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 102. 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 102, 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 102. 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 102 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 102, 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 102. 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 102. 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

[0013] SEQ ID NO: 2n, wherein n is an integer between 1 and 102 and a pharmaceutically acceptable carrier. In another embodiment, the invention involves a kit, including, in one or more containers, this pharmaceutical composition.

[0014] 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 102 wherein said therapeutic is the polypeptide selected from this group.

[0015] 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 102 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.

[0016] 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 102 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.

[0017] 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 102, 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.

[0018] 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 102, 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.

[0019] 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 102, 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.

[0020] 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 102, 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.

[0021] 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 102, 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.

[0022] 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 102 or a biologically active fragment thereof.

[0023] 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 102; 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 102 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 102; 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 102, 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 102 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.

[0024] 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 102, wherein the nucleic acid molecule comprises the nucleotide sequence of a naturally occurring allelic nucleic acid variant.

[0025] 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 102 that encodes a variant polypeptide, wherein the variant polypeptide has the polypeptide sequence of a naturally occurring polypeptide variant.

[0026] 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 102, 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 102.

[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 102, 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 102; 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 102 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 102; 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 102 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.

[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 102, 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 102, or a complement of the nucleotide sequence.

[0029] 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 102, 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.

[0030] 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 102. This vector can have a promoter operably linked to the nucleic acid molecule. This vector can be located within a cell.

[0031] 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 102 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.

[0032] 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 102 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.

[0033] 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.

[0034] 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.

[0035] 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.

[0036] 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.

[0037] Other features and advantages of the invention will be apparent from the following detailed description and claims.

DETAILED DESCRIPTION OF THE INVENTION

[0038] 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 arc 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 ID NO	SEQ ID NO
NOVX	Internal	(nucleic	(amino
Assignment	Identification	acid)	acid)	Homology
1a	CG113254-01	1	2	Fibrillin like
				homo sapiens
1b	CG113254-02	3	4	Fibrillin like
				homo sapiens
1c	211648303	5	6	Fibulin
1d	212170920	7	8	Fibulin
2a	CG122729-01	9	10	FAN like homo
				sapiens
3a	CG122777-01	11	12	P-type trefoil
				domain containing
				protein like homo
				sapiens
4a	CG124229-01	13	14	Insulin-like
				growth factor binding
				protien 3
				like homo sapiens
5a	CG124445-02	15	16	transmembrane
				kuzbanian like homo
				sapiens
6a	CG124590-02	17	18	Integrin Beta 4
				like homo sapiens
7a	CG124916-01	19	20	Selenoprotein P
				like homo sapiens
8a	CG126224-01	21	22	Type II Membrane
				Protein with C2
				domains like homo
				sapiens
9a	CG126233-01	23	24	CTL2 PROTEIN like
				homo sapiens
1Oa	CG126600-01	25	26	Fibronectin type
				III Domain-Membrane
				Protein like homo
				sapiens
11a	CG127888-01	27	28	Secretory Protein
				like homo sapiens
12a	CG128249-02	29	30	EPHRIN-A4 like
				homo sapiens
13a	CG128785-01	31	32	Alternatively
				spliced SPUF like
				homo sapiens
14a	CG129005-01	33	34	54TM like homo
				sapiens
15a	CG132086-01	35	36	Membrane Protein
				containing Alanine
				dehydrogenase and
				pyridine nucleotide
				transhydrogenase
				domain like homo
				sapiens
16a	CG132297-01	37	38	Elastin like homo
				sapiens
16b	CG132297-02	39	40	Elastin like homo
				sapiens
17a	CG132343-01	41	42	transmembrane protein
				like homo sapiens
18a	CG132423-01	43	44	PREGNANCY-SPECIFIC
				BETA-1-GLYCOPROTEIN
				2 like homo sapiens
18b	225029377	45	46	Pregnancy Specific
				Beta-1 Glycoprotein 2
				Precursor
19a	CG132541-01	47	48	Cadherin like
				homo sapiens
19b	CG132541-02	49	50	Cadherin
20a	CG132888-02	51	52	M130 Antigen like
				homo sapiens
21a	CG133159-01	53	54	EGF like domain
				and Vacuolar sorting
				protein 9 (VPS9)
				domain containing like
				homo sapiens
22a	CG133508-01	55	56	SYNAPTOTAGMIN VI
				like homo sapiens
22b	225171562	57	58	SYNAPTOTAGMIN VI
23a	CG133548-01	59	60	300003P13RIK
				Homolog (TmMP) like
				homo sapiens
23b	CG133548-02	61	62	300003P13RIK
				Homolog (TmMP) like
				homo sapiens
24a	CG133569-01	63	64	Type I membrane
				protein with SH3
				domain like homo
				sapiens
24b	CG133569-02	65	66	Type I membrane
				protein
25a	CG133858-01	67	68	Granulocyte Peptide
				Zgpal like
				homo sapiens
26a	CG134100-01	69	70	Amidase_2 Domain
				like homo sapiens
26b	CG134100-02	71	72	Amidase_2 Domain
				like homo sapiens
27a	CG134403-01	73	74	2510042P03RIK
				Homolog (TmSP) like
				homo sapiens
28a	CG135049-01	75	76	Fetuin-B like
				homo sapiens
28b	CG135049-02	77	78	Fetuin-B like
				homo sapiens
28c	CG135049-03	79	80	Fetuin-B like
				homo sapiens
28d	CG135049-04	81	82	Fetuin-B like
				homo sapiens
28e	CG135049-05	83	84	Fetuin-B like
				homo sapiens
28f	CG135049-06	85	86	Fetuin-B like
				homo sapiens
29a	CG54912-02	87	88
29b	207601301	89	90
29c	207601309	91	92
29d	207601313	93	94
29e	207601331	95	96
29f	207639332	97	98
30a	CG56315-03	99	100	Bioactive Peptide
				Connexin
30b	CG56315-04	101	102	Bioactive Peptide
				Connexin
30c	CC56315-05	103	104	Bioactive Peptide
				Connexin
30d	CG56315-06	105	106	Bioactive Peptide
				Connexin
30e	CG56315-07	107	108	Bioactive Peptide
				Connexin
30f	CG56315-08	109	110	Bioactive Peptide
				Connexin
30g	CG56315-01	111	112	Gap Junction
				Beta-5 Connexin -
				isoform 1
30h	CG56315-02	113	114	Connexin
31a	CG56326-01	115	116
31b	175070268	117	118
32a	CG56711-01	119	120
32b	166280659	121	122
32c	166280667	123	124
32d	166280670	125	126
32e	166280673	127	128
32f	166280680	129	130
32g	166280703	131	132
32h	166280730	133	134
33a	CG57658-02	135	136	Bioactive Peptide
				Connexin
33b	CG57658-03	137	138	Bioactive Peptide
				Connexin
33c	CG57658-04	139	140	Bioactive Peptide
				Connexin
33d	CG57658-05	141	142	Bioactive Peptide
				Connexin
33e	CG57658-06	143	144	Bioactive Peptide
				Connexin
33f	CG57658-07	145	146	Bioactive Peptide
				Connexin
33g	CG57658-01	147	148	Connexin - isoform I
34a	CG57664-02	149	150	Bioactive Peptide
				MHC Class I
34b	CG57664-01	151	152	MHC Class I
				antigen - isoform I
35a	CG57668-02	153	154	Bioactive Peptide
				MHC Class I
35b	CG57668-01	155	156	HLA Class I
				Histocompatibiliy
				antigen - isoform I
36a	CG59256-02	157	158	Bioactive Peptide
				MHC Class I
36b	CG59256-01	159	160	MHC Class I
				antigen - isoform I
37a	CG59437-01	161	162
37b	170108827	163	164
37c	170108863	165	166
38a	CG59739-01	167	168
38b	169679148	169	170
39a	CG94630-02	171	172	Bioactive Peptide
				MHC Class I
39b	CG94630-01	173	174	MHC Class I
				antigen - isoform I
40a	CG95205-02	175	176	TEM-1 like homo
				sapiens

[0039]

TABLE B
Sequences and Corresponding SEQ ID Numbers
		SEQ ID	SEQ ID
		NO	NO
NOVX	Internal	(nucleic	(amino
Assignment	Identification	acid)	acid)	Homology
41a	CG55676-01	177	178	GPCR like
41b	CG55676-02	179	180	GPCR like
41c	CG55676-03	181	182	GPCR like
41d	CG55676-04	183	184	GPCR like
41e	CG55676-05	185	186	GPCR like
41f	CG55676-06	187	188	GPCR like
41g	CG55676-07	189	190	GPCR like
41h	248209538	191	192	GPCR like
41i	248209591	193	194	GPCR like
41j	248209663	195	196	GPCR like
41k	248209745	197	198	GPCR like
42a	CG53677-01	199	200	GPCR like
42b	CG53677-02	201	202	GPCR like
42c	116781634	203	204	GPCR like

[0040] Table A and B indicate 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.

[0041] 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.

[0042] 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.

[0043] 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.

[0044] 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.

[0045] 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.

[0046] Additional utilities for NOVX nucleic acids and polypeptides according to the invention are disclosed herein.

[0047] NOVX Clones

[0048] 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.

[0049] 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.

[0050] 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.

[0051] 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 102; (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 102, 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 102; (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 102 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).

[0052] 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 102; (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 102 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 102; (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 102, 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 102 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.

[0053] 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 102; (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 102 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 102; 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 102 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.

[0054] NOVX Nucleic Acids and Polypeptides

[0055] 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.

[0056] 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.

[0057] 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 many 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.

[0058] 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.

[0059] 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 102, 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 102, 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.)

[0060] 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.

[0061] 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 n is an integer between 1 and 102, or a complement thereof. Oligonucleotides may be chemically synthesized and may also be used as probes.

[0062] 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 102, 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 102, is one that is sufficiently complementary to the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, 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 102, thereby forming a stable duplex.

[0063] 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.

[0064] 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.

[0065] 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.

[0066] 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.

[0067] 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.

[0068] 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 102, as well as a polypeptide possessing NOVX biological activity. Various biological activities of the NOVX proteins are described below.

[0069] 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 bona fide 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.

[0070] 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 102; or an anti-sense strand nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; or of a naturally occurring mutant of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102.

[0071] 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.

[0072] “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 102, 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.

[0073] NOVX Nucleic Acid and Polypeptide Variants

[0074] 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 102, 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 102. 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 102.

[0075] In addition to the human NOVX nucleotide sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, 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.

[0076] 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 102, 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.

[0077] 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 102. 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.

[0078] 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.

[0079] 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% oifthe 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.

[0080] 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 102, 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).

[0081] 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 102, 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.

[0082] 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 102, 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 Kiegler, 1990, GENE TRANSFER AND EXPRESSION, A LABORATORY MANUAL, Stockton Press, NY; Shilo and Weinberg, 1981. Proc Natl Acad Sci USA 78: 6789-6792.

[0083] Conservative Mutations

[0084] 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 102, 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 102. 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.

[0085] 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 102, 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 102. 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 102; more preferably at least about 70% homologous to SEQ ID NO: 2n, wherein is an integer between 1 and 102; still more preferably at least about 80% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102; even more preferably at least about 90% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102; and most preferably at least about 95% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102.

[0086] 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 102, 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 102, such that one or more amino acid substitutions, additions or deletions are introduced into the encoded protein.

[0087] Mutations can be introduced any one of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, 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 102, the encoded protein can be expressed by any recombinant technology known in the art and the activity of the protein can be determined.

[0088] 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.

[0089] 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).

[0090] 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).

[0091] Antisense Nucleic Acids

[0092] 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 102, 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 102, 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 102, are additionally provided.

[0093] 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).

[0094] 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).

[0095] 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-carboxymethylaminomethyluracil, 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-manniosylqueosine, 5′-methoxycarboxymethyluracil, 2-methylthio-N6-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).

[0096] 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 II or pol III promoter are preferred.

[0097] In yet another embodiment, the antisense nucleic acid molecule of the invention is an α-anomeric nucleic acid molecule. An α-anomeric nucleic acid molecule forms specific double-stranded hybrids with complementary RNA in which, contrary to the usual β-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.

[0098] Ribozymes and PNA Moieties

[0099] 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.

[0100] In one embodiment, an antisense nucleic acid of the invention is a ribozyme. Ribozymes arc 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 102). 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.

[0101] 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.

[0102] 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.

[0103] PNAs of NOVX can be used in therapeutic and diagnostic applications. For example, PNAs can be used as antisense or antigens 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).

[0104] 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.

[0105] 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.

[0106] NOVX Polypeptides

[0107] 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 102. 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 102, while still encoding a protein that maintains its NOVX activities and physiological functions, or a functional fragment thereof.

[0108] 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.

[0109] 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.

[0110] 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 preferaibly less than about 10%, and most preferably less than about 5% of the volume of the NOVX protein preparation.

[0111] 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.

[0112] 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 102) 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.

[0113] 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.

[0114] In an embodiment, the NOVX protein has an amino acid sequence of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. In other embodiments, the NOVX protein is substantially homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102, and retains the functional activity of the protein of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, 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 102, and retains the functional activity of the NOVX proteins of SEQ ID NO: 2n, wherein n is an integer between 1 and 102.

[0115] Determining Homology Between Two or More Sequences

[0116] 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”).

[0117] 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 102.

[0118] 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.

[0119] Chimeric and Fusion Proteins

[0120] 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 102, 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.

[0121] 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.

[0122] 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.

[0123] 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.

[0124] 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.

[0125] NOVX Agonists and Antagonists

[0126] 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.

[0127] 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.

[0128] Polypeptide Libraries

[0129] 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.

[0130] 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.

[0131] Anti-NOVX Antibodies

[0132] 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.

[0133] 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 or SEQ ID NO: 2n, wherein n is an integer between 1 and 102, 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.

[0134] 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 arc 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.

[0135] 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 pM to about 1 pM, as measured by assays such as radioligand binding assays or similar assays known to those skilled in the art.

[0136] 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.

[0137] 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.

[0138] Polyclonal Antibodies

[0139] 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).

[0140] The polyclonal antibody molecules directed against the immunogenic protein can be isolated from the mammal (e.g, from the blood) and further purifed 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).

[0141] Monoclonal Antibodies

[0142] 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.

[0143] 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.

[0144] 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.

[0145] 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).

[0146] 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.

[0147] 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.

[0148] 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.

[0149] 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. One 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.

[0150] Humanized Antibodies

[0151] 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 (Fc), typically that of a human immunoglobulin (Jones et al., 1986; Riechmann et al., 1988; and Presta, Curr. Op. Struct. Biol., 2:593-596 (1992)).

[0152] Human Antibodies

[0153] 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).

[0154] 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)).

[0155] 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.

[0156] 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.

[0157] 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.

[0158] 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.

[0159] Fab Fragments and Single Chain Antibodies

[0160] 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.

[0161] Bispecific Antibodies

[0162] 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.

[0163] 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).

[0164] 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 (CH1) 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).

[0165] 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 it 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.

[0166] 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.

[0167] 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.

[0168] 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 VL and VH 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).

[0169] Antibodies with more than two valencies are contemplated. For example, trispecific antibodies can be prepared. Tutt et al., J. Immunol. 147:60 (1991).

[0170] 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).

[0171] Heteroconjugate Antibodies

[0172] 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.

[0173] Effector Function Engineering

[0174] 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).

[0175] Immunoconjugates

[0176] 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).

[0177] 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, cirotin, 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, 131I, 131In, 90Y, and 186Re.

[0178] 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 glutareldelhyde), bis-azido compounds (such as bis (p-azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), diisocyanates (such as tolyene 2,6-dilsocyanate), 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.

[0179] 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.

[0180] Immunoliposomes

[0181] 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.

[0182] 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).

[0183] Diagnostic Applications of Antibodies Directed Against the Proteins of the Invention

[0184] 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.

[0185] 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”).

[0186] 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, β-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 phycocrythrin; 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.

[0187] Antibody Therapeutics

[0188] 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.

[0189] 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.

[0190] 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.

[0191] Pharmaceutical Compositions of Antibodies

[0192] 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.

[0193] 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.

[0194] 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.

[0195] The formulations to be used for in vivo administration must be sterile. This is readily accomplished by filtration through sterile filtration membranes.

[0196] 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.

[0197] ELISA Assay

[0198] 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.

[0199] NOVX Recombinant Expression Vectors and Host Cells

[0200] 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.

[0201] 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).

[0202] 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.).

[0203] 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.

[0204] 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.

[0205] 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).

[0206] 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.

[0207] 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.).

[0208] 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).

[0209] 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.

[0210] 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).

[0211] 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.

[0212] 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.

[0213] 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.

[0214] 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.

[0215] 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).

[0216] 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.

[0217] Transgenic NOVX Animals

[0218] 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 nonhuman 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.

[0219] 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 102, 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 arc 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.

[0220] 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 102), 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 102, 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).

[0221] 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.

[0222] 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.

[0223] 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.

[0224] 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.

[0225] Pharmaceutical Compositions

[0226] 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 arc 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.

[0227] 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. She parenteral preparation can be enclosed in ampoules, disposable syringes or multiple dose vials made of glass or plastic.

[0228] 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, Cremophior 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 carrier 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.

[0229] 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.

[0230] 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 call 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 tragacanith 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.

[0231] 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.

[0232] 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.

[0233] 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.

[0234] 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.

[0235] 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.

[0236] 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.

[0237] The pharmaceutical compositions can be included in a container, pack, or dispenser together with instructions for administration.

[0238] Screening and Detection Methods

[0239] 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.

[0240] The invention further pertains to novel agents identified by the screening assays described herein and uses thereof for treatments as described, supra.

[0241] Screening Assays

[0242] 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.

[0243] 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.

[0244] 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.

[0245] 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. Chem. 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.

[0246] 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. USA. 87: 6378-6382; Felici, 1991. J. Mol. Biol. 222: 301-310; Ladner, U.S. Pat. No. 5,233,409.).

[0247] 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.

[0248] 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.

[0249] 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.

[0250] 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.

[0251] 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.

[0252] 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.

[0253] 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).

[0254] 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.

[0255] 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 all enzymatic activity associated with the NOVX protein or target molecule.

[0256] 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.

[0257] 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.

[0258] 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.

[0259] The invention further pertains to novel agents identified by the aforementioned screening assays and uses thereof for treatments as described herein.

[0260] Detection Assays

[0261] 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 arc described in the subsections, below.

[0262] Chromosome Mapping

[0263] 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 102, 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.

[0264] 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.

[0265] 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.

[0266] 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.

[0267] 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).

[0268] 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.

[0269] 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.

[0270] 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.

[0271] 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.

[0272] Tissue Typing

[0273] 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).

[0274] 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.

[0275] 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).

[0276] 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 102, are used, a more appropriate number of primers for positive individual identification would be 500-2,000.

[0277] Predictive Medicine

[0278] 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.

[0279] 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.)

[0280] 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.

[0281] These and other agents are described in further detail in the following sections.

[0282] Diagnostic Assays

[0283] 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 102, 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.

[0284] 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.

[0285] 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.

[0286] 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.

[0287] 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.

[0288] Prognostic Assays

[0289] 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.

[0290] 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).

[0291] 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.

[0292] 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. Nacl. 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.

[0293] 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. BioTechnology 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.

[0294] 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.

[0295] 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. Natl. 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.

[0296] 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).

[0297] Other methods for detecting mutations in the NOVX gene include methods in which protection from cleavage agents is used to detect mismatched bases 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.

[0298] 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.

[0299] 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 Appl 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 chance. 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.

[0300] 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.

[0301] 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.

[0302] 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.

[0303] 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.

[0304] 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.

[0305] Pharmacogenomics

[0306] 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 proteins such as those summarized in Table A.

[0307] 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.

[0308] 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.

[0309] 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.

[0310] 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.

[0311] Monitoring of Effects During Clinical Trials

[0312] 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.

[0313] 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.

[0314] 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.

[0315] Methods of Treatment

[0316] 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.

[0317] These methods of treatment will be discussed more fully, below.

[0318] Diseases and Disorders

[0319] 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.

[0320] 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.

[0321] 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).

[0322] Prophylactic Methods

[0323] 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.

[0324] Therapeutic Methods

[0325] 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.

[0326] Stimulation of NOVX activity is desirable in situations in which NOVX is abnormally downregulatcd 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).

[0327] Determination of the Biological Effect of the Therapeutic

[0328] 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.

[0329] 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.

[0330] Prophylactic and Therapeutic Uses of the Compositions of the Invention

[0331] 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.

[0332] 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.

[0333] 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.

