RA	0.0	2.7	7.0
Match				Cartilage
Control				Rep2
Crohns-F
112725	0.0	3.3	11.0	113492	2.7	4.9	15.6
Crohns-M				Bone2 RA
112387	0.0	3.6	5.8	113493	0.0	2.2	6.6
Match				Synovium2
Control				RA
Crohns-M
112378	0.0	0.1	0.9	113494 Syn	0.0	4.3	13.4
Crohns-M				Fluid Cells
				RA
112390	3.7	27.7	25.2	113499	0.0	5.8	16.5
Match				Cartilage4
Control				RA
Crohns-M
112726	3.3	22.2	18.9	113500	1.6	4.5	19.3
Crohns-M				Bone4 RA
112731	4.8	18.8	23.3	113501	3.7	3.7	17.9
Match				Synovium4
Control				RA
Crohns-M
112380	2.1	14.6	11.5	113502 Syn	0.0	4.1	12.2
Ulcer Col-F				Fluid Cells4
				RA
112734	12.9	59.5	73.2	113495	2.1	3.5	11.3
Match				Cartilage3
Control				RA
Ulcer Col-F
112384	3.4	16.6	20.9	113496	0.0	3.4	10.9
Ulcer Col-F				Bone3 RA
112737	0.0	6.0	7.9	113497	1.7	2.3	6.7
Match				Synovium3
Control				RA
Ulcer Col-F
112386	0.0	3.3	7.6	113498 Syn	0.0	5.2	12.5
Ulcer Col-F				Fluid Cells3
				RA
112738	0.0	8.2	7.7	117106	0.0	0.4	1.2
Match				Normal
Control				Cartilage
Ulcer Col-F				Rep20
112381	0.0	0.1	0.0	113663	0.0	0.0	0.0
Ulcer				Bone3
Col-M				Normal
112735	0.0	1.2	3.1	113664	0.0	0.0	0.0
Match				Synovium3
Control				Normal
Ulcer
Col-M
112382	0.0	6.0	11.3	113665 Syn	0.0	0.0	0.2
Ulcer				Fluid Cells3
Col-M				Normal
112394	0.0	1.9	4.4	117107	0.0	1.3	4.1
Match				Normal
Control				Cartilage
Ulcer				Rep22
Col-M
112383	100.0	22.2	17.8	113667	0.0	6.1	12.4
Ulcer				Bone4
Col-M				Normal
112736	0.0	5.6	6.2	113668	0.0	7.0	15.9
Match				Synovium4
Control				Normal
Ulcer
Col-M
112423	1.3	11.7	29.5	113669 Syn	0.0	16.5	15.8
Psoriasis-F				Fluid Cells4
				Normal

[0873]

TABLE ME
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag7397,		(%) Ag7397,
	Run		Run
Tissue Name	306066639	issue Name	306066639
Adipose	36.6	Renal ca. TK-10	9.2
Melanoma*	5.2	Bladder	91.4
Hs688(A).T
Melanoma*	7.0	Gastric ca. (liver met.)	36.3
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	12.6
Melanoma*	2.8	Colon ca. SW-948	5.6
LOXIMVI
Melanoma*	11.4	Colon ca. SW480	30.6
SK-MEL-5
Squamous cell	2.1	Colon ca.* (SW480	17.8
carcinoma SCC-4		met) SW620
Testis Pool	29.3	Colon ca. HT29	2.3
Prostate ca.* (bone	11.3	Colon ca. HCT-116	20.9
met) PC-3
Prostate Pool	4.4	Colon ca. CaCo-2	24.1
Placenta	0.0	Colon cancer tissue	100.0
Uterus Pool	12.0	Colon ca. SW1116	0.0
Ovarian ca.	3.8	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	8.5	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	42.0
OVCAR-4
Ovarian ca.	48.3	Small Intestine Pool	69.3
OVCAR-5
Ovarian ca.	0.0	Stomach Pool	38.4
IGROV-1
Ovarian ca.	7.3	Bone Marrow Pool	12.2
OVCAR-8
Ovary	29.1	Fetal Heart	14.9
Breast ca. MCF-7	11.8	Heart Pool	8.4
Breast ca.	12.9	Lymph Node Pool	43.8
MDA-MB-231
Breast ca. BT 549	24.3	Fetal Skeletal Muscle	15.7
Breast ca. T47D	0.0	Skeletal Muscle Pool	0.0
Breast ca. MDA-N	0.0	Spleen Pool	70.7
Breast Pool	56.6	Thymus Pool	78.5
Trachea	15.4	CNS cancer (glio/	11.2
		astro) U87-MG
Lung	33.9	CNS cancer (glio/	45.1
		astro) U-118-MG
Fetal Lung	76.3	CNS cancer (neuro;	14.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	9.1
		SF-539
Lung ca. LX-1	19.2	CNS cancer (astro)	23.3
		SNB-75
Lung ca. NCI-H146	4.3	CNS cancer (glio)	4.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	44.4
		SF-295
Lung ca. A549	11.8	Brain (Amygdala)	0.0
		Pool
Lung ca. NCI-H526	6.1	Brain (cerebellum)	11.1
Lung ca. NCI-H23	36.3	Brain (fetal)	28.1
Lung ca. NCI-H460	14.8	Brain (Hippocampus)	21.0
		Pool
Lung ca. HOP-62	12.7	Cerebral Cortex Pool	32.3
Lung ca. NCI-H522	5.6	Brain (Substantia	22.4
		nigra) Pool
Liver	0.0	Brain (Thalamus) Pool	27.5
Fetal Liver	6.2	Brain (whole)	14.1
Liver ca. HepG2	0.0	Spinal Cord Pool	28.9
Kidney Pool	0.0	Adrenal Gland	14.2
Fetal Kidney	2.0	Pituitary gland Pool	0.0
Renal ca. 786-0	11.3	Salivary Gland	0.0
Renal ca. A498	4.4	Thyroid (female)	10.4
Renal ca. ACHN	14.7	Pancreatic ca.	3.3
		CAPAN2
Renal ca. UO-31	5.2	Pancreas Pool	16.7

[0874]

TABLE MF
Panel 4.1D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	g7397,	Ag7478,		Ag7397,	Ag7478,
	Run	Run		Run	Run
Tissue Name	305065214	306413263	Tissue Name	305065214	306413263
Secondary Th1 act	0.0	0.5	HUVEC IL-1beta	0.0	0.0
Secondary Th2 act	2.0	1.1	HUVEC IFN gamma	1.5	0.0
Secondary Tr1 act	0.0	0.0	HUVEC TNF alpha +	0.0	0.0
			IFN gamma
Secondary Th1 rest	0.0	0.0	HUVEC TNF alpha +	0.4	0.0
			IL4
Secondary Th2 rest	0.3	0.0	HUVEC IL-11	0.3	0.2
Secondary Tr1 rest	0.0	0.0	Lung Microvascular	2.3	0.3
			EC none
Primary Th1 act	0.0	0.0	Lung Microvascular	0.0	0.0
			EC TNFalpha +
			IL-1beta
Primary Th2 act	2.2	0.4	Microvascular	0.0	0.0
			Dermal EC none
Primary Tr1 act	1.7	0.0	Microsvasular	1.0	0.0
			Dermal EC
			TNFalpha + IL1beta
Primary Th1 rest	0.0	0.0	Bronchial epithelium	0.0	0.0
			TNFalpha + IL1beta
Primary Th2 rest	0.0	0.0	Small airway	0.0	0.0
			epithelium none
Primary Tr1 rest	0.0	0.0	Small airway	1.9	0.0
			epithelium TNFalpha +
			IL-1beta
CD45RA CD4	1.3	0.0	Coronery artery SMC	0.0	0.0
lymphocyte act			rest
CD45RO CD4	0.7	7.4	Coronery artery SMC	0.0	0.0
lymphocyte act			TNFalpha + IL-1beta
CD8 lymphocyte act	0.7	0.2	Astrocytes rest	0.3	0.0
Secondary CD8	0.4	0.0	Astrocytes TNFalpha +	0.7	0.0
lymphocyte rest			IL-1beta
Secondary CD8	0.0	0.0	KU-812 (Basophil)	0.0	0.0
lymphocyte act			rest
CD4 lymphocyte none	0.6	0.2	KU-812 (Basophil)	2.1	1.0
			PMA/ionomycin
2ry	0.0	0.0	CCD1106	1.5	0.0
Th1/Th2/Tr1_anti-CD95			(Keratinocytes) none
CH11
LAK cells rest	37.1	8.6	CCD1106	1.4	0.0
			(Keratinocytes)
			TNFalpha + IL-1beta
LAK cells IL-2	0.0	0.0	Liver cirrhosis	1.9	1.4
LAK cells IL-2 + IL-12	0.0	0.0	NCI-H292 none	1.5	1.9
LAK cell IL-2 + IFN	1.0	0.3	NCI-H292 IL-4	2.9	0.0
gamma
LAK cells IL-2 + IL-18	1.0	0.0	NCI-H292 IL-9	1.5	0.0
LAK cells	40.6	73.7	NCI-H292 IL-13	0.3	2.6
PMA-ionomycin
NK Cells IL-2 rest	3.0	1.6	NCI-H292 IFN	0.0	0.0
			gamma
Two Way MLR 3 day	17.8	45.7	HPAEC none	0.0	0.0
Two Way MLR 5 day	3.3	0.0	HPAEC TNF alpha +	0.0	3.5
			IL-1 beta
Two Way MLR 7 day	0.0	0.0	Lung fibroblast none	3.0	2.4
PBMC rest	6.8	14.5	Lung fibroblast TNF	2.9	0.0
			alpha + IL-1 beta
PBMC PWM	0.0	7.0	Lung fibroblast IL-4	1.1	0.0
PBMC PHA-L	6.8	8.8	Lung fibroblast IL-9	2.0	4.4
Ramos (B cell) none	0.0	0.0	Lung fibroblast IL-13	0.2	0.0
Ramos (B cell)	0.9	0.8	Lung fibroblast IFN	2.5	0.6
ionomycin			gamma
B lymphocytes PWM	0.0	0.0	Dermal fibroblast	1.4	1.1
			CCD1070 rest
B lymphocytes CD40L	23.8	35.6	Dermal fibroblast	0.4	1.4
and IL-4			CCD1070 TNF alpha
EOL-1 dbcAMP	6.7	7.6	Dermal fibroblast	0.5	0.0
			CCD1070 IL-1beta
EOL-1 dbcAMP	3.8	0.5	Dermal fibroblast	1.2	0.0
PMA-ionomycin			IFN gamma
Dendritic cells none	92.7	52.5	Dermal fibroblast	1.8	1.7
			IL-4
Dendritic cells LPS	31.2	20.7	Dermal Fibroblasts	1.0	0.0
			rest
Dendritic cells	62.0	75.8	Neutrophils	14.4	29.1
anti-CD40			TNFa + LPS
Monocytes rest	48.3	85.3	Neutrophils rest	100.0	100.0
Monocytes LPS	49.7	92.7	Colon	0.0	0.0
Macrophages rest	8.7	21.8	Lung	1.2	0.0
Macrophages LPS	6.6	23.0	Thymus	1.4	0.5
HUVEC none	0.0	0.0	Kidney	1.1	0.0
HUVEC starved	1.3	0.0

[0875] AI_comprehensive panel_v1.0 Summary: Ag7397/Ag7478 Two experiments with two different probe and primer sets produce results that are in excellent agreement, with highest expression detected in an osteoarthritic bone sample (CTs=27-29). Low to moderate expression is seen in many of the samples on this panel, with slightly higher expression in clusters of samples derived from psoriasis and OA samples. Thus, this gene may be involved in the pathogenesis and/or treatment of these diseases.

[0876] Ag7094 Low levels of expression of this gene are detected in a single ulcerative colitis sample (CT=33.3). Interestingly, expression of this gene is higher in colitis sample as compared to the matched control sample (CT=40). Therefore, expression of this gene may be used as marker to detect the presence of ulcerative colitis and also, therapeutic modulation of this gene or its protein product may be useful in the treatment of ulcerative colitis.

[0877] General_screening_panel_v1.6 Summary: Ag7397 Detectable levels of expression are limited to samples from fetal lung, bladder, thymus, colon cancer, and small intestine (CTs=34-35). Ag6531 Expression of this gene is low/undetectable in all samples on this panel (CTs>35). (Data not shown.)

[0878] Panel 4.1D Summary: Ag7397/Ag7478 Two experiments with two different probe and primer sets produce results that are in excellent agreement, with highest expression detected in resting neutrophils (CTs=30-31). In addition, prominent expression is seen in dendritic cells, macrophages, monocytes, and LAK cells. This transcript appears to be down-regulated in activated neutrophils (CTs=32-33), suggesting that the protein encoded by this gene is produced by resting neutrophils but not by activated neutrophils. Thus, expression of this gene could be used to differentiate between resting and activated neutrophils. Furthermore, the gene product may reduce activation of these inflammatory cells and be useful as a protein therapeutic to reduce or eliminate the symptoms in patients with Crohn's disease, ulcerative colitis, multiple sclerosis, chronic obstructive pulmonary disease, asthma, emphysema, rheumatoid arthritis, lupus erythematosus, or psoriasis. In addition, modulation of this gene product may be effective in increasing the immune response in patients with AIDS or other immunodeficiencies. Ag6531/Ag7094 Expression of this gene is low/undetectable in all samples on this panel (CTs>35). (Data not shown.)

[0879] N. CG145978-01: DUF221 Domain Containing Membrane Protein

[0880] Expression of gene CG145978-01 was assessed using the primer-probe set Ag7596, described in Table NA. Results of the RTQ-PCR runs are shown in Tables NB and NC.

TABLE NA
Probe Name Ag7596
Primers	Length	Start Position	SEQ ID No.
Forward	5′-acagatgcagacagccatga-3′	20	250	281
Probe	TET-5′-tctcacctctgtctccagctccgttg	26	282	282
	-3′-TAMRA
Reverse	5′-cacattgtccctttggtcaaa-3′	21	310	283

[0881]

TABLE NB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7596,		(%) Ag7596,
	Run		Run
Tissue Name	311288611	issue Name	311288611
AD 1 Hippo	4.9	Control (Path) 3	5.2
		Temporal Ctx
AD 2 Hippo	15.9	Control (Path) 4	12.9
		Temporal Ctx
AD 3 Hippo	5.3	AD 1 Occipital Ctx	9.3
AD 4 Hippo	4.7	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	100.0	AD 3 Occipital Ctx	4.1
AD 6 Hippo	15.9	AD 4 Occipital Ctx	8.2
Control 2 Hippo	27.5	AD 5 Occipital Ctx	62.0
Control 4 Hippo	4.5	AD 6 Occipital Ctx	12.2
Control (Path) 3	2.8	Control 1 Occipital	4.0
Hippo		Ctx
AD 1 Temporal Ctx	13.9	Control 2 Occipital	61.1
		Ctx
AD 2 Temporal Ctx	19.8	Control 3 Occipital	9.0
		Ctx
AD 3 Temporal Ctx	5.4	Control 4 Occipital	4.8
		Ctx
AD 4 Temporal Ctx	9.9	Control (Path) 1	62.0
		Occipital Ctx
AD 5 Inf Temporal	36.3	Control (Path) 2	6.3
Ctx		Occipital Ctx
AD 5 Sup Temporal	33.0	Control (Path) 3	2.3
Ctx		Occipital Ctx
AD 6 Inf Temporal	29.1	Control (Path) 4	11.3
Ctx		Occipital Ctx
AD 6 Sup Temporal	34.6	Control 1 Parietal Ctx	4.5
Ctx
Control 1 Temporal	2.8	Control 2 Parietal Ctx	27.2
Ctx
Control 2 Temporal	32.8	Control 3 Parietal Ctx	10.0
Ctx
Control 3 Temporal	19.9	Control (Path) 1	67.8
Ctx		Parietal Ctx
Control 3 Temporal	6.7	Control (Path) 2	15.6
Ctx		Parietal Ctx
Control (Path) 1	49.3	Control (Path) 3	2.0
Temporal Ctx		Parietal Ctx
Control (Path) 2	18.0	Control (Path) 4	30.4
Temporal Ctx		Parietal Ctx

[0882]

TABLE NC
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	() Ag7596,		(%) Ag7596,
	Run		Run
Tissue Name	310113205	Tissue Name	310113205
Secondary Th1 act	12.3	HUVEC IL-1beta	31.0
Secondary Th2 act	20.0	HUVEC IFN gamma	20.6
Secondary Tr1 act	9.3	HUVEC TNF alpha +	2.7
		IFN gamma
Secondary Th1 rest	3.4	HUVEC TNF alpha +	10.0
		IL4
Secondary Th2 rest	4.6	HUVEC IL-11	9.7
Secondary Tr1 rest	3.7	Lung Microvascular	64.6
		EC none
Primary Th1 act	3.3	Lung Microvascular	25.7
		EC TNFalpha +
		IL-1beta
Primary Th2 act	16.6	Microvascular Dermal	6.5
		EC none
Primary Tr1 act	16.8	Microsvasular Dermal	14.7
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	2.0	Bronchial epithelium	46.3
		TNFalpha + IL-1beta
Primary Th2 rest	0.6	Small airway	42.6
		epithelium none
Primary Tr1 rest	0.5	Small airway	71.7
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	27.7	Coronery artery SMC	16.0
lymphocyte act		rest
CD45RO CD4	17.8	Coronery artery SMC	30.4
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	9.3	Astrocytes rest	32.8
Secondary CD8	7.6	Astrocytes	69.3
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	5.5	KU-812 (Basophil)	59.9
lymphocyte act		rest
CD4 lymphocyte	2.2	KU-812 (Basophil)	88.9
none		PMA/ionomycin
2ry Th1/Th2/	3.4	CCD1106	72.7
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	4.6	CCD1106	35.1
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	6.8	Liver cirrhosis	9.9
LAK cells IL-2 +	0.0	NCI-H292 none	42.9
IL-12
LAK cells IL-2 +	5.0	NCI-H292 IL-4	72.2
IFN gamma
LAK cells IL-2 +	4.0	NCI-H292 IL-9	91.4
IL-18
LAK cells PMA/	36.3	NCI-H292 IL-13	50.7
ionomycin
NK Cells IL-2 rest	18.6	NCI-H292 IFN gamma	31.0
Two Way MLR 3	16.4	HPAEC none	17.3
day
Two Way MLR 5	5.7	HPAEC TNF alpha +	64.6
day		IL-1 beta
Two Way MLR 7	4.4	Lung fibroblast	36.6
day		none
PBMC rest	3.1	Lung fibroblast TNF	29.9
		alpha + IL-1 beta
PBMC PWM	7.9	Lung fibroblast IL-4	30.6
PBMC PHA-L	4.8	Lung fibroblast IL-9	33.0
Ramos (B cell) none	1.3	Lung fibroblast IL-13	15.2
Ramos (B cell)	7.0	Lung fibroblast IFN	27.0
ionomycin		gamma
B lymphocytes	7.7	Dermal fibroblast	22.2
PWM		CCD1070 rest
B lymphocytes	17.1	Dermal fibroblast	46.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	16.3	Dermal fibroblast	19.2
		CCD1070 IL-1 beta
EOL-1 dbcAMP	18.0	Dermal fibroblast IFN	16.8
PMA/ionomycin		gamma
Dendritic cells none	24.3	Dermal fibroblast IL-4	33.4
Dendritic cells LPS	100.0	Dermal Fibroblasts	21.3
		rest
Dendritic cells	12.1	Neutrophils TNFa +	2.8
anti-CD40		LPS
Monocytes rest	3.1	Neutrophils rest	11.8
Monocytes LPS	60.3	Colon	2.5
Macrophages rest	15.7	Lung	8.4
Macrophages LPS	28.1	Thymus	4.9
HUVEC none	12.9	Kidney	28.9
HUVEC starved	22.1

[0883] CNS_neurodegeneration_v1.0 Summary: Ag7596 This panel does not show differential expression of this gene in Alzheimer's disease. However, this profile confirms the expression of this gene at moderate levels in the brain, including the cortex and hipppocampus. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurological disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, multiple sclerosis, stroke and epilepsy.

[0884] Panel 4.1D Summary: Ag7956 Highest expression of this gene is seen in LPS treated dendritic cells (CT=31.8). Moderate levels of expression are seen in many samples on this panel and particularly in cells derived from the lung and skin including IL-4, IL-9, IL-13 and IFN gamma activated-NCI-H292 mucoepidermoid cells as well as untreated NCI-H292 cells, IL-4, IL-9, IL-13 and IFN gamma activated lung and dermal fibroblasts, human pulmonary aortic endothelial cells (treated and untreated), small airway epithelium (treated and untreated), treated bronchial epithelium and lung and dermal microvascular endothelial cells (treated and untreated). The expression of this gene in cells derived from or within the lung and skin suggests that this gene may be involved in normal conditions as well as pathological and inflammatory lung and skin disorders that include chronic obstructive puimonai y disease, asthma, allergy, psoriasis and emphysema.

[0885] O. CG145997-01: Similar to Drosophila FRY Gene

[0886] Expression of gene CG145997-01 was assessed using the primer-probe set Ag7557, described in Table OA.

TABLE OA
Probe Name Ag7557
Primers	Sequencs	Length	Start Position	SEQ ID No
Forward	5′-ctgagctcgagaaagaagcat-3′	21	976	284
Probe	TET-5′-cgagacattttcggatctttatttaat	30	1002	285
	acc-3′-TAMRA
Reverse	5′-atctatacaaagattccagtgcaact-3′	26	1032	286

[0887] CNS_neurodegeneration_v1.0 Summary: Ag7557 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0888] Panel 4.1D Summary: Ag7557 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0889] P. CG146119-01: Papilin

[0890] Expression of gene CG146119-01 was assessed using the primer-probe set Ag7571, described in Table PA.

TABLE PA
Probe Name Ag7571
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-gcttctacagtaagtgtctggaacac-3′	26	2362	287
Probe	TET-5′-cactcactgggctcattctgctgg-	24	2403	288
	3′-TAMRA
Reverse	5′-gttgtcatagcaacagccaaac-3′	22	2439	289

[0891] CNS_neurodegeneration_v1.0 Summary: Ag7571 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0892] Panel 4.1D Summary: Ag7571 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0893] Q. CG146202-01: Membrane-Associated Lectin Type—

[0894] Expression of full-length physical clone CG146202-01 was assessed using the primer-probe set Ag7047, described in Table QA. Results of the RTQ-PCR runs are shown in Table QB.

TABLE OA
Probe Name Ag7047
Primers	Length	Start Position	SEQ ID No
Forward	5′-tgcagtggaacgcctgt-3′	17	564	290
Probe	TET-5′-ctgtccctgggaatggacattcttcc	26	588	291
	-3′-TAMRA
Reverse	5′-gtgatggagtcgtgccagt-3′	19	650	292

[0895]

TABLE QB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag7047,		(%) Ag7047,
	Run		Run
Tissue Name	282273803	issue Name	282273803
Adipose	68.3	Renal ca. TK-10	0.8
Melanoma*	0.0	Bladder	47.3
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.0
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.0
Melanoma*	0.0	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	0.4	Colon ca. SW480	0.7
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	13.9	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	0.0
met) PC-3
Prostate Pool	6.2	Colon ca. CaCo-2	0.0
Placenta	100.0	Colon cancer tissue	93.3
Uterus Pool	2.2	Colon ca. SW1116	0.0
Ovarian ca.	0.0	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.0	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	24.1
OVCAR-4
Ovarian ca.	0.0	Small Intestine Pool	9.0
OVCAR-5
Ovarian ca.	0.0	Stomach Pool	27.5
IGROV-1
Ovarian ca.	0.0	Bone Marrow Pool	16.8
OVCAR-8
Ovary	20.7	Fetal Heart	4.8
Breast ca. MCF-7	0.0	Heart Pool	7.2
Breast ca.	0.0	Lymph Node Pool	12.3
MDA-MB-231
Breast ca. BT 549	0.0	Fetal Skeletal Muscle	24.7
Breast ca. T47D	0.0	Skeletal Muscle Pool	5.3
Breast ca. MDA-N	0.0	Spleen Pool	4.1
Breast Pool	14.7	Thymus Pool	35.1
Trachea	43.2	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	3.3	CNS cancer (glio/	0.4
		astro) U-118-MG
Fetal Lung	51.4	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.0
		SF-295
Lung ca. A549	0.0	Brain (Amygdala)	1.0
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	20.6
Lung ca. NCI-H23	0.0	Brain (fetal)	5.5
Lung ca. NCI-H460	0.0	Brain (Hippocampus)	0.4
		Pool
Lung ca. HOP-62	0.0	Cerebral Cortex Pool	3.3
Lung ca. NCI-H522	0.0	Brain (Substantia	2.3
		nigra) Pool
Liver	10.3	Brain (Thalamus) Pool	1.3
Fetal Liver	55.5	Brain (whole)	5.9
Liver ca. HepG2	0.0	Spinal Cord Pool	2.7
Kidney Pool	32.1	Adrenal Gland	49.7
Fetal Kidney	9.0	Pituitary gland Pool	2.5
Renal ca. 786-0	0.0	Salivary Gland	19.5
Renal ca. A498	0.0	Thyroid (female)	6.3
Renal ca. ACHN	0.0	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	0.6	Pancreas Pool	1.7

[0896] General_screening_panel_v1.6 Summary: Ag7047 Highest expression of this gene is detected in placenta (CT=29). Moderate to low levels of expression of this gene are also seen in, tissues with metabolic/endocrine functions, including pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[0897] Moderate levels of expression are also seen in a sample derived from colon cancer. Thus, therapeutic modulation of the expression or function of this gene may be useful in the treatment of colon cancer.

[0898] In addition, moderate levels of expression of this gene are also detected in fetal brain and cerebellum. Thus, therapeutic modulation of this gene may be useful in the treatment of neurological disorders such as ataxia and autism.

[0899] Interestingly, this gene is expressed at much higher levels in fetal (CT=30) when compared to adult lung (CT=34). This observation suggests that expression of this gene can be used to distinguish fetal from adult lung. In addition, the relative overexpression of this gene in fetal tissue suggests that the protein product may enhance lung growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of lung related diseases.

[0900] R. CG146250-02: Novel Membrane Protein

[0901] Expression of full-length physical clone CG146250-02 was assessed using the primer-probe set Ag7566, described in Table RA. Results of the RTQ-PCR runs are shown in Table RB.

TABLE RA
Probe Name Ag7566
Primers	Sequence	Length	Start Position	SEQ ID No
Forward	5′-agcttccaccatcactttca-3′	20	198	293
Probe	TET-5′-cacatgccgtgtccaaggagctc-3	23	218	294	123	218	294
	′-TAMRA
Reverse	5′-gacaaagaggaagtcattatccagtag-3	27	246	295

[0902]

TABLE RB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7566,		(%) Ag7566,
	Run		Run
Tissue Name	308751128	issue Name	308751128
AD 1 Hippo	0.0	Control (Path) 3	0.0
		Temporal Ctx
AD 2 Hippo	10.4	Control (Path) 4	10.4
		Temporal Ctx
AD 3 Hippo	5.5	AD 1 Occipital Ctx	10.6
AD 4 Hippo	0.0	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	22.8	AD 3 Occipital Ctx	2.9
AD 6 Hippo	0.0	AD 4 Occipital Ctx	29.9
Control 2 Hippo	0.0	AD 5 Occipital Ctx	0.0
Control 4 Hippo	11.2	AD 6 Occipital Ctx	0.0
Control (Path) 3	2.5	Control 1 Occipital	0.0
Hippo		Ctx
AD 1 Temporal Ctx	0.0	Control 2 Occipital	0.0
		Ctx
AD 2 Temporal Ctx	13.6	Control 3 Occipital	38.7
		Ctx
AD 3 Temporal Ctx	7.8	Control 4 Occipital	6.3
		Ctx
AD 4 Temporal Ctx	11.0	Control (Path) 1	28.1
		Occipital Ctx
AD 5 Inf Temporal	29.9	Control (Path) 2	12.8
Ctx		Occipital Ctx
AD 5 Sup Temporal	25.9	Control (Path) 3	0.0
Ctx		Occipital Ctx
AD 6 Inf Temporal	52.9	Control (Path) 4	0.0
Ctx		Occipital Ctx
AD 6 Sup Temporal	100.0	Control 1 Parietal Ctx	0.0
Ctx
Control 1 Temporal	11.2	Control 2 Parietal Ctx	61.6
Ctx
Control 2 Temporal	12.4	Control 3 Parietal Ctx	11.7
Ctx
Control 3 Temporal	31.4	Control (Path) 1	48.0
Ctx		Parietal Ctx
Control 3 Temporal	12.4	Control (Path) 2	0.0
Ctx		Parietal Ctx
Control (Path) 1	14.9	Control (Path) 3	0.0
Temporal Ctx		Parietal Ctx
Control (Path) 2	17.3	Control (Path) 4	12.7
Temporal Ctx		Parietal Ctx

[0903] CNS_neurodegeneration_v1.0 Summary: Ag7566 Low levels of expression of this gene is restricted to a sample derived from Alzheimer's patient (CT=34.5). Thus, expression of this gene may be useful in distinguishing this sample from other samples used in this panel.

[0904] Panel 4.1D Summary: Ag7566 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0905] S. CG146625-01: Type IIIa Membrane Protein

[0906] Expression of full-length physical clone CG146625-01 was assessed using the primer-probe set Ag7052, described in Table SA. Results of the RTQ-PCR runs are shown in Table SB.

TABLE SA
Probe Name Ag7052
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-tgagaacctgcagcatcaga-3′	20	279	296
Probe	TET-5′-atacggcagctgactgcaaacctcagc-3′-TAMRA	27	305	1297
Reverse	5′-tcctggtggtgaaaggatgt-3′	120	360	298

[0907]

TABLE SB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag7052,		(%) Ag7052,
	Run		Run
Tissue Name	282273862	issue Name	282273862
Adipose	5.9	Renal ca. TK-10	55.5
Melanoma*	19.2	Bladder	13.5
Hs688(A).T
Melanoma*	26.1	Gastric ca. (liver met.)	100.0
Hs688(B).T		NCI-N87
Melanoma* M14	37.1	Gastric ca. KATO III	40.3
Melanoma*	13.7	Colon ca. SW-948	17.9
LOXIMVI
Melanoma*	23.8	Colon ca. SW480	47.3
SK-MEL-5
Squamous cell	26.6	Colon ca.* (SW480	29.9
carcinoma SCC-4		met) SW620
Testis Pool	37.6	Colon ca. HT29	38.7
Prostate ca.* (bone	51.4	Colon ca. HCT-116	55.1
met) PC-3
Prostate Pool	9.9	Colon ca. CaCo-2	45.7
Placenta	17.4	Colon cancer tissue	14.4
Uterus Pool	4.5	Colon ca. SW1116	15.0
Ovarian ca.	22.1	Colon ca. Colo-205	24.5
OVCAR-3
Ovarian ca.	28.1	Colon ca. SW-48	24.5
SK-OV-3
Ovarian ca.	14.3	Colon Pool	15.4
OVCAR-4
Ovarian ca.	76.3	Small Intestine Pool	17.2
OVCAR-5
Ovarian ca.	29.3	Stomach Pool	7.7
IGROV-1
Ovarian ca.	47.3	Bone Marrow Pool	7.6
OVCAR-8
Ovary	12.0	Fetal Heart	4.7
Breast ca. MCF-7	46.3	Heart Pool	10.3
Breast ca.	64.2	Lymph Node Pool	24.1
MDA-MB-231
Breast ca. BT 549	26.4	Fetal Skeletal Muscle	5.2
Breast ca. T47D	9.5	Skeletal Muscle Pool	3.2
Breast ca. MDA-N	9.4	Spleen Pool	9.0
Breast Pool	12.0	Thymus Pool	16.6
Trachea	18.6	CNS cancer (glio/	66.4
		astro) U87-MG
Lung	3.8	CNS cancer (glio/	74.7
		astro) U-118-MG
Fetal Lung	14.1	CNS cancer (neuro;	29.1
		met) SK-N-AS
Lung ca. NCI-N417	6.8	CNS cancer (astro)	23.8
		SF-539
Lung ca. LX-1	45.1	CNS cancer (astro)	54.0
		SNB-75
Lung ca. NCI-H146	7.0	CNS cancer (glio)	30.6
		SNB-19
Lung ca. SHP-77	26.4	CNS cancer (glio)	82.9
		SF-295
Lung ca. A549	35.8	Brain (Amygdala)	10.1
		Pool
Lung ca. NCI-H526	4.8	Brain (cerebellum)	42.3
Lung ca. NCI-H23	59.9	Brain (fetal)	11.7
Lung ca. NCI-H460	22.1	Brain (Hippocampus)	11.7
		Pool
Lung ca. HOP-62	44.4	Cerebral Cortex Pool	14.4
Lung ca. NCI-H522	45.7	Brain (Substantia	10.1
		nigra) Pool
Liver	17.6	Brain (Thalamus) Pool	12.8
Fetal Liver	35.4	Brain (whole)	13.9
Liver ca. HepG2	36.3	Spinal Cord Pool	11.3
Kidney Pool	27.4	Adrenal Gland	24.3
Fetal Kidney	11.4	Pituitary gland Pool	5.0
Renal ca. 786-0	48.6	Salivary Gland	13.1
Renal ca. A498	7.0	Thyroid (female)	19.3
Renal ca. ACHN	25.9	Pancreatic ca.	62.4
		CAPAN2
Renal ca. UO-31	39.8	Pancreas Pool	9.7

[0908] General_screening_panel_v1.6 Summary: Ag7052 Highest expression of this gene is seen in a gastric cancer cell line (CT=28). This gene is widely expressed in this panel, with moderate expression seen in brain, colon, gastric, lung, breast, ovarian, and melanoma cancer cell lines. This expression profile suggests a role for this gene product in cell survival and proliferation. Modulation of this gene product may be useful in the treatment of cancer.