[0334] 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

[0335] Polynucleotide and Polypeptide Sequences, and Homology Data

Example 1

[0336] 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	3163 bp
NOV1a,	CTCCCCACGGCGCCAGGAGGAGGGGCGAGGGCCGGCAGCCCCCTCTCCCCCGCGCGGC
CG113254-01
DNA Sequence	GCAGGAGCCGAGCCCAGCCCCGGGGACCCGCCGCCGCCGGTCATGTGGGCCGGACTGC
	TCCTTCGGGCCGCCTGTGTCGCGCTCCTGCTGCCGGGGGCACCAGCCCGAGGCTACAC
	CGGGAGGAAGCCGCCCGGGCACTTCGCGGCCGAGAGACGCCGACTGGGCCCCCACGTC
	TGCCTCTCTGGGTTTGGGAGTGGCTGCTGCCCTGGCTGGGCGCCCTCTATGGGTGGTG
	GGCACTGCACCCTACCCCTCTACTCCTTCGGCTGTGGGAGTGGCATCTGCATCGCTCC
	CAATGTCTGCTCCTGCCAGGATGGAGAGCAAGGGCCCACCTGCCCAGAAACCCATGGA
	CCATGTGGGGAGTACGGCTGTGACCTTACCTGCAACCATGGAGGCTGTCAGGAGGTGG
	CCCGAGTGTGCCCCGTGGGCTTCTCGATGACGGAGACAGCTGTTGGCATCAGGTGTAC
	AGACATTGACGAATGTGTAACCTCCTCCTGCGAGGGCCACTGTGTGAACACAGAAGGT
	GGGTTTGTGTGCGAGTGTGGGCCGGGCATGCAGCTGTCTGCCGACCGCCACAGCTGCC
	AAGACACTGACGAATGCCTAGGGACTCCCTGTCAGCAGAGATGTAAAAACAGCATTGG
	CAGCTACAAGTGTTCCTGTCGAACTGGCTTCCACCTTCATGGCAACCGGCACTCCTGT
	GTAGATGTAAACGAGTGTCGGAGGCCATTGGAGAGGCGAGTCTGTCACCATTCCTCCC
	ACAACACCGTGGGCAGCTTCCTATGCACATGCCGACCTGGCTTCAGGCTCCGAGCTGA
	CCGCGTGTCCTGTGAAGCTTTCCCGAAAGCCGTGCTGGCCCCATCTGCCATCCTGCAA
	CCCCGGCAACACCCGTCCAAGATGCTTCTGTTGCTTCCTGAGGCCGGCCGGCCTGCCC
	TGTCCCCAGGACATAGCCCTCCTTCTGGGGCTCCAGGGCCCCCAGCCGGAGTCAGGAC
	CACCCGCCTGCCATCTCCCACCCCACGACTACCCACATCCTCCCCTTCTGCCCCTGTG
	TGGCTGCTGTCCACCCTGCTGGCCACCCCAGTGCCTACTGCCTCCCTGCTGCGGAACC
	TCAGACCCCCCTCACTCCTTCAGGGGGAGGTGATGGGGACCCCTTCCTCACCCAGGGG
	CCCTGAGTCCCCCCGACTGGCAGCAGGGCCCTCTCCCTGCTGGCACCTGGGAGCCATG
	CATGAATCAAGGAGTCGCTGGACAGAGCCTGGGTGTTCCCAGTGCTGGTGCGAGGACG
	GGAAGGTGACCTGTGAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCCAATTCCCTC
	CAGAGATGGTGGGTGCTGCCCATCGTGCACAGGCTGTTTTCACACTGGTGTCGTCCGA
	GCTGAAGGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTCTGTCTGG
	CTGGAAACGTGTCCTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCACACCCCCCC
	ACAGACGGATTGCTGTACTTGTGTTCCAGTGAGATGCTATTTCCACGGCCGGTGGTAC
	GCAGACGGGGCTGTGTTCAGTGGGGGTGGTGACGAGTGTACCACCTGTGTTTGCCAGA
	ATGGGGACGTCGAGTGCTCCTTCATGCCCTGCCCTGAGCTGGCCTGCCCCCGAGAAGA
	GTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCAGGAGCCCACACCCTCGACA
	GGTTGCTCTCTTGACGACAACGGGGTTGAGTTTCCGATTGGACAGATCTGGTCGCCTG
	GTGACCCCTGTAGATGGCTCGGTGAGCTGCAAGAGGACAGACTGTGTGGACTCCTGCC
	CTCACCCGATCCGGATCCCTGGACAGTGCTGCCCAGACTGTTCAGCAGGTTGCACCTA
	CACAGGCAGAATCTTCTATAACAACGAGACCTTCCCGTCTGTGCTGGACCCATGTCTG
	AGCTCCATCTGCCTGACAGACTGCAACTACGAGGGAAGGAAGGTGGCGAATGGCCAGG
	TGTTCACCTTGGATGATGAACCCTGCACCCGGTGCACGTGCCAGCTAGATTCCCTGTC
	TCCTCTGGAAGAAAAGCAGGGGCTCTCCCCTCACGGAAATGTGGCATTCAGCAAAGCT
	GGTCGGAGCCTGCATGGAGACACTGAGGCCCCTGTCAACTGTAGCTCCTGTCCTCGGC
	CCCCGACAGCATCACCCTCGAGGCCGGTGCTTCATCTCCTCCAGCTCCTTTTAAGAAC
	GAACTTGATGAAAACACAGACTTTACCTACAAGCCCGGCAGGAGCTCATGGTCCACAC
	TCACTCGCTTTGGGGCTGACACCCACTTTCCCAGGGGAGCCTGGGGCCTCCCCTCGAC
	TCTCACCAGGGCCTTCGACCCCTCCAGGAGCCCCCACTCTACCTCTAGCTTCCCCAGG
	GGCTCCTCAGCCACCTCCTGTGACTCCAGAGCGCTCGTTCTCAGCCTCTGGGGCCCAG
	ATAGTGTCCAGGTGGCCTCCTCTGCCTGGCACCCTCCTGACGGAAGCTTCAGCACTTT
	CCATGATGGACCCCAGCCCCTCGAAGACCCCCATCACCCTCCTCGGGCCTCGCGTGCT
	TTCTCCCACCACCTCTAGACTCTCCACAGCCCTTGCAGCCACCACCCACCCTGGCCCC
	CAGCAGCCCCCAGTGGGGGCTTCTCGGGGGGAAGAGTCCACCATGTAAGGAGGTCACT
	GTGTCCGGGAGACTCTGGAGAGAGGACCTCTGCCAGTGGCCCAGGGTGTGTGCAGGGC
	AGCTCCAAGGATGAACCTGGTGGGGATGCCTGGGCTCCCTCCTGCAGGGGCCCTGGTG
	AGGATGGAAGACCCCCAAGGCTGGATGTAACCTTGTTCCCAAGAAGTGTTTGGAATGT
	GCTGTAAGAATGGAGGAAGTCGTTTCCACTGTCAGCATCCTCCCTGGACCGCGTGGCT
	GGCTCATCTTTTGAGAAGGGTTGGGACTGCCAAGTTCTCCTGGAGGAAGAGTTGCGTC
	CGGCTGGGATTCCACTCACTGGGACTGTACCGCCAGGTGTCATGCGTCTCTCTGAGGT
	TTCCTGATTAAAGGTTGTCTCGGTTTCAAAA
	ORF Start: ATG at 101	ORF Stop: TAA at 1991
	SEQ ID NO: 2	630 aa	MW at 66952.5 kD
NOV1a,	MWAGLLLRAACVALLLPGAPARGYTGRKPPGHFAAERRRLGPHVCLSGFGSGCCPGWA
CG113254-01
Protein Sequence	PSMGGGHCTLPLYSFGCGSGICIAPNVCSCQDGEQGATCPETHGPCGEYGCDLTCNHG
	CCQEVARVCPVGFSMTETAVGIRCTDIDECVTSSCEGHCVNThGGFVCECGPGMQLSA
	DRHSCQDTDECLGTPCQQRCKNSIGSYKCSCRTGFHLHGNRHSCVDVNECRRPLERRV
	CHHSCHNTVGSFLCTCRPGFRLRADRVSCEAFPKAVLAPSAILQPRQHPSKMLLLLPE
	AGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLPTSSPSAPVWLLSTLLATPVPTA
	SLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGAMHESRSRWTEPGCSQ
	CWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVVRAEGDVFSPPNENCT
	VCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPVRCYFHGRWYADGAVFSGGGDECT
	TCVCQNGEWECSFMPCPELACPREEWRLGPGQCCFTCQEPTPSTCCSLDDNGVEFPIG
	QIWSPGDPCRWLGELQEDRLCGLLPSPDPDPWTVLPRLFSRLHLHRQNLL
	SEQ ID NO:3	1830 bp
NOV1b,	GGTCATGTGCGCCGGACTGCTCCTTCGGGCCGCCTGTGTCGCGCTCCTGCTGCCGGGG
CG113254-02
DNA Sequence	CCACCAGCCCGAGGCTACACCCCGACGAAGCCGCCCGGGCACTTCGCGGCCGAGAGAC
	GCCGACTGGGCCCCCACGTCTGCCTCTCTGGGTTTGGGAGTGCCTGCTGCCCTGGCTG
	GGCGCCCTCTATGGGTGGTGGGCACTGCACCCTGCCCCTCTGCTCCTTCGGCTGTGGG
	AGTGGCATCTCCATCGCTCCCAATGTCTGCTCCTGCCAGGATGGAGAOCAACGGGCCA
	CCTGCCCAGAAACCCATGGACCATGTGGGGAGTACGGCTGTGACCTTACCTGCAGCCA
	TGGAGGCTGTCAGGAGGTGGCCCGAGTGTGCCCCGTGGGCTTCTCGATGACGGAGACA
	GCTGTTCGCATCACGTGTACAGACATTGACGAATGTGTAACCTCCTCCTGCGACGGCC
	ACTGTGTGAACACAGAAGGTGGGTTTGTGTGCGAGTGTGGGCCGGGCATGCAGCTGTC
	TGCCGACCGCCACAGCTGCCAAGACACTGACGAATGCCTAGGGACTCCCTCTCAGCAG
	AGATGTPAAAACAGCATTGGCACCTACAAGTCTTCCTGTCGAACTGGCTTCCACCTTC
	ATGCCAACCGGCACTCCTGTGTAGCTTTCCCGAAACCCGTGCTGGCCCCATCTGCCAT
	CCTGCAACCCCGGCAACACCCGTCCAAGATGCTTCTGTTGCTTCCTGAGGCCGGCCGG
	CCTGCCCTGTCCCCAGGACATAGCCCTCCTTCTGGGGCTCCAGGGCCCCCAGCCGGAG
	TCAGGACCACCCGCCTGCCATCTCCCACCCCACGACTACCCACATCCTCCCCTTCTGC
	CCCTGTGTGGCTGCTGTCCACCCTGCTGGCCACCCCAGTGCCTACTGCCTCCCTGCTC
	GGGAACCTCAGACCCCCCTCACTCCTTCAGGGGGAGGTGATGGGGACCCCTTCCTCAC
	CCAGGCGCCCTGAGTCCCCCCGACTGGCAGCAGGGCCCTCTCCCTGCTGGCACCTGGG
	AGCCATGCATGAATCAAGGAGTCGCTCGACAGAGCCTGGGTGTTCCCAGTGCTGGTGC
	GAGGACGGGAACCTCACCTGTCAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCCAA
	TTCCCTCCAGAGATGGTCGCTCCTGCCCATCGTGCACACGCTGTTTTCACACTGGTGT
	CCTCCGAGCTGAACGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTC
	TGTCTGGCTGGAAACGTGTCCTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCAGA
	CCCCCCCACAGACGGATTGCTGTACTTGTGTTCCAGTGAGATGCTATTTCCACGGCCG
	GTGGTACGCAGACGGAGCTGTGTTCAGTGGGGGTGGTGACGAGTGTACCACCTGTGTT
	TGCCAGAATCCCGAGGTGGAGTGCTCCTTCATGCCCTGCCCTGAGCTGGCCTCCCCCC
	GAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCAGGAGCCCACACC
	CTCGACAGGCTGCTCTCTTGACGACAACGGGGTTGAGTTTCCGATTGGACAGATCTGG
	TCGCCTGGTGACCCCTGTGAGTTATGCATCTGCCAGGCAGATGGCTCGGTGAGCTGCA
	AGAGGACAGACTGTGTGGACTCCTGCCCTCACCCGATCCGGATCCCTGGACAGTGCTC
	CCCAGACTGTTCAGCAGGTAATCCCCTGCCTCTGCCCCAAGCCCCCAGGGCAGGGCAT
	ORF Start: ATG at 5	ORF Stop: TAA at 1817
	SEQ ID NO: 4	604 aa	MW at 63127.1 kD
NOV1b,	MWAGLLLRAACVALLLPGAPARGYTGRKPPGHFAAERRRLGPHVCLSGFGSCCCPGWA
CG113254-02
Protein Sequence	PSMGGGHCTLPLCSFGCGSGICIAPNVCSCQDGEQGATCPETHGPCGEYGCDLTCSHC
	GCQEVARVCPVGFSMTETAVGIRCTDIDECVTSSCEGHCVNTEGGFVCECGPGMQLSA
	DRHSCQDTDECLGTPCQQRCKNSIGSYKCSCRTGFHLHGNRHSCVAFPKAVLAPSAIL
	QPRQHPSKMLLLLPEAGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLPTSSPSAP
	VWLLSTLLATPVPTASLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGA
	MHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVV
	RAEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPVRCYFHGRW
	YADGAVFSGGGDECTTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCFTCQEPTPS
	TGCSLDDNGVEFPIGQIWSPGDPCELCICQADGSVSCKRTDCVDSCPHPIRIPCQCCP
	DCSAGNPLPLPQAPRAGHLRHRAP
	SEQ ID NO:5	597 bp
NOV1c,	GGTACCTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTG
211648303 DNA
Sequence	GGTGTTCCCAGTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGA
	AGCTCCTTGTTCCCACCCAATTCCCTCCAGAGATGGTGGGTGCTGCCCATCGTGCACA
	GGCTGTTTTCACAGTGGTGTCGTCCGAGCTGAAGGGGATGTGTTTTCACCTCCCAATG
	AGAACTGCACCGTCTGTGTCTGTCTGGCTGGAAACGTGTCCTGCATCTCTCCTGAGTG
	TCCTTCTGGCCCCTGTCAGACCCCCCCACAGACGGATTGCTGTACTTGTGTTCCAGTG
	AGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTGTTCAGTGGCGGTGGTG
	ACGAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTG
	CCCTGAGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTC
	ACCTGCCAGGAGCCCACACCCTCGACAGGCTGCTCTCTTGACGACAACGGGGTTGAGT
	TTCCGATTGGAGTCGAC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO:6	199 aa	MW at 21235.6 kD
NOV1c,	GTCWHLGAMHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCT
211648303
Protein Sequence	GCFHSGVVRAEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPV
	RCYFHGRWYADGAVFSGGGDECTTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCF
	TCQEPTPSTGCSLDDNGVEFPIGVD
	SEQ ID NO:7	597 bp
NOV1d,	GGTACCTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTG
212170920 DNA
Sequence	GGTGTTCCCAGTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGA
	AGCTGCTTGTTCCCACCCAATTCCCTCCACAGATGGTCGGTGCTGCCCATCGTGCACA
	GGCTGTTTTCACAGTGGTGTCGTCCGAGCTGAAGGGGATGTGTTTTCACCTCCCAATG
	AGAACTGCACCGTCTGTGTCTGTCTGGCTGQAAACGTGTCCTGCATCTCTCCAGAGTG
	TCCTTCTGGCCCCTGTCAGGCCCCCCCACAGACCGATTGCTGTACTTGTGTTCCAGTG
	AGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTATTCACTGGGGGTGGTG
	ACGAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTA
	CCCTGAGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTC
	ACCTGCCAGGAGCCCACACCCTCGACAGGCTGCTCTCTTGACGACAACGGGGTTGAGT
	TTCCGATTGGAGTCGAC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO:8	199 aa	MW at 21265.6 kD
NOV1d,	GTCWHLGAMHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCT
212170920
Protein Sequence	GCFHSGVVRAEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQAPPQTDCCTCVPV
	RCYFHGRWYADGAVFSGGGDECTTCVCQNGEVECSFMPYPELACPREEWRLGPGQCCF
	TCQEPTPSTGCSLDDNGVEFPIGVD

[0337] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 1B.

TABLE 1B
Comparison of NOV1a against NOV1b through NOV1d.
			Identities/
			Similarities
		NOV1a Residues/	for the
	Protein Sequence	Match Residues	Matched Region
	NOV1b	1 . . . 589	477/589 (80%)
		1 . . . 546	478/589 (80%)
	NOV1c	386 . . . 580	179/195 (91%)
		3 . . . 197	179/195 (91%)
	NOV1d	386 . . . 580	193/195 (98%)
		3 . . . 197	193/195 (98%)

[0338] Further analysis of the NOV1a protein yielded the following properties shown in Table 1C.

TABLE 1C
Protein Sequence Properties NOV1a
PSort     0.5947 probability located in outside; 0.1900
analysis: probability located in lysosome (lumen);
          0.1000 probability located in endoplasmic
          reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 22 and 23
analysis:

[0339] 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 1D.

TABLE 1D
Geneseq Results for NOV1a
	Protein/		Identities/
	Organism/	NOV1a	Similarities
	Length	Residues/	for the
Geneseq	[Patent #,	Match	Matched	Expect
Identifier	Date]	Residues	Region	Value
AAM99920	Human polypeptide	389 . . . 589	201/201 (100%)	e−133
	SEQ ID NO 36 -	5 . . . 205	201/201 (100%)
	Homo sapiens, 272
	aa. [WO200155173-
	A2, 02 AUG. 2001]
AAM99933	Human polypeptide	389 . . . 589	197/201 (98%)	e−131
	SEQ ID NO 49 - Homo	5 . . . 205	198/201 (98%)
	sapiens, 212 aa
	[WO200155173-A2,
	02 AUG. 2001]
AAB85364	Novel Von	284 . . . 489	206/206 (100%)	e−128
	Willebrand/	1 . . . 206	206/206 (100%)
	thrombosporin-
	like polypeptide -
	Homo sapiens, 235 aa.
	[WO200153485-A1,
	26 JUL. 2001]
AAB85365	Novel Von	302 . . . 489	188/188 (100%)	e−117
	Willebrand/	1 . . . 188	188/188 (100%)
	thrombosporin-
	like mature protein
	sequence -
	Homo sapiens, 217 aa.
	[WO200153485-A1,
	26 JUL. 2001]
ABG15393	Novel human	70 . . . 138	68/69 (98%)	2e−37
	diagnostic	959 . . . 1027	68/69 (98%)
	protein #15384 -
	Homo sapiens,
	1028 aa.
	[WO200175067-A2,
	11 OCT. 2001]

[0340] 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 1E.

TABLE 1E
Public BLASTP Results for NOV1a
			Identities/
		NOV1a	Similarities
Protein	Protein/	Residues/	for the
Accession	Organism/	Match	Matched	Expect
Number	Length	Residues	Portion	Value
Q96DN2	CDNA FLJ32009 fis,	1 . . . 589	587/589 (99%)	0.0
	clone	1 . . . 589	587/589 (99%)
	NT2RP7009498,
	weakly similar to
	fibulin-1, isoform
	A precursor -
	Homo sapiens
	(Human), 955 aa.
Q9DBE2	1300015B04Rik	1 . . . 615	517/615 (84%)	0.0
	protein - Mus	1 . . . 607	547/615 (88%)
	musculus (Mouse),
	608 aa.
Q9IBG7	Kielin - Xenopus	368 . . . 589	79/227 (34%)	2e−32
	laevis (African	1483 . . . 1695	109/227 (47%)
	clawed frog),
	2327 aa.
Q91V88	POEM (NEPHRONECTIN	44 . . . 373	103/364 (28%)	1e−31
	short	35 . . . 383	153/364 (41%)
	isoform) - Mus
	musculus (Mouse),
	561 aa.
Q9CXD8	6130401L20Rik	53 . . . 261	79/221 (35%)	7e−31
	protein - Mus	96 . . . 308	101/221 (44%)
	musculus (Mouse),
	528 aa.

[0341] PFam analysis indicates that the NOV1a protein contains the domains shown in the Table 1F.

TABLE 1F
Domain Analysis of NOV1a
		Identities/
		Similarities
	NOV1a Match	for the Matched
Pfam Domain	Region	Region	Expect Value
EGF	146 . . . 179	16/47 (34%)	0.0045
		23/47 (49%)
EGF	185 . . . 218	12/47 (26%)	0.011
		25/47 (53%)
TIL	166 . . . 224	13/70 (19%)	0.53
		40/70 (57%)
EGF	224 . . . 261	12/48 (25%)	0.034
		26/48 (54%)
vwc	386 . . . 440	21/84 (25%)	7.8e−08
		40/84 (48%)
vwc	443 . . . 496	21/84 (25%)	5.8e−05
		37/84 (44%)
vwc	501 . . . 559	22/84 (26%)	1.3e−09
		41/84 (49%)

Example 2

[0342] 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: 9	4036 bp
NOV2a,	TCCTGGATGAGGCAGCTCAGTCACAGAGGGTGGGCCCCCAGAGAAGGGAAAATTGTGA
CG122729-01
DNA Sequence	GCAGCCCACACTGCTGGCAGATGCGGCATAAGTGTCCCAGCCAGGCTAGGGAGGCGGT
	GGGCACTGGGTGCACACGATGGCCCTGTGGTTGCTGTCTCAGTCCCGGGCTGTGCTTC
	CAGGCTTCTCCAGACCACGCCACCAGCCAACAGAAGCGAGACTTCCAGTCCGAGGTCC
	TGCTTTCTGCTATGGAACTATTCCACATGACAAGTGGAGGTGATGCAGCCATGTTCAG
	AGACGGCAAAGAGCCTCAGCCAAGTGCAGAAGCTGCTGCTGCCCCTTCTCTTGCCAAC
	ATCTCCTGCTTCACCCAGAAGCTGGTGGAGAAGCTGTACAGTGGGATGTTCTCGGCAG
	ACCCCAGGCATATCCTCCTCTTCATCCTGGAGCACATCATGGTGGTCATTGAGACTGC
	CTCTTCTCAAAGGGACACTGTCCTCAGCACTTTATACAGCAGTTTAAATAAAGTCATT
	CTTTATTGCCTATCCAAGCCCCAGCAGTCCCTCTCCGAATGCCTCGGCCTTCTCAGCA
	TCCTGCGCTTTCTGCAGGAGCACTGGGATGTTGTCTTTGCCACCTACAATTCCAACAT
	CACCTTCCTCCTGTGTCTCATGCATTGCCTTTTGCTACTCAATGAGAGAAGTTACCCA
	GAAGGATTTGGATTGGAGCCCAAGCCTAGAATGTCTACTTATCATCAAGTCTTCCTTT
	CCCCAAATGAAGACGTGAAAGAAAAAAGAGAAGACTTACCAAGTTTCAGTGATGTCCA
	ACACAACATCCAGAAGACAGTGCACACTCTCTGGCAGCAGCTGGTGGCACAAAGGCAG
	CAGACCCTGGAGGATGCCTTCAAGATCGATCTCTCTGTGAAACCTGGAGAGAGCGAAG
	TGAAGATTGAAGAGGTCACACCGCTCTGGGAGGAGACGATGCTCAAGGCCTGGCAGCA
	TTACTTAGCATCTGAGAAGAAGTCACTGGCAAGTCGTTCAAATGTTGCACACCACACC
	AAAGTCACTTTGTGGAGTGGAAGCCTGTCCTCAGCCATCAAGCTGATGCCCGGGCGGC
	AGGCCAAGGACCCTGAGTGCAAGACAGAGGATTTTGTGTCATGTATAGAGAACTACAG
	AAGAAGAGGACAAGAGCTATATGCATCTTTATACAAAGACCATGTGCAPAGGCGAAAA
	TGTGGCAACATCAAGGCAGCCAACGCCTGGGCCAGGATCCAGGAGCAGCTTTTTGGGG
	AGCTGGGCTTGTGGAGCCAGGGGGAAGAAACCAAGCCCTGTTCCCCATCGGAACTCGA
	CTGGAGAGAAGGACCAGCTCGAATGAGGAAACGCATCAAACGCTTGTCTCCTTTGGAG
	GCCCTCAGCTCAGGAAGGCACAAGGAAAGCCAAGACAAAAATGATCATATTTCTCAAA
	CAAATGCTGAAAACCAAGATGAACTGACACTGAGGGAGGCTGAGGGCGAGCCGGACGA
	GGTGGGGGTGGACTGCACCCAGCTCACCTTCTTCCCAGCCTTACACGAAAGTCTGCAC
	TCAGAAGACTTCTTGGAACTGTGTCGGGAAAGACAAGTTATTTTACAAGAGCTTCTTG
	ATAAAGAAAAGGTGACGCAGAAGTTCTCCCTGGTGATTGTGCAGGGCCACCTGGTGTC
	AGAAGGGCTCCTGCTTTTTGGCCACCAACACTTCTACATCTGCGAGAACTTCACACTG
	TCTCCCACGGGTGATGTCTACTGTACCCGTCACTGCTTATCCAACATCAGCGATCCGT
	TCATTTTCAACCTGTGCACCAAAGACAGGTCCACTGACCATTACTCGTGCCAGTCCCA
	CAGCTACGCTGACATGCGGGAGCTACGGCAGGCTCGCTTCCTCCTGCAGGACATCGCC
	CTGGAGATCTTCTTCCACAATGGATATTCCAAGTTTCTTGTCTTCTACAACAATGATC
	GGAGTAAGCCCTTTAAAACCTTCTGCTCTTTCCAACCCAGCCTGAAGGGGAAAGCCAC
	CTCGGAGGACACCCTCAATCTAAGGAGATACCCCCCCTCTGACACCATCATGCTGCAG
	AAGTGGCAGAAAAGGGACATCAGCAATTTTGAGTATCTCATCTACCTCAACACCGCGG
	CTGGGAGAACCTGCAATGACTACATGCAGTACCCAGTGTTCCCCTGGGTCCTCGCAGA
	CTACACCTCAGACACATTGAACTTGGCAAATCCGAAGATTTTCCGGGATCTTTCAAAG
	CCCATGGGGGCTCAGACCAAGGAAAGCAAGCTGAAATTTATCCAGAGGTTTAAAGAAG
	TTGAGAAUXCTGAAGGAGACATGACTGTCCACTGCCACTACTACACCCACTACTCCTC
	GGCCATCATCGTGGCCTCCTACCTGGTCCGGATGCCACCCTTCACCCAGGCCTTCTGC
	GCTCTGCAGGGCGGAAGCTTCGACGTGGCAGACAGAATGTTCCACAGTGTGAAGAGCA
	CGTGGGAGTCGGCCTCCAGAGAGAACATGAGTGACGTCAGGGAGCTGACCCCAGAGTT
	CTTCTACCTGCCTGAGTTCTTAACCAACTGCAACGGGGTAGAGTTCGGCTGCGTGCAG
	GACGGGACTGTGCTAGGAGACGTGCAGCTCCCTCCCTGGGCTGATGGGGACCCTCGGA
	AATTCATCAGCCTGCACAGAAAGGCCCTGGAAAGTGACTTTGTCAGTGCCAACCTCCA
	CCATTGGATAGACCTTATTTTTGGGTACAAGCAGCAGGGGCCAGCCGCAGTGGATGCT
	GTTAATATCTTCCACCCCTACTTCTACGGTGACAGAATGGACCTCAGCAGCATCACTG
	ACCCCCTCATCAAAAGCACCATCCTGGGGTTTGTCAGCAACTTTGGACAGGTGCCCAA
	ACAGCTCTTTACCAAACCTCACCCAGCCAGGACTGCAGCAGGGAAGCCTCTGCCTGGA
	AAGGATATCTCCACCCCCGTGAGCCTGCCTGGCCACCCACAGCCCTTTTTCTACAGCC
	TGCAGTCGCTGAGGCCCTCCCAGGTCACGGTCAAAGATATGTACCTCTTTTCTCTAGG
	CTCAGAGTCCCCCAAAGGGGCCATTGGCCACATTGTCTCTACTGAGAAGACCATTCTG
	GCTGTAGAGAGGAACAAAGTGCTGCTGCCTCCTCTCTGGAACAGGACCTTCAGCTGCG
	GCTTTGATGACTTCAGCTGCTGCTTGGGGAGCTACGGCTCCGACAAGGTCCTGATGAC
	ATTCGAGAACCTGGCTGCCTGGGGCCGCTGTCTGTGCGCCGTGTGCCCATCCCCAACA
	ACGATTGTCACCTCTGGGACCAGCACTGTGGTGTGTGTGTGGGAGCTCAGCATGACCA
	AAGGCCGCCCGAGGCGCTTGCGCCTCCGGCAGGCCTTGTATGGACACACACAGGCTGT
	CACGTGCCTGGCAGCGTCAGTCACCTTCAGCCTCCTGGTGAGCGGCTCCCAGGACTGC
	ACCTGTATCCTGTGGGATCTGGACCACCTCACCCACGTGACCCGCCTGCCCCCCCATC
	GGGAAGGCATCTCAGCCATCACCATCAGTGACGTCTCAGGCACCATTGTCTCCTGTGC
	GGGAGCACACTTGTCCCTGTGGAATCTCAATGGACAGCCCCTGGCCAGCATCACCACA
	GCCTGGGGCCCAGAAGGAGCCATAACCTGTTGCTGCCTGATGGAGGGCCCAGCATGGG
	ACACAAGCCAGATCATCATCACCGGGAGTCAAGACGGCATGGTCCGGGTTTGGAAGAC
	TGAGGATGTGAAGATGTCTGTTCCTCGACGGCCAGCAGGAGAGGAGCCCCTGGCTCAG
	CCTCCAAGCCCAAGAGGCCACAAGTGGGAGAAGAACCTGGCCTTGAGTCGAGAGCTGG
	ACGTTAGCATTGCTTTGACAGGGAAGCCCAGCAAAACCAGCCCCGCAGTGACTGCTCT
	GGCCGTGTCCAGAAACCACACCAAACTCCTGGTTGGTGATGAGAGGGGGAGAATATTC
	TGCTGGTCTGCAGATGGGTAGGAAGAGAGAGGCA
	ORF Start: ATG at 7	ORF Stop: TAG at 4021
	SEQ ID NO 10	1338 aa	MW at 150546.1 kD
NOV2a,	MRQLSHRGWAPREGKIVSSPHCWQMRHKCPSQAREAVGTGCTRWPCGCCLSPGLCFQA
CG122729-01
Protein Sequence	SPDHATSQQKRDFQSEVLLSAMELFHMTSGGDAAMFRDGKEPQPSAEAAAAPSLANIS
	CFTQKLVEKLYSGMFSADPRHILLFILEHIMVVIETASSQRDTVLSTLYSSLNKVILY
	CLSKPQQSLSECLGLLSILGFLQEHWDVVFATYNSNISFLLCLMHCLLLLNERSYPEG
	FGLEPKPRMSTYHQVFLSPNEDVKEKREDLPSLSDVQHNIQKTVQTLWQQLVAQRQQT
	LEDAFKIDLSVKPGEREVKIEEVTPLWEETMLKAWQHYLASEKKSLASRSNVAHHSKV
	TLWSGSLSSAMKLMPGRQAKDPECKTEDFVSCIENYRRRGQELYASLYKDHVQRRKCG
	NIKAANAWARIQEQLFGELGLWSQGEETKPCSPWELDWREGPARMRKRIKRLSPLEAL
	SSGRHKESQDKNDHISQTNAENQDELTLREAEGEPDEVGVDCTQLTFFPALHESLHSE
	DFLELCRERQVILQELLDKEKVTQKFSLVIVQGHLVSEGVLLFGHQHFYICENFTLSP
	TGDVYCTRHCLSNISDPFIFNLCSKDRSTDHYSCQCHSYADMRELRQARFLLQDIALE
	IFFHNGYSKFLVFYNNDRSKAFKSFCSFQPSLKGKATSEDTLNLRRYPGSDRIMLQKW
	QKRDTSNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPM
	GAQTKERKLKFIQRFKEVEKTEGDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCAL
	QGGSFDVADRMFHSVKSTWESASRENNSDVRELTPEFFYLPEFLTNCNGVEFGCVQDG
	TVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVN
	IFHPYFYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPARTAAGKPLPGKD
	ISTPVSLPGHPQPFFYSLQSLRPSQVTVKDMYLFSLGSESPKGATGHIVSTEKTILAV
	ERNKVLLPPLWNRTFSWGFDDFSCCLGSYGSDKVLMTFENLAAWGRCLCALCPSPTTI
	VTSGTSTVVCVWELSMTKGRPRGLRLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTC
	ILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGAHLSLWNVNGQPLASITTAW
	GPEGAITCCCLMEGPAWDTSQIIITGSQDGMVRVWKTEDVKMSVPGRPAGEEPLAQPP
	SPRGHKWEKNLALSRELDVSIALTGKPSKTSPAVTALAVSRNHTKLLVGDERGRIFCW
	SADG

[0343] Further analysis of the NOV2a protein yielded the following properties shown in Table 2B.