[0909] Among tissues with metabolic function, this gene is expressed at moderate to low levels in pituitary, adipose, adrenal gland, pancreas, thyroid, and adult and fetal skeletal muscle, heart, and liver. This widespread expression among these tissues suggests that this gene product may play a role in normal neuroendocrine and metabolic function and that disregulated expression of this gene may contribute to neuroendocrine disorders or metabolic diseases, such as obesity and diabetes.

[0910] This gene is also expressed at moderate levels in the CNS, including the hippocampus, thalamus, substantia nigra, amygdala, cerebellum and cerebral cortex. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurologic disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, multiple sclerosis, stroke and epilepsy.

[0911] T. CG146625-02: Type IIIa Membrane Protein

[0912] Expression of full-length physical clone CG146625-02 was assessed using the primer-probe set Ag6939, described in Table TA. Results of the RTQ-PCR runs are shown in Table TB.

TABLE TA
Probe Name Ag6939
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gctgagccttccacgagtt-3′	19	680	299
Probe	TET-5′-tcatcccagatcaccatgcagaagc-3′-TAMRA	25	740	300
Reverse	5′-gtgctgagggtttgcagtcag-3′	20	809	301

[0913]

TABLE TB
General_screening_panel_v1.6
	Rel. Exp.		Rel. Exp.
	(%) Ag6939,		(%) Ag6939,
	Run		Run
Tissue Name	278700426	issue Name	278700426
Adipose	8.7	Renal ca. TK-10	59.9
Melanoma*	47.6	Bladder	13.4
Hs688(A).T
Melanoma*	36.9	Gastric ca. (liver met.)	88.3
Hs688(B).T		NCI-N87
Melanoma* M14	38.7	Gastric ca. KATO III	39.8
Melanoma*	18.2	Colon ca. SW-948	5.6
LOXIMVI
Melanoma*	22.2	Colon ca. SW480	55.5
SK-MEL-5
Squamous cell	54.3	Colon ca.* (SW480	25.7
carcinoma SCC-4		met) SW620
Testis Pool	24.3	Colon ca. HT29	36.3
Prostate ca.* (bone	60.3	Colon ca. HCT-116	35.4
met) PC-3
Prostate Pool	15.7	Colon ca. CaCo-2	32.8
Placenta	12.4	Colon cancer tissue	22.5
Uterus Pool	7.9	Colon ca. SW1116	19.3
Ovarian ca.	29.9	Colon ca. Colo-205	21.8
OVCAR-3
Ovarian ca.	27.2	Colon ca. SW-48	28.7
SK-OV-3
Ovarian ca.	14.8	Colon Pool	20.6
OVCAR-4
Ovarian ca.	50.7	Small Intestine Pool	16.5
OVCAR-5
Ovarian ca.	37.9	Stomach Pool	10.8
IGROV-1
Ovarian ca.	52.1	Bone Marrow Pool	5.3
OVCAR-8
Ovary	12.6	Fetal Heart	2.4
Breast ca. MCF-7	47.3	Heart Pool	11.9
Breast ca.	100.0	Lymph Node Pool	53.2
MDA-MB-231
Breast ca. BT 549	23.0	Fetal Skeletal Muscle	1.1
Breast ca. T47D	12.1	Skeletal Muscle Pool	1.5
Breast ca. MDA-N	16.3	Spleen Pool	8.1
Breast Pool	25.3	Thymus Pool	11.8
Trachea	18.0	CNS cancer (glio/	54.7
		astro) U87-MG
Lung	8.2	CNS cancer (glio/	70.7
		astro) U-118-MG
Fetal Lung	12.2	CNS cancer (neuro;	20.7
		met) SK-N-AS
Lung ca. NCI-N417	8.1	CNS cancer (astro)	25.2
		SF-539
Lung ca. LX-1	22.1	CNS cancer (astro)	39.8
		SNB-75
Lung ca. NCI-H146	7.1	CNS cancer (glio)	33.9
		SNB-19
Lung ca. SHP-77	18.7	CNS cancer (glio)	77.4
		SF-295
Lung ca. A549	29.9	Brain (Amygdala)	7.6
		Pool
Lung ca. NCI-H526	5.0	Brain (cerebellum)	17.3
Lung ca. NCI-H23	8.2	Brain (fetal)	8.3
Lung ca. NCI-H460	23.0	Brain (Hippocampus)	12.4
		Pool
Lung ca. HOP-62	39.8	Cerebral Cortex Pool	10.0
Lung ca. NCI-H522	36.3	Brain (Substantia	11.7
		nigra) Pool
Liver	11.6	Brain (Thalamus) Pool	11.7
Fetal Liver	41.2	Brain (whole)	10.4
Liver ca. HepG2	23.7	Spinal Cord Pool	9.9
Kidney Pool	39.2	Adrenal Gland	24.0
Fetal Kidney	6.1	Pituitary gland Pool	6.4
Renal ca. 786-0	39.0	Salivary Gland	12.2
Renal ca. A498	4.6	Thyroid (female)	23.0
Renal ca. ACHN	20.6	Pancreatic ca.	52.5
		CAPAN2
Renal ca. UO-31	33.2	Pancreas Pool	10.3

[0914] General_screening_panel_v1.6 Summary: Ag6939 Highest expression of this gene is detected in a breast cancer MDA-MB-231 cell line (CT=32). Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, liver, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of pancreatic, gastric, colon, lung, liver, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0915] Low levels of expression of this gene is also seen in samples derived from normal tissues represented by testis, prostate, ovary, trachea, fetal liver, colon, small intestine, lymph node, cerebellum, thyroid and adrenal gland. Therefore, therapeutic modulation of this gene or its protein product may be useful in the treatment of diseases related to these tissues.

[0916] U. CG147284-01: Cadherin-6 Precursor

[0917] Expression of full-length physical clone CG147284-01 was assessed using the primer-probe set Ag7567, described in Table UA.

TABLE UA
Probe Name Ag7567
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-cgtgttgtctttgttgtcttga-3′	22	285	302
Probe	TET-5′-tgtgggcaagttacattcaaactttacca-3′-TAMRA	29	255	303
Reverse	5′-gaatacacaggatccgattatcagta-3′	26	229	304

[0918] CNS_neurodegeneration_v1.0 Summary: Ag7567 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0919] Panel 4.1D Summary: Ag7567 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[0920] V. CG148221-01 and CG148221-02: Claudin Domain Containing Novel TmMP

[0921] Expression of gene CG148221-01 and full-length physical clone was assessed using the primer-probe set Ag5625, described in Table VA. Results of the RTQ-PCR runs are shown in Tables VB, VC and VD.

TABLE VA
Probe Name Ag5625
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-tttctgctggcagacatgat-3′	20	469	305
Probe	TET-5′-agcaccgacgccatcagtggatt-3′-TAMRA	23	496	306
Reverse	5′-caggctgcagtcacagaca-3′	19	526	307

[0922]

TABLE VB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag5625,		(%) Ag5625,
	Run		Run
Tissue Name	244647005	issue Name	244647005
AD 1 Hippo	23.5	Control (Path) 3	20.4
		Temporal Ctx
AD 2 Hippo	62.4	Control (Path) 4	44.8
		Temporal Ctx
AD 3 Hippo	2.8	AD 1 Occipital Ctx	11.7
AD 4 Hippo	10.5	AD 2 Occipital Ctx	3.0
		(Missing)
AD 5 Hippo	45.7	AD 3 Occipital Ctx	4.7
AD 6 Hippo	76.8	AD 4 Occipital Ctx	20.7
Control 2 Hippo	30.4	AD 5 Occipital Ctx	37.9
Control 4 Hippo	10.4	AD 6 Occipital Ctx	40.6
Control (Path) 3	17.9	Control 1 Occipital	8.5
Hippo		Ctx
AD 1 Temporal Ctx	27.2	Control 2 Occipital	52.1
		Ctx
AD 2 Temporal Ctx	57.8	Control 3 Occipital	17.7
		Ctx
AD 3 Temporal Ctx	7.9	Control 4 Occipital	15.6
		Ctx
AD 4 Temporal Ctx	24.5	Control (Path) 1	52.1
		Occipital Ctx
AD 5 Inf Temporal	100.0	Control (Path) 2	5.3
Ctx		Occipital Ctx
AD 5 SupTemporal	69.7	Control (Path) 3	10.5
Ctx		Occipital Ctx
AD 6 Inf Temporal	74.7	Control (Path) 4	20.4
Ctx		Occipital Ctx
AD 6 Sup Temporal	57.8	Control 1 Parietal Ctx	14.7
Ctx
Control 1 Temporal	24.1	Control 2 Parietal Ctx	54.0
Ctx
Control 2 Temporal	33.9	Control 3 Parietal Ctx	31.6
Ctx
Control 3 Temporal	19.8	Control (Path) 1	54.0
Ctx		Parietal Ctx
Control 4 Temporal	18.2	Control (Path) 2	15.7
Ctx		Parietal Ctx
Control (Path) 1	34.9	Control (Path) 3	15.6
Temporal Ctx		Parietal Ctx
Control (Path) 2	44.1	Control (Path) 4	40.1
Temporal Ctx		Parietal Ctx

[0923]

TABLE VC
General_screening_panel_v1.5
	Rel. Exp.		Rel. Exp.
	(%) Ag5625,		(%) Ag5625,
	Run		Run
Tissue Name	244646965	issue Name	244646965
Adipose	18.4	Renal ca. TK-10	29.5
Melanoma*	3.7	Bladder	22.2
Hs688(A).T
Melanoma*	2.4	Gastric ca. (liver met.)	12.2
Hs688(B).T		NCI-N87
Melanoma* M14	14.5	Gastric ca. KATO III	23.0
Melanoma*	1.7	Colon ca. SW-948	12.0
LOXIMVI
Melanoma*	4.8	Colon ca. SW480	82.9
SK-MEL-5
Squamous cell	4.0	Colon ca.* (SW480	36.6
carcinoma SCC-4		met) SW620
Testis Pool	30.6	Colon ca. HT29	24.0
Prostate ca.* (bone	7.8	Colon ca. HCT-116	31.2
met) PC-3
Prostate Pool	2.9	Colon ca. CaCo-2	31.2
Placenta	0.4	Colon cancer tissue	8.1
Uterus Pool	2.6	Colon ca. SW1116	4.2
Ovarian ca.	2.8	Colon ca. Colo-205	2.8
OVCAR-3
Ovarian ca.	8.2	Colon ca. SW-48	4.6
SK-OV-3
Ovarian ca.	10.6	Colon Pool	5.6
OVCAR-4
Ovarian ca.	23.2	Small Intestine Pool	12.3
OVCAR-5
Ovarian ca.	13.7	Stomach Pool	7.8
IGROV-1
Ovarian ca.	6.0	Bone Marrow Pool	6.7
OVCAR-8
Ovary	3.3	Fetal Heart	2.1
Breast ca. MCF-7	8.1	Heart Pool	3.0
Breast ca.	29.3	Lymph Node Pool	9.3
MDA-MB-231
Breast ca. BT 549	7.1	Fetal Skeletal Muscle	4.1
Breast ca. T47D	4.3	Skeletal Muscle Pool	4.9
Breast ca. MDA-N	22.1	Spleen Pool	5.0
Breast Pool	6.0	Thymus Pool	9.3
Trachea	1.8	CNS cancer (glio/	30.8
		astro) U87-MG
Lung	16.6	CNS cancer (glio/	28.1
		astro) U-118-MG
Fetal Lung	3.7	CNS cancer (neuro;	11.9
		met) SK-N-AS
Lung ca. NCI-N417	6.4	CNS cancer (astro)	3.0
		SF-539
Lung ca. LX-1	100.0	CNS cancer (astro)	25.9
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	17.1
		SNB-19
Lung ca. SHP-77	18.4	CNS cancer (glio)	24.0
		SF-295
Lung ca. A549	51.4	Brain (Amygdala)	8.7
		Pool
Lung ca. NCI-H526	7.0	Brain (cerebellum)	28.5
Lung ca. NCI-H23	15.3	Brain (fetal)	11.3
Lung ca. NCI-H460	15.7	Brain (Hippocampus)	10.2
		Pool
Lung ca. HOP-62	3.3	Cerebral Cortex Pool	11.4
Lung ca. NCI-H522	29.5	Brain (Substantia	11.6
		nigra) Pool
Liver	1.7	Brain (Thalamus) Pool	14.3
Fetal Liver	8.5	Brain (whole)	7.3
Liver ca. HepG2	57.8	Spinal Cord Pool	7.9
Kidney Pool	24.1	Adrenal Gland	6.7
Fetal Kidney	7.4	Pituitary gland Pool	3.0
Renal ca. 786-0	10.4	Salivary Gland	6.8
Renal ca. A498	18.9	Thyroid (female)	5.2
Renal ca. ACHN	1.7	Pancreatic ca.	34.9
		CAPAN2
Renal ca. UO-31	2.5	Pancreas Pool	6.4

[0924]

TABLE VD
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	() Ag5625,		(%) Ag5625,
	Run		Run
Tissue Name	246490692	Tissue Name	246490692
Secondary Th1 act	17.1	HUVEC IL-1beta	1.8
Secondary Th2 act	30.4	HUVEC IFN gamma	0.0
Secondary Tr1 act	15.2	HUVEC TNF alpha +	0.7
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	2.6
Secondary Tr1 rest	1.3	Lung Microvascular	1.0
		EC none
Primary Th1 act	0.0	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	15.0	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	10.2	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	1.7
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	1.8
		epithelium none
Primary Tr1 rest	0.5	Small airway	1.1
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	5.6	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	9.7	Coronery artery SMC	1.6
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	1.3	Astrocytes rest	0.6
Secondary CD8	4.8	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	6.7	KU-812 (Basophil)	1.3
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	2.3
none		PMA/ionomycin
2ry Th1/Th2/	0.1	CCD1106	2.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	3.4	CCD1106	1.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	8.5	Liver cirrhosis	2.6
LAK cells IL-2 +	2.6	NCI-H292 none	1.7
IL-12
LAK cells IL-2 +	5.8	NCI-H292 IL-4	0.7
IFN gamma
LAK cells IL-2 +	2.0	NCI-H292 IL-9	6.0
IL-18
LAK cells PMA/	16.4	NCI-H292 IL-13	1.8
ionomycin
NK Cells IL-2 rest	100.0	NCI-H292 IFN gamma	0.6
Two Way MLR 3	3.6	HPAEC none	0.0
day
Two Way MLR 5	0.0	HPAEC TNF alpha +	0.8
day		IL-1 beta
Two Way MLR 7	1.6	Lung fibroblast	1.3
day		none
PBMC rest	0.7	Lung fibroblast TNF	1.3
		alpha + IL-1 beta
PBMC PWM	2.0	Lung fibroblast IL-4	1.4
PBMC PHA-L	1.3	Lung fibroblast IL-9	0.7
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	4.2	Lung fibroblast IFN	0.6
ionomycin		gamma
B lymphocytes	7.4	Dermal fibroblast	1.7
PWM		CCD1070 rest
B lymphocytes	6.0	Dermal fibroblast	31.4
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	14.2	Dermal fibroblast	0.3
		CCD1070 IL-1 beta
EOL-1 dbcAMP	1.1	Dermal fibroblast IFN	1.0
PMA/ionomycin		gamma
Dendritic cells none	3.2	Dermal fibroblast IL-4	1.9
Dendritic cells LPS	1.3	Dermal Fibroblasts	0.0
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.6
anti-CD40		LPS
Monocytes rest	0.5	Neutrophils rest	2.7
Monocytes LPS	3.5	Colon	0.7
Macrophages rest	0.7	Lung	0.0
Macrophages LPS	0.7	Thymus	0.0
HUVEC none	1.2	Kidney	2.3
HUVEC starved	2.5

[0925] CNS_neurodegeneration_v1.0 Summary: Ag5625 This panel does not show differential expression of this gene in Alzheimer's disease. However, this profile confirms the expression of this gene at moderate levels in the brain. Please see Panel 1.5 for discussion of utility of this gene in the central nervous system.

[0926] General_screening_panel_v1.5 Summary: Ag5625 Highest expression of this gene is seen in a lung cancer cell line (CT=29.4). This gene is widely expressed in this panel, with moderate expression seen in brain, colon, gastric, lung, breast, ovarian, and melanoma cancer cell lines. This expression profile suggests a role for this gene product in cell survival and proliferation. This gene encodes a protein with homology to claudin, a family of proteins that are integral components of the tight junction. Members of this family have been shown to be upregulated in pancreatic cancer and colon cancer and in the former case proposed as novel targets for the treatment of this disease (Michl P. Gastroenterology 2001 September;121(3):678-84; Miwa, N. Oncol Res 2001;12(11-12):469-76) Therefore, therapeutic modulation of the expression or function of this protein may be of use in the treatment of these cancers.

[0927] Among tissues with metabolic function, this gene is expressed at low but significant levels in pituitary, adipose, adrenal gland, pancreas, thyroid, fetal liver and adult and fetal skeletal muscle and heart. This widespread expression among these tissues suggests that this gene product may play a role in normal neuroendocrine and metabolic function and that disregulated expression of this gene may contribute to neuroendocrine disorders or metabolic diseases, such as obesity and diabetes.

[0928] This gene is also expressed at low but significant levels in the CNS, including the hippocampus, thalamus, substantia nigra, amygdala, cerebellum and cerebral cortex. Claudin 11 has been shown to be a component of the CNS myelin and has been implicated in the regulation of growth and differentiation via signal transduction pathways. Furthermore, evidence has been presented that shows that claudin 11 may be involved in the autoantigen that is responsible for the development of autoimmune demyelinating disease.(Bronstein J M. J Neurosci Res Mar. 15, 2000;59(6):706-11). Therefore, therapeutic modulation of the expression or function of this putative claudin may be of use in the treatment of demyelinating diseases such as multiple sclerosis and in restoring normal function to the CNS.

[0929] Panel 4.1D Summary: Ag5625 Highest expression of this gene is seen in IL-2 treated NK cells (CT=29). This observation suggests that therapeutic modulation of this gene could be of use in the treatment of viral or bacterial intracellular infections.

[0930] W. CG149332-01: Interferon Induced Transmembrane Protein 3 (1-8U)—Like

[0931] Expression of gene CG149332-01 was assessed using the primer-probe set Ag7580, described in Table WA. Results of the RTQ-PCR runs are shown in Tables WB and WC.

TABLE WA
Probe Name Ag7580
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gagaagcatgaggtggctgt-3′	20	76	308
Probe	TET-5′-accccacaaccctgtgcctccag-3′-TAMRA	23	105	309
Reverse	5′-gcagatgtggatcatggtga-3′	20	131	310

[0932]

TABLE WB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7580,		(%) Ag7580,
	Run		Run
Tissue Name	308752173	issue Name	308752173
AD 1 Hippo	17.2	Control (Path) 3	17.4
		Temporal Ctx
AD 2 Hippo	30.4	Control (Path) 4	27.7
		Temporal Ctx
AD 3 Hippo	3.7	AD 1 Occipital Ctx	12.9
AD 4 Hippo	29.7	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	24.3	AD 3 Occipital Ctx	0.0
AD 6 Hippo	100.0	AD 4 Occipital Ctx	14.8
Control 2 Hippo	8.7	AD 5 Occipital Ctx	7.0
Control 4 Hippo	40.1	AD 6 Occipital Ctx	3.5
Control (Path) 3	7.5	Control 1 Occipital	8.2
Hippo		Ctx
AD 1 Temporal Ctx	7.9	Control 2 Occipital	12.1
		Ctx
AD 2 Temporal Ctx	23.2	Control 3 Occipital	13.8
		Ctx
AD 3 Temporal Ctx	5.7	Control 4 Occipital	7.5
		Ctx
AD 4 Temporal Ctx	11.8	Control (Path) 1	16.4
		Occipital Ctx
AD 5 Inf Temporal	44.8	Control (Path) 2	3.5
Ctx		Occipital Ctx
AD 5 Sup Temporal	87.7	Control (Path) 3	3.2
Ctx		Occipital Ctx
AD 6 Inf Temporal	56.6	Control (Path) 4	10.2
Ctx		Occipital Ctx
AD 6 Sup Temporal	56.3	Control 1 Parietal Ctx	4.1
Ctx
Control 1 Temporal	14.4	Control 2 Parietal Ctx	62.0
Ctx
Control 2 Temporal	28.7	Control 3 Parietal Ctx	2.9
Ctx
Control 3 Temporal	28.5	Control (Path) 1	38.7
Ctx		Parietal Ctx
Control 3 Temporal	6.1	Control (Path) 2	13.4
Ctx		Parietal Ctx
Control (Path) 1	40.3	Control (Path) 3	3.7
Temporal Ctx		Parietal Ctx
Control (Path) 2	53.2	Control (Path) 4	29.1
Temporal Ctx		Parietal Ctx

[0933]

TABLE WC
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	( ) Ag7580,		(%) Ag7580,
	Run		Run
Tissue Name	308748674	Tissue Name	308748674
Secondary Th1 act	9.5	HUVEC IL-1beta	2.5
Secondary Th2 act	21.3	HUVEC IFN gamma	19.8
Secondary Tr1 act	4.2	HUVEC TNF alpha +	0.7
		IFN gamma
Secondary Th1 rest	3.0	HUVEC TNF alpha +	1.4
		IL4
Secondary Th2 rest	11.1	HUVEC IL-11	2.9
Secondary Tr1 rest	15.1	Lung Microvascular	2.4
		EC none
Primary Th1 act	1.8	Lung Microvascular	1.1
		EC TNFalpha +
		IL-1beta
Primary Th2 act	25.0	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	12.1	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	12.4	Bronchial epithelium	10.1
		TNFalpha + IL-1beta
Primary Th2 rest	21.2	Small airway	2.0
		epithelium none
Primary Tr1 rest	2.8	Small airway	14.5
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	21.0	Coronery artery SMC	5.5
lymphocyte act		rest
CD45RO CD4	63.3	Coronery artery SMC	7.9
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	15.1	Astrocytes rest	0.0
Secondary CD8	10.7	Astrocytes	2.1
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	1.5	KU-812 (Basophil)	3.3
lymphocyte act		rest
CD4 lymphocyte	19.3	KU-812 (Basophil)	8.4
none		PMA/ionomycin
2ry Th1/Th2/	9.9	CCD1106	13.7
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	33.0	CCD1106	8.6
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	12.3	Liver cirrhosis	3.5
LAK cells IL-2 +	2.1	NCI-H292 none	19.3
IL-12
LAK cells IL-2 +	20.6	NCI-H292 IL-4	20.7
IFN gamma
LAK cells IL-2 +	11.1	NCI-H292 IL-9	31.6
IL-18
LAK cells PMA/	14.5	NCI-H292 IL-13	22.2
ionomycin
NK Cells IL-2 rest	100.0	NCI-H292 IFN gamma	5.3
Two Way MLR 3	31.9	HPAEC none	1.2
day
Two Way MLR 5	4.9	HPAEC TNF alpha +	5.9
day		IL-1 beta
Two Way MLR 7	5.7	Lung fibroblast	1.1
day		none
PBMC rest	6.1	Lung fibroblast TNF	1.1
		alpha + IL-1 beta
PBMC PWM	9.9	Lung fibroblast IL-4	0.6
PBMC PHA-L	11.2	Lung fibroblast IL-9	2.0
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.9
Ramos (B cell)	1.9	Lung fibroblast IFN	4.2
ionomycin		gamma
B lymphocytes	5.9	Dermal fibroblast	16.2
PWM		CCD1070 rest
B lymphocytes	60.3	Dermal fibroblast	59.9
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	2.8	Dermal fibroblast	10.6
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN	1.5
PMA/ionomycin		gamma
Dendritic cells none	4.0	Dermal fibroblast IL-4	2.3
Dendritic cells LPS	1.8	Dermal Fibroblasts	0.4
		rest
Dendritic cells	0.0	Neutrophils TNFa +	6.3
anti-CD40		LPS
Monocytes rest	0.3	Neutrophils rest	5.5
Monocytes LPS	4.7	Colon	0.6
Macrophages rest	2.0	Lung	0.6
Macrophages LPS	0.6	Thymus	1.2
HUVEC none	2.5	Kidney	4.2
HUVEC starved	1.4

[0934] CNS_neurodegeneration_v1.0 Summary: Ag7580 This panel does not show differential expression of this gene in Alzheimer's disease. However, this profile confirms the expression of this gene at moderate levels in the brain, including the hippocampus and cortex. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurological disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, multiple sclerosis, stroke and epilepsy.

[0935] Panel 4.1D Summary: Ag7580 Highest expression of this gene is seen in IL-2 treated NK cells. Moderate to low levels of expression are seen in many samples on this panel, inlucding TNF-a treated and resting dermal fibroblasts, TNF-a and LPS treated neutrophils, activated primary and secondary T cells, and LAK cells. This expression suggests that modulation of the expression or function of this gene may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.

[0936] X. CG149649-01: Type IIIA Membrane Protein

[0937] Expression of gene CG149649-01 was assessed using the primer-probe set Ag7568, described in Table XA. Results of the RTQ-PCR runs are shown in Tables XB and XC.

TABLE XA
Probe Name Ag7568
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-ggcctcttggccctctact-3′	19	226	311
Probe	TET-5′-cctcctgcttttgctcttctggatctacag-3′-TAMRA	30	246	312
Reverse	5′-tatagcacccctgtgggagt-3′	20	290	313

[0938]

TABLE XB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7568,		(%) Ag7568,
	Run		Run
Tissue Name	308751131	issue Name	308751131
AD 1 Hippo	18.7	Control (Path) 3	10.4
		Temporal Ctx
AD 2 Hippo	40.6	Control (Path) 4	20.2
		Temporal Ctx
AD 3 Hippo	12.0	AD 1 Occipital Ctx	15.1
AD 4 Hippo	8.7	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	60.7	AD 3 Occipital Ctx	11.0
AD 6 Hippo	100.0	AD 4 Occipital Ctx	26.8
Control 2 Hippo	41.2	AD 5 Occipital Ctx	32.1
Control 4 Hippo	29.7	AD 6 Occipital Ctx	19.5
Control (Path) 3	14.2	Control 1 Occipital	9.9
Hippo		Ctx
AD 1 Temporal Ctx	20.2	Control 2 Occipital	55.5
		Ctx
AD 2 Temporal Ctx	50.7	Control 3 Occipital	16.6
		Ctx
AD 3 Temporal Ctx	10.7	Control 4 Occipital	12.0
		Ctx
AD 4 Temporal Ctx	28.7	Control (Path) 1	68.8
		Occipital Ctx
AD 5 Inf Temporal	60.3	Control (Path) 2	17.8
Ctx		Occipital Ctx
AD 5 Sup Temporal	47.3	Control (Path) 3	6.1
Ctx		Occipital Ctx
AD 6 Inf Temporal	76.3	Control (Path) 4	11.9
Ctx		Occipital Ctx
AD 6 Sup Temporal	82.9	Control 1 Parietal Ctx	16.5
Ctx
Control 1 Temporal	10.7	Control 2 Parietal Ctx	43.8
Ctx
Control 2 Temporal	42.6	Control 3 Parietal Ctx	15.1
Ctx
Control 3 Temporal	21.5	Control (Path) 1	59.0
Ctx		Parietal Ctx
Control 3 Temporal	13.0	Control (Path) 2	21.2
Ctx		Parietal Ctx
Control (Path) 1	39.2	Control (Path) 3	10.2
Temporal Ctx		Parietal Ctx
Control (Path) 2	34.7	Control (Path) 4	21.5
Temporal Ctx		Parietal Ctx

[0939]

TABLE XC
Panel 4.1D
	Rel. Ep.		Rel. Exp.
	(%) Ag7568,		(%) Ag7568,
	Run		Run
Tissue Name	308748452	Tissue Name	308748452
Secondary Th1 act	45.4	HUVEC IL-1beta	39.5
Secondary Th2 act	70.2	HUVEC IFN gamma	47.3
Secondary Tr1 act	26.8	HUVEC TNF alpha +	13.6
		IFN gamma
Secondary Th1 rest	4.5	HUVEC TNF alpha +	10.5
		IL4
Secondary Th2 rest	5.5	HUVEC IL-11	19.1
Secondary Tr1 rest	10.4	Lung Microvascular	51.1
		EC none
Primary Th1 act	5.4	Lung Microvascular	22.1
		EC TNFalpha +
		IL-1beta
Primary Th2 act	38.2	Microvascular Dermal	6.0
		EC none
Primary Tr1 act	33.9	Microsvasular Dermal	14.7
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	2.4	Bronchial epithelium	6.8
		TNFalpha + IL-1beta
Primary Th2 rest	4.5	Small airway	27.0
		epithelium none
Primary Tr1 rest	0.8	Small airway	39.8
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	24.7	Coronery artery SMC	40.3
lymphocyte act		rest
CD45RO CD4	38.4	Coronery artery SMC	31.6
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	13.1	Astrocytes rest	8.8
Secondary CD8	13.9	Astrocytes	7.5
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	6.2	KU-812 (Basophil)	36.9
lymphocyte act		rest
CD4 lymphocyte	2.7	KU-812 (Basophil)	63.3
none		PMA/ionomycin
2ry Th1/Th2/	6.0	CCD1106	48.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	18.8	CCD1106	14.9
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	18.7	Liver cirrhosis	7.4
LAK cells IL-2 +	1.4	NCI-H292 none	45.4
IL-12
LAK cells IL-2 +	7.4	NCI-H292 IL-4	49.3
IFN gamma
LAK cells IL-2 +	6.0	NCI-H292 IL-9	100.0
IL-18
LAK cells PMA/	20.4	NCI-H292 IL-13	43.5
ionomycin
NK Cells IL-2 rest	47.6	NCI-H292 IFN gamma	19.8
Two Way MLR 3	22.2	HPAEC none	9.2
day
Two Way MLR 5	6.8	HPAEC TNF alpha +	43.8
day		IL-1 beta
Two Way MLR 7	7.5	Lung fibroblast	47.6
day		none
PBMC rest	5.0	Lung fibroblast TNF	53.6
		alpha + IL-1 beta
PBMC PWM	7.7	Lung fibroblast IL-4	26.4
PBMC PHA-L	10.2	Lung fibroblast IL-9	32.8
Ramos (B cell) none	9.3	Lung fibroblast IL-13	15.4
Ramos (B cell)	40.9	Lung fibroblast IFN	9.5
ionomycin		gamma
B lymphocytes	11.3	Dermal fibroblast	42.0
PWM		CCD1070 rest
B lymphocytes	27.7	Dermal fibroblast	70.7
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	32.3	Dermal fibroblast	24.7
		CCD1070 IL-1 beta
EOL-1 dbcAMP	3.7	Dermal fibroblast IFN	24.8
PMA/ionomycin		gamma
Dendritic cells none	32.3	Dermal fibroblast IL-4	37.9
Dendritic cells LPS	9.8	Dermal Fibroblasts	35.4
		rest
Dendritic cells	10.7	Neutrophils TNFa +	2.8
anti-CD40		LPS
Monocytes rest	13.7	Neutrophils rest	27.2
Monocytes LPS	36.3	Colon	6.4
Macrophages rest	14.2	Lung	4.7
Macrophages LPS	17.4	Thymus	4.9
HUVEC none	26.4	Kidney	36.9
HUVEC starved	26.4

[0940] CNS_neurodegeneration_v1.0 Summary: Ag7568 This panel confirms the expression of this gene at low levels in the brain in an independent group of individuals. This gene appears to be slightly upregulated in the temporal cortex of Alzheimer's disease patients. Therefore, therapeutic modulation of the expression or function of this gene may decrease neuronal death and be of use in the treatment of this disease.

[0941] Panel 4.1D Summary: Ag7568 Highest expression of this gene is seen in IL-9 treated NCI-H292 cells (CT=31.2). In addition, this gene is also expressed at moderate to low levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthnrtis.

[0942] Y. CG149680-01 and CG149680-02: Prostate Cancer Overexpressed Gene 1

[0943] Expression of gene CG149680-02 and variant CG149680-01 was assessed using the primer-probe sets Ag4870 and Ag5280, described in Tables YA and YB. Results of the RTQ-PCR runs are shown in Tables YC, YD, YE and YF. Please note that Ag5280 is specific to CG149680-02.

TABLE YA
Probe Name Ag4870
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gcctgccttatctttctgaact-3′	22	707	314
Probe	TET-5′-ctttcctgcccctgaggaagtcaatt-3′-TAMRA	26	754	315
Reverse	5′-cactcagcttgatcttcttcgt-3′	22	782	316

[0944]

TABLE YB
Probe Name Ag5280
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gctccctgttgatcattctg-3′	20	147	317
Probe	TET-5′-aacgagggcttctattccagcacgt-3′-TAMRA	25	170	318
Reverse	5′-cagcacatgacaccaggaa-3′	19	204	319

[0945]

TABLE YC
AI comprehensive panel v1.0
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag5280,	Ag5280,		Ag5280,	Ag5280,
	Run	Run		Run	Run
Tissue Name	234222214	237378555	issue Name	234222214	237378555
110967 COPD-F	17.2	17.6	112427 Match Control	100.0	100.0
			Psoriasis-F
110980 COPD-F	14.8	24.1	112418 Psoriasis-M	14.5	18.2
110968 COPD-M	10.5	25.3	112723 Match Control	5.8	5.6
			Psoriasis-M
110977 COPD-M	39.0	65.5	112419 Psoriasis-M	19.5	20.6
110989	43.2	33.0	112424 Match Control	6.8	3.6
Emphysema-F			Psoriasis-M
110992	10.5	20.0	112420 Psoriasis-M	56.3	40.9
Emphysema-F
110993	14.5	27.2	112425 Match Control	62.4	47.3
Emphysema-F			Psoriasis-M
110994	12.2	20.0	104689 (MF) OA	11.2	13.7
Emphysema-F			Bone-Backus
110995	20.7	29.5	104690 (MF) Adj	11.5	8.8
Emphysema-F			“Normal”
			Bone-Backus
110996	5.6	11.3	104691 (MF) OA	5.9	14.0
Emphysema-F			Synovium-Backus
110997 Asthma-M	0.0	0.0	104692 (BA) OA	0.0	0.0
			Cartilage-Backus
111001 Asthma-F	13.8	22.5	104694 (BA) OA	14.7	14.3
			Bone-Backus
111002 Asthma-F	23.0	22.4	104695 (BA) Adj	14.8	15.9
			“Normal”
			Bone-Backus
111003 Atopic	19.6	20.4	104696 (BA) OA	6.3	13.2
Asthma-F			Synovium-Backus
111004 Atopic	30.4	69.7	104700 (SS) OA	28.5	20.4
Asthma-F			Bone-Backus
111005 Atopic	20.6	23.5	104701 (SS) Adj	23.7	13.0
Asthma-F			“Normal”
			Bone-Backus
111006 Atopic	2.6	7.9	104702 (SS) OA	16.6	20.9
Asthma-F			Synovium-Backus
111417 Allergy-M	22.8	26.8	117093 OA Cartilage	22.1	16.3
			Rep7
112347 Allergy-M	0.0	0.0	112672 OA Bone5	31.0	39.8
112349 Normal	0.0	0.0	112673 OA	16.5	9.3
Lung-F			Synovium5
112357 Normal	59.5	79.0	112674 OA Synovial	11.8	11.3
Lung-F			Fluid cells5
112354 Normal	17.6	13.6	117100 OA Cartilage	2.6	5.7
Lung-M			Rep14
112374 Crohns-F	23.5	2.9	112756 OA Bone9	95.3	81.8
112389 Match	10.3	2.8	112757 OA	11.9	11.6
Control Crohns-F			Synovium9
112375 Crohns-F	19.6	12.8	112758 OA Synovial	13.8	5.3
			Fluid Cells9
112732 Match	18.3	26.6	117125 RA Cartilage	11.7	25.0
Control Crohns-F			Rep2
112725 Crohns-M	2.5	3.0	113492 Bone2 RA	6.1	8.4
112387 Match	9.6	13.5	113493 Synovium2	6.7	5.2
Control Crohns-M			RA
112378 Crohns-M	0.0	0.0	113494 Syn Fluid	0.0	1.7
			Cells RA
112390 Match	35.1	46.3	113499 Cartilage4 RA	1.6	10.6
Control Crohns-M
112726 Crohns-M	36.9	26.2	113500 Bone4 RA	11.9	11.7
112731 Match	17.6	11.1	113501 Synovium4	0.0	4.0
Control Crohns-M			RA
112380 Ulcer	19.9	24.0	113502 Syn Fluid	0.0	0.0
Col-F			Cells4 RA
112734 Match	14.8	20.9	113495 Cartilage3 RA	7.8	2.2
Control Ulcer
Col-F
112384 Ulcer	31.0	24.3	113496 Bone3 RA	20.6	9.0
Col-F
112737 Match	6.4	5.4	113497 Synovium3	2.6	0.0
Control Ulcer			RA
Col-F
112386 Ulcer	2.7	6.1	113498 Syn Fluid	5.4	10.5
Col-F			Cells3 RA
112738 Match	3.8	5.7	117106 Normal	5.9	15.4
Control Ulcer			Cartilage Rep20
Col-F
112381 Ulcer	0.0	0.0	113663 Bone3 Normal	0.0	0.0
Col-M
112735 Match	0.0	1.6	113664 Synovium3	0.0	0.0
Control Ulcer			Normal
Col-M
112382 Ulcer	12.9	8.4	113665 Syn Fluid	0.0	0.0
Col-M			Cells3 Normal
112394 Match	9.5	5.1	117107 Normal	3.4	0.0
Control Ulcer			Cartilage Rep22
Col-M
112383 Ulcer	9.4	17.2	113667 Bone4 Normal	13.4	9.5
Col-M
112736 Match	6.8	14.4	113668 Synovium4	11.2	4.1
Control Ulcer			Normal
Col-M
112423 Psoriasis-F	5.2	0.0	113669 Syn Fluid	9.0	22.8
			Cells4 Normal

[0946]

TABLE YD
General_screening_panel_v1.5
	Rel. Exp.		Rel. Exp.
	(%) Ag4870,		(%) Ag4870,
	Run		Run
Tissue Name	228903631	issue Name	228903631
Adipose	2.0	Renal ca. TK-10	31.4
Melanoma*	6.0	Bladder	26.6
Hs688(A).T
Melanoma*	4.2	Gastric ca. (liver met.)	7.4
Hs688(B).T		NCI-N87
Melanoma* M14	20.4	Gastric ca. KATO III	66.0
Melanoma*	0.9	Colon ca. SW-948	10.2
LOXIMVI
Melanoma*	7.8	Colon ca. SW480	16.8
SK-MEL-5
Squamous cell	0.5	Colon ca.* (SW480	63.7
carcinoma SCC-4		met) SW620
Testis Pool	1.3	Colon ca. HT29	17.1
Prostate ca.* (bone	24.7	Colon ca. HCT-116	4.4
met) PC-3
Prostate Pool	4.0	Colon ca. CaCo-2	36.6
Placenta	3.5	Colon cancer tissue	4.0
Uterus Pool	5.0	Colon ca. SW1116	5.7
Ovarian ca.	0.8	Colon ca. Colo-205	6.7
OVCAR-3
Ovarian ca.	1.2	Colon ca. SW-48	17.1
SK-OV-3
Ovarian ca.	0.5	Colon Pool	6.3
OVCAR-4
Ovarian ca.	17.1	Small Intestine Pool	5.0
OVCAR-5
Ovarian ca.	2.8	Stomach Pool	5.4
IGROV-1
Ovarian ca.	5.8	Bone Marrow Pool	2.3
OVCAR-8
Ovary	7.5	Fetal Heart	1.0
Breast ca. MCF-7	1.9	Heart Pool	3.3
Breast ca.	8.5	Lymph Node Pool	6.1
MDA-MB-231
Breast ca. BT 549	3.2	Fetal Skeletal Muscle	2.5
Breast ca. T47D	0.4	Skeletal Muscle Pool	9.0
Breast ca. MDA-N	15.6	Spleen Pool	1.8
Breast Pool	8.0	Thymus Pool	4.2
Trachea	7.3	CNS cancer (glio/	1.6
		astro) U87-MG
Lung	1.5	CNS cancer (glio/	0.9
		astro) U-118-MG
Fetal Lung	11.6	CNS cancer (neuro;	7.0
		met) SK-N-AS
Lung ca. NCI-N417	1.6	CNS cancer (astro)	3.1
		SF-539
Lung ca. LX-1	49.3	CNS cancer (astro)	14.9
		SNB-75
Lung ca. NCI-H146	2.4	CNS cancer (glio)	4.2
		SNB-19
Lung ca. SHP-77	3.5	CNS cancer (glio)	10.0
		SF-295
Lung ca. A549	1.6	Brain (Amygdala)	0.5
		Pool
Lung ca. NCI-H526	0.2	Brain (cerebellum)	1.1
Lung ca. NCI-H23	0.8	Brain (fetal)	1.0
Lung ca. NCI-H460	1.2	Brain (Hippocampus)	0.4
		Pool
Lung ca. HOP-62	5.3	Cerebral Cortex Pool	0.4
Lung ca. NCI-H522	6.5	Brain (Substantia	0.3
		nigra) Pool
Liver	21.6	Brain (Thalamus) Pool	0.6
Fetal Liver	100.0	Brain (whole)	3.0
Liver ca. HepG2	68.3	Spinal Cord Pool	0.4
Kidney Pool	9.3	Adrenal Gland	8.1
Fetal Kidney	1.8	Pituitary gland Pool	0.3
Renal ca. 786-0	0.5	Salivary Gland	9.3
Renal ca. A498	0.1	Thyroid (female)	1.7
Renal ca. ACHN	0.1	Pancreatic ca.	1.4
		CAPAN2
Renal ca. UO-31	2.3	Pancreas Pool	16.6

[0947]

TABLE YE
Oncology_cell_line_screening_panel_v3.1
	Rel. Exp.		Rel. Exp.
	(%) Ag4870,		(%) Ag4870,
	Run		Run
Tissue Name	225053014	Tissue Nme	225053014
Daoy	1.8	Ca Ski_Cervical	2.1
Medulloblastoma/		epidermoid carcinoma
Cerebellum		(metastasis)
TE671	2.6	ES-2_Ovarian clear	13.9
Medulloblastoma/		cell carcinoma
Cerebellum
D283 Med	11.2	Ramos/6h	94.6
Medulloblastoma/		stim_Stimulated with
Cerebellum		PMA/ionomycin 6h
PFSK-1 Primitive	9.8	Ramos/14h	27.7
Neuroectodermal/		stim_Stimulated with
Cerebellum		PMA/ionomycin 14h
XF-498_CNS	3.4	MEG-01_Chronic	14.5
		myelogenous leukemia
		(megokaryoblast)
SNG-78_CNS/	2.7	Raji_Burkitt's	11.7
glioma		lymphoma
SF-268_CNS/	0.9	Daudi_Burkitt's	27.5
glioblastoma		lymphoma
T98G_Glio-	5.7	U266_B-cell	0.9
blastoma		plasmacytoma/
		myeloma
SK-H-SH_Neuro-	3.5	CA46_Burkitt's	24.3
blastoma		lymphoma
(metastasis)
SF-295_CNS/	1.1	RL_non-Hodgkin's	32.8
glioblastoma		B-cell lymphoma
Cerebellum	0.3	JM1_pre-B-cell	3.5
		lymphoma/leukemia
Cerebellum	0.5	Jurkat_T cell	14.5
		leukemia
NCI-H292_Muco-	0.3	TF-1_Erythro-	37.6
epidermoid lung ca.		leukemia
DMS-114_Small	0.6	HUT 78_T-cell	3.8
cell lung cancer		lymphoma
DMS-79_Small cell	1.4	U937_Histiocytic	48.6
cancer/neuro-		lymphoma
endocrine
NCI-H146_Small	8.4	KU-812_Myelo-	100.0
cell lung cancer/		genous leukemia
neuro-endocrine
NCI-H526_Small	1.7	769-P_Clear cell renal	0.4
cell lung cancer/		ca.
neuro-endocrine
NCI-H417_Small	5.1	Caki-2_Clear cell	0.0
cell lung cancer/		renal ca.
neuro-endocrine
NCI-H82_Small	10.1	SW 839_Clear cell	1.1
cell lung cancer/		renal ca.
neuro-endocrine
NCI-	2.0	G401_Wilms' tumor	5.4
H157_Squamous
cell lung cancer
(metastasis)
NCI-H1155_Large	13.8	Hs766T_Pancreatic	10.5
cell lung cancer/		ca. (LN metastasis)
neuroendocrine
NCI-H1299_Large	1.2	CAPAN-1_Pancreatic	4.3
cell lung cancer/		adenocarcinoma (liver
neuroendocrine		metastasis)
NCI-H727_Lung	23.7	SU86.86_Pancreatic	6.5
carcinoid		carcinoma (liver
		metastasis)
NCI-UMC-	52.1	BxPC-3_Pancreatic	0.7
11_Lung		adenocarcinoma
carcinoid
LX-1_Small cell	13.1	HPAC_Pancreatic	1.5
lung cancer		adenocarcinoma
Colo-205_Colon	13.0	MIA	0.0
cancer		PaCa-2_Pancreatic ca.
KM12_Colon	2.5	CFPAC-1_Pancreatic	2.2
cancer		ductal adenocarcinoma
KM20L2_Colon	10.8	PANC-1_Pancreatic	0.3
cancer		epithelioid ductal ca.
NCI-H716_Colon	21.0	T24_Bladder ca.	6.5
cancer		(transitional cell)
SW-48_Colon	44.1	5637_Bladder ca.	1.7
adenocarcinoma
SW1116_Colon	8.7	HT-1197_Bladder ca.	0.2
adenocarcinoma
LS 174T_Colon	10.1	UM-UC-3_Bladder	0.4
adenocarcinoma		ca. (transitional cell)
SW-948_Colon	21.3	A204_Rhab-	0.3
adenocarcinoma		domyosarcoma
SW-480_Colon	12.9	HT-1080_Fibro-	9.3
adenocarcinoma		sarcoma
NCI-SNU-	12.3	MG-63_Osteosarcoma	1.7
5_Gastric ca.		(bone)
KATO III_Stomach	43.2	SK-LMS-1_Leiomyo-	6.6
		sarcoma (vulva)
NCI-SNU-	4.1	SJRH30_Rhabdomyo-	4.6
16_Gastric ca.		sarcoma (met to bone
		marrow)
NCI-SNU-	49.0	A431_Epidermoid ca.	0.4
1_Gastric ca.
RF-1_Gastric	6.6	WM266-4_Melanoma	4.1
adenocarcinoma
RF-48_Gastric	6.0	DU 145_Prostate	2.0
adenocarcinoma
MKN-45_Gastric	21.5	MDA-MB-468_Breast	0.8
ca.		adenocarcinoma
NCI-N87_Gastric	2.7	SSC-4_Tongue	0.3
ca.
OVCAR-5_Ovarian	0.7	SSC-9_Tongue	0.2
ca.
RL95-2_Uterine	0.3	SSC-15_Tongue	1.5
carcinoma
HelaS3_Cervical	0.1	CAL 27_Squamous	0.4
adenocarcinoma		cell ca. of tongue

[0948]

TABLE YF
Panel 4.1D
	Rel. Ep.		Rel. Exp.
	(%) Ag5280,		(%) Ag5280,
	Run		Run
Tissue Name	230500483	Tissue Name	230500483
Secondary Th1 act	28.5	HUVEC IL-1beta	12.6
Secondary Th2 act	26.1	HUVEC IFN gamma	2.2
Secondary Tr1 act	11.0	HUVEC TNF alpha +	6.1
		IFN gamma
Secondary Th1 rest	5.7	HUVEC TNF alpha +	12.7
		IL4
Secondary Th2 rest	2.7	HUVEC IL-11	6.0
Secondary Tr1 rest	4.0	Lung Microvascular	14.9
		EC none
Primary Th1 act	2.9	Lung Microvascular	5.3
		EC TNFalpha +
		IL-1beta
Primary Th2 act	25.2	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	8.2	Microsvasular Dermal	5.1
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	1.8	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	0.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	5.4	Coronery artery SMC	1.5
lymphocyte act		rest
CD45RO CD4	2.4	Coronery artery SMC	3.6
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	4.2	Astrocytes rest	0.0
Secondary CD8	8.3	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	3.0	KU-812 (Basophil)	100.0
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	90.8
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	7.6	Liver cirrhosis	9.8
LAK cells IL-2 +	0.0	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	3.8	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	3.3	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	8.4	NCI-H292 IL-13	2.9
ionomycin
NK Cells IL-2 rest	9.9	NCI-H292 IFN gamma	0.0
Two Way MLR 3	0.9	HPAEC none	4.8
day
Two Way MLR 5	3.8	HPAEC TNF alpha +	4.5
day		IL-1 beta
Two Way MLR 7	2.1	Lung fibroblast	27.4
day		none
PBMC rest	2.6	Lung fibroblast TNF	7.6
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	1.0
PBMC PHA-L	7.1	Lung fibroblast IL-9	7.1
Ramos (B cell) none	21.8	Lung fibroblast IL-13	7.2
Ramos (B cell)	85.9	Lung fibroblast IFN	14.7
ionomycin		gamma
B lymphocytes	8.3	Dermal fibroblast	3.1
PWM		CCD1070 rest
B lymphocytes	28.5	Dermal fibroblast	19.5
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	20.2	Dermal fibroblast	9.9
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN	9.4
PMA/ionomycin		gamma
Dendritic cells none	3.5	Dermal fibroblast IL-4	13.8
Dendritic cells LPS	0.0	Dermal Fibroblasts	15.3
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	1.5
Monocytes LPS	0.0	Colon	0.0
Macrophages rest	0.0	Lung	2.6
Macrophages LPS	0.0	Thymus	0.0
HUVEC none	9.9	Kidney	2.7
HUVEC starved	7.0

[0949] AI_comprehensive panel_v1.0 Summary: Ag5280 Two experiments with the same probe and primer produce results that are in excellent agreement. Highest expression is in a sample derived from normal tissue adjacent to psoriasis (CTs=33). Low levels of expression are also seen in an osteoarthritic bone sample.

[0950] CNS_neurodegeneration_v1.0 Summary: Ag5280 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0951] General_screening_panel_v1.5 Summary: Ag4870 Highest expression of this gene, a PB39 homolog, is seen in the fetal liver (CT=25.6). Significant levels of expression are also seen in cell lines derived from lung, gastric, colon, renal, liver, ovarian, breast, prostate, melanoma and brain cancers. This expression in proliferetive samples suggests a role for this gene in cell proliferation and growth. This is consistent with data that shows to be upregulated in prostate cancer and tissues undergoing growth and differentiation. Thus, expression of this gene could be used to differentiate between these samples and other samples on this panel and as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of these cancers.

REFERENCES

[0952] Cole K A, Chuaqui R F, Katz K, Pack S, Zhuang Z, Cole C E, Lyne J C, Linehan W M, Liotta L A, Emmert-Buck M R. cDNA sequencing and analysis of POV1 (PB39): a novel gene up-regulated in prostate cancer. Genomics Jul. 15, 1998;51(2):282-7

[0953] Stuart R O, Pavlova A, Beier D, Li Z, Krijanovski Y, Nigam S K. EEG1, a putative transporter expressed during epithelial organogenesis: comparison with embryonic transporter expression during nephrogenesis. Am J Physiol Renal Physiol December 2001;281(6):F1148-56

[0954] Oncology_cell_line_screening_panel_v3.1 Summary: Ag4870 Highest expression of this gene is seen in a myelogenous leukemia cell line (CT=27.2). Moderate levels of expression are seen in other cell line samples on this panel, including samples from colon, gastric, and lung cancers, leukemias, and lymphomas. Please see Panel 1.5 for discussion of utility of this gene in cancer.

[0955] Panel 4.1D Summary: Ag5280 Prominent expression is seen in two samples derived from the basophil cell line KU-812 (CTs=32.3). Basophils release histamines and other biological modifiers in reponse to allergens and play all important role in the pathology of asthma and hypersensitivity reactions. Therefore, therapeutics designed against the putative protein encoded by this gene may reduce or inhibit inflammation by blocking basophil function in these diseases. In addition, these cells are a reasonable model for the inflammatory cells that take part in various inflammatory lung and bowel diseases, such as asthma, Crohn's disease, and ulcerative colitis. Therefore, expression of this gene could be used to differentiate between these samples and other samples on this panel adn as a marker of these cells. Furthermore, therapeutics that modulate the function of this gene product may reduce or eliminate the symptoms of patients suffering from asthma, Crohn's disease, and ulcerative colitis.

[0956] Z. CG149777-02: Cystatin D Precursor

[0957] Expression of full-length physical clone CG149777-02 was assessed using the primer-probe set Ag6903, described in Table ZA.

TABLE ZA
Probe Name Ag6903
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-ccacagacctcaatgacaagag-3′	22	110	320
Probe	TET-5′-cctggactttgccttcaatgaccag-3′-TAMRA	25	144	321
Reverse	5′-gaactcttcctctttcagttttgg-3′	24	169	322

[0958] General_screening_panel_v1.6 Summary: Ag6903 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0959] AA. CG150005-01: Glutamate Binding Protien

[0960] Expression of gene CG150005-01 was assessed using the primer-probe set Ag5633, described in Table AAA.

TABLE AAA
Probe Name Ag5633
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-ccacctcctgtctactcattgt-3′	22	1341	323
Probe	TET-5′-catgagccctgtctgccagcttc-3′-TAMRA	23	1365	324
Reverse	5′-gctcaatccttggacctgtt-3′	20	1412	325

[0961] AI_comprehensive panel_v1.0 Summary: Ag5633 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0962] CNS_neurodegeneration_v1.0 Summary: Ag5633 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0963] General_screening_panel_v1.5 Summary: Ag5633 The amp plot indicates that there were experimental difficulties with this run; therefore, no conclusions can be drawn from this data. (Data not shown)

[0964] Panel 4.1D Summary: Ag5633 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0965] Panel 5D Summary: Ag5633 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0966] Panel CNS—1.1 Summary: Ag5633 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0967] AB. CG150189-01: Acetyl LDL Receptor

[0968] Expression of gene CG150189-01 was assessed using the primer-probe sets Ag3183 and Ag372, described in Tables ABA and ABB. Results of the RTQ-PCR runs are shown in Tables ABC, ABD, ABE, ABF, ABG and ABH.

TABLE ABA
Probe Name Ag3183
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-aaggggacgagtgtgggatt-3′	20	212	326
Probe	TET-5′-tggcaccgaagtagccgtggcg-3′-TAMRA	22	301	327
Reverse	5′-gcgggcacttggtgtcgca-3′	19	325	328

[0969]

TABLE ABB
Probe Name Ag372
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-tgtaaccatgtcaccggcaa-3′	20	574	329
Probe	TET-5′-cgatccagcccgcgttgca3-′-TAMRA	19	604	330
Reverse	5′-ctcgccgtaagtgccattg-3′	19	648	331

[0970]

TABLE ABC
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag3183,		(%) Ag3183,
	Run		Run
Tissue Name	216861424	issue Name	216861424
Adipose	5.2	Renal ca. TK-10	2.2
Melanoma*	82.9	Bladder	10.5
Hs688(A).T
Melanoma*	100.0	Gastric ca. (liver met.)	2.0
Hs688(B).T		NCI-N87
Melanoma* M14	67.8	Gastric ca. KATO III	1.7
Melanoma*	4.1	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	9.8	Colon ca. SW480	0.8
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.5
carcinoma SCC-4		met) SW620
Testis Pool	2.7	Colon ca. HT29	0.0
Prostate ca.* (bone	3.7	Colon ca. HCT-116	0.5
met) PC-3
Prostate Pool	3.0	Colon ca. CaCo-2	0.0
Placenta	6.4	Colon cancer tissue	19.8
Uterus Pool	5.0	Colon ca. SW1116	0.8
Ovarian ca.	3.6	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	5.3	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	6.7	Colon Pool	9.7
OVCAR-4
Ovarian ca.	4.9	Small Intestine Pool	3.7
OVCAR-5
Ovarian ca.	37.1	Stomach Pool	8.5
IGROV-1
Ovarian ca.	84.1	Bone Marrow Pool	1.3
OVCAR-8
Ovary	18.3	Fetal Heart	2.4
Breast ca. MCF-7	0.0	Heart Pool	5.1
Breast ca.	8.2	Lymph Node Pool	12.1
MDA-MB-231
Breast ca. BT 549	14.5	Fetal Skeletal Muscle	2.4
Breast ca. T47D	15.5	Skeletal Muscle Pool	2.1
Breast ca. MDA-N	15.6	Spleen Pool	5.4
Breast Pool	10.7	Thymus Pool	12.2
Trachea	8.2	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	0.8	CNS cancer (glio/	21.8
		astro) U-118-MG
Fetal Lung	18.2	CNS cancer (neuro;	34.2
		met) SK-N-AS
Lung ca. NCI-N417	1.0	CNS cancer (astro)	90.8
		SF-539
Lung ca. LX-1	0.9	CNS cancer (astro)	71.7
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	31.2
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	82.9
		SF-295
Lung ca. A549	1.4	Brain (Amygdala)	3.5
		Pool
Lung ca. NCI-H526	6.3	Brain (cerebellum)	0.0
Lung ca. NCI-H23	0.0	Brain (fetal)	2.0
Lung ca. NCI-H460	0.5	Brain (Hippocampus)	1.4
		Pool
Lung ca. HOP-62	7.2	Cerebral Cortex Pool	1.0
Lung ca. NCI-H522	7.3	Brain (Substantia	6.2
		nigra) Pool
Liver	2.1	Brain (Thalamus) Pool	1.1
Fetal Liver	2.1	Brain (whole)	1.7
Liver ca. HepG2	9.9	Spinal Cord Pool	6.8
Kidney Pool	24.5	Adrenal Gland	1.3
Fetal Kidney	18.8	Pituitary gland Pool	1.1
Renal ca. 786-0	1.8	Salivary Gland	0.0
Renal ca. A498	0.0	Thyroid (female)	4.2
Renal ca. ACHN	7.3	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	7.3	Pancreas Pool	15.6

[0971]

TABLE ABD
Panel 4.1D
	Rel. Ex.		Rel. Exp.
	(%)		(%)
	Ag372,		Ag372,
	Run		Run
Tissue Name	98747566	Tissue Name	98747566
Endothelial cells	13.1	Renal ca. 786-0	14.3
Endothelial cells	6.1	Renal ca. A498	4.4
(treated)
Pancreas	9.7	Renal ca. RXF 393	14.3
Pancreatic ca.	0.0	Renal ca. ACHN	15.7
CAPAN 2
Adrenal gland	27.0	Renal ca. UO-31	8.5
Thyroid	31.0	Renal ca. TK-10	0.4
Salivary gland	9.7	Liver	26.4
Pituitary gland	41.2	Liver (fetal)	11.8
Brain (fetal)	13.0	Liver ca. (hepatoblast)	25.3
		HepG2
Brain (whole)	11.0	Lung	41.8
Brain (amygdala)	15.1	Lung (fetal)	32.5
Brain (cerebellum)	9.7	Lung ca. (small cell)	2.6
		LX-1
Brain (hippocampus)	12.9	Lung ca. (small cell)	8.2
		NCI-H69
Brain (substantia	10.2	Lung ca. (s. cell var)	2.9
nigra)		SHP-77
Brain (thalamus)	11.8	Lung ca. (large cell)	22.5
		NCI-H460
Brain (hypothalamus)	42.9	Lung ca. (non-sm. cell)	7.4
		A549
Spinal cord	15.7	Lung ca. (non-s. cell)	4.3
		NCI-H23
glio/astro U87-MG	1.0	Lung ca. (non-s. cell)	29.5
		HOP-62
glio/astro U-118-MG	12.2	Lung ca. (non-s. cl)	44.8
		NCI-H522
astrocytoma SW1783	25.9	Lung ca. (squam.) SW	10.3
		900
neuro*; met SK-N-AS	66.4	Lung ca. (squam.)	4.7
		NCI-H596
astrocytoma SF-539	56.3	Mammary gland	41.5
astrocytoma SNB-75	23.3	Breast ca.* (pl. ef)	3.5
		MCF-7
glioma SNB-19	23.5	Breast ca.* (pl. ef)	6.1
		MDA-MB-231
glioma U251	18.2	Breast ca.* (pl. ef)	14.6
glioma SF-295	48.3	Breast ca. BT-549	4.0
		T47D
Heart	32.1	Breast ca. MDA-N	32.8
Skeletal muscle	16.0	Ovary	67.8
Bone marrow	7.0	Ovarian ca. OVCAR-3	13.3
Thymus	11.3	Ovarian ca. OVCAR-4	9.4
Spleen	25.2	Ovarian ca. OVCAR-5	4.0
Lymph node	15.4	Ovarian ca. OVCAR-8	100.0
Colon (ascending)	5.9	Ovarian ca. IGROV-1	21.9
Stomach	10.2	Ovarian ca. (ascites)	6.3
		SK-OV-3
Small intestine	62.9	Uterus	35.8
Colon ca. SW480	0.0	Placenta	33.9
Colon ca.* SW620	2.1	Prostate	31.4
(SW480 met)
Colon ca. HT29	0.2	Prostate ca.* (bone met)	23.7
		PC-3
Colon ca. HCT-116	2.4	Testis	16.5
Colon ca. CaCo-2	0.3	Melanoma Hs688(A).T	44.4
Colon ca. HCT-15	5.9	Melanoma* (met)	55.9
		Hs688(B).T
Colon ca. HCC-2998	12.1	Melanoma UACC-62	70.2
Gastric ca.* (liver met)	6.4	Melanoma M14	45.1
NCI-N87
Bladder	51.4	Melanoma LOX IMVI	6.5
Trachea	21.0	Melanoma* (met)	27.2
		SK-MEL-5
Kidney	32.8	Melanoma SK-MEL-28	0.0
Kidney (fetal)	67.8

[0972]

TABLE ABE
Panel 1.3D
	Rel. Exp.		Rel. Exp.
	(% Ag3183,		(%) Ag3183,
	Run		Run
Tissue Name	167927219	Tissue Name	167927219
Liver adenocarcinoma	5.5	Kidney (fetal)	100.0
Pancreas	0.0	Renal ca. 786-0	5.1
Pancreatic ca.	0.0	Renal ca. A498	16.6
CAPAN 2
Adrenal gland	4.7	Renal ca. RXF 393	9.9
Thyroid	2.8	Renal ca. ACHN	17.8
Salivary gland	6.1	Renal ca. UO-31	1.8
Pituitary gland	1.6	Renal ca. TK-10	0.0
Brain (fetal)	0.9	Liver	0.0
Brain (whole)	0.0	Liver (fetal)	9.9
Brain (amygdala)	1.7	Liver ca.	7.3
		(hepatoblast) HepG2
Brain (cerebellum)	0.0	Lung	7.4
Brain (hippocampus)	0.0	Lung (fetal)	11.2
Brain (substantia	1.1	Lung ca. (small cell)	1.7
nigra)		LX-1
Brain (thalamus)	2.5	Lung ca. (small cell)	0.0
		NCI-H69
Cerebral Cortex	0.0	Lung ca. (s. cell	5.1
		var) SHP-77
Spinal cord	3.5	Lung ca. (large cell)	2.9
		NCI-H460
glio/astro U87-MG	0.0	Lung ca. (non-sm.	0.0
		cell) A549
glio/astro U-118-MG	7.7	Lung ca. (non-s.	0.0
		cell) NCI-H23
astrocytoma SW1783	14.4	Lung ca. (non-s.	6.0
		cell) HOP-62
neuro*; met SK-N-AS	7.5	Lung ca. (non-s. cl)	5.2
		NCI-H522
astrocytoma SF-539	52.1	Lung ca. (squam.)	5.1
		SW 900
astrocytoma SNB-75	49.7	Lung ca. (squam.)	1.0
		NCI-H596
glioma SNB-19	3.1	Mammary gland	10.2
glioma U251	13.9	Breast ca.* (pl. ef)	0.0
		MCF-7
glioma SF-295	25.9	Breast ca.* (pl. ef)	3.7
		MDA-MB-231
Heart (fetal)	14.4	Breast ca.* (pl. ef)	11.8
		T47D
Heart	7.0	Breast ca. BT-549	1.5
Skeletal muscle (fetal)	10.7	Breast ca. MDA-N	5.9
Skeletal muscle	0.0	Ovary	13.0
Bone marrow	1.7	Ovarian ca.	1.5
		OVCAR-3
Thymus	3.3	Ovarian ca.	1.8
		OVCAR-4
Spleen	6.9	Ovarian ca.	0.6
		OVCAR-5
Lymph node	9.2	Ovarian ca.	5.3
		OVCAR-8
Colorectal	1.6	Ovarian ca.	0.0
		IGROV-1
Stomach	4.7	Ovarian ca.*	2.2
		(ascites) SK-OV-3
Small intestine	11.7	Uterus	27.9
Colon ca. SW480	0.0	Placenta	0.0
Colon ca.* SW620	0.0	Prostate	0.8
(SW480 met)
Colon ca. HT29	0.0	Prostate ca.* (bone	4.6
		met) PC-3
Colon ca. HCT-116	0.0	Testis	1.7
Colon ca. CaCo-2	0.0	Melanoma	50.3
		Hs688(A).T
Colon ca. tissue	15.2	Melanoma* (met)	84.7
(ODO3866)		Hs688(B).T
Colon ca. HCC-2998	0.0	Melanoma	42.3
		UACC-62
Gastric ca.* (liver met)	0.9	Melanoma M14	13.9
NCI-N87
Bladder	2.0	Melanoma LOX	10.3
		IMVI
Trachea	5.8	Melanoma* (met)	0.0
		SK-MEL-5
Kidney	22.8	Adipose	9.0