TABLE 2B
Protein Sequence Properties NOV2a
PSort     0.9000 probability located in Golgi body; 0.7900
analysis: probability located in plasma membrane; 0.6000
          probability located in nucleus; 0.5147 probability
          located in microbody (peroxisome)
SignalP   No Known Signal Sequence Indicated
analysis:

[0344] 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 2C.

TABLE 2C
Geneseq Results for NOV2a
	Protein/		Identities/
	Organism/	NOV2a	Similarities
	Length	Residues/	for the
Geneseq	[Patent #,	Match	Matched	Expect
Identifier	Date]	Residues	Region	Value
AAY79179	Haematopoietic stem	675 . . . 1329	563/656 (85%)	0.0
	cell specific	1 . . . 656	603/656 (91%)
	protein - Mus
	musculus, 693 aa.
	[WO200011168-A2,
	02 MAR. 2000]
ABB64158	Drosophila	54 . . . 1262	450/1303 (34%)	0.0
	melanogaster	1758 . . . 3021	674/1303 (51%)
	polypeptide SEQ
	ID NO 19266 -
	Drosophila
	melanogaster,
	3309 aa.
	[WO200171042-A2,
	27 SEP. 2001]
AAR99800	NTII-1 nerve	649 . . . 1269	334/633 (52%)	0.0
	protein, facilitates	4 . . . 621	441/633 (68%)
	regeneration of
	nerve cells -Homo
	sapiens, 887 aa.
	[WO9617865-A2,
	13 JUN. 1996]
AAM40075	Human polypeptide	1017 . . . 1338	322/322 (100%)	0.0
	SEQ ID NO	1 . . . 322	322/322 (100%)
	3220 -homo sapiens,
	322 aa.
	[WO200153312-A1,
	26 JUL. 2001]
AAM41861	Human polypeptide	1016 . . . 1338	283/339 (83%)	e−160
	SEQ ID NO6792 - Homo	9 . . . 331	290/339 (85%)
	sapiens, 346 aa.
	[WO200153312-A1,
	26 JUL. 2001]

[0345] 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 2D.

TABLE 2D
Public BLASTP Results for NOV2a
			Identities/
		NOV2a	Similarities
Protein	Protein/	Residues/	for the
Accession	Organism/	Match	Matched	Expect
Number	Length	Residues	Portion	Value
Q9HCG5	KIAA1607 protein -	69 . . . 1338	1268/1270 (99%)	0.0
	Homo sapiens	1 . . . 1270	1270/1270 (99%)
	(Human), 1270 aa
	(fragment).
Q8TEN7	FLJ00156 protein -	57 . . . 1288	1212/1237 (97%)	0.0
	Homo sapiens	614 . . . 1850	1218/1237 (97%)
	(Human), 1887 aa
	(fragment).
BAA76837	KIAA0993 protein -	49 . . . 1269	498/1314 (37%)	0.0
	Homo sapiens	5 . . . 1288	747/1314 (55%)
	(Human), 1556 aa
	(fragment).
Q96N85	CDNA FLJ31244 fis,	708 . . . 1335	339/649 (52%)	0.0
	clone KIDNE2005042,	1 . . . 634	450/649 (69%)
	moderately similar
	to lysosomal
	trafficking
	regulator -Homo
	sapiens
	(Human), 722 aa.
Q96BE1	Hypothetical	1019 . . . 1338	319/320 (99%)	0.0
	34.6 kDa protein -	4 . . . 323	319/320 (99%)
	Homo sapiens
	(Human), 323 aa
	(fragment).

[0346] PFam analysis indicates that the NOV2a protein contains the domains shown in the Table 2E.

TABLE 2E
Domain Analysis of NOV2a
		Identities/
		Similarities
	NOV2a Match	for the	Expect
Pfam Domain	Region	Matched Region	Value
Beach	693 . . . 975	174/287 (61%)	1.8e−181
		240/287 (84%)
WD40	1128 . . . 1164	16/37 (43%)	0.00021
		28/37 (76%)
WD40	1213 . . . 1254	11/42 (26%)	0.25
		32/42 (76%)

Example 3

[0347] 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:11	552 bp
NOV3a,	GTGACATGTTGGGCTGTGGGATCCCAGCGCTGGGCCTGCTCCTGCTGCTGCAGGGCTC
CG122777-01
DNA Sequence	GGCAGACGGAAATGGAATCCAGGGATTCTTCTACCCATGGAGTTCCCCAGGCTGTGAG
	GGTGACATATGGGACCGGGAGAGCTGTGGGGGCCAGGCGGCCATCGATAGCCCCAACC
	TCTGCCTGCGTCTCCGGTGCTGCTACCGCAATGGGGTCTGCTACCACCAGCGTCCAGA
	CGAAAACGTGCGGAGGAAGCACATGTGGCCGCTGGTCTGGACGTGCAGCGGCCTCCTC
	CTCCTGAGCTGCAGCATCTGCTTGTTCTGGTGGGCCAAGCGCCGGGACGTGCTGCATA
	TGCCCGGTTTCCTGGCGGGTCCGTGTGACATGTCCAAGTCCGTCTCGCTGCTCTCCAA
	GCACCGAGGGACCAAGAAGACGCCGTCCACGGGCAGCGTGCCAGTCGCCCTGTCCAAA
	GAGTCCAGGGATGTGGAGGGAGGCACCGAGGGGGAAGGGACGGAGGAGGGTGAGGAGA
	CAGAGGGCGAGGAAGAGGAGGATTAGGGGA
	ORF Start: ATG at 6	ORF Stop: TAG at 546
	SEQ ID NO: 12	180 aa	Mw at 19698.1 kD
NOV3a,	MLGCGIPALGLLLLLQGSADGNGIQGFFYPWSSPGCEGDIWDRESCGGQAAIDSPNLC
CG122777-01
Protein Sequence	LRLRCCYRNGVCYHQRPDENVRRKHMWALVWTCSGLLLLSCSICLFWWAKRRDVLHMP
	GFLAGPCDMSKSVSLLSKHRGTKKTPSTGSVPVALSKESRDVEGGTEGEGTEEGEETE
	GEEEED

[0348] Further analysis of the NOV3a protein yielded the following properties shown in Table 3B.

TABLE 3B
Protein Sequence Properties NOV3a
PSort     0.4600 probability located in plasma membrane; 0.1000
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:

[0349] 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 3C.

TABLE 3C
Geneseq Results for NOV3a
		NOV3a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAW75084	Human secreted protein encoded by	1 . . . 180	177/180 (98%)	e−105
	gene 28 clone HHFGL62 - Homo	1 . . . 177	177/180 (98%)
	sapiens, 178 aa. [WO9839446-A2,
	11 SEP. 1998]
AAW75146	Human secreted protein encoded by	1 . . . 52	48/52 (92%)	2e−21
	gene 28 clone HHFGL62 - Homo	1 . . . 49	48/52 (92%)
	sapiens, 50 aa. [WO9839446-A2,
	11 SEP. 1998]
ABP25902	Streptococcus polypeptide SEQ ID	110 . . . 177	25/72 (34%)	1.0
	NO 980 - Streptococcus agalactiae,	432 . . . 502	31/72 (42%)
	1266 aa. [WO200234771-A2,
	02 MAY 2002]
ABP25903	Streptococcus polypeptide SEQ ID	110 . . . 177	24/72 (33%)	1.3
	NO 982 - Streptococcus pyogenes,	423 . . . 493	31/72 (42%)
	1257 aa. [WO200234771-A2,
	02 MAY 2002]
AAO12986	Human polypeptide SEQ ID NO	124 . . . 179	20/56 (35%)	1.3
	26878 - Homo sapiens, 984 aa.	271 . . . 326	25/56 (43%)
	[WO200164835-A2, 07 SEP. 2001]

[0350]

TABLE 3D
Public BLASTP Results for NOV3a
			Identities/
		NOV3a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q8WZ59	MDAC1 - Homo sapiens (Human),	1 . . . 180	177/180 (98%)	e−105
	177 aa.	1 . . . 177	177/180 (98%)
Q9D2E9	4930572D21Rik protein - Mus	1 . . . 177	112/178 (62%)	4e−60
	musculus (Mouse), 166 aa.	1 . . . 166	129/178 (71%)
AAH27748	Similar to complement component 8,	36 . . . 70	16/35 (45%)	2.3
	alpha polypeptide-Mus musculus	74 . . . 102	18/35 (50%)
	(Mouse), 587 aa.
AAL96855	Putative	110 . . . 177	24/72 (33%)	3.1
	phosphoribosylformylglycinamidine	423 . . . 493	31/72 (42%)
	synthase II - Streptococcus pyogenes
	(serotype M18), 1257 aa.
Q9A1Z2	Putative	110 . . . 177	24/72 (33%)	3.1
	phosphoribosylformylglycinamidine	423 . . . 493	31/72 (42%)
	synthase II - Streptococcus pyogenes,
	1257 aa.

[0351] PFam analysis indicates that the NOV3a protein contains the domains shown in the Table 3E.

TABLE 3E
Domain Analysis of NOV3a
		Identities/
		Similarities
	NOV3a Match	for the
Pfam Domain	Region	Matched Region	Expect Value
No Significant Matches Found

Example 4

[0352] 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: 13	994 bp
NOV4a,	TGTCGCCCCATCCCTGCGCGCCCAGCCTGCCAAGCAGCGTGCCCCGGTTGCAGGCGTC
CG124229-01
DNA Sequence	ATGCAGCGGGCGCGACCCACGCTCTGGGCCGCTGCGCTGACTCTGCTGGTGCTGCTCC
	GCGGGCCGCCGGTGGCGCGGGCTGGCGCGAGCTCGGGGGGCTTGGGTCCCGTGGTGCG
	CTGCGAGCCGTGCGACGCGCGTGCACTGGCCCAGTGCGCGCCTCCGCCCGCCGTGTGC
	GCGGAGCTGGTGCGCGAGCCGGGCTQCGGCTGCTGCCTGACGTGCGCACTGACCGAGG
	GCCAGCCGTGCGGCATCTACACCGAGCGCTGTGGCTCCGGCCTTCGCTGCCAGCCGTC
	GCCCGACGAGGCGCGACCGCTGCAGGCGCTGCTGGACGGCCGCGGGCTCTGCGTCAAC
	GCTAGTGCCGTCAGCCGCCTGCGCGCCTACCTGCTGCCACCCCCGCCAGCTCCAGGTG
	AGCCGCCCGCTCCAGGAAATGCTAGTGAGTCGGAGGAAGACCGCAGCGCCGCCAGTGT
	GGAGAGCCCGTCCGTCTCCAGCACGCACCGGGTGTCTGATCCCAAGTTCCACCCCCTC
	CATTCAAAGATAATCATCATCAAGAAAGGGCATGCTAAAGACAGCCAGCGCTACAAAG
	TTGACTACGAGTCTCAGAGCACACATACCCAGAACTTCTCCTCCGAGTCCAAGCGGGA
	GACAGAATATGGTCCCTGCCCTAGAGAAATGGAAOACACACTGAATCACCTGAAGTTC
	CTCAATGTGCTGAGTCCCAGGGGTGTACACATTCCCAACTGTGACAAGAAGGGATTTT
	ATAAGAAAAAGCAGTGTCGCCCTTCCAAAGGCAGGAAGCGGGGCTTCTGCTGGTGTGT
	GGATAAGTATGGGCAGCCTCTCCCAGGCTACACCACCAAGGGGAAGGAGGACGTGCAC
	TGCTACAGCATGCAGAGCAAGTAGACGCCTGCCGCAAGGTTAATGTGGAGCTCAAATA
	TGCCTTAT
	ORF Start: ATG at 59	ORF Stop: TAG at 950
	SEQ ID NO 14	297 aa	MW at 32208.4 kD
NOV4a,	MQRARPTLWAAALTLLVLLRGPPVARAGASSGGLGPVVRCEPCDARALAQCAPPPAVC
CG124229-01
Protein Sequence	AELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVN
	ASAVSRLRAYLLPAPPAPGEPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPL
	HSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNRLKF
	LNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVH
	CYSMQSK

[0353] Further analysis of the NOV4a protein yielded the following properties shown in Table 4B.

TABLE 4B
Protein Sequence Properties NOV4a
PSort     0.3703 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 28 and 29
analysis:

[0354] 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 4C.

TABLE 4C
Geneseq Results for NOV4a
			Identities/
		NOV4a	Similarities
		Residues/	for the
Geneseq	Protein/Organism/Length	Match	Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB09209	Human ibp3 CNN family protein	1 . . . 297	291/297 (97%)	e−175
	sequence SEQ ID NO: 19 - Homo	1 . . . 291	291/297 (97%)
	sapiens, 291 aa. [US2002049304-
	A1, 25 APR. 2002]
AAU85512	Clone #19095 (L549S) of lung	1 . . . 297	291/297 (97%)	e−175
	tumour protein - Homo sapiens,	1 . . . 291	291/297 (97%)
	291 aa. [WO200204514-A2, 17
	JAN. 2002]
AAB59880	IGFBP-3 protein - Homo sapiens,	1 . . . 297	291/297 (97%)	e−175
	291 aa. [WO200078341-A1, 28	1 . . . 291	291/297 (97%)
	DEC. 2000]
AAB76857	Human lung tumour protein related	1 . . . 297	291/297 (97%)	e−175
	protein sequence SEQ ID NO: 333 -	1 . . . 291	291/297 (97%)
	Homo sapiens, 291 aa.
	[WO200100828-A2, 04 JAN. 2001]
AAR89273	Insulin like growth factor binding	1 . . . 297	291/297 (97%)	e−175
	protein-3 - Homo sapiens, 291 aa.	1 . . . 291	291/297 (97%)
	[WO9601636-A1, 25 JAN. 1996]

[0355] 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 4D.

TABLE 4D
Public BLASTP Results for NOV4a
			Identities/
		NOV4a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
P17936	Insulin-like growth factor binding	1 . . . 297	291/297 (97%)	e−174
	protein 3 precursor (IGFBP-3) (IBP-	1 . . . 291	291/297 (97%)
	3) (IGF-binding protein 3) - Homo
	sapiens (Human), 291 aa.
Q9TTIO	Insulin-like growth factor-binding	1 . . . 297	243/299 (81%)	e−147
	protein 3 - Sus scrofa (Pig), 293 aa.	1 . . . 293	260/299 (86%)
Q9GJV5	Insulin-like growth factor binding	1 . . . 297	242/299 (80%)	e−145
	protein-3 - Bos taurus (Bovine), 291	1 . . . 291	257/299 (85%)
	aa.
P20959	Insulin-like growth factor binding	1 . . . 297	239/299 (79%)	e−143
	protein 3 precursor (IGFBP-3) (IBP-	1 . . . 291	255/299 (84%)
	3) (IGF-binding protein 3) - Bos
	taurus (Bovine), 291 aa.
P15473	Insulin-like growth factor binding	1 . . . 297	239/299 (79%)	e−142
	protein 3 precursor (IGFBP-3) (IBP-	1 . . . 292	255/299 (84%)
	3) (IGF-binding protein 3) - Rattus
	norvegicus (Rat), 292 aa.

[0356] PFam analysis indicates that the NOV4a protein contains the domains shown in the Table 4E.

TABLE 4E
Domain Analysis of NOV4a
		Identities/
		Similarities
Pfam Domain	NOV4a Match Region	for the Matched Region	Expect Value
IGFBP	40 . . . 99	39/84 (46%)	2.1e−26
		56/84 (67%)
thyroglobulin_1	219 . . . 291	37/81 (46%)	1.6e−32
		66/81 (81%)

Example 5

[0357] 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: 15	1854 bp
NOV5a,	GGACGAAGGAAACGAACGAGGGGGAGGGAGGTCCCTGTTTTGGAGGAGCTAGGAGCGT
CG124445-02
DNA Sequence	TGCCGGCCCCTGAAGTGGAGCGAGAGGGAGGTCCTTCGCCGTTTCTCCTGCCAGGGGA
	GGTCCCGGCTTCCCGTGGAGGCTCCGGACCAAGCCCCTTCAGCTTCTCCCTCCGGATC
	GATGTGCTGCTGTTAACCCGTGAGGAGGCGGCGGCGGCCACCAGCGGCAGCGGAAGATG
	GTGTTGCTGAGAGTGTTAATTCTGCTCCTCTCCTGGGCGGCGGGGATGGGAGGTCAGT
	ATGGGAATCCTTTAAATAAATATATCAGACATTATGAAGGATTATCTTACAATGTGGA
	TTCATTACACCAAAAACACCAGCGTGCCAAAAGAGCAGTCTCTCACATTACTTTTGCT
	CACGAAGTTGGACATAACTTTGGATCCCCACATGATTCTGGAACAGAGTGCACACCAG
	GAGAATCTAAGAATTTGGGTCAAAAAGAAAATGGCAATTACATCATGTATGCAAGAGC
	AACATCTGGGGACAAACTTAACAACAATAAATTCTCACTCTGTAGTATTAGAAATATA
	AGCCAAGTTCTTGAGAAGAAGAGAAACAACTGTTTTGTTGAATCTGGCCAACCTATTT
	TAAAGATGAATCCTGCTTCGATGCAAATCAACCAGAGCGAAGAAAATGCAAACTGAAA
	CCTGGGAAACAGTGCAGTCCAAGTCAAGGTCCTTGTTGTACAGCACAGTGTGCATTCA
	AGTCAAAGTCTGAGAAGTGTCGGGATGATTCAGACTGTGCAAGGGAAGGAATATGTAA
	TGGCTTCACAGCTCTCTGCCCAGCATCTGACCCTAAACCAAACTTCACAGACTGTAAT
	AGGCATACACAACTGTCCATTAATGGGCAATGTGCAGGTTCTATCTGTGAGAAATATG
	GCTTAGAGGAGTGTACGTGTGCCAGTTCTGATGGCAAAGATGATAAAGAATTATGCCA
	TGTATGCTGTATGAAGAAAATGGACCCATCAACTTGTGCCAGTACAGGGTCTGTGCAG
	TGGAGTAGGCACTTCAGTGGTCGAACCATCACCCTGCAACCTGGATCCCCTTGCAACG
	ATTTTAGAGGTTACTGTGATGTTTTCATGCGGTGCAGATTAGTAGATGCTGATGGTCC
	TCTAGCTAGGCTTAAAAAAGCAATTTTTAGTCCAGAGCTCTATGAAAACATTGCTGAA
	TGGATTGTGGCTCATTGGTGGGCAGTATTACTTATGGGAATTGCTCTGATCATGCTAA
	TGGCTGGATTTATTAAGATATGCAGTGTTCATACTCCAAGTAGTAATCCAAAGTTGCC
	TCCTCCTAAACCACTTCCAGGCACTTTAAAGAGGAGGAGACCTCCACAGCCCATTCAG
	CAACCCCAGCGTCAGCGGCCCCGAGAGACTTATCAAATGGGACACATGAGACGCTAAC
	TGCAGCTTTTGCCTTGGTTCTTCCTAGTGCCTACAATGGGAAAACTTCACTCCAAAGA
	GAAACCTATTAAGTCATCATCTCCAAACTAAACCCTCACAAGTAACAGTTGAAGAAAA
	AATGGCAAGAGATCATATCCTCAGACCAGGTGGAATTACTTAAATTTTAAAGCCTGAA
	AATTCCAATTTGGGGGTGGGAGGTGGAAAAGGAACCCAATTTTCTTATGAACAGATAT
	TTTTAACTTAATGGCACAAAGTCTTAGAATATTATTATGTGCCCCGTGTTCCCTGTTC
	TTCGTTGCTGCATTTTCTTCACTTGCAGGCAAACTTGGCTCTCAATAAACTTTTCG
	ORF Start: ATG at 230	ORF Stop: TAA at 1505
	SEQ ID NO: 16	425 aa	MW at 47237.5 kD
NOV5a,	IVIVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHITF
CG124445-02
Protein Sequence	AHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCS IRN
	ISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKL~
	KPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDC
	NRHTQVCINGQCACSICEKYGLEECTCASSDGKDDKELCHVCCMKKNDPSTCASTGSV
	QWSRHFSGRTITLQPGSPCNDFRGYCDVPMRCRLVDADGPLARLKKAIFSPELYENIA
	EWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPI
	QQPQRQRPRESYQMGHMRR

[0358] Further analysis of the NOV5protein yielded the following properties shown in

TABLE 5B
Table 5B. Protein Sequence Properties NOV5a
PSort     0.4600 probability located in plasma membrane;
analysis: 0.1800 probability located in nucleus; 0.1000 probability
          located in endoplasmic reticulum (membrane); 0.1000
          probability located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 20 and 21
analysis:

[0359] 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 5C.

TABLE 5C
Geneseq Results for NOV5a
		NOV5a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB62520	Human ADAM10 polypeptide -	8 . . . 425	381/422 (90%)	0.0
	Homo sapiens, 748 aa.	327 . . . 748	389/422 (91%)
	[US6228648-B1, 08 MAY 2001]
AAG64048	Human ADAM10 protein - Homo	8 . . . 425	381/422 (90%)	0.0
	sapiens, 748 aa. [JP2001128677-A,	327 . . . 748	389/422 (91%)
	15 MAY 2001]
AAY79033	Human Kuz amino acid sequence -	8 . . . 425	381/422 (90%)	0.0
	Homo sapiens, 691 aa.	270 . . . 691	389/422 (91%)
	[WO200002897-A2, 20 JAN. 2000]
AAY16776	Human disintegrin metalloprotease	8 . . . 425	381/422 (90%)	0.0
	(KUZ) polypeptide - Homo sapiens,	327 . . . 748	389/422 (91%)
	748 aa. [EP921197-A2, 09 JUN.
	1999]
AAW56132	Homo sapiens transmembrane KUZ	8 . . . 425	381/422 (90%)	0.0
	protein - Homo sapiens, 748 aa.	327 . . . 748	389/422 (91%)
	[WO9808933-A1, 05 MAR. 1998]

[0360] 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 5D.

TABLE 5D
Public BLASTP Results for NOV5a
			Identities/
		NOV5a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
S52920	disintegrin (EC 3.4.24.-) - human,	8 . . . 425	381/422 (90%)	0.0
	491 aa (fragment).	70 . . . 491	389/422 (91%)
Q10742	Disintegrin-metalloprotease MADM -	8 . . . 425	381/422 (90%)	0.0
	Homo sapiens (Human), 691 aa	270 . . . 691	389/422 (91%)
	(fragment).
O14672	ADAM10 - Homo sapiens (Human),	8 . . . 425	381/422 (90%)	0.0
	748 aa.	327 . . . 748	389/422 (91%)
Q10743	Disintegrin-metalloprotease	8 . . . 425	371/422 (87%)	0.0
	precursor (EC 3.4.24.-)(Myelin-	123 . . . 544	386/422 (90%)
	associated metalloproteinase)
	(MADM)-Rattus norvegicus (Rat),
	544 aa(fragment).
O35598	Kuzbanian - Mus musculus (Mouse),	8 . . . 425	370/422 (87%)	0.0
	749 aa.	328 . . . 749	385/422 (90%)

[0361] PFam analysis indicates that the NOV5a protein contains the domains shown in the Table 5E.

TABLE 5E
Domain Analysis of NOV5a
			Identities/
			Similarities
			for the
	Pfam	NOV5a Match	Matched	Expect
	Domain	Region	Region	Value
	squash	200 . . . 221	8/22 (36%)	0.25
			12/22 (55%)
	disintegrin	143 . . . 226	33/85 (39%)	2.2e−08
			54/85 (64%)

Example 6

[0362] 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:17	725 bp
NOV6a,	GAGGTAGGTCCAGGACGGGCGCACAGCAGCAGCCGAGGCTGGCCGGGAGAGGGAGGAA
CG124590-02
DNA Sequence	GAGGATGGCAGGGCCACGCCGCAGCCCATGGGCCAGGCTGCTCCTGGCAGCCTTGATC
	AGCGTCACCCTCTCTGGGACCTTGGCAAACCGCTGCAAGAAGGCCCCAGTGAAGAGCT
	GCACGGAGTGTGTCCGTGTGGATAAGGACTGCGCCTACTGCGCAGACGAGATGTTCAG
	GGACCGGCGCTGCAACACCCAGGCGGAGCTGCTGGCCGCGGGCTGCCAGCGGGAGAGC
	ATCGTGGTCATGGAGAGCAGCTTCCAAATCACAGAGGAGACCCAGATTGACACCACCC
	TGCGGCGCAGCCAGATGTCCCCCCAAGGCCTGCGGGTCCGTCTGCGGCCCGGTGAGGA
	GCGGCATTTTGAGCTGGAGGTGTTTGACCCACTGGACAGCCCCGTGGACCTGTACATC
	CTCATGGACTTCTCCAACTCCATGTCCGATGATCTGGACAACCTCAAGAAGATGGGGC
	AGAACCTGGCTCGGGTCCTGAGCCAGCTCACCAGCGCCACCGAGCCCTTCCTAGTGGA
	TGGGCCGACCCTGGGGGCCCAGCACCTGGAGGCAGGCGGCTCCCTCACCCGGCATGTG
	ACCCAGGAGTTTGTGAGCCGGACACTGACCACCAGCGGAACCCTTAGCACCCACATGG
	ACCAACAGTTCTTCCAAACTTGACCGCAC
	ORF Start: ATG at 63	ORF Stop: TGA at 717
	SEQ ID NO: 18	218 aa	MW at 24305.3 kD
NOV6a,	MAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCADEMFRD
CG124590-02
Protein Sequence	RRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEER
	HFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSATEPFLVDG
	PTLGAQHLEAGGSLTRHVTQEFVSRTLTTSGTLSTHMDQQFFQT

[0363] Further analysis of the NOV6a protein yielded the following properties shown in Table 6B.