[0973]

TABLE ABF
Panel 4D
	Rel.		Rel.
	Ep. (%)		Exp. (%)
	Ag83183,		Ag3183,
	Run		Run
Tissue Name	164317572	Tissue Name	164317572
Secondary Th1 act	0.0	HUVEC IL-1 beta	5.7
Secondary Th2 act	0.0	HUVEC IFN gamma	18.4
Secondary Tr1 act	0.0	HUVEC TNF alpha + IFN gamma	9.6
Secondary Th1 act	0.0	HUVEC TNF alpha + IL4	11.2
Secondary Th2 rest	0.0	HUVEC IL-11	19.3
Secondary Tr1 rest	2.5	Lung Microvascular EC none	21.6
Primary Th1 act	0.0	Lung Microvascular EC TNF-	32.1
		alpha + IL-1 beta
Primary Th2 act	0.0	Microvascular Dermal EC none	10.7
Primary Tr1 act	0.0	Microvascular Dermal EC	5.0
		THFalpha + IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium TNFalpha +	11.7
		IL1beta
Primary Th2 rest	2.3	Small airway epithelium none	5.6
Primary Tr1 rest	0.7	Small airway epithelium TNF-	4.9
		alpha + IL-1beta
CD45RA CD4 lymphocyte act	29.9	Coronery artery SMC rest	47.0
CD45RO CD4 lymphocyte act	0.0	Coronery artery SMC TNFalpha +	45.4
		IL-1beta
CD8 lymphocyte act	0.0	Astrocyte rest	82.4
Secondary CDS lymphocyte rest	0.0	Astrocytes TNFalpha + IL-1beta	75.3
Secondary CD8 lymphocyte act	0.0	KU-812 (Basophil) rest	0.0
CD4 lymphocyte none	0.4	KU-812 (Basophil)	0.0
		PMA/ionomycin
2ry Th1/Th2/Tr1_anti-CD95	2.1	CCD1106 (Keratinocytes) none	0.0
CH11
LAK cells rest	0.0	CCD1106 (Keratinocytes)	0.0
		TNFalpha + IL-1beta
LAK cells IL-2	0.0	Liver cirrhosis	5.6
LAK cell IL-2 + IL-12	0.0	Lupus kidney	9.3
LAK cells IL-2 + IFN gamma	0.0	NCI-H292 none	2.5
LAK cells IL-2 + IL-18	0.0	NCI-H292 IL-4	0.0
LAK cells PMA/ionomycin	0.0	NCI-H292 IL-9	0.0
NK Cells IL-2 rest	0.0	NCI-H292 IL-13	3.8
Two Way MLR 3 day	0.0	NCI-H292 IFN gamma	0.0
Two Way MLR 5 day	0.0	HPAEC none	32.1
Two Way MLR 7 day	0.0	HPAEC TNF alpha + IL-1 beta	22.4
PBMC rest	0.0	Lung fibroblast none	44.4
PBMC PWM	1.8	Lung fibroblast TNF alpha + IL-1	28.3
		beta
PBMC PHA-L	0.0	Lung fibroblast IL-4	62.9
Ramos (B cell) none	0.0	Lung fibroblast IL-9	100.0
Ramos (B cell) ionomycin	0.0	Lung fibroblast IL-13	73.7
B lymphocytes PWM	0.0	Lung fibroblast IFN gamma	57.0
B lymphocytes CD40L and IL-4	0.0	Dermal fibroblast CCD1070 rest	91.4
EOL-1 dbcAMP	0.0	Dermal fibroblast CCD1070 TNF	31.2
		alpha
EOL-1 dbcAMP	1.2	Dermal fibroblast CCD1070 IL-1	69.7
PMA/ionomycin		beta
Dendritic cells none	1.8	Dermal fibroblast IFN gamma	18.3
Dendritic cells LPS	0.0	Dermal fibroblast IL-4	22.4
Dendritic cells anti-CD40	0.4	IBD Colitis 2	0.0
Monocytes rest	2.8	IBD Crohn's	0.8
Monocytes LPS	0.0	Colon	8.9
Macrophages rest	0.0	Lung	18.6
Macrophages LPS	0.0	Thymus	9.5
HUVEC none	8.4	Kidney	3.0
HUVEC starved	29.9

[0974]

TABLE ABG
Panel 5D
	Rel. Exp.		Rel. Exp.
	(%) Ag313,		(%) Ag3183,
	Run		Run
Tissue Name	172171149	Tissue Name	172171149
97457_Patient-02go_adipose	11.3	94709_Donor 2 AM—A_adipose	31.6
97476_Patient-07sk_skeletal muscle	21.3	94710_Donor 2 AM—B_adipose	47.0
97477_Patient-07ut_uterus	3.3	94711_Donor 2 AM—C_adipose	36.3
97478_Patient-07pl_placenta	0.0	94712_Donor 2 AD—A_adipose	33.0
97481_Patient-08sk_skeletal muscle	9.0	94713_Donor 2 AD—B_adipose	27.0
97482_Patient-08ut_uterus	0.0	94714_Donor 2 AD—C_adipose	13.5
97483_Patient-08pl_placenta	5.4	94742_Donor 3 U—A_Mesenchymal Stem Cells	27.9
97486_Patient-09sk_skeletal muscle	2.4	94743_Donor 3 U—B_Mesenchymal Stem Cells	100.0
97487_Patient-09ut_uterus	11.3	94730_Donor 3 AM—A_adipose	69.3
97488_Patient-09pl_placenta	0.0	94731_Donor 3 AM—B_adipose	58.6
97492_Patient-10ut_uterus	3.4	94732_Donor 3 AM—C_adipose	11.2
97493_Patient-10pl_placenta	8.4	94733_Donor 3 AD—A_adipose	47.0
97495_Patient-11go_adipose	8.1	94734_Donor 3 AD—B_adipose	31.6
97496_Patient-11sk_skeletal muscle	0.0	94735_Donor 3 AD—C_adipose	44.8
97497_Patient-11ut_uterus	17.4	77138_Liver_HepG2untreated	9.1
97498_Patient-11pl_placenta	0.0	73556_Heart_Cardiac stromal cells (primary)	0.0
97500_Patient-12go_adipose	15.7	81735_Small Intestine	6.3
97501_Patient-12sk_skeletal muscle	0.0	72409_Kidney_Proximal Convoluted Tubule	0.0
97502_Patient-12ut_uterus	13.8	82685_Small intestine_Duodenum	0.0
97503_Patient-12pl_placenta	4.8	90650_Adrenal_Adrenocortical adenoma	15.4
94721_Donor 2 U—A_Mesenchymal Stem Cells	31.2	72410_Kidney_HRCE	14.2
94722_Donor 2 U—B_Mesenchymal Stem Cells	33.7	72411_Kidney_HRE	7.0
94723_Donor 2 U—C_Mesenchymal Stem Cells	20.7	73139_Uterus_Uterine smooth muscle cells	11.3

[0975]

TABLE ABH
general oncology screening panel_v_2.4
	Rel. Exp.		Rel. Exp.
	(%) Ag3183,		(%) Ag3183,
	Run		Run
Tissue Name	259733268	Tissue Name	259733268
Colon cancer 1	24.7	Bladder NAT 2	0.0
Colon NAT 1	19.2	Bladder NAT 3	0.0
Colon cancer 2	6.6	Bladder NAT 4	15.9
Colon NAT 2	0.0	Prostate	3.2
		adenocarcinoma 1
Colon cancer 3	23.8	Prostate	0.0
		adenocarcinoma 2
Colon NAT 3	10.4	Prostate	4.5
		adenocarcinoma 3
Colon malignant	3.1	Prostate	16.7
cancer 4		adenocarcinoma 4
Colon NAT 4	0.0	Prostate NAT 5	14.7
Lung cancer 1	21.5	Prostate	0.0
		adenocarcinoma 6
Lung NAT 1	0.0	Prostate	7.6
		adenocarcinoma 7
Lung cancer 2	100.0	Prostate	0.0
		adenocarcinoma 8
Lung NAT 2	0.0	Prostate	5.3
		adenocarcinoma 9
Squamous cell	39.2	Prostate NAT 10	0.0
carcinoma 3
Lung NAT 3	6.3	Kidney cancer 1	9.8
Metastatic melanoma 1	11.1	Kidney NAT 1	6.1
Melanoma 2	5.8	Kidney cancer 2	15.0
Melanoma 3	0.0	Kidney NAT 2	18.9
Metastatic melanoma 4	61.1	Kidney cancer 3	11.1
Metastatic melanoma 5	49.7	Kidney NAT 3	7.5
Bladder cancer 1	0.0	Kidney cancer 4	6.9
Bladder NAT 1	0.0	Kidney NAT 4	8.6
Bladder cancer 2	4.3

[0976] General_screening_panel_v1.4 Summary: Ag3183 Highest expression of this gene is seen in a melanoma cell line (CT=31.5). Prominent expression is seen in a cluster of cell lines derived ovarian, melanoma, and brain cells. Thus, expression of this gene could be used to differentiate between these samples and other samples on this panel and as a marker of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of ovarian, melanoma and brain cancers.

[0977] Panel 1 Summary: Ag4337 Highest expression of this gene is detected in a ovarian cancer OVCAR-8 cell line (CT=26.5). High to Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from liver, gastric, colon, lung, renal, breast, ovarian, melanoma and brain cancers. Therefore, therapeutic modulation of this gene may be useful in the treatment of these cancers.

[0978] Among tissues with metabolic or endocrine function, this gene is expressed at high to moderate levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, and adult and fetal liver. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[0979] In addition, this gene is expressed at moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer's disease, Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[0980] Panel 1.3D Summary: Ag3183 Highest expression of this gene is seen in fetal kidney (CT=32.2). In addition, prominent expression is seen in clusters of cell lines derived from melanoma, and brain cancer cell lines. Please see Panel 1 for discussion of utility of this gene in cancer. In another experiment (run 167966980) the amp plot indicates that there were experimental difficulties with this run; therefore, no conclusions can be drawn from this data (Data not shown).

[0981] Panel 4D Summary: Ag3183 Highest expression of this gene is detected in activated lung fibroblast (CT=31.9). This gene is also expressed in resting and treated fibroblasts, endothelium, and epithelium and activated naive T cells (CD4+ CD45RA cells). Interestingly, this gene is up-regulated activated in naive T cells (CD4+ CD45RA cells; CT=33.6) as compared to resting CD4 cells (CT=40). Furthermore, in activated memory T cells (CD45RO CD4 lymphocyte) or CD4 Th1 or Th2 cells (CTs>37), the expression of this gene is strongly down regulated suggesting a role for this putative protein in differentiation or activation of naive T cells. Activated T cells then initiate the inflammatory process by secreting cytokines and chemokines, activating B cells and inducing B cell antibody production, and inducing the extravasation of leukocytes including other T cells into inflammatory sites. Therefore, therapeutics that inhibit the action of this gene product may block T cell activation in response to tissue transplant and reduce or block rejection. These therapeutic drugs may also reduce or prevent inflammation in asthma/allergy, psoriasis, arthritis and diabetes in which activated T cells play a pivotal role. Expression of this gene may also serve as a diagnostic or experimental tools to identify naive activated T cells and discriminate them from more differentiated activated T cells (memory T cells).

REFERENCES

[0982] Study of LDL and acetylated LDL endocytosis by mononuclear cells in 1HV infection. Juompan L, Puel J, Fournie G J, Benoist H Biochim Biophys Acta Aug. 15, 1995;1272(1):21-8.

[0983] Panel 5D Summary: Ag3182 Highest expression of this gene is seen in a sample of mesenchymal stem cells (CT=34.2). Low but significant levels of expression are also seen in adipose tissue, in agreement with expression in Panel 1. Please see Panel 1 for discussion of this gene in metabolic disease.

[0984] general oncology screening panel_V—2.4 Summary: Ag3183 Expression is seen in a lung cancer sample (CT=34.9). Thus, expression of this gene could be used to differentiate between this sample and other samples on this panel and as a marker to detect the presence of lung cancer. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of lung cancer.

[0985] AC. CG150267-01: Type Ia Membrane Protein

[0986] Expression of gene CG150267-01 was assessed using the primer-probe set Ag7560, described in Table ACA. Results of the RTQ-PCR runs are shown in Tables ACB and ACC.

TABLE ACA
Probe Name Ag7560
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-gcacctgcttcggatatttt-3′	20	560	332
Probe	TET-5′-tttccctctgtacttatgccgccagt-3′-TAMRA	26	586	333
Reverse	5′-ggagccggttcaaatcatac-3′	20	617	334

[0987]

TABLE ACB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7560,		(%) Ag7560,
	Run		Run
Tissue Name	308750602	issue Name	308750602
AD 1 Hippo	8.8	Control (Path) 3	6.7
		Temporal Ctx
AD 2 Hippo	12.3	Control (Path) 4	26.4
		Temporal Ctx
AD 3 Hippo	10.7	AD 1 Occipital Ctx	22.5
AD 4 Hippo	8.2	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	51.4	AD 3 Occipital Ctx	8.1
AD 6 Hippo	24.7	AD 4 Occipital Ctx	26.4
Control 2 Hippo	25.0	AD 5 Occipital Ctx	29.5
Control 4 Hippo	9.8	AD 6 Occipital Ctx	13.4
Control (Path) 3	1.1	Control 1 Occipital	5.3
Hippo		Ctx
AD 1 Temporal Ctx	21.2	Control 2 Occipital	51.4
		Ctx
AD 2 Temporal Ctx	23.2	Control 3 Occipital	4.5
		Ctx
AD 3 Temporal Ctx	6.1	Control 4 Occipital	7.9
		Ctx
AD 4 Temporal Ctx	19.2	Control (Path) 1	62.4
		Occipital Ctx
AD 5 Inf Temporal	100.0	Control (Path) 2	9.7
Ctx		Occipital Ctx
AD 5 Sup Temporal	34.2	Control (Path) 3	1.1
Ctx		Occipital Ctx
AD 6 Inf Temporal	18.6	Control (Path) 4	11.1
Ctx		Occipital Ctx
AD 6 Sup Temporal	19.2	Control 1 Parietal Ctx	5.9
Ctx
Control 1 Temporal	3.2	Control 2 Parietal Ctx	19.5
Ctx
Control 2 Temporal	19.1	Control 3 Parietal Ctx	17.6
Ctx
Control 3 Temporal	9.5	Control (Path) 1	71.2
Ctx		Parietal Ctx
Control 3 Temporal	5.5	Control (Path) 2	17.0
Ctx		Parietal Ctx
Control (Path) 1	48.3	Control (Path) 3	5.0
Temporal Ctx		Parietal Ctx
Control (Path) 2	17.6	Control (Path) 4	22.2
Temporal Ctx		Parietal Ctx

[0988]

TABLE ACC
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(%) Ag7560,		(%) Ag7560,
	Run		Run
Tissue Name	308748085	Tissue Name	308748085
Secondary Th1 act	0.0	HUVEC IL-1beta	3.2
Secondary Th2 act	0.0	HUVEC IFN gamma	5.2
Secondary Tr1 act	0.0	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	6.5
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	0.0
Secondary Tr1 rest	0.0	Lung Microvascular	3.8
		EC none
Primary Th1 act	0.0	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.0	Microvascular Dermal	20.0
		EC none
Primary Tr1 act	0.0	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	3.5
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	0.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.0	Coronery artery SMC	4.6
lymphocyte act		rest
CD45RO CD4	0.0	Coronery artery SMC	2.9
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.0	Astrocytes rest	75.3
Secondary CD8	0.0	Astrocytes	23.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.0	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	5.6
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	6.1
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.0	Liver cirrhosis	1.8
LAK cells IL-2 +	0.0	NCI-H292 none	10.6
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	3.8
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	6.1
IL-18
LAK cells PMA/	0.0	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	0.0
Two Way MLR 3	0.0	HPAEC none	4.2
day
Two Way MLR 5	0.0	HPAEC TNF alpha +	0.0
day		IL-1 beta
Two Way MLR 7	4.9	Lung fibroblast	3.0
day		none
PBMC rest	0.0	Lung fibroblast TNF	10.3
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.0	Lung fibroblast IL-9	16.3
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	0.0	Lung fibroblast IFN	3.5
ionomycin		gamma
B lymphocytes	0.0	Dermal fibroblast	0.0
PWM		CCD1070 rest
B lymphocytes	0.0	Dermal fibroblast	4.2
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	11.2	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	6.2	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	3.8	Dermal fibroblast IL-4	4.2
Dendritic cells LPS	0.0	Dermal Fibroblasts	0.0
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.0	Colon	4.0
Macrophages rest	6.5	Lung	3.8
Macrophages LPS	0.0	Thymus	10.5
HUVEC none	0.0	Kidney	100.0
HUVEC starved	7.5

[0989] CNS_neurodegeneration_v1.0 Summary: Ag7560 No differential expression of this gene was detected between Alzheimer's diseased postmortem brains and those of non-demented controls in this experiment. However, this panel confirms the expression of this gene at low levels in the brains of an independent group of individuals. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[0990] Panel 4.1D Summary: Ag7560 Highest expression of this gene is detected in kidney (CT=33.8). Therefore, expression of this gene could be used to differentiate the kidney-derived sample from other samples on this panel and as a marker of kidney tissue. In addition, therapeutic targeting of the expression or function of this gene may modulate kidney function and be important in the treatment of inflammatory or autoimmune diseases that affect the kidney, including lupus and glomerulonephritis.

[0991] Low but significant levels of expression of this gene is also seen in resting astrocytes. Therefore, therapeutic modulation of this gene or the encoded protein could be important in the treatment of multiple sclerosis or other inflammatory diseases of the CNS.

[0992] AD. CG150362-01: Otoferlin

[0993] Expression of gene CG150362-01 was assessed using the primer-probe set Ag5684, described in Table ADA. Results of the RTQ-PCR runs are shown in Table ADB.

TABLE ADA
Probe Name Ag5684
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-cctggtatttgagcagttgatc-3′	22	3187	335
Probe	TET 5′-atcactaatggaggctcctcctgcag-3′-TAMRA	26	3230	336
Reverse	5′-gccaaacttattgtggtcaaat-3′	22	3265	337

[0994]

TABLE ADB
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(%) Ag5684,		(%) Ag5684,
	Run		Run
Tissue Name	246498693	Tissue Name	246498693
Secondary Th1 act	0.0	HUVEC IL-1beta	1.9
Secondary Th2 act	0.0	HUVEC IFN gamma	15.0
Secondary Tr1 act	0.0	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	2.6
Secondary Tr1 rest	0.0	Lung Microvascular	17.3
		EC none
Primary Th1 act	0.0	Lung Microvascular	1.1
		EC TNFalpha +
		IL-1beta
Primary Th2 act	1.9	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	0.0	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	6.4
		TNFalpha + IL-1beta
Primary Th2 rest	1.7	Small airway	1.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	5.3
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	2.0	Coronery artery SMC	13.7
lymphocyte act		rest
CD45RO CD4	1.6	Coronery artery SMC	25.3
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	2.3	Astrocytes rest	0.0
Secondary CD8	0.0	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.6	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	2.5	KU-812 (Basophil)	0.0
none		PMA/ionomycin
2ry Th1/Th2/	0.4	CCD1106	7.2
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	5.7
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.0	Liver cirrhosis	6.4
LAK cells IL-2 +	0.0	NCI-H292 none	66.0
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	57.8
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	92.7
IL-18
LAK cells PMA/	1.7	NCI-H292 IL-13	100.0
ionomycin
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	51.8
Two Way MLR 3	0.0	HPAEC none	0.0
day
Two Way MLR 5	0.0	HPAEC TNF alpha +	3.0
day		IL-1 beta
Two Way MLR 7	0.5	Lung fibroblast	6.3
day		none
PBMC rest	0.0	Lung fibroblast TNF	3.8
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	1.5
PBMC PHA-L	2.3	Lung fibroblast IL-9	3.5
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	16.0	Lung fibroblast IFN	2.1
ionomycin		gamma
B lymphocytes	0.0	Dermal fibroblast	0.3
PWM		CCD1070 rest
B lymphocytes	2.3	Dermal fibroblast	0.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	0.0	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	0.0	Dermal fibroblast IL-4	1.5
Dendritic cells LPS	0.0	Dermal Fibroblasts	1.9
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.0	Colon	0.0
Macrophages rest	0.0	Lung	0.0
Macrophages LPS	0.0	Thymus	0.0
HUVEC none	0.0	Kidney	4.5
HUVEC starved	2.9

[0995] CNS_neurodegeneration_v1.0 Summary: Ag5684 Expression of this gene is low/undetectable (CTs>34.8) across all of the samples on this panel (data not shown).

[0996] General_screening_panel_v1.5 Summary: Ag5684 The amp plot indicates that there were experimental difficulties with this run; therefore, no conclusions can be drawn from this data. (Data not shown).

[0997] Panel 4.1D Summary: Ag5684 Highest expression of this gene is detected in IL-13 treated NCI-H292 cell line (CT=30.4). This gene is also expressed in a cluster of treated and untreated NCI-H292 cell line, a human airway epithelial cell line that produces mucins. Mucus overproduction is an important feature of bronchial asthma and chronic obstructive pulmonary disease samples. This gene is also expressed at lower but still significant levels in ionomycin treated Ramos B cells, activated HUVEC cells, activated bronchial epithelium and small airway epithelium, resting lung fibroblasts, coronery artery SMC and keratinocytes. Therefore, therapeutics designed with the protein encoded by this gene may reduce or eliminate symptoms caused by inflammation in lung epithelia in chronic obstructive pulmonary disease, asthma, allergy, and emphysema.

[0998] AE. CG150637-02: T-Cell Surface Glycoprotein CD1B Precursor

[0999] Expression of full-length physical clone CG150637-02 was assessed using the primer-probe set Ag7126, described in Table AEA. Results of the RTQ-PCR runs are shown in Table AEB.

TABLE AEA
Probe Name Ag7126
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-ggatgcggggaaacc-3′	15	718	338
Probe	TET-5′-acctccattggctcaattgttttggc-3′-TAMRA	26	735	339
Reverse	5′-ccataatgcaaggcatagca-3′	20	787	340

[1000]

TABLE AEB
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(% Ag7126,		(%) Ag7126,
	Run		Run
Tissue Name	306518354	Tissue Name	306518354
Secondary Th1 act	0.0	HUVEC IL-1beta	0.0
Secondary Th2 act	0.0	HUVEC IFN gamma	0.0
Secondary Tr1 act	0.0	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	0.0
Secondary Tr1 rest	0.0	Lung Microvascular	0.0
		EC none
Primary Th1 act	0.0	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.0	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	0.0	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	0.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.0	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	0.0	Coronery artery SMC	0.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.0	Astrocytes rest	0.0
Secondary CD8	0.0	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.0	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	0.0
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	12.0	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.0	Liver cirrhosis	0.0
LAK cells IL-2 +	0.0	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	11.2	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	0.0
Two Way MLR 3	0.0	HPAEC none	0.0
day
Two Way MLR 5	0.0	HPAEC TNF alpha +	0.0
day		IL-1 beta
Two Way MLR 7	0.0	Lung fibroblast	0.0
day		none
PBMC rest	0.0	Lung fibroblast TNF	0.0
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.0	Lung fibroblast IL-9	0.0
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	0.0	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	0.0	Dermal fibroblast	0.0
PWM		CCD1070 rest
B lymphocytes	0.0	Dermal fibroblast	0.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	1.1	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	100.0	Dermal fibroblast IL-4	0.0
Dendritic cells LPS	64.6	Dermal Fibroblasts	0.0
		rest
Dendritic cells	86.5	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.0	Colon	0.0
Macrophages rest	0.0	Lung	0.0
Macrophages LPS	0.0	Thymus	19.5
HUVEC none	0.0	Kidney	0.0
HUVEC starved	0.0

[1001] CNS_neurodegeneration_v1.0 Summary: Ag7126 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[1002] Panel 4.1D Summary: Ag7126 Highest expression of this gene is detected in dendritic cells (CT=32). Moderate to low levels of expression of this gene is restricted to resting and activated dendritic cells, and thymus. Dendritic cells are powerful antigen-presenting cells (APC), whose function is pivotal in the initiation and maintenance of normal immune responses. Autoimmunity and inflammation may be reduced by suppression of this function. Therefore, therapeutic modulation of the protein encoded by this gene may be important in the treatment of autoimmune and inflammatory diseases such as troin's disease, ulcerative colitis, multiple sclerosis, chronic obstructive pulmonary disease, asthma, emphysema, rheumatoid arthritis, lupus erythematosus, or psoriasis.

[1003] AF. CG150694-01: Microfibril-Associated Glycoprotein 2 Precursor

[1004] Expression of full-length physical clone CG150694-01 was assessed using the primer-probe set Ag7144, described in Table AFA. Results of the RTQ-PCR runs are shown in Tables AFB and AFC.

TABLE AFA
Probe Name Ag7144
			Start	SEQ ID
Primers	Sequence	Length	Position	No
Forward	5′-gatgaaacagagtgctgggat-3′	21	166	341
Probe	TET-5′-atttacctgcacaaggctctactctgtgc-3′-TAMRA	29	192	342
Reverse	5′-actgatgaatgcattgtttaacc-3′	23	228	343

[1005]

TABLE AFB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7144,		(%) Ag7144,
	Run		Run
Tissue Name	306518753	issue Name	306518753
AD 1 Hippo	19.1	Control (Path) 3	13.1
		Temporal Ctx
AD 2 Hippo	28.1	Control (Path) 4	2.6
		Temporal Ctx
AD 3 Hippo	3.1	AD 1 Occipital Ctx	4.0
AD 4 Hippo	6.0	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	14.1	AD 3 Occipital Ctx	5.3
AD 6 Hippo	100.0	AD 4 Occipital Ctx	1.6
Control 2 Hippo	3.0	AD 5 Occipital Ctx	7.4
Control 4 Hippo	20.2	AD 6 Occipital Ctx	7.0
Control (Path) 3	0.0	Control 1 Occipital	9.2
Hippo		Ctx
AD 1 Temporal Ctx	2.9	Control 2 Occipital	15.0
		Ctx
AD 2 Temporal Ctx	15.7	Control 3 Occipital	0.0
		Ctx
AD 3 Temporal Ctx	0.0	Control 4 Occipital	3.2
		Ctx
AD 4 Temporal Ctx	12.0	Control (Path) 1	31.0
		Occipital Ctx
AD 5 Inf Temporal	51.1	Control (Path) 2	5.3
Ctx		Occipital Ctx
AD 5 Sup Temporal	39.5	Control (Path) 3	0.0
Ctx		Occipital Ctx
AD 6 Inf Temporal	22.2	Control (Path) 4	8.0
Ctx		Occipital Ctx
AD 6 Sup Temporal	23.8	Control 1 Parietal Ctx	0.0
Ctx
Control 1 Temporal	0.0	Control 2 Parietal Ctx	27.5
Ctx
Control 2 Temporal	1.0	Control 3 Parietal Ctx	2.3
Ctx
Control 3 Temporal	0.0	Control (Path) 1	17.9
Ctx		Parietal Ctx
Control 3 Temporal	1.1	Control (Path) 2	15.1
Ctx		Parietal Ctx
Control (Path) 1	5.3	Control (Path) 3	0.0
Temporal Ctx		Parietal Ctx
Control (Path) 2	4.7	Control (Path) 4	8.7
Temporal Ctx		Parietal Ctx

[1006]

TABLE AFC
Panel 4.1D
	Rel. Ex.		Rel. Exp.
	(%) Ag7144,		(%) Ag7144,
	Run		Run
Tissue Name	306518356	Tissue Name	306518356
Secondary Th1 act	0.0	HUVEC IL-1beta	0.0
Secondary Th2 act	0.1	HUVEC IFN gamma	0.0
Secondary Tr1 act	0.0	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	0.0
Secondary Tr1 rest	0.0	Lung Microvascular	0.0
		EC none
Primary Th1 act	0.0	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.0	Microvascular Dermal	0.3
		EC none
Primary Tr1 act	0.0	Microsvasular Dermal	0.3
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	2.3
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	0.7
		epithelium none
Primary Tr1 rest	0.0	Small airway	2.5
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.8	Coronery artery SMC	91.4
lymphocyte act		rest
CD45RO CD4	0.0	Coronery artery SMC	100.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.0	Astrocytes rest	24.7
Secondary CD8	0.0	Astrocytes	55.9
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.0	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	0.0
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	3.2
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	1.4
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.0	Liver cirrhosis	0.4
LAK cells IL-2 +	0.0	NCI-H292 none	13.0
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	25.2
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	39.2
IL-18
LAK cells PMA/	0.0	NCI-H292 IL-13	41.5
ionomycin
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	11.8
Two Way MLR 3	0.0	HPAEC none	0.1
day
Two Way MLR 5	0.1	HPAEC TNF alpha +	0.0
day		IL-1 beta
Two Way MLR 7	0.0	Lung fibroblast	0.0
day		none
PBMC rest	0.0	Lung fibroblast TNF	0.0
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.0	Lung fibroblast IL-9	0.0
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	0.0	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	0.0	Dermal fibroblast	5.7
PWM		CCD1070 rest
B lymphocytes	0.1	Dermal fibroblast	4.3
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	0.0	Dermal fibroblast	3.3
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN	3.9
PMA/ionomycin		gamma
Dendritic cells none	0.0	Dermal fibroblast IL-4	5.6
Dendritic cells LPS	0.0	Dermal Fibroblasts	10.3
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.7	Colon	1.3
Macrophages rest	0.0	Lung	0.2
Macrophages LPS	0.0	Thymus	1.4
HUVEC none	0.0	Kidney	0.2
HUVEC starved	0.0

[1007] CNS_neurodegeneration_v1.0 Summary: Ag7144 This panel confirms the expression of this gene at low levels in the brain in an independent group of individuals. This gene is found to be slightly upregulated in the temporal cortex of Alzheimer's disease patients. Therefore, therapeutic modulation of the expression or function of this gene may decrease neuronal death and be of use in the treatment of this disease.

[1008] Panel 4.1D Summary: Ag7144 Highest expression of this gene is detected in resting and activated coronery artery SMC (CTs=28). Moderate levels of expression of this gene is also seen in astrocytes, keratinocytes, mucoepidermoid NCI-H292 cells, activated bronchial and small airway epithelius and dermal fibroblasts. In addition, low levels of expression of this gene are also seen in colon and thymus. Therefore, therapeutic modulation of this gene or its protein product through the use of antibody or small molecule drug may be useful in the treatment of autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, osteoarthritis, multiple sclerosis and other inflammatory diseases of the CNS.

[1009] AG. CG151069-01: Membrane Protein AK027056.1

[1010] Expression of gene CG151069-01 was assessed using the primer-probe set Ag7562, described in Table AGA. Results of the RTQ-PCR runs are shown in Tables AGB and AGC.