TABLE 6B
Protein Sequence Properties NOV6a
PSort     0.5135 probability located in outside; 0.1000 probability
analysis: located in endoplasmic reticulum (membrane); 0.1000
          probability located in endoplasmic reticulum (lumen);
          0.1000 probability located in microbody (peroxisome)
SignalP   Cleavage site between residues 28 and 29
analysis:

[0364] 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 6C.

TABLE 6C
Geneseq Results for NOV6a
			Identities/
		NOV6a	Similarities
		Residues/	for the
Geneseq	Protein/Organism/Length	Match	Matched	Expect
Identifier	[Patent#, Date]	Residues	Region	Value
AAB68089	Amino acid sequence of the beta4	1 . . . 165	164/165 (99%)	2e−90
	part of alpha6beta4 integrin - Homo	1 . . . 165	164/165 (99%)
	sapiens, 1875 aa. [WO200130854-
	A2, 03 MAY 2001]
AAR55273	Beta subunit of integrin cell surface	1 . . . 165	164/165 (99%)	2e−90
	receptor - Homo sapiens, 1822 aa.	1 . . . 165	164/165 (99%)
	[US5320942-A, 14 JUN. 1994]
AAM35512	Peptide #9549 encoded by probe for	89 . . . 156	68/68 (100%)	1e−32
	measuring placental gene expression -	1 . . . 68	68/68 (100%)
	Homo sapiens, 68 aa.
	[WO200157272-A2, 09 AUG. 2001]
AAM20582	Peptide #7016 encoded by probe for	89 . . . 156	68/68 (100%)	1e−32
	measuring cervical gene expression -	1 . . . 68	68/68 (100%)
	Homo sapiens, 68 aa.
	[WO200157278-A2, 09 AUG. 2001]
AAM75399	Human bone marrow expressed	89 . . . 156	68/68 (100%)	1e−32
	probe encoded protein SEQ ID NO:	1 . . . 68	68/68 (100%)
	35705 - Homo sapiens, 68 aa.
	[WO200157276-A2, 09 AUG. 2001]

[0365] 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 6D.

TABLE 6D
Public BLASTP Results for NOV6a
			Identities/
		NOV6a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
JC5545	integrin beta-4 precursor, splice	1 . . . 165	164/165 (99%)	4e−90
	form E - human, 964 aa.	1 . . . 165	164/165 (99%)
A36429	integrin beta-4 chain precursor -	1 . . . 165	164/165 (99%)	4e−90
	human, 1875 aa.	1 . . . 165	164/165 (99%)
P16144	Integrin beta-4 precursor (GP150)	1 . . . 165	164/165 (99%)	4e−90
	(CD104 antigen) - Homo sapiens	1 . . . 165	164/165 (99%)
	(Human), 1822 aa.
Q64632	Integrin beta-4 precursor (GP150)	1 . . . 165	123/165 (74%)	5e−69
	(CD104 antigen) - Rattus	1 . . . 165	145/165 (87%)
	norvegicus (Rat), 1807 aa.
JN0786	integrin beta-4 chain precursor -	1 . . . 165	126/166 (75%)	1e−67
	mouse, 1748 aa.	1 . . . 166	145/166 (86%)

[0366] PFam analysis indicates that the NOV6a protein contains the domains shown in the Table 6E.

TABLE 6E
Domain Analysis of NOV6a
			Identities/
			Similarities
			for the
	Pfam	NOV6a Match	Matched	Expect
	Domain	Region	Region	Value
	integrin_B	37 . . . 165	65/143 (45%)	2.3e−89
			129/143 (90%)

Example 7

[0367] 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:19	1140 bp
NOV7a,	AGGACAACCCCAGCAATGTGGAGAAGCCTGGGGCTTGCCCTGGCTCTCTGTCTCCTCC
CG124916-01
DNA Sequence	CATCGGGAGGAACACAGAGCCAGGACCAAAGCTCCTTATGTAAGCAACCCCCAGCCTG
	GAGCATAAGAGATCAAGATCCAATGCTAAACTCCAATGGTTCAGTGACTGTGGTTGCT
	CTTCTTCAAGCCTCATTTTATGTATTTCTTCCCAAATATTTTAGATTAGAAGACCTGC
	GAGTAAAACTGAAGAAAGAAGGATATTCTAATATTTCTTATATTGTTGTTAATCATCA
	AGCAATCTCTTCTCGATTAAAATACACACATCTTAAGAATAAGGTTTCAGAGCATATT
	CCTGTTTATCAACAAGAAGAAAACCAAACAGATGTCTGGACTCTTTTAAATGGAAGCA
	AAGATGACTTCCTCATATATGATAGGTGTGGCCGTCTTGTATATCATCTTGGTTTGCC
	TTTTTCCTTCCTAACTTTCCCATATGTAGAAGAAGCCATTAAGATTGCTTACTGTGAA
	AAGAAATGTGGAAACTGCTCTCTCACGACTCTCAAAGATGAAGACTTTTGTAAACGTG
	TATCTTTGGCTACTGTGGATAAAACAGTTGAAACTCCATCGCCTCATTACCATCATGA
	GCATCATCACAATCATGGACATCAGCACCTTGGCAGCAGTGAGCTTTCAGAGAATCAC
	CAACCAGGAGCACCAAATGCTCCTACTCATCCTGCTCCTCCACGCCTTCATCACCACC
	ATAAGCACAAGGGTCAGCATAGGCAGGGTCACCCAGAGAACCGAGATATGCCAGCAAG
	TGAAGATTTACAAGATTTACAAAAGAAGCTCTGTCGAAAGAGATGTATAAATCAATTA
	CTCTGTAAATTGCCCACAGATTCAGAGTTGGCTCCTAGGAGCTGATGCTGCCATTGTC
	GACATCTGATATTTGAAAAAACAGGGTCTGCAATCACCTGACAGTGTAAAGAAAACCT
	CCCATCTTTATGTAGCTGACAGGGACTTCGGGCAGAGGAGAACATAACTGAATCTTGT
	CAGTGACGTTTGCCTCCAGCTGCCTGACAPATAAGTCAGCAGCTTATACCCACAGAAG
	CCAGTGCCAGTTGACGCTGAAAGAATCAGGCAAAAAAG
	ORF Start: ATG at 16	ORF Stop: TGA at 913
	SEQ ID NO 20	299 aa	MW at 34008.2 kD
NOV7a,	MWRSLGLALALCLLPSGGTESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQAS
CG124916-01
Protein Sequence	FYVFLPKYFRLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQ
	EENQTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGN
	CSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAP
	NAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLP
	TDSELAPRS

[0368] Further analysis of the NOV7a protein yielded the following properties shown in Table 7B.

TABLE 7B
Protein Sequence Properties NOV7a
PSort     0.5135 probability located in outside; 0.1900 probability
analysis: located in lysosome (lumen); 0.1000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 22 and 23
analysis:

[0369] 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 7C.

TABLE 7C
Geneseq Results for NOV7a
			Identities/
		NOV7a	Similarities
		Residues/	for the
Geneseq	Protein/Organism/Length	Match	Matched	Expect
Identifier	[Patent#, Date]	Residues	Region	Value
AAU84306	Human endometrial cancer related	1 . . . 299	290/299 (96%)	e−176
	protein, SEPP1 - Homo sapiens, 381	1 . . . 299	294/299 (97%)
	aa. [W0200209573-A2, 07 FEB.
	2002]
AAB03188	Human selenoprotein P - Homo	1 . . . 299	290/299 (96%)	e−176
	sapiens, 381 aa. [WO200031131-	1 . . . 299	294/299 (97%)
	A1, 02 JUN. 2000]
AAB57080	Human prostate cancer antigen	60 . . . 299	232/240 (96%)	e−142
	protein sequence SEQ ID NO: 1658 -	1 . . . 240	236/240 (97%)
	Homo sapiens, 240 aa.
	[WO200055174-A1, 21 SEP. 2000]
AAG03755	Human secreted protein, SEQ ID	219 . . . 299	81/81 (100%)	8e−45
	NO:7836 - Homo sapiens, 110 aa.	30 . . . 110	81/81 (100%)
	[EP1033401-A2, 06 SEP. 2000]
AAO06297	Human polypeptide SEQ ID NO	70 . . . 147	64/113 (56%)	8e−24
	20189 - Homo sapiens, 113 aa.	1 . . . 113	69/113 (60%)
	[WO200164835-A2, 07 SEP. 2001]

[0370] 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 7D.

TABLE 7D
Public BLASTP Results for NOV7a
			Identities/
		NOV7a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
P49908	Selenoprotein P precursor (SeP) -	1 . . . 299	290/299 (96%)	e−176
	Homo sapiens (Human), 381	1 . . . 299	294/299 (97%)
	aa.
Q9N2H6	Selenoprotein P - Bos taurus	1 . . . 296	217/300 (72%)	e−124
	(Bovine), 386 aa.	1 . . . 300	241/300 (80%)
P25236	Selenoprotein P precursor (SeP) -	1 . . . 299	215/304 (70%)	e−123
	Rattus norvegicus (Rat), 385	1 . . . 304	243/304 (79%)
	aa.
AAA42129	Selenoprotein P precursor -	1 . . . 299	214/304 (70%)	e−122
	Rattus norvegicus (Rat), 385 aa.	1 . . . 304	242/304 (79%)
P70274	Selenoprotein P precursor (SeP) -	1 . . . 299	211/301 (70%)	e−121
	Mus musculus (Mouse), 380	1 . . . 299	244/301 (80%)
	aa.

[0371] PFam analysis indicates that the NOV7a protein contains the domains shown in the Table 7E.

TABLE 7E
Domain Analysis of NOV7a
			Identities/
			Similarities
		NOV7a	for the
	Pfam	Match	Matched	Expect
	Domain	Region	Region	Value
	No Significant Matches Found

Example 8

[0372] 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 21	3123 bp
NOV 8a,	GATTCCAAGTCGCTGCTGTGCAGAGCAGCAAGTGCTCCGTGCAGGGCTGTTGCTATCA
CG126224-01
DNA Sequence	CTTGGAGGTGAACAGCCTCTTTGCCGGTATTCAGTGAAGAAAGCAAGTCTAAATATGC
	AGTTCTCTCACTGGAGTGAAAGATGTTTGTTCATTTCTAATCAACTATGCTAGACAGC
	TGCAAGCTGAAAAGTGCCTGCAATTTGCCATTTATTTGTAATAAGAAAATAATAAACA
	CTGCTGGAACCAGTAATGCAGAAGTCCCCTTGGCTGATCCCGGAATGTACCAGCTGGA
	CATTACATTAAGAAGGGGTCAAAGTTTAGCTGCTCGAGATCGAGGAGGGACGAGTGAT
	CCATATGTGAAGTTTAAAATCGGAGGAAAAGAAGTTTTTAGAAGTAAGATAATACACA
	AGAACCTCAACCCTGTGTGGGAAGAAAAAGCTTGTATTCTGGTTGATCATCTTAGGGA
	GCCATTGTATATAAAGGTATTTGACTATGATTTTGGACTACAGGATGACTTTATGGGC
	TCAGCCTTTCTGGATCTGACACAATTGGAGTTAAACAGGCCCACAGATGTGACCCTTA
	CTCTGAAAGATCCTCATTATCCTGACCATGATCTTGGAATCATTTTGCTCTCAGTCAT
	CCTTACCCCTAAAGAAGGAGAGTCCAGGGAGTTTCAGACCCAAAGTTTACGCCTATCA
	GACCTACACAGAAAATCGCATCTTTGGAGAGGAATAGTCAGCATCACCTTGATTGAAG
	GGAGAGACCTCAAGGCCATGGATTCCAACGGGTTGAGCGATCCCTACGTGAAGTTCCG
	GCTTGGGCATCAGAAGTACAAGAGCAAGATTATGCCAAAAACGTTGAATCCTCAGTGG
	AGGGAACAATTTGATTTTCACCTTTATGAAGAAAGAGGAGGAGTCATTGATATCACTG
	CATGGGACAAAGATGCTGGGAAAAGGGATGATTTCATTGGCAGGTGCCAGGTCGACCT
	GTCAGCCCTCAGTAGGGAACAGACGCACAAGCTGGAGTTGCAGCTGGAAGAGGGTGAG
	GGACACCTGGTGCTGCTGGTCACTCTGACAGCATCAGCCACAGTCAGCATCTCTGACC
	TGTCTGTCAACTCCCTGGAGGACCAGAAGGAACGAGAGGAGATATTAAAGAGATATAG
	CCCATTGAGGATATTTCACAACCTGAGAGATGTGGGATTTCTCCAGGTGAAAGTCATC
	AGAGCGGAAGGGTTAATCGCTGCCGACGTCACTGGAAAAAGTGACCCATTTTGTGTGG
	TAGAACTGAACAAAGATAGACTGCTAACACATACTGTCTACAAAAATCTCAATCCTGA
	GTGGAATAAAGTCTTCACGTTCAACATTAAAGATATCCATTCAGTTCTTGAAGTGACA
	GTTTATGATGAAGATCGGGATCGAAGTGCTGACTTTCTGGGCAAAGTTGCTATACCAT
	TGCTGTCTATTCAAAATGGTGAACAGAAAGCCTACGTCTTGAAAAACAGGCAGCTGAC
	AGGGCCAACAAAGGGGGTCATCTATCTTGAAATAGATGTGATTTTTAATGCTGTGAAA
	GCCAGCTTACGAACATTAATACCCAAAGAACAGAAGTACATTGAAGAGGAAAACAGAC
	TCTCTAAACAGCTGCTACTAAGAAACTTTATCAGAATGAAACGTTGTGTCATGGTGCT
	GGTAAATGCTGCATACTACGTTAATAGTTGCTTTGATTGGGATTCACCCCCAAGGAGT
	CTCGCTGCTTTTGTGGTAGTGGAGGACATGCTAGAGGACGAGGAAGAAGAAGATGACA
	AAGATGACAAGGACAGTGPAAAAAAGGGATTTATAAATAAAATCTATGCCATCCAGGA
	GGTATGTGTCAGTGTCCAGAACATCCTAGATGAAGTGGCTTCCTTTGGCGAAAGGATA
	AAGAGTACTTTCAACTGGACTGTCCCATTCTTAAGCTGGCTGGCCATTGTAGCCCTCT
	GTGTGTTCACAGCCATCCTGTACTGCATTCCGCTGAGATACATTGTCCTTGTCTGGGC
	CATCAATAAATTTACAAAAAAGCTTCGCAGTCCATATGCAATTGATAACAATGAACTA
	CTTGACTTCCTTTCCAGAGTCCCTTCAGATGTACAAGTGGTGCAATACCAAGAACTGA	ee
	AACCAGATCCTTCTCATAGCCCATATAAAAGAAAGAAAAACAATCTTGGCTAGCCAGC
	TCCCAGCACTGAGGAGACCAGCATCTGTTTGGGAAGATAAAAGAAAAAGCCCTCAGCC
	TCAGCAGCATTTCCTTTCTTTCTGCTTTTTATTTATTTTGCCTTTTTATCATGATCGA
	GAGAATCTGTAAATAGTGTACAAAGGCATATGTCTTTGAATATATACTTCTATTGTAC
	AGACTCAACTTGATAAAGGTTTTGCTACTGCTGTGTCAAAACCTTGTTAGCTGTGGAT
	AATAATATAACACACTGAAAGAACAAATATAAGAATGATAACACTGGAAGATATATTC
	TTATCTAATTACAAGTGGATTkAATACTCACCTGTGCTCTGATTAAATCTACATCAAT
	TGTAAATGTCGATTTGATTTTAAAGTTTTTTTTTAATGCGACTATTTTTTATCTGAAA
	AGTAATCCATTACACTTTTCTATGTTTTATACATTTCAAAAGGGAGGGAAATTCCAAA
	GCCTGAATAATGGAATGGATACATTTCAATTTAACATATATTCTGGCTTTAGATCCCG
	ACATTCACTCCTGTGCAAATTACTTAGGTATGACTTAGGCTAATTTTAAGCTAATAAG
	TGAAGGTACATTCACTCCCTCAAGAGAATCAATACTCAGAAGGTTACAAAGTTTTCTT
	TATAGAATTTCAATCAATCATTCCATCTAAAACCTTAAAATCTCTACAGGACTACATA
	ACATAAATACTGCCAGTTTATAAACGATTGCCTATCTGAATTTTTATACCTACCACTA
	CTTTAATTTATACAGTTAGTTAGCAAATTAGCAACCCAGTAAGTACAGTTATCAAAAA
	TACTAGGAAACTATATCCATATCGCTTTTGGTGTCAGATTGTATCTGTGCATCTAAAA
	ATATTTTAATAAATACTCAAGTGCTCTCAGAGAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 163	ORF Stop: TAG at 2197
	SEQ ID NO: 22	678 aa	MW at 77717.4 kD
NOV8a,	MLDSCKLKSACNLPFICNKKIINTAGTSNAEVPLADPGMYQLDITLRRGQSLAARDRC
CG126224-01
Protein Sequence	GTSDPYVKFKIGGKEVFRSKIIHKNLNPVWEEKACILVDHLREPLYIKVFDYDFGLQD
	DFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGESREFQTQS
	LRLSDLHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTL
	NPQWREQFDFHLYEERGGVIDITAWDKDAGKRDDFIGRCQVDLSALSREQTHKLELQL
	EEGEGHLVLLVTLTASATVSISDLSVNSLEDQKEREEILKRYSPLRIFHNLRDVGFLQ
	VKVIRAEGLMAADVTGKSDPFCVVELNKDRLLTHTVYKNLNPEWNKVFTFNIKDIHSV
	LEVTVYDEDRDRSADFLGKVAIPLLSIQNGEQKAYVLKNRQLTGPTKGVIYLEIDVIF
	NAVKASLRTLIPKEQKYIEEENRLSKQLLLRNFIRMKRCVMVLVNAAYYVNSCFDWDS
	PPRSLAAFVVVEDMLEDEEEEDDKDDKDSEKKGFINKIYAIQEVCVSVQNILDEVASF
	GERIKSTFNWTVPFLSWLAIVALCVFTAILYCIPLRYIVLVWGINKFTKKLRSPYAID
	NNELLDFLSRVPSDVQVVQYQELKPDPSHSPYKRKKNNLG

[0373] Further analysis of the NOV8a protein yielded the following properties shown in Table 8B.

TABLE 8B
Protein Sequence Properties NOV8a
PSort     0.8500 probability located in endoplasmic reticulum
analysis: (membrane); 0.4400 probability located in plasma membrane;
          0.3000 probability located in microbody (peroxisome);
          0.1000 probability located in mitochondrial
          inner membrane
SignalP   No Known Signal Sequence Indicated
analysis:

[0374] 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 8C.

TABLE 8C
Geneseq Results for NOV8a
		NOV8a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB93562	Human protein sequence SEQ ID	250 . . . 677	254/465 (54%)	e−140
	NO: 12957 - Homo sapiens, 466 aa.	2 . . . 466	329/465 (70%)
	[EP1074617-A2, 07 FEB. 2001]
ABB11104	Human C2 domain homologue, SEQ	168 . . . 400	226/233 (96%)	e−129
	ID NO: 1474 - Homo sapiens, 485	18 . . . 250	230/233 (97%)
	aa. [WO200157188-A2, 09 AUG.
	2001]
ABB70130	Drosophila melanogaster	168 . . . 676	228/552 (41%)	e−102
	polypeptide SEQ ID NO 37182 -	452 . . . 975	326/552 (58%)
	Drosophila melanogaster, 983 aa.
	[WO200171042-A2, 27 SEP. 2001]
AAU87251	Novel central nervous system	201 . . . 365	164/165 (99%)	4e−90
	protein #161 - Homo sapiens, 166	1 . . . 165	165/165 (99%)
	aa. [WO200155318-A2, 02 AUG.
	2001]
AAG66417	Human C2 domains protein,	532 . . . 678	146/147 (99%)	4e−81
	BioHC2 - Homo sapiens, 175 aa.	29 . . . 175	147/147 (99%)
	[CN1296954-A, 30 MAY 2001]

[0375] 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 8D.

TABLE 8D
Public BLASTP Results for NOV8a
		NOV8a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q96LX0	CDNA FLJ33132 fis, clone	1 . . . 678	672/692 (97%)	0.0
	UMVEN2000133, weakly similar	1 . . . 692	677/692 (97%)
	to rabphilin-3A - Homo sapiens
	(Human), 692 aa.
AAH30005	Hypothetical 68.5 kDa protein -	1 . . . 533	514/593 (86%)	0.0
	Homo sapiens (Human), 600 aa.	1 . . . 593	522/593 (87%)
Q9H6E8	CDNA: FLJ22344 fis, clone	358 . . . 678	320/321 (99%)	0.0
	HRC06080 - Homo sapiens	1 . . . 321	320/321 (99%)
	(Human), 321 aa.
Q8SZ34	RE18318p - Drosophila	168 . . . 676	238/552 (43%)	e−113
	melanogaster (Fruit fly), 596 aa.	51 . . . 588	337/552 (60%)
Q9V8M4	CG15078 protein - Drosophila	168 . . . 676	228/552 (41%)	e−102
	melanogaster (Fruit fly), 983 aa.	452 . . . 975	326/552 (58%)

[0376] PFam analysis indicates that the NOV8a protein contains the domains shown in the Table 8E.

TABLE 8E
Domain Analysis of NOV8a
			Identities/
			Similarities
	Pfam	NOV8a	for the	Expect
	Domain	Match Region	Matched Region	Value
	C2	42 . . . 123	30/97 (31%)	4e−18
			61/97 (63%)
	C2	191 . . . 272	37/97 (38%)	3e−27
			68/97 (70%)
	C2	347 . . . 427	37/97 (38%)	1.9e−20
			61/97 (63%)

Example 9

[0377] The NOV9 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 9A.

TABLE 9A
NOV9 Sequence Analysis
	SEQ ID NO: 23	2376 bp
NOV9a,	ATGAATGACACAGAAAAACCAGCAGATACTCCCTCTGAGGAAGAGGACTTTGGTGATC
CG126233-01
DNA Sequence	CAAGGACATATGACCCAGATTTCAAGGGGCCTGTTGCCAACAGGAGTTGTACAGATGT
	TCTGTGCTGTATGATCTTCCTACTGTGTATTATTGGCTACATTGTTTTAGGACTTGTC
	GCCTGGGTACATGGGGACCCCAGAAGAGCAGCCTATCCTACAGACAGCCAGGGCCACT
	TTTGTGGCCAGAAGGGCACTCCCAATGAGAACAAGACCATTTCGTTTTACTTTAACCT
	GTTACGCTGTACCAGTCCCTCCGTATTCCTAAACCTACAGTGCCCTACCACACAGATC
	TGTGTCTCCAAGTGCCCAGAAAAATTTTTAACCTATGTGGAAATGCAACTTTTGTACA
	CAAAAGACAAAAGCTACTGGGAAGACTACCGTCAGTTCTGTAAGACCACTGCTAAGCC
	TGTGAAGTCTCTCACACAGCTTTTACTGGATGATGATTGTCCAACAGCGATTTTTCCC
	AGCAAACCTTGTCTCCAGAGATGTTTCCCTGACTTCTCTACCAAAAATGGCACTTTAA
	CAATAGGAAGTAACATGATGTTCCAAGATGGAAATGGACGGACAAGAAGTGTTGTAGA
	ACTCGGGATTGCTGCAAATGGTATCAATAAACTTCTTGATGCAAAGTCACTTGGATTG
	AAAGTGTTTGAAGACTATGCAAGAACTTGGTATTGGATTCTCATTGGCCTGACGATTG
	CCATGGTCCTTAGTTGGATATTTTTGATACTTCTGAGGTTCATAGCTGGATGCCTCTT
	CTGGGTCTTCATGATTGGTGTGATTGGAATTATAGGTTATGGAATATGGCACTGTTAC
	CAGCAGTACACCAATCTTCAGGAACGCCCAAGTTCTGTATTAACTATCTATGACATCG
	GGATTCAGACTAACATAAGCATGTACTTTGAACTGCAACAAACATGGTTCACATTTAT
	GATAATACTCTGCATCATTGAAGTGATTGTCATCCTCATGCTGATCTTCCTCAGGAAT
	CGAATCCGAGTCGCCATTATCCTGCTGAAGGAAGGAAGCAAAGCCATTGGATATGTTC
	CTAGTACATTAGTCTATCCAGCTTTAACTTTCATTTTGCTCTCAATCTGCATTTGCTA
	CTGGGTCGTGACACCAGTGTATCAGATTTTTAATACAACTGAAATTGCCAAAGCTTGC
	CCTGGGGCTCTGTGTAACTTTGCTTTCTATGGTGGAAAGAGCTTGTACCATCAGTACA
	TCCCTACCTTCCATGTATACAACTTATTTGTCTTTCTCTGGCTTATAAACTTCGTCAT
	TGCATTAGGTCAGTGCGCCCTTGCTGGTGCATTCGCTACTTATTACTGGCCCATGAAA
	AAACCTGATGACATCCCACGATATCCACTTTTTACTGCATTTGGACGAGCCATACCAT
	ATCACACAGGATCCCTAGCATTTGGATCTTTAATTATTGCATTAATTCAAATGTTTAA
	AATTGTACTAGAATACTTGGACCACCGTCTTAAACGTACCCAGAACACATTGTCTAAA
	TTCCTACAATGCTGCCTGAGATGCTGCTTCTGGTGTTTGGAAAATGCAATAAAGTTTT
	TAAACAGAAATGCCTATATTATGATTGCAATATATGGCAGAAACTTCTGCAGGTCAGC
	AAAAGATGCTTTCAATCTGCTGATGAGAAATATACTAAAAGTTGCAGTTACAGATGAA
	GTTACATACTTTGTATTATTCCTGGGGAAACTTCTAGTTGCTGGAAGTATAGGTGTTC
	TGGCCTTCCTATTCTTCACACAAAGACTGCCAGTGATTGCACAACGACCAGCATCTTT
	AAATTACTACTGGGTACCTTTGCTGACAGTCATTTTTGGGTCTTACCTGATTGCACAT
	GGGTTCTTCACCGTCTATGCAATGTGTGTTGAAACAATTTTCATCTGCTTCTTGGAAG
	ATTTAGAAAGAAATGATGGTTCTACTGCPAGACCTTATTATGTGAGTCAACCTTTGCT
	GAAGATTTTCCAGGAGGAATCCACAAACTAGGAAGCAGTAGAAGAGCAAAACTGGTC
	GTCCTACAGCTGTGTGTTACCTTTTCTCCATCTGCTGTGTCTGTGCAACATTTGTTTC
	ATAAGTGCTTTGTGTTTAGCAACACTGTATTCACGACCTTGTTGGCTTGCATTTGCAT
	GTTTTATACCAAAGCTTATACTGTACTATGTGAAGCCATCAGAAGTCGCAAGGGAATT
	GTTAATAACATAAAACATTTTTATACTAAGATCATTTGTTTTGTIATTCGTTTTTAAA
	GAGTGGCTTGGATGTTTTGAAAATACTACTGAATATGTTAATATTCTTTTAAATCT
	ORf Start: ATG at 1	ORf Stop: TAG at 2071
	SEQ ID NO:24	690 aa	MW at 78829.8 kD
NOV9a,	MNDTEKPADTPSEEEDFGDPRTYDPDFKGPVANRSCTDVLCCMIFLLCIIGYIVLGLV
CG126233-01
Protein Sequence	AWVHGDPRRAAYPTDSQGHFCGQKGTPNENKTISFYFNLLRCTSPSVLLNLQCPTTQI
	CVSKCPEKFLTYVEMQLLYTKDKSYWEDYRQFCKTTAKPVKSLTQLLLDDDCPTAIFP
	SKPCLQRCFPDFSTKNGTLTIGSKMMFQDGNGRTRSVVELGIAANGINKLLDAKSLGL
	KVFEDYARTWYWILIGLTIAMVLSWIFLILLRFIAGCLFWVFMIGVIGIIGYGIWHCY
	QQYTNLQERPSSVLTIYDIGIQTNISMYEELQQTWFTFMIILCIIEVIVILMLIFLRN
	RIRVAIILLKEGSKAIGYVPSTLVYPALTPILLSICICYWVVTAVYQIFNTTEIAKAC
	PGALCNFAFYGGKSLYHQYIPTFHVYNLFVFLWLINFVIALGQCALAGAFATYYWANK
	KPDDIPRYPLFTAFGRAIRYHTGSLAFGSLIIALIQMFKIVLEYLDHRLKRTQNTLSK
	FLQCCLRCCFWCLENAIKFLNRNAYIMIAIYGRNFCRSAKDAFNLLMRNILKVAVTDE
	VTYFVLFLGKLLVAGSIGVLAFLFFTQRLPVIAQGPASLNYYWVPLLTVIFGSYLIAH
	GFFSVYAMCVETIFICFLEDLERNDGSTARPYYVSQPLLKIFQEENPQTRKQ

[0378] Further analysis of the NOV9a protein yielded the following properties shown in Table 9B.

TABLE 9B
Protein Sequence Properties NOV9a
PSort     0.6000 probability located in plasma membrane; 0.4000
analysis: probability located in Golgi body; 0.3000 probability
          located in endoplasmic reticulum (membrane); 0.0300
          probability located in mitochondrial inner membrane
SignalP   Cleavage site between residues 64 and 65
analysis:

[0379] 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
AAB95155	Human protein sequence SEQ ID	17 . . . 684	374/694 (53%)	0.0
	NO: 17188 - Homo sapiens, 704 aa.	10 . . . 698	499/694 (71%)
	[EP1074617-A2, 07 FEB. 2001]
AAM40010	Human polypeptide SEQ ID NO	18 . . . 684	374/693 (53%)	0.0
	3155 - Homo sapiens, 706 aa.	13 . . . 700	499/693 (71%)
	[WO200153312-A1, 26 JUL. 2001]
AAB42144	Human ORFXORF 1908	18 . . . 684	374/694 (53%)	0.0
	polypeptide sequence SEQ ID	13 . . . 701	499/694 (71%)
	NO: 3816 - Homo sapiens, 707 aa.
	[WO200058473-A2, 05 OCT. 2000]
AAB24284	Human H38087 (clone GTB6)	17 . . . 684	373/694 (53%)	0.0
	protein sequence SEQ ID NO: 7 -	10 . . . 698	499/694 (71%)
	Homo sapiens, 704 aa.
	[WO200061746-A1, 19 OCT. 2000]
AAB68406	Amino acid sequence of a human	18 . . . 684	373/693 (53%)	0.0
	choline transporter like protein 2 -	13 . . . 700	498/693 (71%)
	Homo sapiens, 706 aa.
	[WO200132704-A1, 10 MAY
	2001]

[0380] 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
Q95JW2	Hypothetical 81.6 kDa protein -	1 . . . 690	661/717 (92%)	0.0
	Macaca fascicularis (Crab eating	1 . . . 717	677/717 (94%)
	macaque) (Cynomolgus monkey),
	717aa.
AAH28743	Hypothetical 81.7 kDa protein -	1 . . . 690	666/719 (92%)	0.0
	Homo sapiens (Human), 719 aa.	1 . . . 719	677/719 (93%)
Q95JX5	Hypothetical 53.6 kDa protein -	251 . . . 690	424/467 (90%)	0.0
	Macaca fascicularis (Crab eating	2 . . . 468	434/467 (92%)
	macaque) (Cynomolgus monkey),
	468 aa.
Q9NY68	CTL2 protein - Homo sapiens	18 . . . 684	374/693 (53%)	0.0
	(Human), 706 aa.	13 . . . 700	499/693 (71%)
Q91VA1	RIKEN CDNA 2210409B01 gene	12 . . . 684	320/711 (45%)	0.0
	(NG22) - Mus musculus (Mouse),	6 . . . 696	457/711 (64%)
	707 aa.

[0381] PFam analysis indicates that the NOV9a protein contains the domains shown in the Table 9E.

TABLE 9E
Domain Analysis of NOV9a
			Identities/
			Similarities
	Pfam	NOV9a	for the	Expect
	Domain	Match Region	Matched Region	Value
No Significant Matches Found

Example 10

[0382] 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: 25	6065 bp
NOV10a,	CCAGAGGAGCGCCTTCTGCCTCAGAACGGCGTGACTCGGAGAATTGGAGCGTTATTCA
CG126600-01
DNA Sequence	GTATATTAATGTCTTATTGATAATGGCAGAACATCCACCACTACTGGATACAACTCAG
	ATCTTAAGTAGTGATATTTCTCTTTTGTCTGCCCCTATTGTGAATGCAGATGGAACAC
	AACAGGTTATTCTGGTACAAGTTAACCCAGGAGAAGCATTTACAATAAGAAGAGAAGA
	TGGACAGTTTCAGTGCATTACAGGTCCTGCTCAGGTTCCAATGATGTCCCCAAATGGT
	TCTGTGCCTCCTATCTATGTGCCTCCTGGATATGCCCCACAGGTTATTGAAGACAATG
	GTCTTCGAAGAGTTGTCGTCGTCCCTCAGGCACCAGAGTTTCACCCTGGTAGTCACAC
	AGTTCTCCACCGTTCTCCACATCCTCCTCTACCTGGTTTCATTTCTGTCCCAACTATG
	ATGCCGCCTCCACCACGTCATATGTACTCACCCGTGACTGGAGCTGGAGACATGACAA
	CACAGTATATGCCACAGTATCAGTCTTCACAAGTCTATGGAGATGTAGATGCTCACTC
	TACACATGGAAGGTCCAACTTTAGAGATGAACGATCTAGTAAAACATATGAACGTTTG
	CAGAAAAAATTGAAGGATCGCCAAGGAACACAGAAAGATAAAATGAGCAGTCCACCAT
	CATCACCCCAGAAATGCCCTTCTCCCATTAATGAACATAATGGACTTATAAAAGGACA
	AATTGCTGGTGGTATAAACACAGGATCAGCAAAAATCAAGTCTGGGAAGGGGAAAGGT
	GGTACACAAGTTGATACAGAAATTGAAGAAAAAGATGAAGAAACTAAAGCATTTGAAG
	CACTTCTTTCCAACATTGTCAAACCAGTGGCCTCCGACATCCAGGCAAGGACAGTAGT
	ACTTACCTGGTCACCACCTTCCAGCCTCATTAATGGTGAAACAGATGAAAGTAGTGTA
	CCAGAGCTCTATGGTTATGAAGTTCTGATCTCAAGTACTGGAAAAGATGGGAAATACA
	AAAGTGTATATGTAGGAGAAGAAACAAATATCACTTTAAATGATCTCAAGCCAGCCAT
	GGATTACCATGCAAAAGTCCAGGCAGAATATAATTCTATAAAGGGAACTCCTTCAGAG
	GCTGAAATCTTTACCACCTTGAGCTGTGAACCTGATATACCTAATCCACCAAGGATAG
	CCAATCGGACCAAAAATTCACTCACTTTGCAATGGAAGGCACCTAGTGACAATGGTTC
	TAAAATCCAAAACTTTGTATTAGAATGGGATGAAGGAAAAGGAAATGGAGAATTTTGT
	CAGTGTTACATGGGCTCACAGAAACAATTTAAAATTACTAAACTTTCACCAGCAATGG
	GCTGTAAATTCAGACTATCGGCCAGAAATGACTATGCTACAAGTGGTTTTAGTGAAGA
	AGTCTTATATTACACCTCAGGCTGTGCTCCTTCTATGCCAGCAAGTCCTGTATTAACC
	AAGGCTGGAATTACTTGGTTATCCTTACAATGGAGTAAGCCCTCAGGAACACCATCAG
	ATGAAGGAATTTCTTACATTTTAGAGATGGAGGAAGAAACTTCAGGATATGGTTTTAA
	GCCTAAATATGATGGAGAAGATCTTGCTTACACAGTGAAAAATCTCAGACGTAGTACT
	AAGTATAAATTTAAGGTTATTGCTTACAACTCAGAAGGTAAAAGTAATCCAAGTGAAG
	TAGTAGAATTTACTACTTGCCCTGATAAACCAGGCATACCTGTAAAGCCTTCAGTGAA
	AGGAAAGATACATTCACACAGTTTTAAAATAACCTGGGATCCACCAAAAGACAATGGC
	GGAGCAACCATCAATAATATGTAGTGGAGATGGCAGAAGGTTCTAAACGGAAACAAAT
	GGGAAATGATATACAGTGGTGCTACCAGGGAACATCTTTGTGATCGACTGAATCCAGG
	CTGTTTCTATCGTTTACGAGTTTACTGCATCAGTGATGGAGGACAGAGTGCGCTCTCT
	GAATCTTTACTTGTGCAGACTCCAGCTGTGCCTCCTGGCCCATGCCTCCCTCCCAGAT
	TACAGGGTAGACCCAAAGCAAAAGAAATACAGTTACGATGGGGACCCCCTCTGGTTGA
	TGGTGGATCACCCATTTCCTGTTACAGTGTGGAAATGTCTCCTATAGAAAAAGATGAA
	CCTAGAGAAGTTTACCAAGGTTCTGAAGTAGAATGTACAGTGAGCAGCCTTCTTCCTG
	GAAAGACATACAGCTTCAGACTACGTGCAGCTAACAAAATGGGGTTTGGACCATTTTC
	AGAAAAATGTGATATTACTACAGCCCCTGGGCCACCAGATCAGTGCAAGCCCCCTCAA
	GTGACATGTAGATCTGCAACTTGTGCACAAGTGAATTGGGAGGTTCCTTTGAGTAATG
	GAACAGATGTCACTGAATATCGACTGGAGTGGGGAGGAGTTGAAGGAAGTATGCAGAT
	ATGTTACTGTGGGCCTGGTCTCAGTTATGAAATAAAAGGACTTTCACCAGCAACTACC
	TATTATTGCAGGGTCCAGGCTCTGAGTGTTGTGGGTGCAGGCCCTTTCAGTGAAGTAG
	TAGCCTGTGTGACTCCACCATCAGTTCCTGGCATTGTGACCTGTCTTCAAGAAATAAG
	CGATGATGAGATAGAAAATCCCCATTATTCACCTTCTACATGCCTTGCAATAAGCTGG
	GAAAAGCCTTGTGATCATGGTTCGGAAATCCTTGCCTACAGCATAGACTTTGGAGATA
	AACAATCCCTAACAGTGGGAAAGGTTACAAGCTATATTATCAACAATTTGCAACCAGA
	TACAACATACAGAATACGAATTCAAGCCTTGAATAGCCTTGGAGCTGGTCCTTTCAGC
	CATATGATAAAATTAAAAACTAAGCCTCTCCCTCCTGATCCACCTCGTCTGGAATGTG
	TTGCCTTTAGCCACCAGAACCTTAAGCTGAAATGGGGAGAAGGAACTCCAAAGACATT
	GTCAACCGATTCTATTCAGTACCACCTTCAGATGGAGGATAAGAATGGACGGTTTGTA
	TCCCTATACAGAGGACCATGTCATACATACAAAGTACAAAGACTTAATGAGTCAACAT
	CCTATAAATTCTGTATTCAAGCTTGTAATGAAGCTCGGGAAGGTCCCCTCTCCCAAGA
	ATATATTTTCACTACTCCAAAATCTGTCCCAGCTGCCTTGAAAGCCCCCAAAATAGAG
	AAAGTAAATGATCACATTTGTGAAATTACATGGGAGTGTTTACAGCCAATGAAAGGTG
	ATCCAGTTATTTACAGTCTTCAAGTTATGTTGGGAAAAGATTCAGAATTCAAACAGAT
	TTACAAGGGTCCCGACTCTTCCTTCCGGTATTCCAGCCTTCAGCTGAACTGTGAATAT
	CGCTTCCGTGTATGTGCCATTCGCCAGTGCCAAGACTCTCTGGGACACCAGGACCTCG
	TAGGTCCCTACAGCACCACAGTGCTCTTCATCTCTCAGAGGACTGAACCACCAGCCAG
	CACCAACAGAGACACTGTGGAAAGCACAAGGACCCGACGGGCACTGAGTGACGAGCAG
	TGTGCTCCCCTCATCCTTGTGCTGTTTGCTTTCTTTTCCATTTTGATTGCCTTTATCA
	TTCAGTACTTTGTAATCAAGTGAAAATATAACTTTATTTTTTAACTCTATTACATTTT
	ATTTTGTCATGTACTAAAATTATTTCTGTATTGCTTTTATAAAAAACAGTGGCATTTA
	GCACTGGCATTGAGACTATAGCACATCATTTTTGCCATTTTCAGTGCTTATATTGTTA
	GGTAGAGGCTGGCACTTTATTAGAATGCAAGCCACAAAAATATCAATTTTGTTTTTTT
	TTGTTAGGGTGGGTCTTCTTTTTTTCTTTCCCTCTCTCTTTTTTTAACAAATGCCTTC
	TTATAGAAAAACTTTCTAAGAGGCAACAATTTAGAATGGATATTTTGACGAATCGGCA
	TGAGTGTAACAGTGATAACCTGATCTGTTTGTTTTAAAGATTATTACCAAGTGAAAAA
	TTCAGAATGAATAGAATTTACACTAACATGCTATATAAAATGTTAAAGTCTGATGCTG
	TGAAAGCAATCTAGTGCTATATTTCTACCTCCTCATTTGTCTTAATTATTTGGTAAGT
	GGGATTATGATGAGTAACTGGAGGGGCTTAGAAACAAAAACTGGATGAAAGAGTATGC
	ATGAAGAAAAGCTTCTTTGATAAATGTGGAGTTCTTCATTATAAATATATATTCATGA
	ATTCACAGATAAGTACTTAAAGAACAGACAGTTTACTTGGCCTAAAAATATTTTGATG
	TTTACTCAAAAAGTACCTCTTCAGGTCTTGAGAACATGGAAAAGAATTGAGTGCTTTT
	AAATACTTTTTAGAAAGTAATCATAAAAGTAAATTGAATTTCAAACCTATTTGGCTTC
	TGTTTTGTGAACCTTTGAACTATATGTATGTGTATAAGGGTATACACATACATATATG
	GCATATAACAAGTGTACACATATACACATAACAAGTGTAGAAGTATATATTACATACA
	TACACTCACTCTGTCTGGTATAGGCTAATTTTGAAGAACTCCCATAAGTTTCTGCTGC
	TTCTCCCATAACTGCTGCCACCACCATCAGAATTCATAATCAAACCTAACCTTTTTGT
	TTGGGGCACCAAATCTGAAGACAAAATTAATTTGCACCAGTAAACTTCAAGCTGCTTT
	CTTTCTTGAAAACTAAACGTTTAACGTATAATGTCTGTTTGGATACTGTTCCAAATTG
	TTGATTGCATGTGGTTAATGTTGCATTAGAGCACTTTGCAATTGCATAATTCATTAAT
	GTTTTGTGAGCTTGCATTTGTGAGTTATTGGATGATCAGACTGAATTTTGTCAAGTAT
	CACATTGTACATCTTGCCTAGATGTCGATGACTGCAAGTAATAATACAGTTTATAATG
	AAACTATCTACAATTCTTGTTTTAGCACATCTGTTATCCGTAAAACACCTGTAACTAG
	CTTTTTTAATTTATTATTTGAATTTTAGGATAGCGAATCACTAATTTTTAGTTGCTGA
	GGTTGGCATTTTAGTGATTATTAAGCACTTCTGTCAGTCTTTGAAAAAAAGAACGTAT
	TTTTTGTGCTTTGAAGATCTCTGAAGAATTTCTTTTATAATAGAATGGGCATGTATTG
	TAACAGTTTTATGTCAAATGATCTGTGCTGTAGAAAAACATTAACCCTTGTTCAAAAA
	AGAAATGGATAAACTTGGCCTTTCTAAGTGGTAAGAATGACCTGTCACTATAATATAC
	TGTATGTTTACATTTTATTTAAATTTAATCTCTTATGTATAGGGTGATAACCTTCCCC
	AGAAACAACAGTGATTGCGATTGTTTTCTAGAAACTTCTTTAAAGTGCCACATTTGGC
	AGTACAAATGAGTCTGAGTGTAATAGCCCAGAGATTTATATATAGTTGAATGTCTAAA
	ATGGTAAAATGTGCCACTGTGTCAAGTTACAGTGGCTTATGTTTTTCATAGTAATTCA
	AATGAACTTCCTATTTTTGATAGTAAATGTCATTTkATAGTATACTTGCCATTTGAGC
	CTCACTGCAAAATTAGTGCAGAGGAGAAAACAATTTTTAATGTAATCTTGATTTTACC
	TCATATACTGTACATTCCAAAAACTCTAAACTTTTTAAAGATTATAGATACACTACCA
	GTTGTATCATTCTTTTTGAGATACGTTTATTGTATTCATATATATTCATTATTTGCTA
	CCTGTTTAAGAAAGTGAAATGTTATGGTCTCCCCTCTTCCAATGAGCTTAAAACATTT
	GTTGTATCATTCTTTTTGAGATACGTTTATTGTATTCATATATATTCATTATTTGCTA
	CCTGTTTAAGAAAGTGAAATGTTATGGTCTCCCCTCTTCCAATGAGCTTAAAACATTT
	TTCCCAACAGTATATAAATCTTCAACATGAGAGGATGTATATTTATTATATAAAGCCC
	AGTAAAGAATAAAATTAGAAGTTTTATCCTAGG
	ORF Start: ATG at 81	ORF Stop: TGA at 3675
	SEQ ID NO 26	1198 aa	MW at 131840.2 kD
NOV10a,	MAEHPPLLDTTQILSSDISLLSAPIVSADGTQQVILVQVNPGEAFTTRREDGQFQCIT
CG126600-01
Protein Sequence	GPAQVPMMSPNGSVPPIYVPPGYAPQVIEDNGVRRVVVVPQAPEFHPGSHTVLHRSPH
	PPLPGFISVPTMMPPPPRHMYSPVTGAGDMTTQYMPQYQSSQVYGDVDAHSTHGRSNF
	IRDERSSKTYERLQKKLKDRQGTQKDKMSSPPSSPQKCPSPINEHNGLIKGQIAGGINT
	GSAKIKSGKGKGGTQVDTEIEEKDEETKJXFEALLSNIVKPVASDIQARTVVLTWSPPS
	SLINGETDESSVPELYGYEVLISSTGKDGKYKSVYXTGEETNITLNDLKPAMDYHAKVQ
	AEYNSIKGTPSEAEIFTTLSCEPDIPNPPRIANRTKNSLTLQWKAPSDNCSKIQNFVL
	EWDEGKGNGEFCQCYMGSQKQFKITKLSPAMGCKFRLSARNDYGTSGFSEEVLYYTSG
	CAPSMPASPVLTKAGITWLSLQWSKPSGTPSDEGISYILEMEEETSGYGFKPKYDGED
	LAYTVKNLRRSTKYKFKVIAYNSEGKSNPSEVVEFTTCPDKPGIPVKPSVKGKIHSHS
	FKITWDPPKDNGGATINKYVVEMAEGSNGNKWEMIYSGATREHLCDRLNPGCFYRLRV
	YCISDGCQSAVSESLLVQTPAVPPGPCLPPRLQCRPKAKEIQLRWGPPLVDGGSPISC
	YSVEMSPIEKDEPREVYQGSEVECTVSSLLPGKTYSFRLRAANKMGFGPFSEKCDITT
	APGPPDQCKPPQVTCRSATCAQVNWEVPLSNGTDVTEYRLEWGGVEGSMQICYCGPGL
	SYEIKGLSPATTYYCRVQALSVVGAGPFSEVVACVTPPSVPGIVTCLQEISDDEIENP
	HYSPSTCLAISWEKPCDHGSEILAYSIDFGDKQSLTVGKVTSYIINNLQPDTTYRIRI
	QALNSLGAGPFSHMIKLKTKPLPPDPPRLECVAFSHQNLKLKWGEGTPKTLSTDSIQY
	HLQMEDKNGRFVSLYRGPCHTYKVQRLNESTSYKFCIQACNEAGEGPLSQEYIFTTPK
	SVPAALKAPKIEKVNDHICEITWECLQPMKGDPVIYSLQVMLGKDSEFKQIYKGPDSS
	FRYSSLQLNCEYRFRVCAIRQCQDSLGHQDLVGPYSTTVLFISQRTEPPASTNRDTVE
	STRTRRALSDEQCAAVILVLFAFFSILIAFIIQYFVIK

[0383] Further analysis of the NOV10a protein yielded the following properties shown in Table 10B.

TABLE 10B
Protein Sequence Properties NOV10a
PSort     0.8500 probability located in endoplasmic reticulum
analysis: (membrane); 0.6640 probability located in plasma membrane;
          0.1000 probability located in mitochondrial inner
          membrane; 0.1000 probability located in Golgi body
SignalP   No Known Signal Sequence Indicated
analysis:

[0384] 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
ABG34076	Human Pro peptide #47 - Homo	351 . . . 1198	459/850 (54%)	0.0
	sapiens, 847 aa. [WO200224888-	2 . . . 847	607/850 (71%)
	A2, 28 MAR. 2002]
AAM93625	Human polypeptide, SEQ ID NO:	437 . . . 1198	405/764 (53%)	0.0
	3462 - Homo sapiens, 760 aa.	1 . . . 760	540/764 (70%)
	[EP1130094-A2, 05 SEP. 2001]
AAU18383	Human endocrine polypeptide SEQ	486 . . . 1198	373/715 (52%)	0.0
	ID No 338 - Homo sapiens, 717 aa.	7 . . . 717	501/715 (69%)
	[WO200155364-A2, 02 AUG.
	2001]
AAM43571	Human polypeptide SEQ ID NO	487 . . . 1198	372/714 (52%)	0.0
	249 - Homo sapiens, 710 aa.	1 . . . 710	499/714 (69%)
	[WO200155308-A2, 02 AUG.
	2001]
AAU12206	Human PRO4979 polypeptide	8 . . . 608	313/614 (50%)	e−168
	sequence - Homo sapiens, 625 aa.	9 . . . 612	409/614 (65%)
	[WO200140466-A2, 07 JUN. 2001]

[0385] 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
Q9Y2H6	KIAA0970 protein - Homo	57 . . . 1198	1139/1142 (99%)	0.0
	sapiens (Human), 1151 aa	10 . . . 1151	1141/1142 (99%)
	(fragment).
Q9H1W1	BA203I16.1 (KIAA0970	422 . . . 1198	733/777 (94%)	0.0
	protein) - Homo sapiens	1 . . . 733	733/777 (94%)
	(Human), 733 aa.
Q96N25	CDNA FLJ31509 fis, clone	1 . . . 326	324/326 (99%)	0.0
	NT2RI1000016 - Homo	1 . . . 326	325/326 (99%)
	sapiens (Human), 326 aa.
Q9H517	CDNA: FLJ23399 fis,	706 . . . 1198	256/494 (51%)	e−151
	clone HEP 18254 - Homo	5 . . . 495	350/494 (70%)
	sapiens (Human), 495 aa.
Q9NSQ8	Hypothetical 52.6 kDa	720 . . . 1198	249/480 (51%)	e−147
	protein - Homo sapiens	1 . . . 477	341/480 (70%)
	(Human), 477 aa
	(fragment).

[0386] PFam analysis indicates that the NOV10a protein contains the domains shown in the Table 10E.