TABLE AGA
Probe Name Ag7562
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-aatctgtggctggggtcat-3′	19	861	344
Probe	TET-5′-cccctggacgtctccgtcacaat-3′-TAMRA	23	887	345
Reverse	5′-cactcattgtgaaaataggctgata-3′	25	923	346

[1011]

TABLE AGB
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag7562,		(%) Ag7562,
	Run		Run
Tissue Name	308750605	issue Name	308750605
AD 1 Hippo	12.9	Control (Path) 3	0.9
		Temporal Ctx
AD 2 Hippo	17.8	Control (Path) 4	9.2
		Temporal Ctx
AD 3 Hippo	9.4	AD 1 Occipital Ctx	24.8
AD 4 Hippo	11.4	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	40.6	AD 3 Occipital Ctx	9.4
AD 6 Hippo	31.4	AD 4 Occipital Ctx	27.5
Control 2 Hippo	15.7	AD 5 Occipital Ctx	15.8
Control 4 Hippo	3.8	AD 6 Occipital Ctx	15.3
Control (Path) 3	3.0	Control 1 Occipital	3.9
Hippo		Ctx
AD 1 Temporal Ctx	38.4	Control 2 Occipital	19.3
		Ctx
AD 2 Temporal Ctx	23.0	Control 3 Occipital	7.2
		Ctx
AD 3 Temporal Ctx	8.9	Control 4 Occipital	9.2
		Ctx
AD 4 Temporal Ctx	23.3	Control (Path) 1	70.7
		Occipital Ctx
AD 5 Inf Temporal	100.0	Control (Path) 2	11.5
Ctx		Occipital Ctx
AD 5 Sup Temporal	35.6	Control (Path) 3	1.4
Ctx		Occipital Ctx
AD 6 Inf Temporal	53.6	Control (Path) 4	7.7
Ctx		Occipital Ctx
AD 6 Sup Temporal	37.9	Control 1 Parietal Ctx	9.1
Ctx
Control 1 Temporal	1.2	Control 2 Parietal Ctx	52.5
Ctx
Control 2 Temporal	14.3	Control 3 Parietal Ctx	9.0
Ctx
Control 3 Temporal	7.9	Control (Path) 1	31.9
Ctx		Parietal Ctx
Control 3 Temporal	6.1	Control (Path) 2	17.2
Ctx		Parietal Ctx
Control (Path) 1	30.8	Control (Path) 3	1.3
Temporal Ctx		Parietal Ctx
Control (Path) 2	10.2	Control (Path) 4	17.4
Temporal Ctx		Parietal Ctx

[1012]

TABLE AGC
Panel 4.1D
	Rel. Exp		Rel. Exp.
	(%) Ag7562,		(%) Ag7562,
	Run		Run
Tissue Name	308748090	Tissue Name	308748090
Secondary Th1 act	0.0	HUVEC IL-1beta	4.2
Secondary Th2 act	0.0	HUVEC IFN gamma	17.2
Secondary Tr1 act	0.0	HUVEC TNF alpha +	1.2
		IFN gamma
Secondary Th1 rest	0.0	HUVEC TNF alpha +	1.2
		IL4
Secondary Th2 rest	0.0	HUVEC IL-11	3.2
Secondary Tr1 rest	0.0	Lung Microvascular	88.3
		EC none
Primary Th1 act	0.0	Lung Microvascular	17.6
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.0	Microvascular Dermal	11.0
		EC none
Primary Tr1 act	0.0	Microsvasular Dermal	8.7
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	0.0	Small airway	0.8
		epithelium none
Primary Tr1 rest	0.7	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	1.8	Coronery artery SMC	1.6
lymphocyte act		rest
CD45RO CD4	0.0	Coronery artery SMC	1.6
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.0	Astrocytes rest	0.0
Secondary CD8	0.0	Astrocytes	0.7
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.0	KU-812 (Basophil)	57.8
lymphocyte act		rest
CD4 lymphocyte	0.0	KU-812 (Basophil)	92.7
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.0	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.5	Liver cirrhosis	3.7
LAK cells IL-2 +	0.0	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	0.0	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	0.0	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	0.0
Two Way MLR 3	0.0	HPAEC none	69.7
day
Two Way MLR 5	0.0	HPAEC TNF alpha +	100.0
day		IL-1 beta
Two Way MLR 7	0.0	Lung fibroblast	40.6
day		none
PBMC rest	0.0	Lung fibroblast TNF	6.4
		alpha + IL-1 beta
PBMC PWM	0.0	Lung fibroblast IL-4	17.1
PBMC PHA-L	0.0	Lung fibroblast IL-9	10.3
Ramos (B cell) none	0.0	Lung fibroblast IL-13	6.6
Ramos (B cell)	0.0	Lung fibroblast IFN	16.2
ionomycin		gamma
B lymphocytes	0.0	Dermal fibroblast	0.0
PWM		CCD1070 rest
B lymphocytes	0.6	Dermal fibroblast	0.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	78.5	Dermal fibroblast	1.7
		CCD1070 IL-1 beta
EOL-1 dbcAMP	40.1	Dermal fibroblast IFN	1.4
PMA/ionomycin		gamma
Dendritic cells none	0.0	Dermal fibroblast IL-4	5.1
Dendritic cells LPS	0.0	Dermal Fibroblasts	18.2
		rest
Dendritic cells	0.0	Neutrophils TNFa +	0.0
anti-CD40		LPS
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.0	Colon	1.8
Macrophages rest	0.0	Lung	5.8
Macrophages LPS	0.0	Thymus	1.2
HUVEC none	9.7	Kidney	3.3
HUVEC starved	7.1

[1013] CNS_neurodegeneration_v1.0 Summary: Ag7562 This panel confirms the expression of this gene at low levels in the brain in an independent group of individuals. This gene is found to be upregulated in the temporal cortex of Alzheimer's disease patients. Therefore, therapeutic modulation of the expression or function of this gene may decrease neuronal death and be of use in the treatment of this disease.

[1014] Panel 4.1D Summary: Ag7562 Highest expression of this gene is detected in alpha+IL-1 beta treated HPAEC (CT=32.2). Moderate to low levels of expression of this gene is also seen in eosinophils, lung microvascular endothelial cells, basophils, HPAEC, and activated lung fibroblasts. Therefore, therapeutic modulation of this gene or its protein product through the use of small molecule drug or antibodies may be useful in the treatment of autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.

[1015] AH. CG151189-01: Type IIIb Membrane Protein

[1016] Expression of gene CG 15119-01 was assessed using the primer-probe set Ag7561, described in Table AHA. Results of the RTQ-PCR runs are shown in Tables AHB and AHC.

TABLE AHA
16/28 Probe Name Ag7561
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-ctggagggcctgtcaaa-3′	17	440	347
Probe	TET-5′-cctccgatggcgaaaccagcatt-3′-TAMRA	23	486	348
Reverse	5′-tcacagaatttagtaagcgttgg-3′	23	524	349

[1017]

TABLE AHB
CNS neurodegeneration v1.0
	Rel.		Rel.
	Exp. (%)		Exp. (%)
	Ag7561,		Ag7561,
	Run		Run
Tissue Name	308750603	issue Name	308750603
AD 1 Hippo	14.7	Control (Path) 3 Temporal Ctx	4.5
AD 2 Hippo	32.5	Control (Path) 4 Temporal Ctx	36.3
AD 3 Hippo	9.7	AD 1 Occipital Ctx	17.3
AD 4 Hippo	7.0	AD 2 Occipital Ctx (Missing)	0.0
AD 5 hippo	84.1	AD 3 Occipital Ctx	7.8
AD 6 Hippo	68.8	AD 4 Occipital Ctx	21.6
Control 2 Hippo	26.8	AD 5 Occipital Ctx	19.5
Control 4 Hippo	12.9	AD 6 Occipital Ctx	37.1
Control (Path) 3 Hippo	7.9	Control 1 Occipital Ctx	5.1
AD 1 Temporal Ctx	20.2	Control 2 Occipital Ctx	51.1
AD 2 Temporal Ctx	35.6	Control 3 Occipital Ctx	18.9
AD 3 Temporal Ctx	6.4	Control 4 Occipital Ctx	10.0
AD 4 Temporal Ctx	27.5	Control (Path) 1 Occipital Ctx	97.3
AD 5 Inf Temporal Ctx	100.0	Control (Path) 2 Occipital Ctx	15.3
AD 5 SupTemporal Ctx	54.0	Control (Path) 3 Occipital Ctx	3.6
AD 6 Inf Temporal Ctx	73.2	Control (Path) 4 Occipital Ctx	19.6
AD 6 Sup Temporal Ctx	74.2	Control 1 Parietal Ctx	9.9
Control 1 Temporal Ctx	6.9	Control 2 Parietal Ctx	55.9
Control 2 Temporal Ctx	33.4	Control 3 Parietal Ctx	21.5
Control 3 Temporal Ctx	14.8	Control (Path) 1 Parietal Ctx	63.7
Control 4 Temporal Ctx	13.9	Control (Path) 2 Parietal Ctx	29.7
Control (Path) 1 Temporal Ctx	57.8	Control (Path) 3 Parietal Ctx	5.0
Control (Path) 2 Temporal Ctx	44.8	Control (Path) 4 Parietal Ctx	34.6

[1018]

TABLE AHC
Panel 4.1D
	Rel.		Rel.
	Exp. (%)		Exp. (%)
	Ag7561,		Ag7561,
	Run		Run
Tissue Name	308748088	Tissue Name	308748088
Secondary Th1 act	128.3	HUVEC IL-1beta	19.2
Secondary Th2 act	100.0	HUVEC IFN gamma	15.3
Secondary Tr1 act	25.0	HUVEC TNF alpha + IFN gamma	5.6
Secondary Th1 rest	1.9	HUVEC TNF alpha + IL4	9.6
Secondary Th2 rest	4.2	HUVEC IL-11	6.1
Secondary Tr1 rest	3.8	Lung Microvascular EC none	40.1
Primary Th1 act	4.7	Lung Microvascular EC TNFalpha +	10.1
		IL-1beta
Primary Th2 act	26.1	Microvascular Dermal EC none	4.7
Primary Tr1 act	18.0	Microsvasular Dermal EC	9.0
		TNFalpha + IL-1beta
Primary Th1 rest	2.3	Bronchial epithelium TNFalpha +	3.7
		IL1beta
Primary Th2 rest	2.4	Small airway epithelium none	2.8
Primary Tr1 rest	0.8	Small airway epithelium TNFalpha +	14.0
		IL-1beta
CD45RA CD4 lymphocyte act	27.0	Coronery artery SMC rest	14.5
CD45RO CD4 lymphocyte act	28.1	Coronery artery SMC TNFalpha +	12.4
		IL-1beta
CD8 lymphocyte act	10.0	Astrocytes rest	14.8
Secondary CD8 lymphocyte rest	7.2	Astrocytes TNFalpha + IL-1beta	12.4
Secondary CD8 lymphocyte act	6.7	KU-812 (Basophil) rest	4.6
CD4 lymphocyte none	2.7	KU-812 (Basophil)	7.4
		PMA/ionomycin
2ry Th1/Th2/Tr1_anti-CD95	6.0	CCD1106 (Keratinobytes) none	22.2
CH11
LAK cells rest	11.0	CCD1106 (Keratinocytes)	6.1
		TNFalpha + IL-1beta
LAK cells IL-2	6.9	Liver cirrhosis	2.3
LAK cells IL-2 + IL-12	0.7	NCI-H292 none	8.6
LAK cells IL-2 + IFN gamma	5.4	NCI-H292 IL-4	12.5
LAK cells IL-2 + IL-18	4.9	NCI-H292 IL-9	15.7
LAK cells PMA/ionomycin	18.9	NCI-H292 IL-13	15.8
NK Cells IL-2 rest	26.2	NCI-H292 IFN gamma	7.0
Two Way MLR 3 day	9.0	HPAEC none	4.5
Two Way MLR 5 day	4.0	HPAEC TNF alpha + IL-1 beta	24.3
Two Way MLR 7 day	3.6	Lung fibroblast none	13.6
PBMC rest	1.4	Lung fibroblast TNF alpha + IL-1	18.8
		beta
PBMC PWM	6.7	Lung fibroblast IL-4	13.9
PBMC PHA-L	8.0	Lung fibroblast IL-9	31.4
Ramos (B cell) none	6.3	Lung fibroblast IL-13	11.1
Ramos (B cell) ionomycin	14.9	Lung fibroblast IFN gamma	26.8
B lymphocytes PWM	6.3	Dermal fibroblast CCD1070 rest	27.2
B lymphocytes CD40L and IL-4	20.7	Dermal fibroblast CCD1070 TNF	45.7
		alpha
EOL-1 dbcAMP	14.4	Dermal fibroblast CCD1070 IL-1	20.7
		beta
EOL-1 dbcAMP	14.1	Dermal fibroblast IFN gamma	6.1
PMA/ionomycin
Dendritic cells none	13.4	Dermal fibroblast IL-4	16.4
Dendritic cells LPS	5.5	Dermal Fibroblasts rest	12.2
Dendritic cells anti-CD40	6.7	Neutrophils TNFa + LPS	3.5
Monocytes rest	3.3	Neutrophils rest	11.7
Monocytes LPS	22.4	Colon	2.0
Macrophages rest	8.3	Lung	1.4
Macrophages LPS	6.5	Thymus	4.6
HUVEC none	12.7	Kidney	10.7
HUVEC started	17.9

[1019] CNS_neurodegeneration_v1.0 Summary: Ag7561 No differential expression of this gene was detected between Alzheimer's diseased postmortem brains and those of non-demented controls in this experiment. However, this panel confirms the expression of this gene at low levels in the brains of an independent group of individuals. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[1020] Panel 4.1D Summary: Ag7561 Highest expression of this gene is detected in activated secondary Th2 cells (CT=29.3). This gene is expressed at moderate to low levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.

[1021] AI. CG151801-01: Occludin Like Membrane Protein

[1022] Expression of gene CG151801-01 was assessed using the primer-probe set Ag7563, described in Table AIA. Results of the RTQ-PCR runs are shown in Table AIB.

TABLE AIA
Probe Name Ag7563
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-actttctcacataaagcaaagaattc-3′	26	1629	350
Probe	TET-5′-ccttgtacatcccaattcattactttatca-3′-TAMRA	30	1662	351
Reverse	5′-gtggtttcaaataagcgttaagaat-3′	25	1694	352

[1023]

TABLE AIB
Panel 4.1D
	Rel.		Rel.
	Ex. (%)		Exp. (%)
	Ag7563,		Ag7563,
	Run		Run
Tissue Name	308748092	Tissue Name	308748092
Secondary Th1 act	0.0	HUVEC IL-1beta	2.8
Secondary Th2 act	0.0	HUVEC IFN gamma	3.8
Secondary Tr1 act	0.0	HUVEC TNF alpha + IFN gamma	0.0
Secondary Th1 rest	0.0	HUVEC TNF alpha + IL4	0.0
Secondary Th2 rest	0.0	HUVEC IL-11	0.0
Secondary Tr1 rest	0.0	Lung Microvascular EC none	20.9
Primary Th1 act	0.0	Lung Microvascular EC TNFalpha +	1.8
		IL-1beta
Primary Th2 act	0.0	Microvascular Dermal EC none	2.5
Primary Tr1 act	0.0	Microsvasular Dermal EC	0.0
		TNFalpha + IL-1beta
Primary Th1 rest	0.0	Bronchial epithelium TNFalpha +	12.2
		IL1beta
Primary Th2 rest	0.0	Small airway epithelium none	18.4
Primary Tr1 rest	0.0	Small airway epithelium THFalpha +	100.0
		IL-1beta
CD45RA CD4 lymphocyte act	0.0	Coronery artery SMC rest	0.0
CD45RO CD4 lymphocyte act	0.0	Coronery artery SMC TNFalpha +	0.0
		IL-1beta
CD8 lymphocyte act	0.0	Astrocytes rest	0.0
Secondary CD8 lymphocyte rest	0.0	Astrocytes TNFalpha + IL-1beta	0.0
Secondary CD8 lymphocyte act	0.0	KU-812 (Basophil) rest	0.0
CD4 lymphocyte none	0.0	KU-812 (Basophil)	0.0
		PMA/ionomycin
2ry Th1/Th2/Tr1_anti-CD95	0.0	CCD1106 (Keratinocytes) none	41.5
CH11
LAK cells rest	0.0	CCD1106 (Keratinocytes)	334
		TNFalpha + IL-1beta
LAX cells IL-2	0.0	Liver cirrhosis	4.3
LAK cells IL-2 + IL-12	0.0	NCI-H292 none	31.6
LAK cells IL-2 + IFN gamma	0.0	NCI-H292 IL-4	57.4
LAK cells IL-2 + IL-18	0.0	NCI-H292 IL-9	45.7
LAK cells PMA/ionomycin	0.0	NCI-H292 IL-13	59.9
NK Cells IL-2 rest	0.0	NCI-H292 IFN gamma	21.6
Two Way MLR 3 day	2.7	HPAEC none	0.0
Two Way MLR 5 day	0.0	HPAEC TNF alpha + IL-1 beta	25.9
Two Way MLR 7 day	0.0	Lung fibroblast none	2.8
PBMC rest	0.0	Lung fibroblast TNF alpha + IL-1	3.7
		beta
PBMC PWM	0.0	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.0	Lungfibroblast IL-9	3.5
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell) ionomycin	0.0	Lung fibroblast IFN gamma	7.1
B lymphocytes PWM	0.0	Dermal fibroblast CCD1070 rest	0.0
B lymphocytes CD40L and IL-4	0.0	Dermal fibroblast CCD1070 TNF	0.0
		alpha
EOL-1 dbcAMP	0.0	Dermal fibroblast CCD1070 IL-1	0.0
		beta
EOL-1 dbcAMP	0.0	Dermal fibroblast IFN gamma	0.0
PMA/ionomycin
Dendritic cells none	0.0	Dermal fibroblast IL-4	2.4
Dendritic cells LPS	0.0	Dermal Fibroblasts rest	0.0
Dendritic cells anti-CD40	29.3	Neutrophils TNFa + LPS	0.0
Monocytes rest	0.0	Neutrophils rest	0.0
Monocytes LPS	0.0	Colon	6.1
Macrophages rest	0.0	Lung	2.3
Macrophages LPS	0.0	Thymus	0.0
HUVEC none	1.9	Kidney	45.7
HUVEC starved	5.3

[1024] CNS_neurodegeneration_v1.0 Summary: Ag7563 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel (data not shown).

[1025] Panel 4.1D Summary: Ag7563 Highest expression of this gene is seen in TNFalpha+IL-1beta treated small airway epithelium (CT=34). Therefore, expression of this gene may be used to distinguish activated small airway epithelium from other samples in this panel. In addition, low levels of expression of this gene are also seen in cytokine activated NCI-H292 cells, a human airway epithelial cell line that produces mucins. Therefore, modulation of the expression or activity of the protein encoded by this gene through the application of small molecule therapeutics or antibodies may be useful in the treatment of asthma, COPD, and emphysema.

[1026] AJ. CG165961-01 and CG165961-02: Secretory Carrier-Associated Membrane Protein 3

[1027] Expression of full-length physical clone CG165961-01 and variant CG165961-02 was assessed using the primer-probe set Ag7569, described in Table AJA. Results of the RTQ-PCR runs are shown in Tables AJB and AJC. Please note that CG165961-01 represents a full-length physical clone of the CG165961-02 gene, validating the prediction of the gene sequence.

TABLE AJA
Probe Name Ag7569
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-ctggctcttctcctgaacttc-3′	21	594	353
Probe	TET-5′-ccagcttctgtgtggaaaccaacaat-3′-TAMRA	26	555	354
Reverse	5′-aggacccagaggatagaaagc-3′	21	520	355

[1028]

TABLE AJB
CNS neurodegeneration v1.0
	Rel.		Rel.
	Exp. (%)		Exp. (%)
	Ag7569,		Ag7569,
	Run		Run
Tissue Name	308751132	issue Name	308751132
AD 1 Hippo	22.8	Control (Path) 3 Temporal Ctx	7.2
AD 2 Hippo	41.5	Control (Path) 4 Temporal Ctx	34.2
AD 3 Hippo	11.3	AD 1 Occipital Ctx	21.8
AD 4 Hippo	9.6	AD 2 Occipital Ctx (Missing)	0.0
AD 5 hippo	88.3	AD 3 Occipital Ctx	10.8
AD 6 Hippo	68.8	AD 4 Occipital Ctx	25.7
Control 2 Hippo	35.4	AD 5 Occipital Ctx	27.9
Control 4 Hippo	19.8	AD 6 Occipital Ctx	49.3
Control (Path) 3 Hippo	8.1	Control 1 Occipital Ctx	6.9
AD 1 Temporal Ctx	21.5	Control 2 Occipital Ctx	86.5
AD 2 Temporal Ctx	37.6	Control 3 Occipital Ctx	18.7
AD 3 Temporal Ctx	8.4	Control 4 Occipital Ctx	9.9
AD 4 Temporal Ctx	21.0	Control (Path) 1 Occipital Ctx	88.3
AD 5 Inf Temporal Ctx	100.0	Control (Path) 2 Occipital Ctx	12.8
AD 5 SupTemporal Ctx	54.0	Control (Path) 3 Occipital Ctx	7.0
AD 6 Inf Temporal Ctx	62.4	Control (Path) 4 Occipital Ctx	16.6
AD 6 Sup Temporal Ctx	57.0	Control 1 Parietal Ctx	9.6
Control 1 Temporal Ctx	6.8	Control 2 Parietal Ctx	44.1
Control 2 Temporal Ctx	50.7	Control 3 Parietal Ctx	25.2
Control 3 Temporal Ctx	18.3	Control (Path) 1 Parietal Ctx	71.2
Control 4 Temporal Ctx	12.1	Control (Path) 2 Parietal Ctx	25.0
Control (Path) 1 Temporal Ctx	56.6	Control (Path) 3 Parietal Ctx	7.2
Control (Path) 2 Temporal Ctx	34.4	Control (Path) 4 Parietal Ctx	44.4

[1029]

TABLE AJC
Panel 4.1D
	Rel.		Rel.
	Ex. (%)		Exp. (%)
	Ag7569,		Ag7569,
	Run		Run
Tissue Name	308748454	Tissue Name	308748454
Secondary Th1 act	80.1	HUVEC IL-1beta	74.2
Secondary Th2 act	72.7	HUVEC IFN gamma	42.9
Secondary Tr1 act	26.2	HUVEC TNF alpha + IFN gamma	24.5
Secondary Th1 rest	3.7	HUVEC TNF alpha + IL4	25.9
Secondary Th2 rest	2.9	HUVEC IL-11	21.5
Second Tr1 rest	4.5	Lung Microvascular EC none	72.7
Primary Th1 act	12.6	Lung Microvascular EC TNFalpha +	41.5
		IL-1beta
Primary Th2 act	59.5	Microvascular Dermal EC none	11.3
Primary Tr1 act	76.3	Microsvasular Dermal EC	26.8
		TNFalpha + IL-1beta
Primary Th1 rest	5.3	Bronchial epithelium TNFalpha +	22.8
		IL1beta
Primary Th2 rest	7.0	Small airway epithelium none	16.6
Primary Tr1 rest	2.5	Small airway epithelium TNFalpha +	33.0
		IL-1beta
CD45RA CD4 lymphocyte act	55.9	Coronery artery SMC rest	32.1
CD45RO CD4 lymphocyte act	72.7	Coronery artery SMC TNFalpha +	39.0
		IL-1beta
CD8 lymphocyte act	31.2	Astrocytes rest	15.7
Secondary CD8 lymphocyte rest	34.9	Astrocytes TNFalpha + IL-1beta	16.0
Secondary CD8 lymphocyte act	15.1	KU-812 (Basophil) rest	31.0
CD4 lymphocyte none	4.5	KU-812 (Basophil)	16.5
		PMA/ionomycin
2ry Th1/Th2/Tr1_anti-CD95	8.5	CCD1106 (Keratinocytes) none	44.4
CH11
LAK cells rest	14.0	CCD1106 (Keratinocytes)	15.7
		TNFalpha + IL-1beta
LAK cells IL-2	16.4	Liver cirrhosis	6.5
LAK cells IL-2 + IL-12	1.5	NCI-H292 none	34.4
LAK cells IL-2 + IFN gamma	8.8	NCI-H292 IL-4	50.3
LAK cells IL-2 + IL-18	8.1	NCI-H292 IL-9	57.8
LAK cells PMA/ionomycin	33.0	NCI-H292 IL-13	44.1
NK Cells IL-2 rest	48.3	NCI-H292 IFN gamma	20.4
Two Way MLR 3 day	24.1	HPAEC none	9.7
Two Way MLR 5 day	11.8	HPAEC TNF alpha + IL-1 beta	68.8
Two Way MLR 7 day	12.5	Lung fibroblast none	48.6
PBMC rest	1.9	Lung fibroblast TNF alpha + IL-1	63.3
		beta
PBMC PWM	25.7	Lung fibroblast IL-4	34.6
PBMC PHA-L	17.0	Lung fibroblast IL-9	59.5
Ramos (B cell) none	31.6	Lung fibroblast IL-13	23.3
Ramos (B cell) ionomycin	80.7	Lung fibroblast IFN gamma	99.3
B lymphocytes PWM	15.8	Dermal fibroblast CCD1070 rest	83.5
B lymphocytes CD40L and IL-4	44.8	Dermal fibroblast CCD1070 TNF	100.0
		alpha
EOL-1 dbcAMP	21.0	Dermal fibroblast CCD1070 IL-1	47.6
		beta
EOL-1 dbcAMP	3.3	Dermal fibroblast IFN gamma	32.8
PMA-ionomycin
Dendritic cells none	14.2	Dermal fibroblast IL-4	33.0
Dendritic cells LPS	13.8	Dermal Fibroblasts rest	47.3
Dendritic cells anti-CD40	8.0	Neutrophils TNFa + LPS	0.5
Monocytes rest	4.5	Neutrophils rest	1.4
Monocytes LPS	37.1	Colon	3.4
Macrophages rest	25.0	Lung	6.7
Macrophages LPS	21.8	Thymus	3.5
HUVEC none	43.5	Kidney	30.6
HUVEC starved	50.0

[1030] CNS_neurodegeneration_v1.0 Summary: Ag7569 No differential expression of this gene was detected between Alzheimer's diseased postmortem brains and those of non-demented controls in this experiment. However, this panel confirms the expression of this gene at low levels in the brains of an independent group of individuals. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[1031] Panel 4.1D Summary: Ag7569 Highest expression of this gene is detected in TNF alpha treated dermal fibroblast (CT=29.9). This gene is expressed at moderate to low levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell farmily, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.

[1032] AK. CG51595-03 and CG51595-06 and CG51595-07:

[1033] Thrombospondin Related Protein

[1034] Expression of gene CG51595-06 and variants CG51595-03 and CG51595-07 was assessed using the primer-probe sets Ag815 and Ag127, described in Tables AKA and AKB. Results of the RTQ-PCR runs are shown in Tables AKC, AKD, AKE, AKF, AKG, AKH, AKI and AKJ. Please note that Ag127 is specific to CG51595-06 and CG51595-07 only.

TABLE AKA
Probe Name Ag815
			Start	SEQ ID
Primers		Length	Position	No
Forward	5′-tgtgctcagcacatggtcta-3′	20	1716	356
Probe	TET-5′-acacctgctcagggaaaacgacagaa-3′-TAMRA	26	1754	357
Reverse	5′-tcgtgctcgtatctgtttcc-3′	20	1781	358

[1035]

TABLE AKB
Probe Name Ag127
			Start	SEQ ID
Primers	Sequence	Length	Position	No
Forward	5′-cctgccaggatgactgtcaatt-3′	22	2516	359
Probe	TET-5′-ccagctggtccaagttttcttcatgcaa-3′-TAMRA	28	2540	360
Reverse	5′-tggtcctaactgcaccacagtct-3′	23	2571	361

[1036]

TABLE AKC
AI comprehensive panel v1.0
	Rel.		Rel.
	Exp. (%)		Exp. (%)
	Ag815,		Ag815,
	Run		Run
Tissue Name	257809397	issue Name	257809397
110967 COPD-F	14.0	112427 Match Control Psoriasis-F	33.2
110980 COPD-F	9.0	112418 Psoriasis-M	10.6
110968 COPD-M	7.5	1112723 Match Control Psoriasis-M	1.1
110977 COPD-M	12.1	112419 Psoriasis-M	10.9
110989 Emphysema-F	18.7	112424 Match Control Psoriasis-M	12.4
110992 Emphysema-F	10.3	112420 Psoriasis-M	36.6
110993 Emphysema-F	10.2	1112425 Match Control Psoriasis-M	27.7
110994 Emphysema-F	3.8	104689 (MF) OA Bone-Backus	18.2
110995 Emphysema-F	20.4	104690 (MF) Adj “Normal”	9.3
		Bone-Backus
110996 Emphysema-F	3.7	104691 (MF) OA Synovium-Backus	7.6
110997 Asthma-M	1.6	104692 (BA) OA Cartilage-Backus	4.5
111001 Asthma-F	9.9	104694 (BA) OA Bone-Backus	10.3
111002 Asthma-F	14.2	104695 (BA) Adj “Normal”	12.8
		Bone-Backus
111003 Atopic Asthma-F	31.4	104696 (BA) OA Synovium-Backus	8.8
111004 Atopic Asthma-F	1.3	104700 (SS) OA Bone-Backus	8.9
111005 Atopic Asthma-F	10.1	104701 (SS) Adj “Normal”	9.0
		Bone-Backus
111006 Atopic Asthma-F	1.2	104702 (SS) OA Synovium-Backus	17.3
111417 Allergy-M	7.6	117093 OA Cartilage Rep7	25.2
112347 Allergy-M	3.1	112672 OA Bone5	29.3
112349 Normal Lung-F	2.1	112673 OA Synovium5	11.8
112357 Normal Lung-F	6.9	112674 OA Synovial Fluid cells5	10.4
112354 Normal Lung-M	6.5	117100 OA Cartilage Rep14	2.0
112374 Crohns-F	8.0	112756 OA Bone9	6.7
112389 Match Control Crohns-F	7.0	112757 OA Synovium9	1.6
112375 Crohns-F	7.4	112758 OA Synovial Fluid Cells9	12.8
112732 Match Control Crohns-F	0.1	117125 RA Cartilage Rep2	14.6
112725 Crohns-M	18.3	113492 Bone2 RA	8.7
112387 Match Control	4.6	113493 Synovium2 RA	2.1
Crohns-M
112378 Crohns-M	2.1	113494 syn Fluid Cells RA	4.4
112390 Match Control	22.7	113499 Cartilage4 RA	6.6
Crohns-M
112726 Crohns-M	31.2	113500 Bone4 RA	7.9
112731 Match Control	18.7	113501 Synovium4 RA	4.8
Crohns-M
112380 Ulcer Col-F	14.9	113502 Syn Fluid Cells4 RA	3.9
112734 Match Control Ulcer	2.1	113495 Cartilage3 RA	4.8
Col-F
112384 Ulcer Col-F	51.4	113496 Bone3 RA	9.0
112737 Match Control Ulcer	13.3	113497 Synovium3 RA	2.5
Col-F
112386 Ulcer Col-F	3.6	113498 Syn Fluid Cells3 RA	9.3
112738 Match Control Ulcer	0.9	117106 Normal Cartilage Rep20	5.7
Col-F
112381 Ulcer Col-M	0.8	113663 Bone3 Normal	8.8
112735 Match Control Ulcer	100.0	113664 Synovium3 Normal	0.9
Col-M
112382 Ulcer Col-M	12.2	113665 Syn Fluid Cells3 Normal	4.0
112394 Match Control Ulcer	3.7	117107 Normal Cartilage Rep22	13.8
Col-M
112383 Ulcer Col-M	36.3	113667 Bone4 Normal	7.2
112736 Match Control Ulcer	1.1	113668 Synovium4 Normal	15.6
Col-M
112423 Psoriasis-F	12.9	113669 Syn Fluid Cells4 Normal	17.7

[1037]

TABLE AKD
Panel 1
	Rel.		Rel.
	Ex. (%)		Exp. (%)
	Ag127,		Ag127,
	Run		Run
Tissue Name	87588501	Tissue Name	87588501
Endothelial cells	9.2	Renal ca. 786-0	0.0
Endothelial cells (treated)	2.2	Renal ca. A498	0.1
Pancreas	1.4	Renal ca. RXF 393	0.1
Pancreatic ca. CAPAN 2	0.4	Renal ca. ACHN	0.1
Adrenal gland	4.9	Renal ca. UO-31	0.6
Thyroid	4.8	Renal ca. TK-10	0.2
Salivary gland	0.7	Liver	2.6
Pituitary gland	4.2	Liver (fetal)	1.1
Brain (fetal)	7.1	Liver ca. (hepatoblast) HepG2	0.0
Brain (whole)	33.9	Lung	4.7
Brain (amygdala)	6.0	Lung (fetal)	3.2
Brain (cerebellum)	47.6	Lung ca. (small cell) LX-1	0.0
Brain (hippocampus)	15.5	Lung ca. (small cell) NCI-H69	7.9
Brain (substantia nigra)	5.8	Lung ca. (s.cell var.) SHP-77	0.0
Brain (thalamus)	7.8	Lung ca. (large cell)NCI-H460	0.0
Brain (hypothalamus)	2.9	Lung ca. (non-sm. cell) A549	15.4
Spinal cord	6.6	Lung ca. (non-s.cell) NCI-H23	12.2
glio/astro U87-MG	1.2	Lung ca (non-s.cell) HOP-62	1.9
glio/astro U-118-MG	1.3	Lung ca. (non-s.cl) NCI-H522	0.1
astrocytoma SW1783	0.7	Lung ca. (squam.) SW 900	7.1
neuro*; met SK-N-AS	18.6	Lung ca. (squam.) NCI-H596	8.4
astrocytoma SF-539	0.0	Mammary gland	12.0
astrocytoma SNB-75	0.4	Breast ca.* (pl.ef) MCF-7	0.0
glioma SNB-19	0.7	Breast ca.* (pl.ef) MDA-MB-231	0.0
glioma U251	3.7	Breast ca.* (pl. ef) T47D	0.9
glioma SF-295	0.3	Breast ca. BT-549	0.0
Heart	1.4	Breast ca. MDA-N	0.1
Skeletal muscle	0.1	Ovary	7.4
Bone marrow	0.2	Ovarian ca. OVCAR-3	1.0
Thymus	2.1	Ovarian ca. OVCAR-4	0.0
Spleen	2.1	Ovarian ca. OVCAR-5	6.0
Lymph node	1.1	Ovarian ca. OVCAR-8	2.9
Colon (ascending)	6.4	Ovarian ca. IGROV-1	4.9
Stomach	5.1	Ovarian ca. (ascites) SK-OV-3	0.3
Small intestine	1.6	Uterus	25.7
Colon ca. SW480	0.0	Placenta	100.0
Colon ca.* SW620 (SW480 met)	0.0	Prostate	4.0
Colon ca. HT29	0.0	Prostate ca.* (bone met) PC-3	0.0
Colon ca. HCT-116	0.0	Testis	33.7
Colon ca. CaCo-2	0.2	Melanoma Hs688(A).T	0.0
Colon ca. HCT-15	0.3	Melanoma* (met) Hs688(B).T	0.1
Colon ca. HCC-2998	1.5	Melanoma UACC-62	0.0
Gastric ca.* (liver met) NCI-N87	2.0	Melanoma M14	0.4
Bladder	11.3	Melanoma LOX IMVI	0.0
Trachea	2.4	Melanoma* (met) SK-MEL-5	15.9
Kidney	17.1	Melanoma SK-MEL-28	0.1
Kidney (fetal)	31.4

[1038]

TABLE AKE
Panel 1.2
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	g815,	Ag815,		Ag815,	Ag815,
	Run	Run		Run	Run
Tissue Name	118424515	122039235	Tissue Name	118424515	112039235
Endothelial cells	94.6	17.9	Renal ca. 786-0	0.1	0.0
Heart (Fetal)	4.7	4.2	Renal ca. A498	0.1	0.0
Pancreas	5.4	0.4	Renal ca. RXF 393	0.0	0.0
Pancreatic ca.	0.3	0.1	Renal ca. ACHN	0.1	0.0
CAPAN 2
Adrenal Gland	6.3	4.7	Renal ca. UO-31	0.4	0.3
Thyroid	9.0	1.0	Renal ca. TK-10	0.2	0.1
Salivary gland	2.1	1.4	Liver	3.6	1.7
Pituitary gland	20.3	4.6	Liver (fetal)	1.9	1.8
Brain (fetal)	31.4	5.9	Liver ca.	0.0	0.0
			(hepatoblast) HepG2
Brain (whole)	19.6	16.8	Lung	3.1	2.9
Brain (amygdala)	4.5	5.9	Lung (fetal)	4.5	2.0
Brain (cerebellum)	6.8	10.3	Lung ca. (small cell)	0.0	0.0
			LX-1
Brain (hippocampus)	8.2	10.8	Lung ca. (small cell)	27.5	8.4
			NCI-H69
Brain (thalamus)	14.2	9.9	Lung ca. (s.cell var.)	8.4	4.1
			SHP-77
Cerebral Cortex	73.7	100.0	Lung ca. (large	26.4	36.6
			cell)NCI-H460
Spinal cord	7.5	5.7	Lung ca. (non-sm.	68.3	36.9
			cell) A549
glio/astro U87-MG	3.4	1.2	Lung ca. (non-s.cell)	21.3	28.1
			NCI-H23
glio/astro U-118-MG	2.0	0.7	Lung ca. (non-s.cell)	7.4	2.3
			HOP-62
astrocytoma	0.8	0.2	Lung ca. (non-s.cl)	0.4	0.0
SW1783			NCI-H522
neuro*; met	88.9	15.2	Lung ca. (squam.)	8.2	9.4
SK-N-AS			SW 900
astrocytoma SF-539	0.1	0.0	Lung ca. (squam.)	47.0	13.3
			NCI-H596
astrocytoma SNB-75	0.3	0.1	Mammary gland	4.3	2.2
glioma SNB-19	1.2	1.1	Breast ca.* (pl.ef)	0.0	0.0
			MCF-7
glioma U251	12.8	7.9	Breast ca.* (pl.ef)	0.0	0.0
			MDA-MB-231
glioma SF-295	0.8	0.2	Breast ca.* (pl.ef)	1.1	0.8
			T47D
Heart	8.0	5.8	Breast ca. BT-549	0.1	0.0
Skeletal Muscle	3.6	0.9	Breast ca. MDA-N	0.4	0.1
Bone marrow	0.4	0.2	Ovary	8.9	6.6
Thymus	0.4	0.4	Ovarian ca.	3.5	0.8
			OVCAR-3
Spleen	1.8	0.6	Ovarian ca.	0.1	0.0
			OVCAR-4
Lymph node	2.6	1.4	Ovarian ca.	21.6	9.2
			OVCAR-5
Colorectal Tissue	1.0	1.3	Ovarian ca.	3.0	2.3
			OVCAR-8
Stomach	2.8	3.2	Ovarian ca.	27.9	5.6
			IGROV-1
Small intestine	3.3	1.2	Ovarian ca. (ascites)	1.8	1.1
			SK-OV-3
Colon ca. SW480	0.0	0.0	Uterus	8.2	4.8
Colon ca.* SW620	0.0	0.0	Placenta	100.0	95.3
(SW480 met)
Colon ca. HT29	0.2	0.0	Prostate	3.5	3.0
Colon ca. HCT-116	0.0	0.0	Prostate ca.* (bone	0.2	0.1
			met) PC-3
Colon ca. CaCo-2	0.3	0.1	Testis	8.5	2.9
Colon ca. Tissue	1.8	2.6	Melanoma	0.0	0.2
(ODO3866)_			Hs688(A).T
Colon ca. HCC-2998	6.2	1.8	Melanoma* (met)	0.1	0.1
			Hs688(B).T
Gastric ca.* (liver	3.5	2.0	Melanoma	0.1	0.1
met) NCI-N87			UACC-62
Bladder	21.6	12.5	Melanoma M14	0.3	0.1
Trachea	1.9	0.8	Melanoma LOX	0.0	0.0
			IMVI
Kidney	34.4	49.0	Melanoma* (met)	26.2	16.7
				SK-MEL-5
Kidney (fetal)	39.2	72.2

[1039]

TABLE AKF
Panel 1.3D
			Rel.
	Rel.		Exp. (%)
	Exp.() Ag815,		Ag815,
	Run		Run
Tissue Name	152862062	Tissue Name	152862062
Liver adenocarcinoma	0.0	Kidney (fetal)	11.3
Pancreas	0.6	Renal ca. 786-0	0.1
Pancreatic ca CAPAN 2	0.0	Renal ca A498	0.7
Adrenal gland	1.4	Renal ca. RXF 393	0.1
Thyroid	0.9	Renal ca. ACHN	0.0
Salivary gland	0.2	Renal ca UO-31	0.0
Pituitary gland	2.8	Renal ca. TK-10	0.2
Brain (fetal)	7.1	Liver	1.1
Brain (whole)	7.4	Liver (fetal)	0.5
Brain (amygdala)	4.3	Liver ca. (hepatoblast) HepG2	0.0
Brain (cerebellum)	3.4	Lung	2.0
Brain (hippocampus)	13.0	Lung (fetal)	5.0
Brain (substantia nigra)	1.1	Lung ca. (small cell) LX-1	5.8
Brain (thalamus)	8.0	Lung ca. (small cell) NCI-H69	23.8
Cerebral Cortex	100.0	Lung ca. (s.cell var.) SHP-77	9.0
Spinal cord	6.1	Lung ca. (large cell)NCI-H460	6.3
glio/astro U87-MG	0.9	Lung ca. (non-sm. cell) A549	13.4
glio/astro U-118-MG	3.8	Lung ca. (non-s.cell) NCI-H23	32.8
astrocytoma SW1783	0.4	Lung ca. (non-s.cell) HOP-62	2.1
neuro*; met SK-N-AS	57.0	Lung ca. (non-s.cl) NCI-H522	0.0
astrocytoma SF-539	0.0	Lung ca. (squam.) SW 900	3.3
astrocytoma SNB-75	3.3	Lung ca. (squam.) NCI-H596	12.1
glioma SNB-19	0.6	Mammary gland	0.6
glioma U251	8.5	Breast ca.* (pl.ef) MCF-7	0.0
glioma SF-295	0.8	Breast ca.* (pl.ef) MDA-MB-231	0.0
Heart (fetal)	4.1	Breast ca.* (pl.ef) T47D	0.5
Heart	1.3	Breast ca. BT-549	0.0
Skeletal muscle (fetal)	28.7	Breast ca. MDA-N	0.0
Skeletal muscle	0.8	Ovary	13.8
Bone marrow	0.7	Ovarian ca. OVCAR-3	1.1
Thymus	0.3	Ovarian ca. OVCAR-4	0.0
Spleen	2.5	Ovarian ca. OVCAR-5	5.4
Lymph node	1.3	Ovarian ca. OVCAR-8	2.5
Colorectal	4.0	Ovarian ca. IGROV-1	2.7
Stomach	1.1	Ovarian ca.* (ascites) SK-OV-3	1.2
Small intestine	1.8	Uterus	3.8
Colon ca. SW480	0.0	Placenta	36.6
Colon ca.* SW620(SW480 met)	0.0	Prostate	2.0
Colon ca. HT29	0.0	Prostate ca.* (bone met)PC-3	0.2
Colon ca. HCT-116	0.0	Testis	1.0
Colon ca. CaCo-2	0.0	Melanoma Hs688(A).T	0.0
Colon ca. tissue(ODO3866)	1.4	Melanoma* (met) Hs688(B).T	0.0
Colon ca. HCC-2998	1.5	Melanoma UACC-62	0.0
Gastric ca.* (liver met) NCI-N87	11.0	Melanoma M14	0.0
Bladder	3.8	Melanoma LOX IMVI	0.0
Trachea	1.3	Melanoma* (met) SK-MEL-5	7.5
Kidney	7.4	Adipose	6.2

[1040]

TABLE AKG
Panel 2D
	Rel.		Rel.
	Exp (%)		Exp. (%)
	Ag815,		Ag815,
	Run		Run
Tissue Name	144791433	Tissue Name	144791433
Normal Colon	5.8	Kidney Margin 8120608	7.0
CC Well to Mod Diff (ODO3866)	1.6	Kidney Cancer 8120613	100.0
CC Margin (ODO3866)	1.1	Kidney Margin 8120614	14.0
CC Gr.2 rectosigmoid (ODO3868)	0.6	Kidney Cancer 9010320	8.2
CC Margin (ODO3868)	0.8	Kidney Margin 9010321	24.7
CC Mod Diff (ODO3920)	0.3	Normal Uterus	6.6
CC Margin (ODO3920)	1.9	Uterus Cancer 064011	10.8
CC Gr.2 ascend colon (ODO3921)	1.8	Normal Thyroid	2.6
CC Margin (ODO3921)	0.7	Thyroid Cancer 064010	4.1
CC from Partial Hepatectomy	1.6	Thyroid Cancer A302152	2.8
(ODO4309) Mets
Liver Margin (ODO4309)	1.3	Thyroid Margin A302153	2.9
Colon mets to lung (ODO4451-01)	0.4	Normal Breast	3.5
Lung Margin (ODO4451-02)	3.1	Breast Cancer (ODO4566)	1.0
Normal Prostate 6546-1	2.5	Breast Cancer (ODO4590-01)	2.3
Prostate Cancer (ODO4410)	13.7	Breast Cancer Mets	3.7
		(ODO4590-03)
Prostate Margin (ODO4410)	10.4	Breast Cancer Metastasis	0.9
		(ODO4655-05)
Prostate Cancer (ODO4720-01)	5.8	Breast Cancer 064006	1.4
Prostate Margin (ODO4720-02)	12.9	Breast Cancer 1024	1.4
Normal Lung 061010	3.2	Breast Cancer 9100266	1.3
Lung Met to Muscle (ODO4286)	0.6	Breast Margin 9100265	0.8
Muscle Margin (ODO4286)	1.0	Breast Cancer A209073	3.0
Lung Malignant Cancer (ODO3126)	11.7	Breast Margin A209073	3.1
Lung Margin (ODO3126)	5.0	Normal Liver	0.9
Lung Cancer (ODO4404)	1.3	Liver Cancer 064003	1.0
Lung Margin (ODO4404)	6.9	Liver Cancer 1025	0.8
Lung Cancer (ODO4565)	0.7	Liver Cancer 1026	2.5
Lung Margin (ODO4565)	3.2	Liver Cancer 6004-T	1.5
Lung Cancer (ODO4237-01)	20.6	Liver Tissue 6004-N	0.3
Lung Margin (ODO4237-02)	5.4	Liver Cancer 6005-T	1.4
Ocular Mel Met to Liver	0.1	Liver Tissue 6005-N	0.5
(ODO4310)
Liver Margin (ODO4310)	1.1	Normal Bladder	3.8
Melanoma Mets to Lung	0.3	Bladder Cancer 1023	0.4
(ODO4321)
Lung Margin (ODO4321)	12.2	Bladder Cancer A302173	2.2
Normal Kidney	81.2	Bladder Cancer (ODO4718-01)	0.6
Kidney Ca, Nuclear grade 2	22.5	Bladder Normal Adjacent	12.6
(ODO4338)		(ODO4718-03)
Kidney Margin (ODO4338)	29.7	Normal Ovary	1.0
Kidney Ca Nuclear grade ≡1/2≢	15.1	Ovarian Cancer 064008	7.7
(ODO4339)
Kidney Margin (ODO4339)	46.3	Ovarian Cancer (ODO4768-07)	0.4
Kidney Ca, Clear cell type	7.2	Ovary Margin (ODO4768-08)	4.9
(ODO4340)
Kidney Margin (ODO4340)	41.5	Normal Stomach	2.8
Kidney Ca, Nuclear grade 3	5.5	Gastric Cancer 9060358	1.0
(ODO4348)
Kidney Margin (ODO4348)	32.3	Stomach Margin 9060359	1.1
Kidney Cancer (ODO4622-01)	4.6	Gastric Cancer 9060395	1.8
Kidney Margin (ODO4622-03)	5.3	Stomach Margin 9060394	0.5
Kidney Cancer (ODO4450-01)	12.6	Gastric Cancer 9060397	0.9
Kidney Margin (ODO4450-03)	37.9	Stomach Margin 9060396	0.1
Kidney Cancer 8120607	0.9	Gastric Cancer 064005	1.9

[1041]

TABLE AKH
Panel 3D
	Rel.		Rel.
	Exp. (%)		Exp. (%)
	Ag815,		Ag815,
	Run		Run
Tissue Name	164886712	Tissue Name	164886712
Daoy- Medulloblastoma	1.9	Ca Ski- Cervical epidermoid	0.0
		carcinoma (metastasis)
TE671- Medulloblastoma	0.3	ES-2- Ovarian clear cell carcinoma	0.0
D283 Med- Medulloblastoma	0.0	Ramos- Stimulated with	0.4
		PMA/ionomycin 6h
PFSK-1- Primitive	0.4	Ramos- Stimulated with	0.5
Neuroectodermal		PMA/ionomycin 14h
XF-498-CNS	0.0	MEG-01- Chronic myelogenous	0.0
		leukemia (megokaryoblast)
SNB-78- Glioma	0.0	Raji- Burkitt's lymphoma	0.0
SF-268- Glioblastoma	0.3	Daudi- Burkitt's lymphoma	0.4
T98G- Glioblastoma	0.0	U2o6- B-cell plasmacytoma	8.1
SK-N-SH- Neuroblastoma	39.0	CA46- Burkitt's lymphoma	0.0
(metastasis)
SF-295- Glioblastoma	0.3	RL- non-Hodgkin's B-cell	0.5
		lymphoma
Cerebellum	22.4	JM1- pre-B-cell lymphoma	0.0
Cerebellum	3.6	Jurkat- T cell leukemia	0.0
NCI-H292- Mucoepidermoid	0.5	TF-1- Erythroleukemia	0.0
lung carcinoma
DMS-114- Small cell lung	12.7	HUT 78- T-cell lymphoma	0.7
cancer
DMS-79- Small cell lung cancer	0.0	U937- Histiocytic lymphoma	0.7
NCI-H146- Small cell lung	9.5	KU-812- Myelogenous leukemia	0.0
NCI-H526- Small cell lung	28.7	769-P- Clear cell renal carcinoma	0.0
cancer
NCI-N417- Small cell lung	55.1	Caki-2- Clear cell renal carcinoma	2.0
cancer
NCI-H82- Small cell lung cancer	0.7	SW 839- Clear cell renal carcinoma	0.0
NCI-H157- Squamous cell lung	0.0	G401- Wilm's tumor	0.0
cancer (metastasis)
NCI-H1155- Large cell lung	71.2	Hs766T- Pancreatic carcinoma (LN	53.6
cancer		metastasis)
NCI-H1299- Large cell lung	0.2	CAPAN-1- Pancreatic	28.5
cancer		adenocarcinoma (liver metastasis)
NCI-H727- Lung carcinoid	7.2	SU86.86- Pancreatic carcinoma	4.6
		(liver metastasis)
NCI-UMC-11- Lung carcinoid	100.0	BxPC-3- Pancreatic	0.0
		adenocarcinoma
LX-1- Small cell lung cancer	0.0	HPAC- Pancreatic adenocarcinoma	10.2
Colo-205- Colon cancer	0.0	MIA PaCa-2- Pancreatic carcinoma	15.6
KM12- Colon cancer	0.0	CFPAC-1- Pancreatic ductal	6.1
		adenocarcinoma
KM20L2- Colon cancer	0.0	PANC-1- Pancreatic epithelioid	51.1
		ductal carcinoma
NCI-H716- Colon cancer	70.2	T24- Bladder carcinma (transitional	0.7
		cell)
SW-48- Colon adenocarcinoma	0.0	5637- Bladder carcinoma	0.0
SW1116- Colon adenocarcinoma	0.3	HT-1197- Bladder carcinoma	0.5
LS 174T- Colon	0.4	UM-UC-3- Bladder carcinma	0.0
adenocarcinoma		(transitional cell)
SW-948- Colon adenocarcinoma	0.0	A204- Rhabdomyosarcoma	0.0
SW-480- Colon adenocarcinoma	0.0	HT-1080-Fibrosarcoma	0.0
NCI-SNU-5- Gastric carcinoma	0.1	MG-63- Osteosarcoma	0.0
KATO III- Gastric carcinoma	1.1	SK-LMS-1- Leiomyosarcoma	0.3
		(vulva)
NCI-SNU-16- Gastric carcinoma	2.2	SJRH30- Rhabdomyosarcoma (met	0.0
		to bone marrow)
NCI-SNU-1- Gastric carcinoma	0.6	A431- Epidermoid carcinoma	0.0
RF-1- Gastric adenocarcinoma	0.0	WM266-4- Melanoma	1.7
RF-48- Gastric adenocarcinoma	0.0	DU 145- Prostate carcinoma (brain	0.0
		metastasis)
MKN-45- Gastric carcinoma	0.0	MDA-MB-468- Breast	1.7
		adenocarcinoma
NCI-N87- Gastric carcinoma	0.0	SCC-4- Squamous cell carcinoma of	0.0
		tongue
OVCAR-5- Ovarian carcinoma	2.1	SCC-9- Squamous cell carcinoma of	0.0
		tongue
RL95-2- Uterine carcinoma	27.2	SCC-15- Squamous cell carcinoma	0.0
		of tongue
HelaS3- Cervical	0.0	CAL27- Squamous cell carcinoma	0.0
adenocarcinoma		of tongue

[1042]

TABLE AM
Panel 4D
	Rel.	Rel.		Rel.	Rel.
	Exp. (%)	Exp. (%)		Exp. (%)	Exp. (%)
	Ag815,	Ag815,		Ag815,	Ag815,
	Run	Run		Run	Run
Tissue Name	145703150	145918553	Tissue Name	145703150	145918553
Secondary Th1 act	0.0	0.0	HUVEC IL-1beta	3.5	10.1
Secondary Th2 act	0.0	0.0	HUVEC IFN gamma	42.6	72.7
Secondary Tr1 act	0.0	0.0	HUVEC TNF alpha +	0.6	3.2
			IFN gamma
Secondary Th1 rest	0.0	0.0	HUVEC TNF alpha +	2.1	5.3
			IL4
Secondary Th2 rest	0.0	0.0	HUVEC IL-11	10.3	22.4
Secondary Tr1 rest	0.0	0.0	Lung Microvascular	15.0	31.9
			EC none
Primary Th1 act	0.0	0.0	Lung Microvascular	3.3	16.2
			EC TNFalpha +
			IL-1beta
Primary Th2 act	0.0	0.0	Microvascular	58.6	68.3
			Dermal EC none
Primary Tr1 act	0.0	0.0	Microvascular	5.9	13.9
			Dermal EC
			TNFalpha + IL-1beta
Primary Th1 rest	0.0	0.4	Bronchial epithelium	0.1	0.0
			TNFalpha + IL1beta
Primary Th2 rest	0.2	0.7	Small airway	0.2	0.0
			epithelium none
Primary Tr1 rest	0.0	0.0	Small airway	0.1	0.0
			epithelium TNFalpha +
			IL-1beta
CD45RA CD4	0.0	0.0	Coronery artery SMC	0.3	1.0
lymphocyte act			rest
CD45RO CD4	0.0	0.0	Coronery artery SMC	0.0	0.2
lymphocyte act			TNFalpha + IL-1beta
CD8 lymphocyte act	0.0	0.0	Astrocytes rest	0.0	0.0
Secondary CD8	0.0	0.0	Astrocytes TNFalpha +	0.2	0.1
lymphocyte rest			IL-1beta
Secondary CD8	0.0	0.0	KU-812 (Basophil)	0.1	0.2
lymphocyte act			rest
CD4 lymphocyte none	0.1	0.1	KU-812 (Basophil)	0.0	0.1
			PMA-ionomycin
2ry	0.1	0.0	CCD1106	0.0	0.0
Th1/Th2/Tr1_anti-CD95	0.1	0.0	(Keratinocytes) none
CH11
LAK cells rest	0.0	0.0	CCD1106	0.0	0.0
			(Keratinocytes)
			TNFalpha + IL-1beta
LAK cells IL-2	0.0	0.0	Liver cirrhosis	2.9	8.9
LAK cells IL-2 + IL-12	0.0	0.0	Lupus kidney	8.7	9.3
LAK cells IL-2 + IFN	0.0	0.2	NCI-H292 none	0.0	0.3
gamma
LAK cells IL-2 + IL-18	0.1	0.0	NCI-H292 IL-4	0.0	0.0
LAK cells	0.0	0.0	NCI-H292 IL-9	0.0	0.0
PMA-ionomycin
NK Cells IL-2 rest	0.0	0.0	NCI-H292 IL-13	0.0	0.0
Two Way MLR 3 day	0.0	0.2	NCI-H292 IFN	0.1	0.0
			gamma
Two Way MLR 5 day	0.0	0.0	HPAEC none	15.6	24.7
Two Way MLR 7 day	0.0	0.0	HPAEC TNF alpha +	2.8	5.0
			IL-1 beta
PBMC rest	0.3	0.4	Lung fibroblast none	0.5	1.5
PBMC PWM	0.0	0.0	Lung fibroblast TNF	0.0	0.2
			alpha + IL-1 beta
PBMC PHA-L	0.0	0.0	Lung fibroblast IL-4	0.3	0.7
Ramos (B cell) none	0.2	0.0	Lung fibroblast IL-9	0.0	1.0
Ramos (B cell)	0.2	0.6	Lung fibroblast IL-13	0.5	0.3
ionomycin
B lymphocytes PWM	0.5	0.1	Lung fibroblat IFN	0.1	0.7
			gamma
B lymphocytes CD40L	0.0	0.0	Dermal fibroblast	0.0	0.0
and IL-4			CCD1070 rest
EOL-1 dbcAMP	0.2	2.0	Dermal fibroblast	0.0	0.0
			CCD1070 TNF alpha
EOL-1 dbcAMP	0.0	0.5	Dermal fibroblast	0.0	0.0
PMA-ionomycin			CCD 1070 IL-1 beta
Dendritic cells none	0.0	0.0	Dermal fibroblast	0.0	0.2
			IFN gamma
Dendritic cells LPS	0.0	0.0	Dermal fibroblast	0.1	0.0
			IL-4
Dendritic cells	0.0	0.0	IBD Colitis 2	0.3	0.5
anti-CD40
Monocytes rest	0.0	0.0	IBD Crohn's	0.7	0.2
Monocytes LPS	0.0	0.0	Colon	1.0	5.3
Macrophages rest	0.0	0.0	Lung	6.9	14.7
Macrophages LPS	0.0	0.0	Thymus	100.0	100.0
HUVEC none	4.9	11.6	Kidney	1.1	3.0
HUVEC starved	16.0	30.6

[1043]

TABLE AKJ
Panel 5 Islet
	Rel. Exp.		Rel. Exp.
	(%) Ag815,		(%) Ag815,
	Run		Run
Tissue Name	254387842	Tissue Name	254387842
97457_Patient-02go_adipose	21.2	94709_Donor 2 AM—A_adipose	0.0
97476_Patient-07sk_skeletal muscle	2.7	94710_Donor 2 AM—B_adipose	0.0
97477_Patient-07ut_uterus	8.5	94711_Donor 2 AM—C_adipose	0.0
97478_Patient-07pl_placenta	100.0	94712_Donor 2 AD—A_adipose	0.1
99167_Bayer Patient 1	0.5	94713_Donor 2 AD—B_adipose	0.4
97482_Patient-08ut_uterus	3.4	94714_Donor 2 AD—C_adipose	0.2
97483_Patient-08pl_placenta	39.5	94742_Donor 3 U—A_Mesenchymal Stem Cells	0.0
97486_Patient-09sk_skeletal muscle	0.2	94743_Donor 3 U—B_Mesenchymal Stem Cells	0.0
97487_Patient-09ut_uterus	3.1	94730_Donor 3 AM—A_adipose	0.2
97488_Patient-09pl_placenta	26.2	94731_Donor 3 AM—B_adipose	0.1
97492_Patient-10ut_uterus	9.2	94732_Donor 3 AM—C_adipose	0.0
97493_Patient-10pl_placenta	89.5	94733_Donor 3 AD—A_adipose	0.3
97495_Patient-11go_adipose	8.5	94734_Donor 3 AD—B_adipose	0.2
97496_Patient-11sk_skeletal muscle	0.4	94735_Donor 3 AD—C_adipose	0.0
97497_Patient-11ut_uterus	12.2	77138_Liver_HepG2untreated	0.0
97498_Patient-11pl_placenta	72.7	73556_Heart_Cardiac stromal cells (primary)	4.2
97500_Patient-12go_adipose	17.0	81735_Small Intestine	1.9
97501_Patient-12sk_skeletal muscle	1.0	72409_Kidney_Proximal Convoluted Tubule	0.9
97502_Patient-12ut_uterus	5.8	82685_Small intestine_Duodenum	0.6
97503_Patient-12pl_placenta	54.0	90650_Adrenal_Adrenocortical adenoma	1.1
94721_Donor 2 U—A_Mesenchymal Stem Cells	0.0	72410_Kidney_HRCE	2.1
94722_Donor 2 U—B_Mesenchymal Stem Cells	0.0	72411_Kidney_HRE	6.7
94723_Donor 2 U—C_Mesenchymal Stem Cells	0.0	73139_Uterus_Uterine smooth muscle cells	1.4

[1044] AI_comprehensive panel_v1.0 Summary: Ag815 Highest expression of this gene is detected in control sample for ulcerative colitis (CT=27.6). This gene shows a widespread expression in this panel. Moderate to low levels of expression of this gene are detected in samples derived from normal and orthoarthitis/rheumatoid arthritis bone, cartilage, synovium and synovial fluid samples, normal lung, COPD lung, emphysema, atopic asthma, asthma, allergy, Crohn's disease (normal matched control and diseased), ulcerative colitis (normal matched control and diseased), and psoriasis (normal matched control and diseased). Therefore, therapeutic modulation of this gene product may ameliorate symptoms/conditions associated with autoimmune and inflammatory disorders including psoriasis, allergy, asthma, inflammatory bowel disease, rheumatoid arthritis and osteoarthritis.

[1045] The amp plot of another experiment (run 249247531) indicates that there were experimental difficulties with this run; therefore, no conclusions can be drawn from this data.

[1046] Panel 1 Summary: Ag127 Highest expression of this gene is detected in placenta (CT=25.4). High expression of this gene is also seen in testis and uterus. Therefore, therapeutic modulation of this gene may be useful in the treatment of reproductive disorders and fertility.

[1047] Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, melanoma, gastric, colon, lung, breast, ovarian, and brain cancers. Thus, therapeutic modulation of the expression or function of this gene or its protein product through the use of small molecule drug or antibodies may be effective in the treatment of pancreatic, gastric, colon, lung, breast, ovarian, and brain cancers.

[1048] Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adrenal gland, thyroid, pituitary gland, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[1049] In addition, this gene is expressed at moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer's disease, Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[1050] Panel 1.2 Summary: Ag815 Two experiments with same probe and primer are in good agreement. Highest expression of this gene is detected in placenta and cerebral cortex (CTs=24-25.6). In addition, expression of this gene is seen in brain, tissues with metabolic/endocrine functions such as pancreas, adrenal gland, thyroid, pituitary gland, heart, liver and the gastrointestinal tract, endothelial cells and in cancer cell lines derived from gastric, colon, lung, breast, ovarian, and brain cancers. This pattern correlates to expression seen in panel 1. Please see panel 1 for further discussion on the utility of this gene.

[1051] Panel 1.3D Summary: Ag815 Highest expression of this gene is detected in cerebral cortex (CTs=27.4). In addition, expression of this gene is seen in brain, tissues with metabolic/endocrine functions such as adipose, pancreas, adrenal gland, thyroid, pituitary gland, heart, liver and the gastrointestinal tract, endothelial cells and in cancer cell lines derived from gastric, colon, lung, ovarian, and brain cancers. This pattern correlates to expression seen in panel 1. Please see panel 1 for further discussion on the utility of this gene.

[1052] Significant expression of this gene is also detected in fetal skeletal muscle. Interestingly, this gene is expressed at much higher levels in fetal (CT=29) when compared to adult skeletal muscle (CT=34). This observation suggests that expression of this gene can be used to distinguish fetal from adult skeletal muscle. In addition, the relative overexpression of this gene in fetal skeletal muscle suggests that the protein product may enhance muscular growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the GPCR encoded by this gene could be useful in treatment of muscle related diseases. More specifically, treatment of weak or dystrophic muscle with the protein encoded by this gene could restore muscle mass or function.

[1053] Panel 2D Summary: Ag815 Highest expression of this gene is detected in a kidney cancer (CT=28.3). Interestingly, expression of this gene is strongly associated with normal kidney samples as compared to kidney cancers. In addition, moderate to low levels of expression of this gene is also seen in colon, prostate, lung, breast, liver, bladder, ovarian, gastric and stomach cancers. Therefore, therapeutic modulation of this gene or its protein product through the use of antibodies and small molecule drug may be useful in the treatment of kidney, colon, prostate, lung, breast, liver, bladder, ovarian, gastric and stomach cancers.

[1054] Panel 3D Summary: Ag815 Highest expression of this gene is detected in a lung cancer cell line (CT=29.6). Moderate levels of expression of this gene is also seen in number of cell lines derived from lung, pancreatic, uterine, brain and colon cancers. Therefore, expression of this gene may be used as marker to detect the presence of these cancers. Furthermore, therapeutic modulation of this gene may be useful in the treatment of these cancers.