TABLE 10E
Domain Analysis of NOV10a
			Identities/
		NOV10a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
	fn3	266 . . . 359	24/97 (25%)	1.6e−05
			65/97 (67%)
	fn3	371 . . . 455	19/88 (22%)	3.2e−06
			62/88 (70%)
	fn3	467 . . . 552	22/87 (25%)	9.7e−07
			59/87 (68%)
	fn3	564 . . . 650	25/88 (28%)	0.00012
			60/88 (68%)
	fn3	661 . . . 747	25/90 (28%)	4.1e−09
			59/90 (66%)
	fn3	759 . . . 841	24/86 (28%)	1.6e−08
			59/86 (69%)
	fn3	863 . . . 940	28/87 (32%)	3.2e−09
			63/87 (72%)
	fn3	952 . . . 1035	23/88 (26%)	0.032
			52/88 (59%)

Example 11

[0387] 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: 27	1175 bp
NOV11a,	ATGGCCACTGCCCAGTTGCAGAGGACTTCCATGACTGCACTGGTATTTCTCAATAAGA
CG127888-01
DNA Sequence	TACCACCTGAACACCAGTCTTTGGTGTTAGTGAAGAGTTTCCTCACAGTTTCAGTATC
	CTGTATCATGTATTTGAGAGGAATATTTCCAGCATGTGCTTATGGAACCAGATATCTA
	GATGATCTTTGTGTCAAAATACTGAGAGAAGATAAAAATTGCCCAGGATCTACACAGT
	TAGTGAAATGGATACTAGGATGTTACGATGCTTTACAGAAAAAAATATACACAAACCC
	AGAAGATCCTCAGACAATTTCAGAATGTTACCAATTCAAATTCAAATACACCAATAAT
	GGACCACTTATGGACTTCATAAGTGAAAGCCPAAGCAATGAGTCTAGCATGTTATGTA
	CTGACACCGAGAAAGCAAGCACTCTCCTAATTCGCAAGATTTATACCCTAATGCAAAA
	TCTGGGGCCTTTACCTAATGTTTGTTTGAGCATGAAACGTTTTTACTATGATGAAGTT
	ACACCCCCAGATTACCAGCCTCCTGGTTTTAAGGATGGTGATTGTGAAGGACTTATAT
	TTGAAGGGGAACTTATGTATTTATCTGGGCGAAGTCTCAAAACACCTTTTCCCACCTT
	CAAAGTAAGTGACCACTGAGAGAGAACGAATGGAAAATATTTATTCAAACTATACTAA
	TCACTAAAACAAATAAAPACAACTTCACAAAATCCTGAGGGACAAAGATGCAGAAAAG
	ATGACCACGCGCATTATACAAGTGATGATTTGGACATTGAAACTAAAATGGAAGAGCA
	GGAAAAAAACCCTCGATTTTCTGAACTTGGAGAACCAAGTTTAGTTTGTGAGGATGAT
	GAAATTGTGAGGTATAAAPAAAGTTCAGATCTTTCCATTTCTCATTCTCAGGTTGAGC
	AGTTAGTCAATAAAACATCGGAACTTGATATGTCTGAAAGCAAAACAAGAAGTGGAAA
	GTCTTTCAGAATAATGGCAAATGGAAATCAACCAGTAACATCTTCCAAAGAAATTCGG
	AAGAGAAGTCAACATGAATCTGGGAGAATAGTGCTCCATCACTCGCATTCTTCTAGTC
	AAGAGTCAGTACCAAAAAGGAGAAAGTTTAGTGAACCAAAGGACATATATAAAAAATT
	ATTTTTCTTCTGTAT
	ORF Start: ATG at 1	ORF Stop: TAA at 1153
	SEQ ID NO: 28	384 aa	MW at 43970.6 kD
NOV11a,	MATAQLQRTSMTALVFLNKIPPEHQSLVLVKSFLTVSVSCIMYLRGIFPACAYGTRYL
CG127888-01
Protein Sequence	DDLCVKILREDKNCPGSTQLVKWILGCYDALQKKIYTNPEDPQTISECYQFKFKYTNN
	GPLMDFISESQSNESSMLCTDTEKASTLLIRKTYTLMQNLGRLPNVCLSMKRFYYDEV
	TPPDYQPPGFKDGDCEGVIFEGELMYLNVGEVSTPFPTFKVKVTTERERMENIYSTIL
	SLKQIKTKLHKILRDKDAEDDQAHYTSDDLDIETKMEEQEKNPRFSELGEPSLVCEDD
	EIVRYKKSSDLSISHSQVEQLVNKTSELDMSESKTRSGKSFRIMANGNQPVTSSKEIR
	KRSQHESGRIVLHHSHSSSQESVPKRRKFSEPKEHI

[0388] Further analysis of the NOV11a protein yielded the following properties shown in Table 11B.

TABLE 11B
Protein Sequence Properties NOV11a
PSort     0.6186 probability located in outside; 0.1900 probability
analysis: located in lysosome (lumen); 0.1000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 53 and 54
analysis:

[0389] 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
Genescq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAG89139	Human secreted protein, SEQ ID	1 . . . 384	339/394 (86%)	0.0
	NO: 259 - Homo sapiens, 394 aa.	1 . . . 394	350/394 (88%)
	[WO200142451-A2, 14 JUN. 2001]
AAB63451	Human breast cancer associated	36 . . . 259	196/233 (84%)	e−109
	antigen protein sequence SEQ ID	2 . . . 234	203/233 (87%)
	NO: 813 - Homo sapiens, 235 aa.
	[WO200073801-A2, 07 DEC. 2000]
AAB63280	Human breast cancer associated	36 . . . 259	196/233 (84%)	e−109
	antigen protein sequence SEQ ID	2 . . . 234	203/233 (87%)
	NO: 642 - Homo sapiens, 235 aa.
	[WO200073801-A2, 07 DEC. 2000]
AAU07870	Polypeptidc sequence for	1 . . . 112	93/121 (76%)	5e−46
	mammalian Spg27 - Mammalia, 121 aa.	1 . . . 121	100/121 (81%)
	[WO200166752-A2, 13 SEP. 2001]
AAG76687	Human colon cancer antigen protein	248 . . . 359	88/113 (77%)	6e−41
	SEQ ID NO: 7451 - Homo sapiens,	22 . . . 134	94/113 (82%)
	155 aa. [WO200122920-A2, 05
	APR. 2001]

[0390] 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		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9H0K8	Hypothetical 44.4 kDa protein -	1 . . . 384	338/387 (87%)	0.0
	Homo sapiens (Human), 387 aa.	1 . . . 387	350/387 (90%)
Q9D5T7	4921522K05Rik protein - Mus	1 . . . 383	272/395 (68%)	e−146
	musculus (Mouse), 392 aa.	1 . . . 391	315/395 (78%)
Q9D473	4921522K05Rik protein - Mus	1 . . . 351	255/363 (70%)	e−138
	musculus (Mouse), 374 aa.	1 . . . 360	294/363 (80%)
Q95JZ3	Hypothetical 30.7 kDa protein -	120 . . . 384	228/267 (85%)	e−123
	Macaca fascicularis (Crab eating	1 . . . 267	239/267 (89%)
	macaque) (Cynomolgus monkey),
	267 aa.
Q9CUF3	4921522K05Rik protein - Mus	1 . . . 288	212/298 (71%)	e−116
	musculus (Mouse), 295 aa	1 . . . 295	242/298 (81%)
	(fragment).

[0391] PFam analysis indicates that the NOV11a protein contains the domains shown in the Table 11E.

TABLE 11E
Domain Analysis of NOV11a
			Identities/
		NOV11a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
	HORMA	22 . . . 225	54/254 (21%)	0.00013
			134/254 (53%)

Example 12

[0392] 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: 29	513 bp
NOV12a,	GCCAGACCAAACCGGACCTCGGGGCCGATGCGGCTGCTGCCCCTGCTGCGGACTGTCC
CG128249-02
DNA Sequence	TCTGGGCCGCGTTCGTCGGCTCCCCTCTGCGCGGGGGCTCCAGCCTCCGCCACGTAGT
	CTACTGGAACTCCAGTAACCCCAGGTTGCTTCGAGGAGACGCCGTGGTGGAGGTGGCC
	CTCAACGATTACCTAGACATTGTCTGCCCCCACTACGAAGGCCCAGGGCCCCCTGAGG
	GCCCCGAGACGTTTGCTTTGTACATGGTGGACTGGCCAGGGTATGAGTCCTGCCAGGC
	AGAGGGCCCCCGGGCCTACAAGCGCTGGGTGTCCTCCCTGCCCTTTGGCCATGTTCAA
	TTCTCAGAGAAGATTCAGCGCTTCACACCCTTCTCCCTCGGCTTTGAGTTCTTACCTG
	GAGAGAGTGGCACATCAGGGTGGCGAGGGGGGGACACTCCCAGCCCCCTCTCTCTCTT
	GCTATTACTGCTGCTTCTGATTCTTCGTCTTCTGCGAATTCTGTGACCC
	ORF Start: ATG at 28	ORF Stop: TGA at 508
	SEQ ID NO: 30	160 aa	MW at 17901.6 kD
NOV12a	MRLLPLLRTVLWAAFVGSPLRGGSSLRHVVYWNSSNPRLLRGDAVVEVGLNDYLDIVC
CG128249-02
Protein Sequence	PHYEGPGPPEGPETFALYMVDWPGYESCQAEGPRAYKRWVCSLPFGHVQFSEKIQRFT
	PFSLGFEFLPGESGTSGWRGGDTPSPLCLLLLLLLLILRLLRIL

[0393] Further analysis of the NOV 12a protein yielded the following properties shown in Table 12B.

TABLE 12B
Protein Sequence Properties NOV12a
PSort     0.9190 probability located in plasma membrane; 0.3000
analysis: probability located in lysosome (membrane); 0.2133
          probability located in microbody (peroxisome); 0.1000
          probability located in endoplasmic reticulum (membrane)
SignalP   Cleavage site between residues 23 and 24
analysis:

[0394] 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 12C.

TABLE 12C
Geneseq Results for NOV12a
		NOV12a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAR71482	Human hek-L protein - Homo	1 . . . 160	158/201 (78%)	4e−87
	sapiens, 201 aa. [WO9506065-A,	1 . . . 201	160/201 (78%)
	02 MAR. 1995]
ABG27837	Novel human diagnostic protein	1 . . . 127	63/131 (48%)	1e−28
	#27828 - Homo sapiens, 335 aa.	111 . . . 240	82/131 (62%)
	[WO200175067-A2, 11 OCT.
	2001]
ABG27837	Novel human diagnostic protein	1 . . . 127	63/131 (48%)	1e−28
	#27828 - Homo sapiens, 335 aa.	111 . . . 240	82/131 (62%)
	[WO200175067-A2, 11 OCT.
	2001]
AAW00035	HEK4 binding protein - Homo	1 . . . 127	63/131 (48%)	1e−28
	sapiens, 228 aa. [WO9623000-A1,	4 . . . 133	82/131 (62%)
	01 AUG. 1996]
AAW02586	Lerk-7 protein - Homo sapiens,	1 . . . 127	63/131 (48%)	1e−28
	228 aa. [WO9617925-A1, 13 JUN.	4 . . . 133	82/131 (62%)
	1996]

[0395]

TABLE 12D
Public BLASTP Results for NOV12a
		NOV12a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
P52798	Ephrin-A4 precursor (EPH-related	1 . . . 160	158/201 (78%)	1e−86
	receptor tyrosine kinase ligand 4)	1 . . . 201	160/201 (78%)
	(LERK-4) - Homo sapiens (Human),
	201 aa.
008542	Ephrin-A4 precursor (EPH-related	1 . . . 160	131/206 (63%)	2e−67
	receptor tyrosine kinase ligand 4)	1 . . . 206	141/206 (67%)
	(LERK-4) - Mus musculus (Mouse),
	206 aa.
Q9CZS8	10 days embryo cDNA, RIKEN full-	1 . . . 160	129/206 (62%)	1e−66
	length enriched library,	1 . . . 206	141/206 (67%)
	clone: 2610529M21, full insert
	sequence - Mus musculus (Mouse),
	206 aa.
Q98TZ1	Ephrin-A6 - Gallus gallus (Chicken),	6 . . . 129	69/127 (54%)	2e−31
	202 aa (fragment).	1 . . . 124	84/127 (65%)
P97605	Ephrin-A5 precursor (EPH-related	1 . . . 127	64/131 (48%)	3e−28
	receptor tyrosine kinase ligand 7)	4 . . . 133	82/131 (61%)
	(LERK-7) (AL-1) - Rattus
	norvegicus (Rat), 228 aa.

[0396] PFam analysis indicates that the NOV12a protein contains the domains shown in the Table 12E.

TABLE 12E
Domain Analysis of NOV12a
			Identities/
		NOV12a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
	Ephrin	22 . . . 129	63/114 (55%)	1.2e−54
			94/114 (82%)

Example 13

[0397] 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: 31	240 bp
NOV13a,	ATGGTGGGCCCCGCGCCGCGGCGGCGGCTGCGGCCGCTGGCAGCGCTGGCCCTGGTCC
CG128785-01
DNA Sequence	TGGCGCTGGCCCCGGGGCTGCCCACAGCCCGGGCCGGGCAGACACCGCGCCCTGCCGA
	GCGGGGGCCCCCAGTGCGGCTTTTCACCGAGGAGGAGCTGGCCCGCTATGGCGGGGAG
	GAGCTTCTCCCCTGCTTTCTAGGAAGATCACCCCATCTACTTGGCAGTGAACGGAGTG
	GTGTTTGA
	ORF Start: ATG at 1	ORF Stop: TGA at 238
	SEQ ID NO: 32	79 aa	MW at 8309.6 kD
NOV13a,	MVGPAPRRRLRPLAALALVLALAPGLPTARAGQTPRPAERGPPVRLFTEEELARYGGE
CG128785-01
Protein Sequence	ELLPCFLGRSAHLLGSEGSGV

[0398] Further analysis of the NOV13a protein yielded the following properties shown in Table 13B.

TABLE 13B
Protein Sequence Properties NOV13a
PSort     0.6854 probability located in outside; 0.1000 probability
analysis: located in endoplasmic reticulum (membrane); 0.1000
          probability located in endoplasmic reticulum (lumen);
          0.1000 probability located in microbody (peroxisome)
SignalP   Cleavage site between residues 32 and 33
analysis:

[0399] 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/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB98325	Human ortholog of r0v0-176.7A	1 . . . 59	59/59 (100%)	1e−27
	(PA27) protein sequence - Homo	1 . . . 59	59/59 (100%)
	sapiens, 120 aa. [WO200132926-A2,
	10 MAY 2001]
AAY94866	Human protein clone HP 10557 -	1 . . . 59	59/59 (100%)	1e−27
	Homo sapiens, 172 aa.	1 . . . 59	59/59 (100%)
	[WO200005367-A2, 03 FEB. 2000]
AAB98322	Human PA27 protein (r0v0-176.7A)	1 . . . 59	58/59 (98%)	1e−25
	SEQ ID NO: 72 - Homo sapiens, 171 aa.	1 . . . 58	58/59 (98%)
	[WO200132926-A2, 10 MAY
	2001]
ABB72158	Rat protein isolated from skin cells	1 . . . 59	46/59 (77%)	4e−17
	SEQ ID NO: 197 - Rattus sp, 171 aa.	1 . . . 58	48/59 (80%)
	[WO200190357-A1, 29 NOV. 2001]
AAB55958	Skin cell protein, SEQ ID NO: 197 -	1 . . . 59	46/59 (77%)	4e−17
	Rattus sp, 171 aa. [WO200069884-	1 . . . 58	48/59 (80%)
	A2, 23 NOV. 2000]

[0400] 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		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9UMX5	Secreted protein of unknown	1 . . . 59	59/59 (100%)	2e−27
	function - Homo sapiens	1 . . . 59	59/59 (100%)
	(Human), 172 aa.
Q9CQ45	1110060M21Rik protein - Mus	1 . . . 59	47/59 (79%)	1e−17
	musculus (Mouse), 171 aa.	1 . . . 58	49/59 (82%)
Q9I6U2	Probable TonB-dependent	6 . . . 44	21/42 (50%)	1.6
	receptor - Pseudomonas	8 . . . 48	23/42 (54%)
	aeruginosa, 790 aa.
Q9AJPO	ORF5 - Streptomyces griseus,	4 . . . 42	18/42 (42%)	2.0
	524 aa.	421 . . . 462	25/42 (58%)
AAA42060	Ornithine aminotransferase -	10 . . . 62	20/56 (35%)	6.0
	Rattus norvegicus (Rat), 97 aa	2 . . . 57	27/56 (47%)
	(fragment).

[0401] PFam analysis indicates that the NOV13a protein contains the domains shown in the Table 13E.

TABLE 13E
Domain Analysis of NOV13a
			Identities/
		NOV13a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
No Significant Matches Found

Example 14

[0402] 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: 33	751 bp
NOV14a,	CGAGCGTCGCGGCTATGGCTTATCACTCGGGCTACGGAGCCCACGGCTCCAAGCACAG
CG129005-01
DNA Sequence	GGCCCGGGCAGCCCCGGATCCCCCTCCCCTCTTCGATGACACAAGCGGTGGTTATTCC
	AGCCAGCCCGGGGGATACCCAGCCACAGGAGCAGACGTGGCCTTCAGTGTCAACCACT
	TGCTTGGGGACCCAATGGCCAATGTGGCTATGGCCTATGGCAGCTCCATCGCATCCCA
	TGGGAAGGACATGGTGCACAAGGAGCTGCACCGTTTTGTGTCTGTGAGCAAACTCAAG
	TATTTTTTTGCTGTGGACACAGCCTACGTGCCCAAGAAGCTAGGGCTGCTGGTCTTCC
	CCTACACACACCAGAACTGGGAAGTGCAGTACAGTCGTGATGCTCCTCTGCCCCCCCG
	GCAAGACCTCAACGCCCCTGACCTCTATATCCCCACGATGGCCTTCATTACTTACGTG
	CTCCTGGCTCGGATGGCACTGGGCATTCAGAAAATGATCCTCAGTGTGCTCACGGGGC
	TGCTGTTCGGCAGCGATGGCTACTACGTGGCGCTGGCCTGGACCTCATCGGCGCTCAT
	GTACTTCATTGTGCGCTCTTTGCGGACAGCAGCCCTGGGCCCCGACAGCATGGGCGGC
	CCCGTCCCCCGGCAGCGTCTCCAGCTCTACCTGACTCTGGGAGCTGCAGCCTTCCAGC
	CCCTCATCATATACTGGCTGACTTTCCACCTGGTCCCGTGACCCCCTGGCCCCAG
	ORF Start: ATG at 15	ORF Stop: TGA at 735
	SEQ ID NO: 34	240 aa	MW at 26221.0 kD
NOV14a,	MAYHSGYGAHGSKHRARAAPDPPPLFDDTSGGYSSQPGGYPATGADVAFSVNHLLGDP
CG129005-01
Protein Sequence	MANVAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQ
	NWEVQYSRDAPLPPRQDLNAPDLYIPTMAFITYVLLAGMALGIQKMILSVLTGLLFGS
	DGYYVALAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGaAAFQPLIiy
	WLTFHLVR

[0403] Further analysis of the NOV14a protein yielded the following properties shown in Table 14B.

TABLE 14B
Protein Sequence Properties NOV14a
PSort     0.7480 probability located in microbody (peroxisome); 0.7000
analysis: probability located in plasma membrane; 0.2000 probability
          located in endoplasmic reticulum (membrane); 0.1000
          probability located in mitochondrial inner membrane
SignalP   No Known Signal Sequence Indicated
analysis:

[0404] 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 14C.

TABLE 14C
Geneseq Results for NOV14a
		NOV14a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB12032	Human SIGP 2328134 homologue,	1 . . . 240	240/293 (81%)	e−132
	SEQ ID NO: 2402 - Homo sapiens,	53 . . . 345	240/293 (81%)
	345 aa. [WO200157188-A2, 09
	AUG. 2001]
AAY21851	Human signal peptide-contianing	1 . . . 240	240/293 (81%)	e−132
	protein (SIGP) (clone ID 2328134) -	54 . . . 346	240/293 (81%)
	Homo sapiens, 346 aa.
	[WO9933981-A2, 08 JUL. 1999]
AAM41111	Human polypeptide SEQ ID NO	11 . . . 240	133/294 (45%)	7e−59
	6042 - Homo sapiens, 351 aa.	61 . . . 351	171/294 (57%)
	[WO200153312-A1, 26 JUL. 2001]
AAO17463	Human liver cancer expressed	21 . . . 240	128/284 (45%)	7e−57
	protein PP4519 - Homo sapiens,	3 . . . 283	165/284 (58%)
	283 aa. [CN1329064-A, 02 JAN.
	2002]
AAU83613	Human PRO protein, Seq ID No 44 -	21 . . . 240	128/284 (45%)	7e−57
	Homo sapiens, 283 aa.	3 . . . 283	165/284 (58%)
	[WO200208288-A2, 31 JAN. 2002]

[0405] 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 14D.

TABLE 14D
Public BLASTP Results for NOV14a
		NOV14a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9BVD0	Putative transmembrane protein -	1 . . . 240	240/293 (81%)	e−131
	Homo sapiens (Human), 293 aa.	1 . . . 293	240/293 (81%)
O95070	54TMp - Homo sapiens (Human),	1 . . . 240	239/293 (81%)	e−131
	293 aa.	1 . . . 293	239/293 (81%)
Q91XB7	Similar to putative transmembrane	1 . . . 240	220/293 (75%)	e−120
	protein, homolog of yeast golgi	1 . . . 293	230/293 (78%)
	membrane protein Yif1p (Yip1p-
	interacting factor) - Mus musculus
	(Mouse), 293 aa.
O35946	Hypothetical 14.9 kDa protein -	1 . . . 132	112/132 (84%)	2e−63
	Rattus norvegicus (Rat), 137 aa.	1 . . . 132	123/132 (92%)
O00606	Putative Rab5-interacting protein -	10 . . . 115	99/107 (92%)	8e−52
	Homo sapiens (Human), 123 aa	1 . . . 107	101/107 (93%)
	(fragment).

[0406] PFam analysis indicates that the NOV14a protein contains the domains shown in the Table 14E.

TABLE 14E
Domain Analysis of NOV14a
			Identities/
		NOV14a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
No Significant Matches Found