[1055] Panel 4D Summary: Ag815 Two experiments with same probe-primer sets are in good agreement. Highest expression of this gene is detected in thymus (CTs-27.7-28). Moderate levels of expression of this gene are also seen in endothelials cells including HUVEC, lung and dermal microvascular EC cells, and HPEAC cells. In addition, moderate to low levels of expression of this gene is also seen in liver cirrhosis, lupus kidney and normal colon, lung and kidney samples. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these endothelial cells and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, osteoarthritis and liver cirrhosis.

[1056] Panel 5 Islet Summary: Ag815 Highest expression of this gene is detected in placenta of a non-diabetic and obese patient (CT=28). Moderate levels of expression of this gene are mainly seen in placenta, uterus, adipose, kidney and small intestine of diabetic and non-diabetic patients. Please see panel 1 for further discussion on the utility of this gene.

[1057] AL. CG57209-02 and CG57209-03: EMR1 Hormone Receptor

[1058] Expression of gene CG57209-02 was assessed using the primer-probe set Ag6343, described in Table ALA. Results of the RTQ-PCR runs are shown in Tables ALB, ALC, ALD, ALE and ALF.

TABLE ALA
Probe Name Ag6343
			Start	SEQ ID
Primers	Sequence	Length	Position No
Forward	5′-caaataaataacatcttcagcgttct-3′	26	1003	362
Probe	TET-5′-cggtcgttttattttcacacactttgtcc-3′-TAMRA	29	1029	363
Reverse	5′-ctctcagttgtattcttcagagaaacta-3′	28	1058	364

[1059]

TABLE ALB
AI_comprehensive panel_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag6343,		(%) Ag6343,
	Run		Run
Tissue Name	276596900	Tissue Name	276596900
110967 COPD-F	1.4	112427 Match Control	5.4
		Psoriasis-F
110980 COPD-F	2.2	112418 Psoriasis-M	2.5
110968 COPD-M	1.7	112723 Match Control	0.3
		Psoriasis-M
110977 COPD-M	6.7	112419 Psoriasis-M	3.4
110989	4.5	112424 Match Control	0.6
Emphysema-F		Psoriasis-M
110992	2.2	112420 Psoriasis-M	14.2
Emphysema-F
110993	1.1	112425 Match Control	6.4
Emphysema-F		Psoriasis-M
110994	2.1	104689 (MF) OA	31.0
Emphysema-F		Bone-Backus
110995	8.4	104690 (MF) Adj	15.5
Emphysema-F		“Normal” Bone-
		Backus
110996	0.5	104691 (MF) OA	3.9
Emphysema-F		Synovium-Backus
110997 Asthma-M	3.8	104692 (BA) OA	0.0
		Cartilage-Backus
111001 Asthma-F	1.7	104694 (BA) OA	9.2
		Bone-Backus
111002 Asthma-F	1.9	104695 (BA) Adj	10.0
		“Normal” Bone-
		Backus
111003 Atopic	1.4	104696 (BA) OA	8.4
Asthma-F		Synovium-Backus
111004 Atopic	0.9	104700 (SS) OA	100.0
Asthma-F		Bone-Backus
111005 Atopic	0.4	104701 (SS) Adj	14.4
Asthma-F		“Normal” Bone-
		Backus
111006 Atopic	0.4	104702 (SS) OA	10.7
Asthma-F		Synovium-Backus
111417 Allergy-M	0.7	117093 OA Cartilage	5.5
		Rep7
112347 Allergy-M	0.0	112672 OA Bone5	23.7
112349 Normal	0.0	112673 OA	6.8
Lung-F		Synovium5
112357 Normal	1.2	112674 OA Synovial	12.2
Lung-F		Fluid cells5
112354 Normal	0.9	117100 OA Cartilage	3.8
Lung-M		Rep14
112374 Crohns-F	3.8	112756 OA Bone9	6.0
112389 Match	0.2	112757 OA	0.7
Control Crohns-F		Synovium9
112375 Crohns-F	6.1	112758 OA Synovial	4.5
		Fluid Cells9
112732 Match	17.4	117125 RA Cartilage	2.6
Control Crohns-F		Rep2
112725 Crohns-M	0.3	113492 Bone2 RA	42.6
112387 Match	1.6	113493 Synovium2	14.9
Control Crohns-M		RA
112378 Crohns-M	0.0	113494 Syn Fluid	26.8
		Cells RA
112390 Match	1.9	113499 Cartilage4 RA	30.1
Control Crohns-M
112726 Crohns-M	1.4	113500 Bone4 RA	29.9
112731 Match	1.9	113501 Synovium4	18.2
Control Crohns-M		RA
112380 Ulcer Col-F	2.5	113502 Syn Fluid	15.1
		Cells4 RA
112734 Match	43.2	113495 Cartilage3 RA	21.5
Control Ulcer Col-F
112384 Ulcer Col-F	10.1	113496 Bone3 RA	25.2
112737 Match	1.6	113497 Synovium3	11.7
Control Ulcer Col-F		RA
112386 Ulcer Col-F	3.6	113498 Syn Fluid	42.9
		Cells3 RA
112738 Match	8.8	117106 Normal	0.3
Control Ulcer Col-F		Cartilage Rep20
112381 Ulcer	0.2	113663 Bone3 Normal	0.0
Col-M
112735 Match	0.8	113664 Synovium3	0.0
Control Ulcer		Normal
Col-M
112382 Ulcer	1.2	113665 Syn Fluid	0.0
Col-M		Cells3 Normal
112394 Match	0.7	117107 Normal	0.8
Control Ulcer		Cartilage Rep22
Col-M
112383 Ulcer	7.3	113667 Bone4 Normal	1.6
Col-M
112736 Match	0.0	113668 Synovium4	1.5
Control Ulcer		Normal
Col-M
112423 Psoriasis-F	11.3	113669 Syn Fluid	1.4
		Cells4 Normal

[1060]

TABLE ALC
CNS_neurodegeneration_v1.0
	Rel. Exp.		Rel. Exp.
	(%) Ag6343,		(%) Ag6343,
	Run		Run
Tissue Name	269225500	issue Name	269225500
AD 1 Hippo	12.4	Control (Path) 3	0.0
		Temporal Ctx
AD 2 Hippo	2.7	Control (Path) 4	3.0
		Temporal Ctx
AD 3 Hippo	0.0	AD 1 Occipital Ctx	14.1
AD 4 Hippo	0.0	AD 2 Occipital Ctx	0.0
		(Missing)
AD 5 Hippo	13.3	AD 3 Occipital Ctx	0.8
AD 6 Hippo	100.0	AD 4 Occipital Ctx	0.0
Control 2 Hippo	0.0	AD 5 Occipital Ctx	21.6
Control 4 Hippo	0.0	AD 6 Occipital Ctx	0.0
Control (Path) 3	3.4	Control 1 Occipital	6.6
Hippo		Ctx
AD 1 Temporal Ctx	21.3	Control 2 Occipital	5.7
		Ctx
AD 2 Temporal Ctx	0.0	Control 3 Occipital	2.4
		Ctx
AD 3 Temporal Ctx	3.4	Control 4 Occipital	3.8
		Ctx
AD 4 Temporal Ctx	3.2	Control (Path) 1	0.0
		Occipital Ctx
AD 5 Inf Temporal	0.0	Control (Path) 2	0.0
Ctx		Occipital Ctx
AD 5 Sup Temporal	14.1	Control (Path) 3	6.5
Ctx		Occipital Ctx
AD 6 Inf Temporal	97.3	Control (Path) 4	0.0
Ctx		Occipital Ctx
AD 6 Sup Temporal	50.0	Control 1 Parietal Ctx	10.7
Ctx
Control 1 Temporal	2.8	Control 2 Parietal Ctx	6.9
Ctx
Control 2 Temporal	1.2	Control 3 Parietal Ctx	10.0
Ctx
Control 3 Temporal	12.9	Control (Path) 1	0.0
Ctx		Parietal Ctx
Control 4 Temporal	0.0	Control (Path) 2	3.5
Ctx		Parietal Ctx
Control (Path) 1	0.0	Control (Path) 3	0.0
Temporal Ctx		Parietal Ctx
Control (Path) 2	2.9	Control (Path) 4	0.0
Temporal Ctx		Parietal Ctx

[1061]

TABLE ALD
General_screening_panel_v1.5
	Rel. Exp.		Rel. Exp.
	(%) Ag6343,		(%) Ag6343,
	Run		Run
Tissue Name	259476287	issue Name	259476287
Adipose	12.2	Renal ca. TK-10	3.6
Melanoma*	0.0	Bladder	16.2
Hs688(A).T
Melanoma*	0.0	Gastric ca. (liver met.)	0.0
Hs688(B).T		NCI-N87
Melanoma* M14	0.0	Gastric ca. KATO III	0.0
Melanoma*	0.0	Colon ca. SW-948	0.0
LOXIMVI
Melanoma*	0.0	Colon ca. SW480	0.0
SK-MEL-5
Squamous cell	0.0	Colon ca.* (SW480	0.0
carcinoma SCC-4		met) SW620
Testis Pool	16.0	Colon ca. HT29	0.0
Prostate ca.* (bone	0.0	Colon ca. HCT-116	1.9
met) PC-3
Prostate Pool	1.0	Colon ca. CaCo-2	0.0
Placenta	15.5	Colon cancer tissue	15.8
Uterus Pool	4.0	Colon ca. SW1116	0.0
Ovarian ca.	1.3	Colon ca. Colo-205	0.0
OVCAR-3
Ovarian ca.	0.0	Colon ca. SW-48	0.0
SK-OV-3
Ovarian ca.	0.0	Colon Pool	1.8
OVCAR-4
Ovarian ca.	0.0	Small Intestine Pool	0.0
OVCAR-5
Ovarian ca.	0.0	Stomach Pool	0.0
IGROV-1
Ovarian ca.	0.0	Bone Marrow Pool	5.3
OVCAR-8
Ovary	4.1	Fetal Heart	3.8
Breast ca. MCF-7	0.0	Heart Pool	0.0
Breast ca.	0.0	Lymph Node Pool	3.3
MDA-MB-231
Breast ca. BT 549	0.0	Fetal Skeletal Muscle	1.1
Breast ca. T47D	0.0	Skeletal Muscle Pool	1.8
Breast ca. MDA-N	0.0	Spleen Pool	100.0
Breast Pool	3.0	Thymus Pool	22.1
Trachea	5.4	CNS cancer (glio/	0.0
		astro) U87-MG
Lung	0.0	CNS cancer (glio/	0.0
		astro) U-118-MG
Fetal Lung	34.4	CNS cancer (neuro;	0.0
		met) SK-N-AS
Lung ca. NCI-N417	0.0	CNS cancer (astro)	0.0
		SF-539
Lung ca. LX-1	0.0	CNS cancer (astro)	0.0
		SNB-75
Lung ca. NCI-H146	0.0	CNS cancer (glio)	0.0
		SNB-19
Lung ca. SHP-77	0.0	CNS cancer (glio)	0.0
		SF-295
Lung ca. A549	1.1	Brain (Amygdala)	0.0
		Pool
Lung ca. NCI-H526	0.0	Brain (cerebellum)	6.5
Lung ca. NCI-H23	0.0	Brain (fetal)	1.1
Lung ca. NCI-H460	0.0	Brain (Hippocampus)	3.0
		Pool
Lung ca. HOP-62	0.0	Cerebral Cortex Pool	2.6
Lung ca. NCI-H522	0.0	Brain (Substantia	3.0
		nigra) Pool
Liver	14.4	Brain (Thalamus) Pool	0.7
Fetal Liver	81.8	Brain (whole)	11.8
Liver ca. HepG2	0.0	Spinal Cord Pool	5.4
Kidney Pool	7.3	Adrenal Gland	12.1
Fetal Kidney	1.4	Pituitary gland Pool	2.4
Renal ca. 786-0	1.0	Salivary Gland	4.0
Renal ca. A498	1.0	Thyroid (female)	1.3
Renal ca. ACHN	0.0	Pancreatic ca.	0.0
		CAPAN2
Renal ca. UO-31	0.5	Pancreas Pool	4.9

[1062]

TABLE ALE
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(% Ag6343,		(%) Ag6343,
	Run		Run
Tissue Name	264776502	Tissue Name	264776502
Secondary Th1 act	0.0	HUVEC IL-1beta	0.0
Secondary Th2 act	0.0	HUVEC IFN gamma	0.0
Secondary Tr1 act	0.1	HUVEC TNF alpha +	0.0
		IFN gamma
Secondary Th1 rest	0.3	HUVEC TNF alpha +	0.0
		IL4
Secondary Th2 rest	0.2	HUVEC IL-11	0.0
Secondary Tr1 rest	0.1	Lung Microvascular	0.0
		EC none
Primary Th1 act	0.1	Lung Microvascular	0.0
		EC TNFalpha +
		IL-1beta
Primary Th2 act	0.5	Microvascular Dermal	0.0
		EC none
Primary Tr1 act	0.4	Microsvasular Dermal	0.0
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	0.1	Bronchial epithelium	0.0
		TNFalpha + IL-1beta
Primary Th2 rest	0.2	Small airway	0.0
		epithelium none
Primary Tr1 rest	0.0	Small airway	0.0
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	0.5	Coronery artery SMC	0.0
lymphocyte act		rest
CD45RO CD4	1.4	Coronery artery SMC	0.0
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	0.2	Astrocytes rest	0.0
Secondary CD8	0.5	Astrocytes	0.0
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	0.0	KU-812 (Basophil)	0.0
lymphocyte act		rest
CD4 lymphocyte	0.8	KU-812 (Basophil)	0.0
none		PMA/ionomycin
2ry Th1/Th2/	0.0	CCD1106	0.0
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	0.1	CCD1106	0.0
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	0.2	Liver cirrhosis	0.1
LAK cells IL-2 +	0.0	NCI-H292 none	0.0
IL-12
LAK cells IL-2 +	0.0	NCI-H292 IL-4	0.0
IFN gamma
LAK cells IL-2 +	0.1	NCI-H292 IL-9	0.0
IL-18
LAK cells PMA/	0.3	NCI-H292 IL-13	0.0
ionomycin
NK Cells IL-2 rest	0.2	NCI-H292 IFN gamma	0.0
Two Way MLR 3	0.9	HPAEC none	0.0
day
Two Way MLR 5	0.1	HPAEC TNF alpha +	0.0
day		IL-1 beta
Two Way MLR 7	0.0	Lung fibroblast	0.0
day		none
PBMC rest	1.0	Lung fibroblast TNF	0.0
		alpha + IL-1 beta
PBMC PWM	1.1	Lung fibroblast IL-4	0.0
PBMC PHA-L	0.5	Lung fibroblast IL-9	0.0
Ramos (B cell) none	0.0	Lung fibroblast IL-13	0.0
Ramos (B cell)	0.0	Lung fibroblast IFN	0.0
ionomycin		gamma
B lymphocytes	0.1	Dermal fibroblast	0.0
PWM		CCD1070 rest
B lymphocytes	0.2	Dermal fibroblast	0.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	1.6	Dermal fibroblast	0.0
		CCD1070 IL-1 beta
EOL-1 dbcAMP	0.4	Dermal fibroblast IFN	0.0
PMA/ionomycin		gamma
Dendritic cells none	0.0	Dermal fibroblast IL-4	0.0
Dendritic cells LPS	0.3	Dermal Fibroblasts	0.0
		rest
Dendritic cells	0.0	Neutrophils TNFa +	2.9
anti-CD40		LPS
Monocytes rest	5.0	Neutrophils rest	17.0
Monocytes LPS	100.0	Colon	0.2
Macrophages rest	0.2	Lung	0.5
Macrophages LPS	1.4	Thymus	0.4
HUVEC none	0.0	Kidney	0.1
HUVEC starved	0.0

[1063]

TABLE ALF
Panel 5 Islet
	Rel. Exp.		Rel. Exp.
	(%) Ag6343,		(%) Ag6343,
	Run		Run
Tissue Name	259494665	Tissue Name	259494665
97457_Patient-02go_adipose	45.1	94709_Donor 2 AM—A_adipose	0.0
97476_Patient-07sk_skeletal muscle	55.5	94710_Donor 2 AM—B_adipose	0.0
97477_Patient-07ut_uterus	13.8	94711_Donor 2 AM—C_adipose	0.0
97478_Patient-07pl_placenta	61.1	94712_Donor 2 AD—A_adipose	0.0
99167_Bayer Patient 1	0.0	94713_Donor 2 AD—B_adipose	0.0
97482_Patient-08ut_uterus	0.0	94714_Donor 2 AD—C_adipose	0.0
97483_Patient-08pl_placenta	18.2	94742_Donor 3 U—A_Mesenchymal Stem Cells	0.0
97486_Patient-09sk_skeletal muscle	16.7	94743_Donor 3 U—B_Mesenchymal Stem Cells	0.0
97487_Patient-09ut_uterus	0.0	94730_Donor 3 AM—A_adipose	0.0
97488_Patient-09pl_placenta	12.1	94731_Donor 3 AM—B_adipose	0.0
97492_Patient-10ut_uterus	24.1	94732_Donor 3 AM—C_adipose	0.0
97493_Patient-10pl_placenta	34.2	94733_Donor 3 AD—A_adipose	0.0
97495_Patient-11go_adipose	28.9	94734_Donor 3 AD—B_adipose	0.0
97496_Patient-11sk_skeletal muscle	17.0	94735_Donor 3 AD—C_adipose	0.0
97497_Patient-11ut_uterus	15.4	77138_Liver_HepG2untreated	0.0
97498_Patient-11pl_placenta	63.3	73556_Heart_Cardiac stromal cells (primary)	0.0
97500_Patient-12go_adipose	30.8	81735_Small Intestine	0.0
97501_Patient-12sk_skeletal muscle	15.3	72409_Kidney_Proximal Convoluted Tubule	0.0
97502_Patient-12ut_uterus	21.6	82685_Small intestine_Duodenum	100.0
97503_Patient-12pl_placenta	0.0	90650_Adrenal_Adrenocortical adenoma	42.3
94721_Donor 2 U—A_Mesenchymal Stem Cells	0.0	72410_Kidney_HRCE	0.0
94722_Donor 2 U—B_Mesenchymal Stem Cells	0.0	72411_Kidney_HRE	0.0
94723_Donor 2 U—C_Mesenchymal Stem Cells	0.0	73139_Uterus_Uterine smooth muscle cells	0.0

[1064] AI_comprehensive panel_v1.0 Summary: Ag6343 Highest expression of this gene is detected in orthoarthritis (OA) bone (CT=29.3). Low to moderate levels of expression of this gene are detected in samples derived from osteoarthritic (OA) bone and adjacent bone as well as OA cartilage, and OA synovial fluid samples. Moderate level expression is also detected in cartilage, bone, synovium and synovial fluid samples from rheumatoid arthritis patients. No significant expression of this gene is detected in normal samples of cartilage, synovium, bone or synovial fluid cells. Low to moderate level of expression is also seen in samples derived from COPD lung, emphysema, asthma, Crohn's disease (normal matched control and diseased), ulcerative colitis (normal matched control and diseased), and psoriasis (normal matched control and diseased). Therefore, therapeutic modulation of this gene product may ameliorate symptoms/conditions associated with autoimmune and inflammatory disorders including psoriasis, allergy, asthma, inflammatory bowel disease, rheumatoid arthritis and osteoarthritis.

[1065] CNS_neurodegeneration_v1.0 Summary: Ag6343 Highest expression of this gene is detected in hippocampus sample derived from an Alzheimer's patient (CT=32.2). Moderate to low level of expression of this gene is alss seen in some of the temporal cortex of Alzheimer's disease patients. Therefore, therapeutic modulation of this gene may be useful in the treatment of Alzheimer's disease.

[1066] General_screening_panel_v1.5 Summary: Ag6343 Highest expression of this gene is detected in spleen (CT=31.4). Moderate to low levels of expression of this gene is also seen in thymus, fetal lung and fetal liver. These tissues may contain monocytes or monocytic derived cell types. This gene codes for EMR1 hormone receptor precursor (human F4/80 homologue). EMR1 is a member of the family of hormone receptors with seven transmembrane segments. In addition, it has six egf-like modules at the N-terminus separated from the transmembrane segments by a serine/threonine-rich domain, a feature reminiscent of mucin-like, single-span, integral membrane glycoproteins with adhesive properties (Baud et al., 1995, Genomics 26(2):334-44, PMID: 7601460). EMR1 is shown to be abundantly expressed by cells of the myelomonocytic lineage (McKnight A J, Gordon S., 1998, J Leukoc Biol 63(3):271-80, PMID: 9500513). A potential role for EMR3, a member of EMR family of proteins, has suggested in myeloid-myeloid interactions during immune and inflammatory responses. Therefore, therapeutic modulation of the EMR1 encoded by this gene through the use of antibodies directed against this molecule or a small molecule drug could inhibit monocyte activation or extravasation into inflamed tissue and may be important for the treatment of a number of inflammatory diseases including asthma and rheumatoid arthritis.

[1067] Among tissues with metabolic or endocrine function, this gene is expressed at low levels in adipose, adrenal gland, and liver. In addition, expression of this gene has been found to be dysregulated in CuraGen GeneCalling studies. It is upregulated in adipose tissue of mice who develop diabetes and obesity after being fed a high-fat diet. The EMRI receptor encoded by this gene may be involved in a pathway leading to induction and release of TNF-alpha, IL-6 and resistin in adipose tissue. These molecules are known to be involved in the promotion of insulin resistance and are associated with obesity (Holst D, Grimaldi P A, 2002, Curr Opin Lipidol. 13(3):241-5, PMID: 12045392; Greenberg et al., 2002, Eur J Clin Invest. 32 Suppl 3:24-34, PMID: 12028372). Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes, including Type 2 diabetes.

[1068] Interestingly, this gene is expressed at much higher levels in fetal (CTs=31.7-32.9) when compared to adult liver and lung (CTs=3440). This observation suggests that expression of this gene can be used to distinguish fetal from adult tissues. In addition, the relative overexpression of this gene in fetal tissues suggests that the protein product may enhance liver and lung growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver and lung related diseases.

[1069] In addition, this gene is expressed at low levels in whole brain. Therefore, therapeutic modulation of this gene product may be useful in the treatment of neurological disorders such as Alzheimer's disease, Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[1070] Panel 4.1D Summary: Ag6343 Highest expression of this gene is detected in LPS treated monocytes (CT=27.3). Expression of this gene is upregulated in activated monocytes as compared resting monocytes (CT=31.6). Therefore, expression of this gene may be used to distinguish between activated from resting monocytes and other samples used in this panel. The expression of this gene in LPS treated monocytes cells suggests that it plays a crucial role in linking innate immunity to adaptive immunity and also in initiating inflammatory reactions. Low to moderate levels of expression of this gene is also seen in neutrophils, eosinophils, PBMC, two way MLR, activated memory T cells, and CD4 lymphocytes. Therefore, modulation of the this gene or its product through the application of monoclonal antibodies or small molecule drug may reduce or prevent early stages of inflammation and reduce the severity of inflammatory diseases such as psoriasis, asthma, inflammatory bowel disease, rheumatoid arthritis, osteoarthritis and other lung inflammatory diseases. Please see panel 1.5 for further discussion on the utility of this gene.

[1071] Panel 5 Islet Summary: Ag6343 Low expression of this gene is restricted to sample derived from small intestine (CT=34.8). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. Please see panel 1.5 for further discussion on the utility of this gene.

[1072] AM. CG97715-01: Transmembrane Protein PT27

[1073] Expression of full-length physical clone CG97715-01 was assessed using the primer-probe set Ag3840, described in Table AMA. Results of the RTQ-PCR runs are shown in Tables AMB, AMC, AMD, AME and AMF.

TABLE AMA
Probe Name Ag3840
			Start	SEQ ID
Primers	Sequence	Length	Position	No
Forward	5′-attcttagcagaatggggtgat-3′	22	693	365
Probe	TET-5′-cgctctcaactaactacaattgtattggca-3′-TAMRA	30	715	366
Reverse	5′-acaccataggggtcctctctag-3′	22	746	367

[1074]

TABLE AMB
General_screening_panel_v1.4
	Rel. Exp.		Rel. Exp.
	(%) Ag3840,		(%) Ag3840,
	Run		Run
Tissue Name	217312795	issue Name	217312795
Adipose	18.9	Renal ca. TK-10	22.7
Melanoma*	53.2	Bladder	27.5
Hs688(A).T
Melanoma*	56.6	Gastric ca. (liver met.)	59.9
Hs688(B).T		NCI-N87
Melanoma* M14	36.9	Gastric ca. KATO III	69.3
Melanoma*	15.1	Colon ca. SW-948	22.2
LOXIMVI
Melanoma*	29.3	Colon ca. SW480	49.0
SK-MEL-5
Squamous cell	19.3	Colon ca.* (SW480	30.1
carcinoma SCC-4		met) SW620
Testis Pool	8.0	Colon ca. HT29	18.6
Prostate ca.* (bone	35.8	Colon ca. HCT-116	31.2
met) PC-3
Prostate Pool	10.7	Colon ca. CaCo-2	24.1
Placenta	7.1	Colon cancer tissue	35.1
Uterus Pool	6.1	Colon ca. SW1116	12.4
Ovarian ca.	26.6	Colon ca. Colo-205	15.8
OVCAR-3
Ovarian ca.	52.9	Colon ca. SW-48	10.8
SK-OV-3
Ovarian ca.	17.4	Colon Pool	14.4
OVCAR-4
Ovarian ca.	50.7	Small Intestine Pool	8.8
OVCAR-5
Ovarian ca.	48.3	Stomach Pool	9.2
IGROV-1
Ovarian ca.	24.8	Bone Marrow Pool	7.6
OVCAR-8
Ovary	8.1	Fetal Heart	5.3
Breast ca. MCF-7	25.2	Heart Pool	7.2
Breast ca.	80.7	Lymph Node Pool	19.8
MDA-MB-231
Breast ca. BT 549	73.2	Fetal Skeletal Muscle	3.6
Breast ca. T47D	100.0	Skeletal Muscle Pool	5.4
Breast ca. MDA-N	22.2	Spleen Pool	11.8
Breast Pool	14.2	Thymus Pool	12.7
Trachea	11.6	CNS cancer (glio/	51.4
		astro) U87-MG
Lung	3.0	CNS cancer (glio/	81.2
		astro) U-118-MG
Fetal Lung	16.5	CNS cancer (neuro;	31.6
		met) SK-N-AS
Lung ca. NCI-N417	12.8	CNS cancer (astro)	29.9
		SF-539
Lung ca. LX-1	21.3	CNS cancer (astro)	61.6
		SNB-75
Lung ca. NCI-H146	9.9	CNS cancer (glio)	50.3
		SNB-19
Lung ca. SHP-77	34.9	CNS cancer (glio)	61.6
		SF-295
Lung ca. A549	28.1	Brain (Amygdala)	9.9
		Pool
Lung ca. NCI-H526	12.9	Brain (cerebellum)	7.3
Lung ca. NCI-H23	30.4	Brain (fetal)	6.2
Lung ca. NCI-H460	17.9	Brain (Hippocampus)	10.0
		Pool
Lung ca. HOP-62	28.5	Cerebral Cortex Pool	9.8
Lung ca. NCI-H522	5.8	Brain (Substantia	9.0
		nigra) Pool
Liver	0.6	Brain (Thalamus) Pool	13.9
Fetal Liver	9.6	Brain (whole)	6.3
Liver ca. HepG2	7.8	Spinal Cord Pool	12.7
Kidney Pool	18.4	Adrenal Gland	14.1
Fetal Kidney	14.1	Pituitary gland Pool	3.7
Renal ca. 786-0	50.7	Salivary Gland	4.2
Renal ca. A498	13.8	Thyroid (female)	10.6
Renal ca. ACHN	12.5	Pancreatic ca.	48.0
		CAPAN2
Renal ca. UO-31	42.3	Pancreas Pool	33.4

[1075]

TABLE AMC
Oncology_cell_line_screening_panel_v3.1
	Rel. Exp.		Rel. Exp.
	(%) Ag3840,		(%) Ag3840,
	Run		Run
Tissue Name	223130227	Tissue Nme	223130227
Daoy	13.3	Ca Ski_Cervical	50.3
Medulloblastoma/		epidermoid carcinoma
Cerebellum		(metastasis)
TE671	11.7	ES-2_Ovarian clear	20.3
Medulloblastoma/		cell carcinoma
Cerebellum
D283 Med	33.0	Ramos/6h	38.7
Medulloblastoma/		stim_Stimulated with
Cerebellum		PMA/ionomycin 6h
PFSK-1 Primitive	36.1	Ramos/14h	20.4
Neuroectodermal/		stim_Stimulated with
Cerebellum		PMA/ionomycin 14h
XF-498_CNS	69.3	MEG-01_Chronic	75.8
		myelogenous leukemia
		(megokaryoblast)
SNG-78_CNS/	38.7	Raji_Burkitt's	13.8
glioma		lymphoma
SF-268_CNS/	35.4	Daudi_Burkitt's	42.6
glioblastoma		lymphoma
T98G_Glio-	29.3	U266_B-cell	11.6
blastoma		plasmacytoma/
		myeloma
SK-H-SH_Neuro-	37.4	CA46_Burkitt's	14.6
blastoma		lymphoma
(metastasis)
SF-295_CNS/	41.5	RL_non-Hodgkin's	9.5
glioblastoma		B-cell lymphoma
Cerebellum	18.4	JM1_pre-B-cell	11.1
		lymphoma/leukemia
Cerebellum	10.0	Jurkat_T cell	24.0
		leukemia
NCI-H292_Muco-	99.3	TF-1_Erythro-	100.0
epidermoid lung ca.		leukemia
DMS-114_Small	7.5	HUT 78_T-cell	28.3
cell lung cancer		lymphoma
DMS-79_Small cell	13.0	U937_Histiocytic	57.0
cancer/neuro-		lymphoma
endocrine
NCI-H146_Small	35.4	KU-812_Myelo-	66.9
cell lung cancer/		genous leukemia
neuroendocrine
NCI-H526_Small	56.6	769-P_Clear cell renal	39.2
cell lung cancer/		ca.
neuroendocrine
NCI-H417_Small	35.6	Caki-2_Clear cell	28.1
cell lung cancer/		renal ca.
neuroendocrine
NCI-H82_Small	15.1	SW 839_Clear cell	47.6
cell lung cancer/		renal ca.
neuroendocrine
NCI-	37.6	G401_Wilms' tumor	17.0
H157_Squamous
cell lung cancer
(metastasis)
NCI-H1155_Large	49.3	Hs766T_Pancreatic	50.3
cell lung cancer/		ca. (LN metastasis)
neuroendocrine
NCI-H1299_Large	26.2	CAPAN-1_Pancreatic	33.4
cell lung cancer/		adenocarcinoma (liver
neuroendocrine		metastasis)
NCI-H727_Lung	61.6	SU86.86_Pancreatic	52.5
carcinoid		carcinoma (liver
		metastasis)
NCI-UMC-	30.8	BxPC-3_Pancreatic	37.4
11_Lung		adenocarcinoma
carcinoid
LX-1_Small cell	37.9	HPAC_Pancreatic	74.7
lung cancer		adenocarcinoma
Colo-205_Colon	48.3	MIA	5.7
cancer		PaCa-2_Pancreatic ca.
KM12_Colon	71.7	CFPAC-1_Pancreatic	92.7
cancer		ductal adenocarcinoma
KM20L2_Colon	17.8	PANC-1_Pancreatic	41.5
cancer		epithelioid ductal ca.
NCI-H716_Colon	83.5	T24_Bladder ca.	31.4
cancer		(transitional cell)
SW-48_Colon	31.2	5637_Bladder ca.	28.1
adenocarcinoma
SW1116_Colon	12.7	HT-1197_Bladder ca.	51.4
adenocarcinoma
LS 174T_Colon	20.7	UM-UC-3_Bladder	11.7
adenocarcinoma		ca. (transitional cell)
SW-948_Colon	24.8	A204_Rhab-	28.9
adenocarcinoma		domyosarcoma
SW-480_Colon	17.8	HT-1080_Fibro-	39.5
adenocarcinoma		sarcoma
NCI-SNU-	37.4	MG-63_Osteosarcoma	24.8
5_Gastric ca.		(bone)
KATO III_Stomach	41.8	SK-LMS-1_Leiomyo-	71.7
		sarcoma (vulva)
NCI-SNU-	18.2	SJRH30_Rhabdomyo-	32.5
16_Gastric ca.		sarcoma (met to bone
		marrow)
NCI-SNU-	75.8	A431_Epidermoid ca.	35.6
1_Gastric ca.
RF-1_Gastric	19.3	WM266-4_Melanoma	33.4
adenocarcinoma
RF-48_Gastric	21.2	DU 145_Prostate	32.8
adenocarcinoma
MKN-45_Gastric	20.7	MDA-MB-468_Breast	27.9
ca.		adenocarcinoma
NCI-N87_Gastric	51.1	SSC-4_Tongue	18.9
ca.
OVCAR-5_Ovarian	15.0	SSC-9_Tongue	37.4
ca.
RL95-2_Uterine	20.4	SSC-15_Tongue	55.1
carcinoma
HelaS3_Cervical	33.9	CAL 27_Squamous	21.8
adenocarcinoma		cell ca. of tongue