Example 15

[0407] 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: 35	9508 bp
NOV15a,	TACTGCCACCATTGGAACTTTTGATGTTGATGGGGAAGAGTTGCAACACCTCCAGGGT
CG132086-01
DNA Sequence	TGTCCTGCTGATGGTGGCTGCGAAGATTTGCCTTGACAATAGCTGAAAAACCACCAT
	CTGCAACACGTGGGAGTAAGACTTCTCCTGCTCTTTGCCAGTGGTCTGACGTGATGAA
	CCACCCTGGCTTGGTGTGCTGTGTCCAGCAAACTACAGGGGTGCCGCTGGTAGTTATG
	GTGAAACCAGACACTTTTCTTATCCACGAGATTAAGACTCTTCCTGCTAAAGCGAAGA
	TCCAAGACATGGTTGCTATTAGGCACACGGCCTGCAATGAGCAGCAGCGGACAACAAT
	GATTCTGCTGTGTGAGGATGGCAGCCTGCGCATTTACATGGCCAACGTGGAGAACACC
	TCCTACTGGCTGCAGCCATCCCTGCAGCCCAGCAGTGTCATCAGCATCATGAAGCCTG
	TTCGAAAGCGCAAAACAGCTACAATCACAACCCGCACGTCTAGCCAGGTGACTTTCCC
	CATTGACTTTTTTOAACACAACCAGCAGCTGACAGATGTGGAGTTTGGTGGTAACGAC
	CTCCTACAGGTCTATAATGCACAACAGATAAAACACCGGCTGAATTCCACTGGCATGT
	ATGTGGCCAACACCAAGCCCGGAGGCTTCACCATTGAGATTAGTAACAACAATAGCAC
	TATGGTGATGACAGGCATGCGGATCCAGATTGGGACTQAAGCAATAGAACCGGCCCCG
	TCATATATCGAGATCTTCGGCACAACTATGCAGCTCAACCTGAGTCGCTCACGCTGGT
	TTGACTTCCCCTTCACCAGAGAAGAAGCCCTGCAGGCTGATAAGAAGCTGAACCTCTT
	CATTGGGGCCTCGGTGGATCCAGCAGGTGTCGCCATGATAGATGCTGTAAAAATTTAT
	GGCAAGACTAAGGACCAGTTTGGCTGGCCTGATGAGCCCCCAGAAGAATTCCCTTCTG
	CCTCTGTCAGCAACATCTOCCCTTCAAATCTGAACCAGAGCAACGGCACTGGAGATAG
	CGACTCAGCTGCCCCCACTACGACCAGTGOAACTGTCCTGGAGAGGCTGGTTGTGAGT
	TCTTTAGAGCCCTGGAAAGCTGCTTTGCCGTTGGCCCAATCATCGAGAAAGGAGAGAA
	ACAAGAATGCTGCTCAGGAGCTGGCCACTTTGCTGTTGTCCCTGCCAGCACCTGCCAG
	TGTCCAGCAGCAGTCCAAGAGCCTTCTGGCCAGCCTGCACACCAGCCGCTCGGCCTAC
	CACAGCCACAAGGATCAGGCCTTGCTGAGCAAAGCTGTGCAGTGTCTCAACACATCTA
	GCAAAGAGGGCAAGGATTTGGACCCTGAGGTGTTCCAGAGGCTAGTGATCACAGCTCG
	CTCCATTGCCATCATGCGCCCCAACAACCTTGTCCACTTTACGGAGTCAAAGCTGCCC
	CAGATGGAAACAGACTGTTTTTTTCCTAGATGTGCCTGCTGGAGTCTAGGGATAGTTG
	GCATATTGATTGGGGCCCCACTTGAAACTCCCTCCCCAGAAGGAATGGATGAAGGGAA
	GGAACCGCAGAAGCAGTTGGAAGGAGATTGCTGTAGTTTCATCACCCAGCTTGTGAAC
	CACTTCTGGAACTCCATGCATCCAAACCGAAAGAATGCCTTCTTGGCACCTGCCTGCC
	TTCCAGGACTAACTCATATTGAAGCTACTGTCAATGCTCTGGTGGACATCATCCATGG
	CTACTGTACCTGTGAGCTGGATTGTATTAACACAGCATCCAAGATCTACATGCAGATG
	CTCTTGTGTCCTGATCCTGCTGTGAGCTTCTCTTGTAAAGAAGCTCTAATTCGAGTCC
	TAAGGCCCAGGAACAAACGGAGACATGTGACTTTACCCTCTTCCCCTCGAAGCAACAC
	TCCAATGGGAGACAAGGATGATGATGACGATGATGATGCAGATGACAAAAAGCAGTCA
	TCAGGGATCCCGAATGGTGGTCACATCCGTCAGGAAGCCAGGAAACAGAGTGAGGTGG
	ACCATCGAGATTTTCAGATGGTGTCTCAGTCCATGGTCCTGGAGACAGCTGAAAATGT
	CAACAATGGCAACCCCTCTCCCCTGGAGGCCCTGCTGGCAGGCGCAGAGGGCTTCCCC
	CCCATGCTGGACATCCCACCTGATGCAGATGACGAGACCATGGTTGAACTAGCCATTG
	CCCTGAGCCTGCAGCAGGACCAACAAGCTCCAGCCTCAGACGACGAGGGCAGTACAGC
	AGCGACAGATGGTTCTACCCTTCGCACCTCTCCTGCTGACCACGGTGGTAGTGTGGGC
	TCGGAGAGCGGGGGCAGTGCAGTGGACTCAGTGGCTGGCGAGCACAGTGTATCTGGCC
	GGAGCAGTGCTTATGGCGATGCTACAGCTGAGGGGCATCCGGCTGGACCAGGAAGTGT
	CAGCTCAAGCACTGGAGCCATCAGCACCACCACTGGGCACCAGGAGGGAGATGGCTCC
	GAGGGAGAAGGAGAAGGAGAAACTGAAGGAGATGTCCACACTAGCAACAGGCTGCACA
	TGGTCCGTCTAATGCTGTTGGAGAGATTACTGCAGACCCTGCCTCAAATTACGAACGT
	TGGCGGTGTCCGGGCCATCCCATACATGCAGGTCATTCTAATGCTCACTACAGATCTG
	GATGGAGAAGATGAGAAAGACAAGQGGGCCCTAGACACCTCCTCTCCCAACTTATTAA
	CTGAGTTGGGTATGGATAAAAAGGATGTCTCCAAGAAGAATGAGCGCAGCGCCTGAAA
	TGAAGTCCATCTGGTAGTAAATGAGACTCCTGAGTGTCTTCATGTCCCCCACCAATCT
	GGATCCAAGTCTTCCATATGTGAGTCATCTTCCCTCATCTCCAGTGCCACAGCAGCAG
	CTCTACTGAGCTCTGGGGCTGTGGACTACTGCCTGCACGTGCTCAAATCACTGCTCGA
	ATATTGGAAGAGCCAACAGAATGACGAGGAGCCTGTGGCTACCAGCCAGTTGCTGAAA
	CCACATACTACCTCCTCCCCACCTGACATGAGCCCATTCTTTCTCCCCCAGTATGTGA
	AGGGTCATGCTGCTGATGTGTTTGAGGCCTATACTCAGCTTCTAACAGAAATGGTACT
	GAGGCTTCCTTACCATCAAAGATTACTGACACCAATTCTCGAATCCCACCTCCGGAAA
	GTCTTTGACCACTCGTGGTTTTACTTTCTCTCCGAGTACCTCATGATCCAGCAGACTC
	CATTTGTGCGCCGTCAAGTCCCCAACTTCTGCTCTTCATCTGTGGATCCAAGAAAAAA
	GTACCGCCAGCTCCGGGATTTGCACACCCTGGACTCTCACGTGCGTGGGATCAACAAG
	CTGCTAGAAGAGCAGGGGATATTCCTCCGGGCAAGTGTGGTTACAGCCAGCTCAGGCT
	CCGCCTTGCAATATGACACACTCATCAGCCTGATGGAGCACCTGAAAGCCTGTGCAGA
	GATTGCCGCCCAGCGAACCATCAAACTGGCAGAAATTCTGCATCAAGATGACTCCGTC
	CTGTACTTCCTCCTCCAAGTCAGTTTCCTTGTGGATGAGGGCGTGTCCCCAGTGCTGC
	TGCAACTGCTCTCCTGTGCTCTGTGCGGCAGCAAGGTGCTCGCTGCACTGCCAGCCTC
	TTCGGGATCCTCCAGTGCTTCTTCCTCCTCAGCCCCTGTGGCTGCCAGTTCTGGACAA
	GCCACAACACAGTCCAAGTCTTCCACTAAAAAGAGCAAGAAAGAAGAAAAAGAAAAGG
	AGAAAGATGGTGAGACCTCTGGCAGCCAGGAGGACCAGCTGTGCACAGCTCTGGTGAA
	CCAGCTGAACAAATTTGCCGATAAGGAAACCCTGATCCAGTTCCTGCGTTGTTTCCTG
	TTAGAGTCCAATTCTTCCTCGGTGCGCTGGCAGGCCCACTGTCTGACACTGCACATCT
	ACAGAAATTCCAGCAAATCTCAACAGGAGCTCCTGCTAGATCTGATGTGGTCCATCTG
	GCCAGAACTCCCAGCCTATGGTCGTAAGGCTGCCCAGTTTGTGGACCTACTAGGATAT
	TTCTCCCTGAACTCCACAACAGAGAAGAAGTTGAAGGAAGTATTCACAGAAAAGCTAA
	TGGAGATTCTGCGGACTCAAAACCATATTCTTACCAACCACCCCAACTCGAACATTTA
	TAACACTTTGTCTGGCTTAGTGGAGTTTGATGGCTATTACCTGGAGAGCGATCCCTGC
	CTGCTGTGTAATAACCCGGAAGTACCGTTCTGTTATATCAAGCTGTCTTCCATTAAAG
	TGGACACGCGGTACACCACCACCCAGCAGGTTGTGAAGCTCATTGGCAGTCACACCAT
	CAGCAAAGTGACAGTGAAATCGGGGATCTGAAACGGACCAIkGATGGTGCGGACCATC
	AACCTGTATTATAACACCGPACCGTGCAGGCCATCGTGGAGTTGAAACAAAAGCCAG
	CTCCCTGCCACAAAGCCAAGAAGGTTCAGCTGACCCCTGGACACACAGAGGTGAAGAT
	TGACCTGCCGTTGCCCATTGTGGCCTCCAATCTGATGATTGAGTTTGCAGACTTCTAT
	GAAAACTACCAGGCCTCCACAOAGACCCTGCAGTGCCCTCGCTGTAGTOCCTCGGTCC
	CTGCCAACCCAGGAGTCTGTGGCAACTGTGGAGAGAATGTGTACCAGTGTCACAAATG
	CAGATCCATCAACTACGATGAAAAGGATCCCTTCCTCTGCAATGCCTGTGGCTTCTGT
	AAATATGCCCGCTTCGACTTCATGCTCTATCACCAGCCTTGCTGTGCAGTGGATCCCA
	TTGAGAATGAAGAGACCGGAAGACGCTGTATCCAACATCAATACACTTTTGGACAAAA
	AGCTGATCGAGTGTATCATCAGCTGATGGGACACCGGCCACAGCTGGAGAACCTGCTC
	TGCAAAGTGAATGAGGCAGCTCCAGAAAAGCCACAGGATGACTCAGGAACAGCAGGGG
	GCATCAGCTCCACTTCTGCCAGTGTGAATCGTTACATCCTGCAGTTGGCTCAGGAGTA
	TTGTGGAGACTCCAAGAACTCTTTTGATGAACTCTCCAAATCATCCAGAAAGTCATTT
	GCTTCGCGCAAAGAGTTGTTGGAATATGACCTACAGCAGAGGGAAGCAGCACTAAAAT
	CATCCCGGACCTCCGTGCAGCCCACATTCACTGCCAGCCAGTACCGTGCCTTATCCGT
	CCTGGGCTGTGGCCACACATCCTCCACCAAGTGCTATGGCTGCGCCTCGGCTGTCACA
	GAACATTGTATCACACTACTTCGGGCCCTGGCCACCAACCCAGCCTTGAGGCACATCC
	TTGTCTCCCAGGGCCTTATCCGGGAGCTCTTTGATTATAATCTTCGCCGAGGGGCTGC
	GGCCATGCGGGAGGAGGTCCGCCAGCTCATGTGCCTCCTAACTCGAGACAAACCCAGA
	GCCACCCAACAGATGAATGACCTGATTATTCGCAAGGTCTCCACACCCCTGAAGGGCC
	ACTGGCCCAACCCCGATCTGGCAGTAGCCTGCAGTATGAAAATGCTGCTGCTGACGGA
	TTCTATCTCCAAGGAGGACAGCTGCTGGGAGCTCCGGTTACGCTGTGCTCTCAGCCTT
	TTCCTCATGGCTGTGAACATTAAGACTCCTGTGGTGGTTGAAAACATTACCCTCATGT
	GCCTGAGGATCTTGCAGAAGCTGATAAAACCACCTGCTCCCACTAGCAAGAAGAACAA
	GGATGTCCCCGTTGAGGCCCTCACCACGGTGAAOCCATACTGCAATGAGATCCATGCC
	CAGGCTCAACTGTGGCTCPIAAGAGAGACCCCAGGCATCCTATCATGCCTGGAAGAAT
	GTCTTCCTATCAGAGGGATAGATGGCAATCGGAAAAGCCCCCAGCAATCAGAGCTCCG
	CCATCTCTATTTGACTGAGAAGTATGTGTGGAGGTGGAAACAGTTCCTGAGTCGTCGG
	GGGAAGAGGACCTCCCCCTTGGATCTCACTGGGGCATAACAACTGGCTGCGACAAAAC
	TGCTTTTCACTCCAGCAACGCAGGCCGCACGGCAGGCAGCCTGTACCATTGTGGAAGC
	TCTAGCCACCATTCCCAGCCGCAAGCAGCAGGTCCTGGACCTGCTTACCAGTTACCTG
	GATGAGCTGAGCATAGCTGGGGAGTGTGCACCTGAGTACCTGGCTCTCTACCAGAAGC
	TCATCACTTCTGCGCACTGGAAAGTCTACTTGGCAGCTCGGGGAGTCCTACCCTATGT
	GGGCAACCTCATCACCAAGGAAATAGCTCGTCTGCTGGCCCTGGAGGAGGCTACCCTG
	AGTACCGATCTGCAGCAGCGTTATGCCCTTAAAGTCTCACAGGCCTTCTCTCCTCCTA
	TTGTTGAGGTGGAATCCATCAAAAAGACATTTTAAAGTCGCTTGGTGGGTACTGTGCT
	GAATGGATACCTGTGCTTGCGGAAGCTGGTGGTGCAGAGGACCAAGCTGATCGATGAG
	ACGCAGGACATGCTGCTGGACATGCTGGAGGACATGACCACAGGTACAGAAAAATCAG
	CCAAGGCCTTCATGGCTGTGTGCATTGAGACAGCCAAGCGCTACAAATCTGGATGACT
	CCGGACCCCGGTGTTCATCTTCGAGAGGCTCTGCAGCATCATTTATCCTGAGGAGAAT
	GAAGTCACTGAGTTCTTTGTGACCCTGGAGAAGGATCCCCAACAAGAAGACTTCTTAC
	AGGGCAGGATGCCTGGGAACCCGTATAGCAGCAATGAGCCAGGCATCGGGCCGCTGAT
	GAGGGATATAAAGAACAAGATTTGCCAGGACTGTGACTTAGTGGCCCTCCTGGAAGAT
	GACAGTGGCATGGAGCTTCTAGTGAZkCAATAAAATCATTAGTTTGGACCTTCCTGTG
	CTGAAGTTTACAAGAAAGTCTGGTGTACCACGAATGAGGGAGAGCCCATGAGGATTGT
	TTATCGTATGCGGGGGCTGCTGGGCGATGCCACAGAGGAGTTCATTGAGTCCCTGGAC
	TCTACTACAGATGAAGAAGAAGATGAAGAAGAAGTGTATAAAAATGGCTGGTGTGATG
	CCCAGTGTGGGGGCCTGGAATGCATGCTTAACAGACTCGCAGGGATCAGAGATTTCAA
	GCAGGGACGCCACCTTCTAACAGTGCTACTGAAATTGTTCAGTTACTGCGTGAAGGTG
	AAAGTCAACCGGCAGCAACTGGTCAAACTGGAAATGAACACCTTGAACGTCATGCTGG
	GGACCCTAACCTGGCCCTTGTAGCTGAACAAGAAAGCAAGGACAGTGGGGGTGCACCA
	TGTGGCTGAGCAGGTGCTTAGCATCATGGAGATCATTCTAGATGAGTCCAATGCTGAG
	CCCCTGAGTGAGGACAAGGGCAACCTCCTCCTGACAGGTGACAAGGATCAACTGGTGA
	TGCTCTTGGACCAGATCAACAGCACCTTTGTTCGCTCCAACCCCAGTGTGCTCCAGGG
	CCTGCTTCGCATCATCCCGTACCTTTCCTTTGGAGAGGTGGAGAAAATGCAGATCTTG
	GTGGAGCGATTCAAACCATACTGCAACTTTGATAAATATGATGAAGATCACAGTGGTG
	ATGATAAAGTCTTCCTGGACTGCTTCTGTAAATAGCTGCTGGCATCAAGAACAACAAG
	CAATGGGCACCAGCTGAAGGATCTGATTCTCCAGAAGGGGATCACCCAGATGCAACTT
	GACTACATGAAAAAGCACATCCCTAGCGCCAAGAATTTGGATGCCGACATCTGGAAAA
	AGTTTTTGTCTCGCCCAGCCTTGCCATTTATCCTAAGGCTGCTTCGGGGCCTGGCCAT
	CCAGCACCCTGGCACCCAGGTTCTGATTGGACTGATTCCATCCCGAACCTGCATAAAA
	CTGGACCAGGTGTCCAGTGATGAGGGCATTGGGACCTTGGCAGAGAACCTGCTGGAAA
	CCCTGCGGCAACACCCTGACGTAAACAAGAAGATTGACGCAGCCCGCAGGGAGACCCG
	GGCAGAGAAGAAGCGCATGGCCATGGCAATGAGGCAGAAGGCCCTGGGCACCCTGGGC
	ATGACGACAATGAAAAGCGCCACGTCGTGACCAAGACAGCACTCCTGAAAGCAGATGG
	AAGAGCTCATCGAGGAGCCTGGCCTCACGTGCTGCATCTGCAGGGAGGGATACAAGTT
	CCAGCCCACAAAGGTCCTGGGCATTTATACCTTCACGAAGCGGGTAGCCTTCGAGGAG
	ATGGAGAATAAGCCCCGGAAACAGCAGGGCTACAGCACCGTGTCCCACTTCAACATTG
	TGCACTACGACTGCCATCTGGCTGCCGTCAGGTTGGCTCGAGGCCGGGAAGAGTGGGA
	GAGTGCCGCCCTGCACAATGCCACACCTTAGTGCAACGGGCTCCTTCCGGTCTGGGGA
	CCTCATGTCCCTGAATCAGCTTTTGCCACTTGCTTGGCAAGACACAACACTTACCTCC
	AAAGCAATGTACAGGCCAGCGGGAGCCCACGTATCAGCTCACATCCATGACATCAACT
	GCTCTTCCTGCGCTTCGCCATGGAGCAGTCGTTCAGCGCAGACACTGGCGGGGGCGGC
	CGGGAGAGCAACATCCACCTGATCCCGTACATCATTCACACTGTGCTTTACGTCCTGA
	ACACACCCGAGCAACTTCCCGAGAAGAGAAGAACCTCCAAGGCTTTCTGGAAACAGCC
	CAAGGAGAAGTGGGTGGAGAGTGCCTTTGAAGTGGACGGGCCCTACTATTTCACAGTC
	TTGGCCCTTCACATCCTGCCCCCTGAGCAGTGGAGAGCCACACGTGTGGAAATCTTGC
	GCAGCCTGTTGGTGACCTCGCAGGCTCGGGCAGTGGCTCCAGGTGGAGCCACCAGGCT
	GACAGATAAGGCAGTGAAGGACTATTCCGCTTACCGTTCTTCCCTTCTCTTTTGGGCC
	CTCGTCGATCTCATTTACAACATGTTTAACAAGGTGCCTACCAGTAACACAGAGGGAG
	GCTGGTCCTGCTCTCTCGCTGAGTACATCCGCCACAACGACATGCCCATCTACGAAGC
	TGCCGACAAAGCCCTGAAAACCTTCCAGGAGGAGTTCATGCCAGTGGAGACCTTCTCA
	GAGTTCCTCGATGTGGCCGGTCTTTTATCAGAAATCACCGATCCAGAGAGCTTCCTGA
	AGGACCTGTTGAACTCAGTCCCCTGACCACCACACAGCAGCTGCGGCGGCGAAGACGA
	AGCTGGCTTGCCTTCCACCCTCTGTTCTCCCTCCTTGTGCATTAAGTTCCCTCCGCGG
	GATGCTGCATTGTTACCCCGCCCTCCCCTCTCTCATTTTTCTTGGTGTGGCTTGGGGT
	TTTTAGGCTTCCTGTTTTATCTCGTGTGTGTGGTGCACCAGCTATGAGGTTGTCTGTA
	ACCCAAGCCATCAAAGGGCCTGTACATACCTAGGAGCCATGAGTTGTCCCGGCCAGCT
	TCATACTTGAGTGTGCACATCTTGAGAAATAAACAAGTGACTTAACACACATTG
	ORF Start: ATG at 170	ORF Stop: TGA at 9188
	SEQ ID NO: 36	3006 aa	MW at 334825.2 kD
NOV15a,	MNHPGLVCCVQQTTGVPLVVMVKPDTFLIHEIKTLPAKAKIQDMVAIRHTACNEQQRT
CG132086-01
Protein Sequence	TMILLCEDGSLRIYMANVENTSYWLQPSLQPSSVISIMKPVRKRKTATITTRTSSQVT
	FPIDFFEHNQQLTDVEFGGNDLLQVYNAQQIKHRLNSTGMYVANTKPGGFTIEISNNN
	STMVMTGMRIQIGTQAIERAPSYTIEIFGRTMQLNLSRSRWFDFPFTREALQADKKLN
	LFIGASVDPAGVAMIDAVKIYGKTKEQFGWPDEPPEEFPSASVSNICPSNLNQSNGTG
	DSDSAAPTTTSGTVLERLVVSSLEALESCFAVGPIIEKERNKNAAQELATLLLSLPAP
	ASVQQQSKSLLASLHTSRSAYHSHKDQALLSKAVQCLNTSSKEGKDLDPEVFQRLVIT
	ARSIAIMRPNNLVHFTESKLPQMETDCFFPRCACWSLGIVGILIGAPLETPSPEGMDE
	GKEPQKQLEGDCCSFITQLVNHFWKLHASKPKNAFLAPACLPGLTHIEATVNALVDII
	HGYCTCELDCINTASKIYMQMLLCPDPAVSFSCKQALIRVLRPRNKRRHVTLPSSPRS
	NTPMGDKDDDDDDDADEKMQSSGIPNGGHIRQESQEQSEVDHGDFEMVSESMVLETAE
	NVNNGNPSPLEALLAGAEGFPPMLDIPPDADDETMVELAIALSLQQDQQAPASDDEGS
	TAATDGSTLRTSPADHGGSVGSESGGSAVDSVAGEHSVSGRSSAYGDATAEGHPAGRG
	SVSSSTGAISTTTGHQEGDGSEGEGEGETEGDVHTSNRLHMVRLMLLERLLQTLPQLR
	NVGGVRAIPYMQVILMLTTDLDGEDEKDKGALDNLLSQLIAELGMDKKDVSKKNERSA
	LNEVHLVVMRLLSVFMSRTKSGSKSSICESSSLISSATAAALLSSGAVDYCLHVLKSL
	LEYWKSQQNDEEPVATSQLLKPHTTSSPPDMSPFFLRQYVKGHAADVFEAYTQLLTEM
	VLRLPYQIKKITDTNSRIPPPVFDHSWFYFLSEYLMIQQTPFVRRQVRKLLLFICGSK
	EKYRQLRDLHTLDSHVRGIKKLLEEQGIFLRASVATASSGSALQYDTLISLMEHLKAC
	AEIAAQRTINWQKFCIKDDSVLYFLLQVSFLVDEGVSPVLLQLLSCALCOSKVLAALA
	ASSGSSSASSSSAPVAASSGQATTQSKSSTKKSKKEEKEKEKDGETSGSQEDQLCTAL
	VNQLNKFADKETLIQFLRCFLLESNSSSVRWQAHCLTLHIYRNSSKSQQELLLDLMWS
	IWPELPAYGRKAAQFVDLLGYFSLKTPQTEKKLKEYSQKAVEILRTQNHILTNHPNSN
	IYNTLSGLVEFDGYYLESDPCLVCNNPEVPFCYIKLSSIKVDTRYTTTQQVVKLIGSH
	TI SKVTVKIGDLKRTKMVRTINLYYNNRTVQAIVELKNKPARWHKAKVQLTPGQTEV
	KIDLPLPIVASNLMIEFADFYENYQASTETLQCPRCSASVPANPGVCGNCGENVYQCH
	KCRSINYDEKDPFLCNACGFCKYARFDFMLYAKPCCAVDPIENEEDRKKAVSNINTLL
	DKADRVYHQLMGHRPQLENLLCKVNEAAPEKPQDDSGTAGGISSTSASVNRYILQLAQ
	EYCGDCKNSFDELSKIIQKVFASRKELLEYDLQQREAATKSSRTSVQPTFTASQYRAL
	SVLGCGHTSSTKCYGCASAVTEHCITLLRALATNPALRHILVSQCLIRELFDYNLRRG
	AAAMREEVRQLMCLLTRDNPEATQQMNDLIIGKVSTALKGHWANPDLASSLQYEMLLL
	TDSISKEDSCWELRLRCALSLFLMAVNIKTPVVVENITLMCLRILQKLIKPPAPTSKK
	NKDVPVEALTTVKPYCNEIHAQAQLWLKRDPKASYDAWKKCLPIRGIDGNGKAPSKSE
	LRHLYLTEKYVWRWKQFLSRRGKRTSPLDLKLGHNNWLRQVLFTPATQAARQAACTIV
	EALATIPSRKQQVLDLLTSYLDELSIAGECAAEYLALYQKLITSAHWKVYLAARGVLP
	YVGNLITKEIARLLALEEATLSTDLQQGYALKSLTGLLSSFVEVESIKRHFKSRLVGT
	VLNGYLCLRKLVVQRTKLIDETQDMLLEMLEDMTTGTESETKAFMAVCIETAKRYNLD
	DYRTPVFIFERLCSIIYPEENEVTEFFVTLEKDPQQEDFLQGRMPGNPYSSNEPCICP
	LMRDIKNKICQDCDLVALLEDDSGMELLVNNKIISLDLPVAEVYKKVWCTTNEGEPMR
	IVYRMRGLLCDATEEFIESLDSTTDEDEEEVYKAVIAGVMAQCGGLECMLNRLAGIRD
	FKQGRHLLTVLLKLFSYCVKVKVNRQQLVKLEMNTLNTMLGTLNLALVAEQESKDSCG
	AAVAEQVLSIMEIILDESNAEPLSEDKGNLLLTGDKDQLVMLLDQINSTFVRSNPSVL
	QGLLRIIPYLSFGEVEKMQILVERFKPYCNFDKYDEDHSGDDKVFLDCFCKLAAGIKN
	NSNGHQLKDLILQKGITQNLDYMKKHIPSAKNLDADIWKKFLSRPALPFIYLRLLRGL
	ATQHPGTQVLIGTDSIPNLHKLEQVSSDEGIGTLAENLLEALREHPDVNKKIDAARRE
	TRAEKKRMAMRQKALGTLGMTTNEKGQVATKTALLKQMEELIEEPGLTCCICREGYAA
	KFQPTKVLGIYTFTKRVALEEMENKPRKQQGYSTVSHFNIVHYDCHLAAVRLARGREE
	WESAALQNANTKCNGLLPVWGPHVPESAFATCLARHNTYLQECTGQREPTYQLNIHDI
	QPKEKWVESAFEVDGPYYFTVLALHILPPEQWRATRVEILRRLLVTSQARAVPGGATA
	RLTDKAVKDYSAYRSSLLFWALVDLIYNMFKKVPTSNTEGGWSCSLAEYIRHNDMPIY
	IEAADKALKTFQEEFMPVETFSEFLDVAGLLSEITDPESFLKDLLNSVP

[0408] Further analysis of the NOV15a protein yielded the following properties shown in Table 15B.

TABLE 15B
Protein Sequence Properties NOV15a
PSort     0.6850 probability located in endoplasmic reticulum
analysis: (membrane); 0.6400 probability located in plasma membrane;
          0.4600 probability located in Golgi body; 0.1800
          probability located in nucleus
SignalP   No Known Signal Sequence Indicated
analysis:

[0409] 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
AAY53675	Mechanical stress induced protein	1 . . . 2938	2834/2974 (95%)	0.0
	274 amino acid sequence - Rattus	318 . . . 3262	2881/2974 (96%)
	sp, 3262 aa. [WO9960164-A1, 25
	NOV. 1999]
AAU28088	Novel human secretory protein,	584 . . . 3006	2423/2458 (98%)	0.0
	Seq ID No 257 - Homo sapiens,	1 . . . 2458	2423/2458 (98%)
	2458 aa. [WO200166689-A2, 13
	SEP. 2001]
AAM39071	Human polypeptide SEQ ID NO	584 . . . 3006	2421/2458 (98%)	0.0
	2216 - Homo sapiens, 2458 aa.	1 . . . 2458	2423/2458 (98%)
	[WO200153312-A1, 26 JUL.
	2001]
AAY53677	Sequence	731 . . . 3006	2276/2278 (99%)	0.0
	gi/3413886/dbj/BAA323071 from	1 . . . 2278	2276/2278 (99%)
	an alignment with protein 274 -
	Unidentified, 2278 aa.
	[WO9960164-A1, 25 NOV. 1999]
AAM40857	Human polypeptide SEQ ID NO 5788 -	731 . . . 3006	2246/2281 (98%)	0.0
	Homo sapiens, 2281 aa.	1 . . . 2281	2253/2281 (98%)
	[WO200153312-A1, 26 JUL.
	2001]

[0410] 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	Protein/	Residues/	Similarities for
Accession	Organism/	Match	the Matched	Expect
Number	Length	Residues	Portion	Value
Q8TDN5	Retinoblastoma-associated	1 . . . 3006	2974/3041 (97%)	0.0
	factor 600 - Homo sapiens	2171 . . . 5183	2975/3041 (97%)
	(Human), 5183 aa.
O75050	KIAA0462 protein - Homo	731 . . . 3006	2276/2276 (100%)	0.0
	sapiens (Human), 2276 aa	1 . . . 2276	2276/2276 (100%)
	(fragment).
Q9XYD2	PUSHOVER - Drosophila	3 . . . 3006	1330/3157 (42%)	0.0
	melanogaster (Fruit fly), 5322	2303 . . . 5316	1891/3157 (59%)
	aa.
Q9VLT5	CG14472 protein - Drosophila	3 . . . 3006	1329/3157 (42%)	0.0
	melanogaster (Fruit fly), 5322	2303 . . . 5316	1892/3157 (59%)
	aa.
O96958	CALO protein - Drosophila	3 . . . 3006	1327/3155 (42%)	0.0
	melanogaster (Fruit fly), 4116	1097 . . . 4110	1890/3155 (59%)
	aa (fragment).