[1076]

TABLE AMD
Panel 4.1D
	Rel. Exp.		Rel. Exp.
	(%) Ag3840,		(%) Ag3840,
	Run		Run
Tissue Name	222546557	Tissue Name	222546557
Secondary Th1 act	41.2	HUVEC IL-1beta	64.6
Secondary Th2 act	41.5	HUVEC IFN gamma	42.6
Secondary Tr1 act	34.2	HUVEC TNF alpha +	40.6
		IFN gamma
Secondary Th1 rest	5.8	HUVEC TNF alpha +	39.0
		IL4
Secondary Th2 rest	9.2	HUVEC IL-11	20.7
Secondary Tr1 rest	5.7	Lung Microvascular	77.4
		EC none
Primary Th1 act	17.1	Lung Microvascular	69.7
		EC TNFalpha +
		IL-1beta
Primary Th2 act	33.7	Microvascular Dermal	34.2
		EC none
Primary Tr1 act	31.6	Microsvasular Dermal	46.7
		EC TNFalpha +
		IL-1beta
Primary Th1 rest	5.2	Bronchial epithelium	39.2
		TNFalpha + IL-1beta
Primary Th2 rest	3.4	Small airway	18.2
		epithelium none
Primary Tr1 rest	12.8	Small airway	69.7
		epithelium
		TNFalpha + IL-1beta
CD45RA CD4	47.0	Coronery artery SMC	47.6
lymphocyte act		rest
CD45RO CD4	36.6	Coronery artery SMC	48.3
lymphocyte act		TNFalpha + IL-1beta
CD8 lymphocyte act	24.8	Astrocytes rest	25.5
Secondary CD8	18.6	Astrocytes	29.1
lymphocyte rest		TNFalpha + IL-1beta
Secondary CD8	7.9	KU-812 (Basophil)	38.2
lymphocyte act		rest
CD4 lymphocyte	2.1	KU-812 (Basophil)	57.4
none		PMA/ionomycin
2ry Th1/Th2/	11.8	CCD1106	43.8
Tr1_anti-CD95		(Keratinocytes) none
CH11
LAK cells rest	27.4	CCD1106	40.3
		(Keratinocytes)
		TNFalpha + IL-1beta
LAK cells IL-2	16.6	Liver cirrhosis	7.4
LAK cells IL-2 +	15.3	NCI-H292 none	31.9
IL-12
LAK cells IL-2 +	10.7	NCI-H292 IL-4	40.6
IFN gamma
LAK cells IL-2 +	19.8	NCI-H292 IL-9	50.3
IL-18
LAK cells PMA/	24.3	NCI-H292 IL-13	47.0
ionomycin
NK Cells IL-2 rest	20.9	NCI-H292 IFN gamma	39.8
Two Way MLR 3	29.1	HPAEC none	21.5
day
Two Way MLR 5	27.4	HPAEC TNF alpha +	100.0
day		IL-1 beta
Two Way MLR 7	17.9	Lung fibroblast	31.9
day		none
PBMC rest	2.3	Lung fibroblast TNF	69.7
		alpha + IL-1 beta
PBMC PWM	31.2	Lung fibroblast IL-4	33.4
PBMC PHA-L	30.4	Lung fibroblast IL-9	52.1
Ramos (B cell) none	26.6	Lung fibroblast IL-13	30.1
Ramos (B cell)	40.1	Lung fibroblast IFN	66.0
ionomycin		gamma
B lymphocytes	20.3	Dermal fibroblast	54.7
PWM		CCD1070 rest
B lymphocytes	19.3	Dermal fibroblast	66.0
CD40L and IL-4		CCD1070 TNF alpha
EOL-1 dbcAMP	31.9	Dermal fibroblast	75.3
		CCD1070 IL-1 beta
EOL-1 dbcAMP	35.4	Dermal fibroblast IFN	29.5
PMA/ionomycin		gamma
Dendritic cells none	39.5	Dermal fibroblast IL-4	39.0
Dendritic cells LPS	49.0	Dermal Fibroblasts	23.8
		rest
Dendritic cells	44.1	Neutrophils TNFa +	3.1
anti-CD40		LPS
Monocytes rest	18.9	Neutrophils rest	5.0
Monocytes LPS	90.1	Colon	5.4
Macrophages rest	35.8	Lung	27.2
Macrophages LPS	28.9	Thymus	10.4
HUVEC none	36.1	Kidney	16.5
HUVEC starved	42.0

[1077]

TABLE AME
Panel 5D
	Rel. Exp.		Rel. Exp.
	(%) Ag380,		(%) Ag3840,
	Run		Run
Tissue Name	169800718	Tissue Name	169800718
97457_Patient-02go_adipose	27.5	94709_Donor 2 AM—A_adipose	100.0
97476_Patient-07sk_skeletal muscle	21.8	94710_Donor 2 AM—B_adipose	58.2
97477_Patient-07ut_uterus	24.5	94711_Donor 2 AM—C_adipose	52.9
97478_Patient-07pl_placenta	29.9	94712_Donor 2 AD—A_adipose	40.9
97481_Patient-08sk_skeletal muscle	39.2	94713_Donor 2 AD—B_adipose	48.6
97482_Patient-08ut_uterus	28.3	94714_Donor 2 AD—C_adipose	52.5
97483_Patient-08pl_placenta	32.1	94742_Donor 3 U—A_Mesenchymal Stem Cells	31.0
97486_Patient-09sk_skeletal muscle	8.3	94743_Donor 3 U—B_Mesenchymal Stem Cells	46.0
97487_Patient-09ut_uterus	44.8	94730_Donor 3 AM—A_adipose	94.6
97488_Patient-09pl_placenta	17.6	94731_Donor 3 AM—B_adipose	55.1
97492_Patient-10ut_uterus	47.6	94732_Donor 3 AM—C_adipose	55.1
97493_Patient-10pl_placenta	36.3	94733_Donor 3 AD—A_adipose	100.0
97495_Patient-11go_adipose	11.3	94734_Donor 3 AD—B_adipose	55.1
97496_Patient-11sk_skeletal muscle	7.4	94735_Donor 3 AD—C_adipose	66.9
97497_Patient-11ut_uterus	31.6	77138_Liver_HepG2untreated	45.7
97498_Patient-11pl_placenta	17.3	73556_Heart_Cardiac stromal cells (primary)	12.2
97500_Patient-12go_adipose	29.7	81735_Small Intestine	15.0
97501_Patient-12sk_skeletal muscle	11.6	72409_Kidney_Proximal Convoluted Tubule	22.1
97502_Patient-12ut_uterus	32.5	82685_Small intestine_Duodenum	14.1
97503_Patient-12pl_placenta	15.9	90650_Adrenal_Adrenocortical adenoma	20.2
94721_Donor 2 U—A_Mesenchymal Stem Cells	41.8	72410_Kidney_HRCE	64.2
94722_Donor 2 U—B_Mesenchymal Stem Cells	55.5	72411_Kidney_HRE	38.2
94723_Donor 2 U—C_Mesenchymal Stem Cells	37.9	73139_Uterus_Uterine smooth muscle cells	15.8

[1078]

TABLE AMF
general oncology screening panel v 2.4
	Rel.		Rel.
	Exp. (%)		Exp. (%)
	Ag3840,		Ag3840,
	Run		Run
Tissue Name	268036414	Tissue Nme	268036414
Colon cancer 1	35.6	Bladder cancer	1.7
		NAT 2
Colon cancer NAT 1	16.0	Bladder cancer	2.6
		NAT 3
Colon cancer 2	88.9	Bladder cancer	4.5
		NAT 4
Colon cancer NAT 2	16.5	Prostate	49.3
		adenocarcinoma 1
Colon cancer 3	77.4	Prostate	6.6
		adenocarcinoma 2
Colon cancer NAT 3	29.1	Prostate	24.3
		adenocarcinoma 3
Colon malignant	100.0	Prostate	25.2
cancer 4		adenocarcinoma 4
Colon normal	8.5	Prostate cancer	8.9
adjacent tissue 4		NAT 5
Lung cancer 1	45.7	Prostate	9.7
		adenocarcinoma 6
Lung NAT 1	4.7	Prostate	14.2
		adenocarcinoma 7
Lung cancer 2	75.8	Prostate	3.4
		adenocarcinoma 8
Lung NAT 2	8.4	Prostate	47.6
		adenocarcinoma 9
Squamous cell	46.0	Prostate cancer	5.3
carcinoma 3		NAT 10
Lung NAT 3	4.4	Kidney cancer 1	24.7
metastatic melanoma 1	14.2	Kidney NAT 1	7.6
Melanoma 2	4.4	Kidney cancer 2	62.9
Melanoma 3	4.8	Kidney NAT 2	23.5
metastatic melanoma 4	39.8	Kidney cancer 3	24.0
metastatic melanoma 5	50.3	Kidney NAT 3	4.1
Bladder cancer 1	7.5	Kidney cancer 4	18.4
Bladder cancer NAT 1	0.0	Kidney NAT 4	8.5
Bladder cancer 2	19.3

[1079] General_screening_panel_v1.4 Summary: Ag3840 Highest expression of this gene is detected in a breast cancer T47D cell line (CT=25.3). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, liver, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of pancreatic, gastric, colon, lung, liver, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[1080] Among tissues with metabolic or endocrine function, this gene is expressed at moderate to high levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.

[1081] In addition, this gene is expressed at high levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer's disease, Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[1082] Interestingly, this gene is expressed at much higher levels in fetal (CT=28.7) when compared to adult liver (CT=32.7). This observation suggests that expression of this gene can be used to distinguish fetal from adult liver. In addition, the relative overexpression of this gene in fetal tissue suggests that the protein product may enhance liver growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver related diseases.

[1083] Oncology_cell_line_screening_panel_v3.1 Summary: Ag3840 Highest expression of this gene is detected in a erythroleukemia TF-1 cell line (CT=26.6). This gene shows a widespread expression in all the cancer cell line and normal tissues in this panel. This pattern is in agreement with the expression profile in General_screening_panel_v1.4 and also suggests a role for the gene product in cell survival and proliferation. Please see panel 1.4 for further discussion on the utility of this gene.

[1084] Panel 4.1D Summary: Ag3840 Highest expression of this gene is detected in TNF alpha and IL-1 beta treated HPAEC cells (CT=27.8). This gene is expressed at high to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is in agreement with the expression profile in General_screening_panel_v1.4 and also suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.

[1085] Panel 5D Summary: Ag3840 Highest expression of this gene is detected in a midway differentiated and differentiated adipose tissue (CTs=29.4). This gene shows a widespread expression in this panel, which correlates to pattern seen in panel 1.4. Please see panel 1.4 for further discussion on the utility of this gene.

[1086] general oncology screening panel_v—2.4 Summary: Ag3840 Highest expression of this gene is detected in a malignant colon cancer sample (CT=26.6). Expression of this gene is seen in both normal and cancer samples derived from colon, lung, melanoma, bladder, prostate and kidney. Interestingly, expression of this gene is consistently higher in the cancer samples as compared to the corresponding normal adjacent tissues. Therefore, expression of this gene may be used as diagnostic marker to detect the presence of colon, lung, bladder, prostate and kidney cancers. Furthermore, therapeutic modulation of this gene or its protein product may be useful in the treatment of colon, lung, melanoma, bladder, prostate and kidney cancers.

Example D

Identification of Single Nucleotide Polymorphisms in NOVX Nucleic Acid Sequences

[1087] Variant sequences are also included in this application. A variant sequence can include a single nucleotide polymorphism (SNP). A SNP can, in some instances, be referred to as a “cSNP” to denote that the nucleotide sequence containing the SNP originates as a cDNA. A SNP can arise in several ways. For example, a SNP may be due to a substitution of one nucleotide for another at the polymorphic site. Such a substitution can be either a transition or a transversion. A SNP can also arise from a deletion of a nucleotide or an insertion of a nucleotide, relative to a reference allele. In this case, the polymorphic site is a site at which one allele bears a gap with respect to a particular nucleotide in another allele. SNPs occurring within genes may result in an alteration of the amino acid encoded by the gene at the position of the SNP. Intragenic SNPs may also be silent, when a codon including a SNP encodes the same amino acid as a result of the redundancy of the genetic code. SNPs occurring outside the region of a gene, or in an intron within a gene, do not result in changes in any amino acid sequence of a protein but may result in altered regulation of the expression pattern. Examples include alteration in temporal expression, physiological response regulation, cell type expression regulation, intensity of expression, and stability of transcribed message.

[1088] SeqCalling assemblies produced by the exon linking process were selected and extended using the following criteria. Genomic clones having regions with 98% identity to all or part of the initial or extended sequence were identified by BLASTN searches using the relevant sequence to query human genomic databases. The genomic clones that resulted were selected for further analysis because this identity indicates that these clones contain the genomic locus for these SeqCalling assemblies. These sequences were analyzed for putative coding regions as well as for similarity to the known DNA and protein sequences. Programs used for these analyses include Grail, Genscan, BLAST, UMMER, FASTA, Hybrid and other relevant programs.

[1089] Some additional genomic regions may have also been identified because selected SeqCalling assemblies map to those regions. Such SeqCalling sequences may have overlapped with regions defined by homology or exon prediction. They may also be included because the location of the fragment was in the vicinity of genomic regions identified by similarity or exon prediction that had been included in the original predicted sequence. The sequence so identified was manually assembled and then may have been extended using one or more additional sequences taken from CuraGen Corporation's human SeqCalling database. SeqCalling fragments suitable for inclusion were identified by the CuraTools™ program SeqExtend or by identifying SeqCalling fragments mapping to the appropriate regions of the genomic clones analyzed.

[1090] The regions defined by the procedures described above were then manually integrated and corrected for apparent inconsistencies that may have arisen, for example, from miscalled bases in the original fragments or from discrepancies between predicted exon junctions, EST locations and regions of sequence similarity, to derive the final sequence disclosed herein. When necessary, the process to identify and analyze SeqCalling assemblies and genomic clones was reiterated to derive the full length sequence (Alderborn et al., Determination of Single Nucleotide Polymorphisms by Real-time Pyrophosphate DNA Sequencing. Genome Research. 10 (8) 1249-1265, 2000).

[1091] Variants are reported individually but any combination of all or a select subset of variants are also included as contemplated NOVX embodiments of the invention.

[1092] NOV1a SNP Data:

[1093] NOV1a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:1 and 2, respectively. The nucleotide sequence of the NOV1a variant differs as shown in Table 51A.

TABLE 51A
data for NOV1a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381211	2786	T	G	829	Ile	Ser

[1094] NOV2b SNP Data:

[1095] NOV2b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:5 and 6, respectively. The nucleotide sequence of the NOV2b variant differs as shown in Table 51B.

TABLE 51b
data for NOV2b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381047	516	T	C	148	Asn	Asn
13381110	1479	G	A	469	Gln	Gln
13381109	1542	C	T	490	Asp	Asp
13381108	1751	A	G	560	Asn	Ser
13381107	1821	C	T	583	Ile	Ile
13381106	3702	C	T	0
13381105	3971	C	T	0
13381104	4111	G	A	0
13381103	4141	G	A	0
13381102	4198	C	T	0

[1096] NOV4c SNP Data:

[1097] NOV4c has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:21 and 22, respectively. The nucleotide sequence of the NOV4c variant differs as shown in Table 51C.

TABLE 51c
data for NOV4c
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13380816	440	A	G	147	Ile	Val
13380815	511	A	G	170	Thr	Thr

[1098] NOV5b SNP Data:

[1099] NOV5b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:27 and 28, respectively. The nucleotide sequence of the NOV5b variant differs as shown in Table 51D.

TABLE 51D
data for NOV5b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381095	372	C	A	97	Ser	Ser
13381096	465	C	T	128	Pro	Pro
13381097	1797	C	T	572	Cys	Cys
13381098	1845	T	C	588	Tyr	Tyr
13381062	2254	T	C	0
13381063	2474	A	T	0
13381100	2593	A	G	0
13381101	2697	C	A	0
13381064	3183	T	C	0
13381065	3352	G	A	0
13381066	3541	C	T	0

[1100] NOV6b SNP Data: NOV6b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:31 and 32, respectively. The nucleotide sequence of the NOV6b variant differs as shown in Table 51E.

TABLE 51E
data for NOV6b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381083	168	T	C	6	Phe	Leu
13381202	181	T	C	10	Leu	Pro
13381084	359	C	A	69	Leu	Leu
13381085	539	A	G	129	Glu	Glu
13381086	545	G	A	131	Gln	Gln
13381087	566	C	T	138	Val	Val
13381088	658	A	T	169	Asn	Ile
13381092	786	T	C	212	Cys	Arg
13381093	908	T	C	252	Cys	Cys
13381094	933	T	C	261	Ser	Pro

[1101] NOV8b SNP Data:

[1102] NOV8b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:39 and 40, respectively. The nucleotide sequence of the NOV8b variant differs as shown in Table 51F.

TABLE 51F
data for NOV8b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381053	770	G	A	257	Arg	Lys
13381052	965	C	T	322	Ser	Phe
13381051	1047	T	C	349	Gly	Gly

[1103] NOV10a SNP Data:

[1104] NOV10a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:45 and 46, respectively. The nucleotide sequence of the NOV10a variant differs as shown in Table 51G.

TABLE 51G
data for NOV10a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381212	700	C	T	193	Ser	Phe
13381213	1445	A	G	0
13381214	1449	A	G	0
13381215	1461	G	T	0
13380817	1463	A	G	0
13381217	1591	C	T	0
13381218	1601	C	A	0

[1105] NOV14b SNP Data:

[1106] NOV14b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:57 and 58, respectively. The nucleotide sequence of the NOV14b variant differs as shown in Table 51H.

TABLE 51H
data for NOV14b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381055	323	G	C	102	Glu	Gln
13377369	324	A	G	102	Glu	Gly

[1107] NOV15a SNP Data:

[1108] NOV15a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:59 and 60, respectively. The nucleotide sequence of the NOV15a variant differs as shown in Table 51I.

TABLE 51I
data for NOV15a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381041	360	T	C	114	Cys	Arg

[1109] NOV17a SNP Data:

[1110] NOV17a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:71 and 72, respectively. The nucleotide sequence of the NOV17a variant differs as shown in Table 51J.

TABLE 51J
data for NOV17a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381195	38	C	A	0
13381227	474	A	G	139	Thr	Thr

[1111] NOV20a SNP Data:

[1112] NOV20a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:85 and 86, respectively. The nucleotide sequence of the NOV20a variant differs as shown in Table 51K.

TABLE 51K
data for NOV20a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381060	1716	A	G	567	Pro	Pro

[1113] NOV21a SNP Data:

[1114] NOV21a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:89 and 90, respectively. The nucleotide sequence of the NOV21a variant differs as shown in Table 51L.

TABLE 51L
data for NOV21a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381080	6069	T	G	2018	Asn	Lys
13381079	7885	G	A	2624	Asp	Asn
13381225	8295	C	T	2760	Phe	Phe
13381078	8365	A	G	2784	Asn	Asp

[1115] NOV24a SNP Data:

[1116] NOV24a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:95 and 96, respectively. The nucleotide sequence of the NOV24a variant differs as shown in Table 51M.

TABLE 51M
data for NOV24a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381045	439	T	C	78	Trp	Arg
13381262	736	A	G	177	Thr	Ala

[1117] NOV27b SNP Data:

[1118] NOV27b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:111 and 112, respectively. The nucleotide sequence of the NOV27b variant differs as shown in Table 51N

TABLE 51N
data for NOV27b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381221	824	T	C	262	Phe	Ser

[1119] NOV28a SNP Data:

[1120] NOV28a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:113 and 114, respectively. The nucleotide sequence of the NOV28a variant differs as shown in Table 51O

TABLE 51O
data for NOV28a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381251	285	C	T	85	Cys	Cys
13381250	341	G	T	104	Gly	Val
13381249	501	C	T	157	Thr	Thr

[1121] NOV29a SNP Data:

[1122] NOV29a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:117 and 118, respectively. The nucleotide sequence of the NOV29a variant differs as shown in Table 51P

TABLE 51P
data for NOV29a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381050	406	G	T	95	Val	Val

[1123] NOV30a SNP Data:

[1124] NOV30a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:119 and 120, respectively. The nucleotide sequence of the NOV30a variant differs as shown in Table 51Q

TABLE 51Q
data for NOV30a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381049	1469	A	T	487	Gln	Leu
13381048	1857	A	G	616	Ile	Met

[1125] NOV32a SNP Data:

[1126] NOV32a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:123 and 124, respectively. The nucleotide sequence of the NOV32a variant differs as shown in Table 51R

TABLE 51R
data for NOV32a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381112	369	C	G	118	Ala	Ala

[1127] NOV32b SNP Data:

[1128] NOV32b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:125 and 126, respectively. The nucleotide sequence of the NOV32b variant differs as shown in Table 51S

TABLE 51S
data for NOV32b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13380823	113	A	G	23	Asn	Asp
13380824	1491	A	G	482	Tyr	Cys
13377028	1596	T	C	517	Val	Ala
13381208	1900	G	T	0
13381207	2002	G	A	0
13381206	2012	T	C	0
13381205	2132	A	G	0

[1129] NOV39b has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:149 and 150, respectively. The nucleotide sequence of the NOV39b variant differs as shown in Table 51T

TABLE 51T
data for NOV39b
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381198	359	A	G	118	Ala	Ala
13381239	581	C	T	192	Leu	Leu
13381238	582	A	G	193	Asn	Asp
13381199	615	A	G	204	Lys	Glu
13381237	625	C	T	207	Ala	Val
13381236	631	T	C	209	Leu	Pro
13381235	705	G	A	234	Val	Met
13381234	714	A	G	237	Met	Val
13381232	777	T	C	258	Leu	Leu
13381231	821	G	A	272	Arg	Arg

[1130] NOV42a SNP Data:

[1131] NOV42a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:155 and 156, respectively. The nucleotide sequence of the NOV42a variant differs as shown in Table 51U

TABLE 51U
data for NOV42a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381081	341	C	T	75	Arg	Cys
13381242	1661	G	A	0
13381241	1678	C	T	0

[1132] NOV43a SNP Data:

[1133] NOV43a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:157 and 158, respectively. The nucleotide sequence of the NOV43a variant differs as shown in Table 51V

TABLE 51V
data for NOV43a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381056	113	C	T	33	Thr	Ile
13381057	166	C	T	51	Leu	Phe
13381058	290	G	A	92	Gly	Glu
13381061	1485	T	C	490	Asp	Asp

[1134] NOV44a SNP Data:

[1135] NOV44a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:159 and 160, respectively. The nucleotide sequence of the NOV44a variant differs as shown in Table 51W

TABLE 51W
data for NOV44a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381043	319	A	G	75	Arg	Gly
13381075	351	A	G	85	Gly	Gly
13381074	603	T	C	169	Thr	Thr
13881073	862	C	T	256	Leu	Leu

[1136] NOV47d SNP Data:

[1137] NOV47d has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:181 and 182, respectively. The nucleotide sequence of the NOV47d variant differs as shown in Table 51X

TABLE 51X
data for NOV47d
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381257	213	C	T	65	Pro	Pro
13375569	1316	C	T	433	Thr	Lie
13375568	1441	C	T	475	Mg	Cys
13375567	1545	G	A	509	Ala	Ala
13375566	1558	G	A	514	Asp	Asn
13375572	4235	A	G	1406	Tyr	Cys
13381256	4342	C	T	1442	Pro	Ser
13377613	4402	A	G	1462	Thr	Ala
13381255	4658	A	G	0

[1138] NOV48c SNP Data:

[1139] NOV48c has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:205 and 206, respectively. The nucleotide sequence of the NOV48c variant differs as shown in Table 51Y

TABLE 51Y
data for NOV48c
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13380257	118	A	G	40	Thr	Ala
13380253	842	T	C	281	Val	Ala
13380743	1435	C	A	479	Gln	Lys
13380741	1714	G	A	572	Val	Ile

[1140] NOV50a SNP Data:

[1141] NOV50a has one SNP variant, whose variant positions for its nucleotide and amino acid sequences is numbered according to SEQ ID NOs:213 and 214, respectively. The nucleotide sequence of the NOV50a variant differs as shown in Table 51Z

TABLE 51Z
data for NOV50a
	Nucleotides	Amino Acids
Variant	Position	Initial	Modified	Position	Initial	Modified
13381219	132	T	C	44	Pro	Pro
13375293	180	A	G	60	Thr	Thr
13381220	243	C	T	81	Ile	Ile
13374623	494	G	A	165	Gly	Asp
13375691	713	A	G	238	Asp	Gly

Other Embodiments

[1142] Although particular embodiments have been disclosed herein in detail, this has been done by way of example for purposes of illustration only, and is not intended to be limiting with respect to the scope of the appended claims, which follow. In particular, it is contemplated by the inventors that various substitutions, alterations, and modifications may be made to the invention without departing from the spirit and scope of the invention as defined by the claims. The choice of nucleic acid starting material, clone of interest, or library type is believed to be a matter of routine for a person of ordinary skill in the art with knowledge of the embodiments described herein. Other aspects, advantages, and modifications considered to be within the scope of the following claims. The claims presented are representative of the inventions disclosed herein. Other, unclaimed inventions are also contemplated. Applicants reserve the right to pursue such inventions in later claims.

Claims

1. An isolated polypeptide comprising the mature form of an amino acid sequenced selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

2. An isolated polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

3. An isolated polypeptide comprising an amino acid sequence which is at least 95% identical to an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

4. An isolated polypeptide, wherein the polypeptide comprises an amino acid sequence comprising one or more conservative substitutions in the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

5. The polypeptide of claim 1 wherein said polypeptide is naturally occurring.

6. A composition comprising the polypeptide of claim 1 and a carrier.

7. A kit comprising, in one or more containers, the composition of claim 6.

8. The use of a therapeutic in the manufacture of a medicament for treating a syndrome associated with a human disease, the disease selected from a pathology associated with the polypeptide of claim 1, wherein the therapeutic comprises the polypeptide of claim 1.

9. A method for determining the presence or amount of the polypeptide of claim 1 in a sample, the method comprising: (a) providing said sample; (b) introducing said sample to an antibody that binds immunospecifically to the polypeptide; and (c) determining the presence of amount of antibody bound to said polypeptide, thereby determining the presence or amount of polypeptide in said sample.

10. A method for determining the presence of or predisposition to a disease associated with altered levels of expression of the polypeptide of claim 1 in a first mammalian subject, the method comprising: a) measuring the level of expression of the polypeptide in a sample from the first mammalian subject; and b) comparing the expression of said polypeptide in the sample of step (a) to the expression of the polypeptide present in a control sample from a second mammalian subject known not to have, or not to be predisposed to, said disease, wherein an alteration in the level of expression of the polypeptide in the first subject as compared to the control sample indicates the presence of or predisposition to said disease.

11. A method of identifying an agent that binds to the polypeptide of claim 1, the method comprising: (a) introducing said polypeptide to said agent; and (b) determining whether said agent binds to said polypeptide.

12. The method of claim 11 wherein the agent is a cellular receptor or a downstream effector.

13. A method for identifying a potential therapeutic agent for use in treatment of a pathology, wherein the pathology is related to aberrant expression or aberrant physiological interactions of the polypeptide of claim 1, the method comprising: (a) providing a cell expressing the polypeptide of claim 1 and having a property or function ascribable to the polypeptide; (b) contacting the cell with a composition comprising a candidate substance; and (c) determining whether the substance alters the property or function ascribable to the polypeptide; whereby, if an alteration observed in the presence of the substance is not observed when the cell is contacted with a composition in the absence of the substance, the substance is identified as a potential therapeutic agent.

14. A method for screening for a modulator of activity of or of latency or predisposition to a pathology associated with the polypeptide of claim 1, said method comprising: (a) administering a test compound to a test animal at increased risk for a pathology associated with the polypeptide of claim 1, wherein said test animal recombinantly expresses the polypeptide of claim 1;(b) measuring the activity of said polypeptide in said test animal after administering the compound of step (a); and (c) comparing the activity of said polypeptide in said test animal with the activity of said polypeptide in a control animal not administered said polypeptide, wherein a change in the activity of said polypeptide in said test animal relative to said control animal indicates the test compound is a modulator activity of or latency or predisposition to, a pathology associated with the polypeptide of claim 1.

15. The method of claim 14, wherein said test animal is a recombinant test animal that expresses a test protein transgene or expresses said transgene under the control of a promoter at an increased level relative to a wild-type test animal, and wherein said promoter is not the native gene promoter of said transgene.

16. A method for modulating the activity of the polypeptide of claim 1, the method comprising contacting a cell sample expressing the polypeptide of claim 1 with a compound that binds to said polypeptide in an amount sufficient to modulate the activity of the polypeptide.

17. A method of treating or preventing a pathology associated with the polypeptide of claim 1, the method comprising administering the polypeptide of claim 1 to a subject in which such treatment or prevention is desired in an amount sufficient to treat or prevent the pathology in the subject.

18. The method of claim 17, wherein the subject is a human.

19. A method of treating a pathological state in a mammal, the method comprising administering to the mammal a polypeptide in an amount that is sufficient to alleviate the pathological state, wherein the polypeptide is a polypeptide having an amino acid sequence at least 95% identical to a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107 or a biologically active fragment thereof.

20. An isolated nucleic acid molecule comprising a nucleic acid sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107.

21. The nucleic acid molecule of claim 20, wherein the nucleic acid molecule is naturally occurring.

22. A nucleic acid molecule, wherein the nucleic acid molecule differs by a single nucleotide from a nucleic acid sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 107.

23. An isolated nucleic acid molecule encoding the mature form of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO:2n, wherein n is an integer between 1 and 107.

24. An isolated nucleic acid molecule comprising a nucleic acid selected from the group consisting of 2n-1, wherein n is an integer between 1 and 107.

25. The nucleic acid molecule of claim 20, wherein said nucleic acid molecule hybridizes under stringent conditions to the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n-1, wherein n is an integer between 1 and 107, or a complement of said nucleotide sequence.

26. A vector comprising the nucleic acid molecule of claim 20.

27. The vector of claim 26, further comprising a promoter operably linked to said nucleic acid molecule.

28. A cell comprising the vector of claim 26.

29. An antibody that immunospecifically binds to the polypeptide of claim 1.

30. The antibody of claim 29, wherein the antibody is a monoclonal antibody.

31. The antibody of claim 29, wherein the antibody is a humanized antibody.

32. A method for determining the presence or amount of the nucleic acid molecule of claim 20 in a sample, the method comprising: (a) providing said sample; (b) introducing said sample to a probe that binds to said nucleic acid molecule; and (c) determining the presence or amount of said probe bound to said nucleic acid molecule, thereby determining the presence or amount of the nucleic acid molecule in said sample.

33. The method of claim 32 wherein presence or amount of the nucleic acid molecule is used as a marker for cell or tissue type.

34. The method of claim 33 wherein the cell or tissue type is cancerous.

35. A method for determining the presence of or predisposition to a disease associated with altered levels of expression of the nucleic acid molecule of claim 20 in a first mammalian subject, the method comprising: a) measuring the level of expression of the nucleic acid in a sample from the first mammalian subject; and b) comparing the level of expression of said nucleic acid in the sample of step (a) to the level of expression of the nucleic acid present in a control sample from a second mammalian subject known not to have or not be predisposed to, the disease; wherein an alteration in the level of expression of the nucleic acid in the first subject as compared to the control sample indicates the presence of or predisposition to the disease.

36. A method of producing the polypeptide of claim 1, the method comprising culturing a cell under conditions that lead to expression of the polypeptide, wherein said cell comprises a vector comprising an isolated nucleic acid molecule comprising a nucleic acid sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107.

37. The method of claim 36 wherein the cell is a bacterial cell.

38. The method of claim 36 wherein the cell is an insect cell.

39. The method of claim 36 wherein the cell is a yeast cell.

40. The method of claim 36 wherein the cell is a mammalian cell.

41. A method of producing the polypeptide of claim 2, the method comprising culturing a cell under conditions that lead to expression of the polypeptide, wherein said cell comprises a vector comprising an isolated nucleic acid molecule comprising a nucleic acid sequence selected from the group consisting of SEQ ID NO:2n−1, wherein n is an integer between 1 and 107.

42. The method of claim 41 wherein the cell is a bacterial cell.

43. The method of claim 41 wherein the cell is an insect cell.

44. The method of claim 41 wherein the cell is a yeast cell.

45. The method of claim 41 wherein the cell is a mammalian cell.