[0411] PFam analysis indicates that the NOV15a protein contains the domains shown in the Table 15E.

TABLE 15E
Domain Analysis of NOV15a
			Identities/
		NOV15a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
	Tub	1417 . . . 1437	8/21 (38%)	0.13
			17/21 (81%)

Example 16

[0412] 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: 37	2178 bp
NOV16a,	TTGACTGTATCGCCGGAATTCATGGCGGGTCTGACGGCGGCGGCCCCGCGGCCCGGAG
CG132297-01
DNA Sequence	TCCTCCTGCTCCTGCTGTCCATCCTCCACCCCTCTCGGCCTGGAGGGGTCCCTGGGGC
	CATTCCTGGTGGAGTTCCTGGAGGAGTCTTTTATCCAGGGGCTGGTCTCGGAGCCCTT
	GGAGGAGGAGCGCTGGGGCCTGGAGGCAAACCTCTTAAGCCAGTTCCCGGAGGGCTTG
	CGGGTGCTGGCCTTGGGGCAGGGCTCGGCGCCTTCCCCGCAGTTACCTTTCCGGGGGC
	TCTGGTGCCTGGTGGAGTGGCTGACGCTGCTGCAGCCTATAAAGCTGCTAAGGCTGGC
	GCTGGGCTTGGTGGTGTCCCAGGAGTTGGTGGCTTAGGAGTGTCTGCAGCCCCTTCTG
	TGCCAGGTGCGGTGGTTCCTCAGCCTGGAGCCGGAGTGAAGCCCGGGAAAGTGCCGGG
	TGTGGGGCTGCCAGGTGTATACCCAGGTGGCGTGCTCCCAGGAGCTCGGTTCCCCGGT
	GTGGGGGTGCTCCCTGGAGTTCCCACTGGAGCAGGAGTTAAGCCCAAGGCTCCAGGTG
	TAGGTGGAGCTTTTGCTGGAATCCCAGGAGTTGGACCCTTTGGGGGACCGCAACCTGG
	AGTCCCACTCGGGTATCCCATCAAGGCCCCCAAGCTGCCTGGTGGCTATGGACTGCCC
	TACACCACAGGGAAACTGCCCTATGGCTATGGGCCCGGAGGAGTGGCTGGTGCAGCGG
	GCAAGGCTGGTTACCCAACAGGGACAGGGGTTGCCCCCCAGGCAGCAGCAGCACCGGC
	AGCTAAAGCAGCAGCAAAGTTCGGTGCTGGAGCAGCCCGAGTCCTCCCTGGTCTTGGA
	GGGGCTGGTGTTCCTGGCGTGCCTGGGGCAATTCCTGGAATTGGACGCATCGCAGCCG
	TTGGGACTCCAGCTGCAGCTGCAGCTGCAGCAGCGGCCGCTAAGGCAGCCAAGTATGG
	AGCTGCTGCAGGCTTAGTGCCTGGTGGGCCAGGCTTTGGCCCGGGAGTAGTTGGTGTC
	CCAGGAGCTGGCGTTCCAGGTGTTGGTGTCCCAGGAGCTGGGATTCCAGTTGTCCCAG
	GTGCTGGGATCCCAGGTGCTGCGGTTCCAGGGGTTGTGTCACCAGAAGCAGCTGCTAA
	GGCAGCTGCAAAGGCAGCCAAATACGGGGCCAGGCCCGGAGTCGGAGTTGGAGGCATT
	CCTACTTACGGGGTTGGAGCTGGGGGCTTTCCCGGCTTTGGTGTCGGAGTCGGAGGTA
	TCCCTGGAGTCGCAGGTGTCCCTAGTGTCGGAGGTGTTCCCGGAGTCGGAGGTGTCCC
	GGGAGTTGGCATTTCCCCCGAAGCTCAGGCAGCAGCTGCCGCCAAGGCTGCCAAGTAC
	GGAGTGGGGACCCCAGCAGCTGCAGCTGCTAAAGCAGCCGCCAAAGCCGCCCAGTTTG
	GGTTAGTTCCTGGTGTCGGCGTGGCTCCTGGAGTTGGCGTGGCTCCTGGTGTCGGTGT
	GGCTCCTGGAGTTGGCTTGGCTCCTGGAGTTGGCGTGGCTCCTGGAGTTGGTGTGGCT
	CCTGGCGTTGGCGTGGCTCCCGGCATTGGCCCTGGTGGAGTTGCAGCTGCAGCAAAAT
	CCGCTGCCAAGGTGGCTGCCAAAGCCCAGCTCCGAGCTGCAGCTGGGCTTGGTGCTGG
	CATCCCTGGACTTGGAGTTGGTGTCGGCGTCCCTGGACTTGGAGTTGGTGCTGGTGTT
	CCTGGACTTGGAGTTGGTGCTGGTGTTCCTGCCTTCGGGGCAGTACCTGGAGCCCTGG
	CTGCCCCTAGAGCAGCCAAATATGGAGCAGCAGTGCCTGGGGTCCTTGGAGGGCTCGG
	GGCTCTCGGTCCACTAGGCATCCCAGGCGGTGTGGTGGGAGCCGGACCCGCCGCCGCC
	GCTGCCGCAGCCAAAGCTGCTGCCAAAGCCGCCCAGTTTGGCCTAGTGGGAGCCGCTG
	GGCTCGGAGGACTCGCAGTCGGAGGGCTTGGAGTTCCAGGTGTTGGGGGCCTTGGAGG
	TATACCTCCAGCTGCAGCCGCTAAAGCAGCTAAATACGGAGTGGCAGCAAGACCTGGC
	TTCGGATTGTCTCCCATTTTCCCAGGTGGGGCCTGCCTGGGCAAAGCTTGTGGCCGGA
	AGAGAAAATGACTGCAGCCAAGCTAATTCCGG
	ORF Start: ATG at 22	ORF Stop: TGA at 2155
	SEQ ID NO: 38	711 bp	MW at 61662.7 kD
NOV16a,	MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGP
CG132297-01
Protein Sequence	GCKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAYKAAAKAGAGLGCVP
	GVGGLGVSAAPSVPGAVVPQPGAGVKPGKVPCVGLPGVYPCCVLPGARFRGVGVLPGV
	PTGAGVKPKAPGVGCGFAGIPGVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLP
	YGYGPGGVAGAAGKAGYPTGTGVCPQAAAAAAAKAAAKFGAGAAGVLPGVGGAGVPGV
	PGAIPGIGGIAGVGTAAAAAAAAAAKAAKYGAAAGLVPGGPCFGPGVVGVPGAGVPGA
	VGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKMAKAAKYGARRGVGVGCIPTYGVGAA
	GGFPGFGVGVGGIPGVAGVPSVGGVPGVCGVPGVGISPEAQAAAAAKAAKYGVGTPAA
	AAAKAAAKAAQFGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAP
	GIGPGGVkAAAKSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVCAGVPGLGVGA
	GVPGFGAVPGALAAARAAKYGAAVPGVLGGLCALGGVGIPGGVVGAGPAAAAAYAAAA
	AKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAAAAKAAKYGVAARPGFGLSPIF
	PGGACLGKACGRKRK
	SEQ ID NO: 39	2100 bp
NOV16b,	TTGACTGTATCGCCGGAATTCATGGCGGGTCTGACGGCGGCGGCCCCGCGGCCCGGAG
CG132297-02
DNA Sequence	TCCTCCTGCTCCTGCTGTCCATCCTCCACCCCTCTCGGCCTGGAGGGGTCCCTCGGGC
	CATTCCTGCTGGAGTTCCTGGAGGAGTCTTTTATCCAGGCGCTGGTCTCGGAGCCCTT
	GGAGCAGGAGCGCTGGGGCCTGGAGGCAAACCTCTTAAGCCAGTTCCCGGAGGGCTTG
	CGGGTGCTGGCCTTCGGGCAGGGCTCGGCGCCTTCCCCGCAGTTACCTTTCCCGGGGC
	TCTGGTGCCTGGTGGAGTCCCTGACGCTGCTGCAGCCTATAAAGCTGCTAAGGCTGGC
	GCTCGGCTTGGTGGTGTCCCAGGAGTTGGTGGCTTAGGAGTGTCTGCAGGTGCCGTGG
	TTCCTCAGCCTGGAGCCGGAGTGAAGCCTGGGAAAGTGCCGGGTGTACGTGGAGCTTT
	TGCTGCAATCCCAGGAGTTGGACCCTTTGGGGGACCGCAACCTGGAGTCCCACTGGGG
	TATCCCATCAAGGCCCCCAAGCTGCCTGGTGGCTATGGACTGCCCTACACCACAGGGA
	AACTGCCCTATGGCTATGGGCCCGGAGGAGTGGCTGGTGCAGCGGGCAAGGCTGGTTA
	CCCAACAGGGACAGGGGTTGGCCCCCAGGCAGCAGCAGCAGCGGCAGCTAAGCACCAA
	GCAAAGTTCGGTGCTGGAGCAGCCGGAGTCCTCCCTGGTGTTGGAGGGGCTGGTGTTC
	CTGGCGTGCCTGGGGCAATTCCTGGAATTGGAGGCATCGCAGGCGTTGGGACTCCAGC
	TGCAGCTGCAGCTGCAGCAGCAGCCGCTAAGGCAGCCAAGTATCGAGCTGCTGCAGGC
	TTAGTGCCTGGTGGCCCAGGCTTTGGCCCGGGAGTAGTTGGTGTCCCAGGAGCTGGCG
	TTCCAGGTGTTGGTGTCCCAGGAGCTGGGATTCCAGTTGTCCCAGGTGCTGGGATCCC
	AGGTGCTGCGGTTCCAGGGGTTGTGTCACCAGAAGCAGCTGCTAAGGCAGCTGCAAAG
	GCAGCCAAATACGGGGCCAGGCCCGCAGTCGGAGTTGGAGGCATTCCTACTTACGGGG
	TTGGAGCTGGGGGCTTTCCCGGCTTTGGTGTCGGAGTCGGAGGTATCCCTGGAGTCGC
	AGGTGTCCCTAGTGTCGGAGGTGTTCCCGGAGTCGGAGGTGTCCCGGGAGTTGGCATT
	TCCCCCGAAGCTCAGGCAGCAGCTGCCGCCAAGGCTGCCAAGTACGGAGTGGGGACCC
	CAGCAGCTGCAGCTGCTAAAGCAGCCGCCAAAGCCGCCCAGTTTGCTCTTCTCAATCT
	TCCAGGGTTAGTTCCTGGTGTCGGCGTGGCTCCTGGAGTTGGCGTGGCTCCTGGTGTC
	GGTGTGGCTCCTGGAGTTGGCTTGGCTCCTGGAGTTGGCGTGGCTCCTGGAGTTGGTG
	TGGCTCCTGGCGTTGGCGTGGCTCCCGGCATTGGCCCTGGTGGAGTTGCAGCTGCAGC
	AAAATCCGCTGCCAAGGTGGCTGCCAAAGCCCAGCTCCGAGCTGCAGCTGGGCTTGGT
	GCTGGCATCCCTGGACTTGGAGTTCGTGTCGGCGTCCCTGGACTTGGAGTTGGTGCTG
	GTGTTCCTGGACTTGGACTTGGTGCTGGTGTTCCTGGCTTCGGGGCAGTACCTGGAGC
	CCTGGCTGCCGCTAAAGCAGCCAAATATGGAGCAGCAGTGCCTGGGGTCCTTGGAGGG
	CTCGGGGCTCTCGGTGGAGTAGGCATCCCAGGCGGTGTGGTGGGAGCCGGACCCGCCG
	CCGCCGCTGCCGCAGCCAAAGCTGCTGCCAAAGCCGCCCAGTTTGCCCTAGTGGGAGC
	CGCTGGGCTCGGAGGACTCGGAGTCCGAGGGCTTGGAGTTCCAGGTGTTGGGGGCCTT
	GGAGGTATACCTCCAGCTGCAGCCGCTAAAGCAGCTAAATACGGTGCTGCTGGCCTTG
	GAGGTGTCCTAGGGGGTGCCGGGCAGTTCCCACTTGGAGGAGTGGCAGCAGAACCTGG
	CTTCGGATTGTCTCCCATTTTCCCAGGTGGGGCCTGCCTGGGGAAAGCTTGTGGCCGG
	AAGAGAAAATGA
	ORF Start: ATG at 22	ORF Stop: TGA at 2098
	SEQ ID NO: 40	692 aa	MW at 59784.4 kD
NOV16b,	MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGP
CG132297-02
Protein Sequence	GGKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAKAAAAYAGAGLGGVP
	GVGGLGVSAGAVVPQPGAGVKPGKVPGVGGAFAGIPGVGPFGGPQPGVPLGYPIKAPK
	LPGGYGLRYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQAAAAAAAKAAAKFGAGA
	AGVLPGVGGAGVPGVPGAIPGIGGIAGVGTRAAAAAAAAAAAKAAKYGAAAGLVRGGP
	FGPGVVGVPGAGVPGVGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKAAAKAAKYGAR
	PGVGVGGIPTYGVGAGGFPGFCVGVGGIPGVAGVPSVGGVPGVGGVPGVGISPEAQAA
	AAAKAAKYGVGTPAAAAAKAAAKAAQFALLNLAGLVPGVGVAPGVGVAPGVGVAPGVG
	LAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKAQLRAAAGLCAGIPGLG
	VGVGVPGLGVGAGVPGLGVGAGVPGFGAvPGALAAAKAAKYGAAVPGVLGGLGALGGV
	GIPGGVVGAGPAAAAAAAKAAAKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAA
	AAKAAKYGAAGLGGVLGGAGQFPLGGVAARPGFGLSPTFPGGACLGKACGRKRK

[0413] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 16B

TABLE 16B
Comparison of NOVl6a against NOV16b.
		Identities/
		Similarities
Protein	NOV16a Residues/	for the
Sequence	Match Residues	Matched Region
NOV16b	686 . . . 711	26/26 (100%)
	667 . . . 692	26/26 (100%)

[0414] Further analysis of the NOV16a protein yielded the following properties shown in Table 16C.

TABLE 16C
Protein Sequence Properties NOV16a
PSort     0.4323 probability located in outside; 0.1376 probability
analysis: located in microbody (peroxisome); 0.1000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 27 and 28
analysis:

[0415] 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	Protcin/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB08630	Amino acid sequence of a human	1 . . . 711	704/717 (98%)	0.0
	elastin polypeptide - Homo sapiens,	1 . . . 712	705/717 (98%)
	712 aa. [WO200050068-A2, 31
	AUG. 2000]
AAB08631	Fusion protein comprising human	2 . . . 711	703/716 (98%)	0.0
	elastin and c-myc - Synthetic, 730	11 . . . 721	704/716 (98%)
	aa. [WO200050068-A2, 31 AUG.
	2000]
AAY69069	Amino acid sequence of a human	27 . . . 711	679/703 (96%)	0.0
	reduced tropoelastin derivative -	1 . . . 698	680/703 (96%)
	Synthetic, 698 aa. [WO200004043-
	A1, 27 JAN. 2000]
AAY01302	Human tropoelastin variant	27 . . . 711	679/703 (96%)	0.0
	SHELdelta26A - Homo sapiens,	1 . . . 698	680/703 (96%)
	698 aa. [WO9903886-A1, 28 JAN.
	1999]
AAW46315	Human elastin containing non-	27 . . . 711	679/735 (92%)	0.0
	natural polypeptide MFU-1	1 . . . 730	680/735 (92%)
	sequence - Homo sapiens, 730 aa.
	[WO9805685-A2, 12 FEB. 1998]

[0416] 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
			Identities/
		NOV16a	Similarities for
Protein		Residues/	the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
P15502	Elastin precursor (Tropoelastin) -	1 . . . 711	705/735 (95%)	0.0
	Homo sapiens (Human), 730 aa.	1 . . . 730	706/735 (95%)
Q14234	Elastin - Homo sapiens (Human),	1 . . . 711	705/762 (92%)	0.0
	757 aa.	1 . . . 757	706/762 (92%)
Q14235	Elastin - Homo sapiens (Human),	1 . . . 711	686/711 (96%)	0.0
	687 aa.	1 . . . 687	687/711 (96%)
EAHU	elastin precursor, long splice	1 . . . 711	705/797 (88%)	0.0
	form - human, 792 aa.	1 . . . 792	706/797 (88%)
O15337	Elastin - Homo sapiens (Human),	29 . . . 600	565/607 (93%)	0.0
	602 aa (fragment).	1 . . . 602	566/607 (93%)

[0417] PFam analysis indicates that the NOV16a protein contains the domains shown in the Table 16F.

TABLE 16F
Domain Analysis of NOV16a
			Identities/
		NOV16a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
No Significant Matches Found

Example 17

[0418] 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: 41	1072 bp
NOV17a,	ATCCGAGTCACCTGCAGGACCGAAATGGAGGAGAGAGCACAGCACTGCCTGTCCAGAT
CG132343-01
DNA Sequence	TACTAGACAACTCTGCCCTGAAGCAGCAGCAGTTACCCATACACCGGCTATATTTCAC
	GGCCAGGAGAGTCCTCTTTGTCTTTTTCGCAACAGGAATATTCTGCCTTTGTATGGGC
	ATCATCCTTATATTGTCTGCAAGGAGCACTCAGGAAATAGAGGTTAATTACACAAGAA
	TATGTGCAAATTGTGCAAAACTGCGAGAAATGCCTCTIAATTTTGACAAGGAATGCAC
	CTGCTCTATTCCCTTTTACCTTTCAGGAAAAATGCAGGGTAATGTTTATATGTACTAC
	AAATTGTATGGCTTCTATCAGAACCTGTATCTATATATTCGATCCAGAAGTAATAGAC
	AACTGGTGGGCAAAGATGTAAAAGTAGTTGAGGATTGTGCCCCATTTAAAATGTCCGA
	CAATAAGACCCCCATCGTTCCTTGTGGTGCTATTGCCAACAGCATGTTCAATGACACC
	ATAATTCTTTCACACAACATTAATTCATCTGTACAAATCAAAGTGCCAATGTTAAAGA
	GTAGACTTACGTGGTGGACAGATAGTATGTCAAATTTCAGAAAATCTAAGTTTCAAGA
	TCTTGCTGATGATTTAGAGGTACCACAAAGCCCCCAACTGGCCCIAAAGCCTATCTAT
	AACTTGGATAAAAAGGATCCAAGAAACAATGGCTTCCTCAATGATGACTTCATTGTGT
	GGATGCGGGCAGCTGCCTTTCCCACTTTCAAAAAACTGTATGGTCGACTCAGTCGAAC
	ACACCATTTTATAGAAGGCTTGCCTGCTGGTAATTATAGTTTCAACATAACCTATAGT
	TTCCCAGTAACCAGGTTCCACGGAGAAAAATCAGTTGTTCTCTCCACCCTGACATGGT
	GTGGGGGTAATAGCCTTTTCTTAGGTCTTGCCTACACAGTGACAGGAGCTATGACATG
	GTTGGCCTCCTTTGCCATGATGGCAATTCACATCATGCTGAAAAAAACAAGAATGTCC
	TTCTTCCATCAATAAAGTCAAGCTTTAA
	ORF Start: ATG at 25	ORF Stop: TAA at 1057
	SEQ ID N0 42	344 aa	MW at 39698.8 kD
NOV17a,	MEERAQHCLSRLLDNSALKQQELPIHRLYFTARRVLFVFFATGIFCLCMCIILILSARAA
CG132343-01
Protein Sequence	STQEIEVNYTRICANCAKLRENASNFDKECTCSIPFYLSGKMQGNVYMYYKLYGFYQNAA
	LYLYIRSRSNRQLVGKDVKVVEDCAPFKMSDNKTPIVPCGAIAASMFNDTIILSHNINAA
	SSVQIKVPMLKSRLTWWTDKYVKFQNLSFKNLADEFRGTTKPPNWPKPIYDLDKKDPR
	INNGFLNDDFIVWMRAAFPTFKKLYGRLSRTHHFIEGLPAGNYSFNITYSFPVTRFHG
	EKSVVLSTLTWCGGNSLFLGLAYTVTGAMTWLASFAMMAIHIMLKNKKAVISFFHQ

[0419] Further analysis of the NOV17a protein yielded the following properties shown in Table 17B.

TABLE 17B
Protein Sequence Properties NOV17a
PSort     0.7900 probability located in plasma membrane; 0.7294
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 60 and 61
analysis:

[0420] 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 17C.

TABLE 17C
Geneseq Results for NOV17a
		NOV17a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB93258	Human protein sequence SEQ ID	10 . . . 336	147/336 (43%)	6e−74
	NO: 12282 - Homo sapiens, 361 aa.	25 . . . 352	206/336 (60%)
	[EP1074617-A2, 07 FEB. 2001]
AAY28810	nn296_2 secreted protein - Homo	10 . . . 336	147/336 (43%)	6e−74
	sapiens, 361 aa. [WO9950405-A1,	25 . . . 352	206/336 (60%)
	07 OCT. 1999]
ABB64777	Drosophila melanogaster	3 . . . 343	141/349 (40%)	3e−65
	polypeptide SEQ ID NO 21123 -	9 . . . 349	203/349 (57%)
	Drosophila melanogaster, 357 aa.
	[WO200171042-A2, 27 SEP. 2001]
ABG20423	Novel human diagnostic protein	10 . . . 336	138/336 (41%)	5e−65
	#20414 - Homo sapiens, 430 aa.	94 . . . 421	194/336 (57%)
	[WO200175067-A2, 11 OCT. 2001]
ABG20423	Novel human diagnostic protein	10 . . . 336	138/336 (41%)	5e−65
	#20414 - Homo sapiens, 430 aa.	94 . . . 421	194/336 (57%)
	[WO200175067-A2, 11 OCT. 2001]

[0421] 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 17D.

TABLE 17D
Public BLASTP Results for NOV17a
		NOV17a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q95JK4	Hypothetical 39.5 kDa protein -	1 . . . 344	324/344 (94%)	0.0
	Macaca fascicularis (Crab eating	1 . . . 344	330/344 (95%)
	macaque) (Cynomolgus monkey),
	344 aa.
Q95JU6	Hypothetical 33.9 kDa protein -	1 . . . 282	268/282 (95%)	e−160
	Macaca fascicularis (Crab eating	1 . . . 282	271/282 (96%)
	macaque) (Cynomolgus monkey),
	292 aa.
Q9D4D7	4933401B01Rik protein - Mus	1 . . . 341	229/341 (67%)	e−135
	musculus (Mouse). 342 aa.	1 . . . 341	272/341 (79%)
Q9UGC2	DJ234P15.3 (novel protein similar	10 . . . 336	147/336 (43%)	2e−73
	to (predicted) yeast and worm	23 . . . 350	206/336 (60%)
	proteins) - Homo sapiens
	(Human), 359 aa.
Q9NV96	CDNA FLJ10856 fis, clone	10 . . . 336	147/336 (43%)	2e−73
	NT2RP4001547 - Homo sapiens	25 . . . 352	206/336 (60%)
	(Human), 361 aa.

[0422] PFam analysis indicates that the NOV17a protein contains the domains shown in the Table 17E.

TABLE 17E
Domain Analysis of NOV17a
			Identities/
			Similarities
	Pfam	NOV17a Match	for the	Expect
	Domain	Region	Matched Region	Value
No Significant Matches Found

Example 18

[0423] 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: 43	1084 bp
NOV 18a,	GAAGCTTCTGGATCCTACGCTCATCTCTACAGAGGAGAACATGCACGCAGCAGAGATC
CG132423-01
DNA Sequence	ATGGGGCCCCTCTCAGCCCCTCCCTGCACAGAGCACATCAAATGGAAGGGGCTCCTGC
	TCACAGCATTACTTTTAAACTTCTGGAACTTGCCTACCACTGCCCAAGTCATGATTGA
	AGCCCAGCCACCCAAAGTGTCCGAGGGGAAGGATGTTCTTCTACTTGTCCAAATCAGG
	GACCTCTACCATTACATTACATCATATGTAGTAGACGGTCAATAAATTATATATGGAC
	CGGCATACAGTGGACGAGAAACAGTATATTCCAATGCATCCCTGCTGATCCAGAATGT
	CACCCGGGAGGACGCAGGATCCTACACCTTACACATCATAAAGCGAGGTGATCGGACT
	AGAGGAGTAACTGGATATTTCACCTTCACCTTATACCTGGAGACTCCCAAGCCCTCCA
	TCTCCAGCAGCAACTTAACCCCAGGGAGGCCATGGAGACTGTGATCTTAACCTGTAAA
	TCCTGAGACTCCGGACGCAAGCTACCTGTGGTGGATGAATGGTCAGAGCCTCCCTATG
	ACTCATAGGATGCAGCTGTCTGAAACCAACAGGACCCTCTTTCTATTTAGTGTCACAA
	AGTATACTGCAGGACCCTATGAATGTGAAATATGGAACTCAGGGAGTGCCAGCCGCAG
	TGACCCAGTCACCCTGAATCTCCTCCATGGTCCAGACCTCCCCACAATTTTCCCTTCA
	GTCACCTCTTACTATTCAGCAGAGAACCTCGACTTGTCCTGCTTCGCAGACTCTAACC
	CACCAGCACAGTATTCTTGGACAATTAAATGGGAAAGTTTCAGCTATCAGGACAAACT
	CTTTATCCCTCAATTACTCCAAAGCATAATGGGCTCTATGCTTGCTCTGCTCGTAAAC
	TCAGCCACTGGCGAGGAAAGCTCCACATCCTTGACAATCAGAGTCATTGCTCCTCCAG
	GATTAGGAACTTTTGCTTTCAATAATCCAACGTAGCAGCCGTGATGTCATTTTTGTAT
	TTCAGGAAGACTGGCAGGAGATTTATGGAAAAGACTATGA
	ORF Start: ATG at 41	ORF Stop: TAG at 1019
	SEQ ID NO: 44	326 aa	MW at 36013.5 kD
NOV18a,	MHAAEIMGPLSAPPCTEHIKWKGLLLTALLLNFWNLPTTAQVMIEAQPPKVSEGKDVL
CG132423-01
Protein Sequence	LLVQIRDLYHYITSYVVDGQIIIYGPAYSGRETVYSNASLLIQNTTREDAGSYTLHII
	KRGDGTRGVTCYFTFTLYLETPKPSISSSNLNPREANETVILTCNPETPDASYLWWMN
	GQSLPMTHRMQLSETNRTLFLFGVTKYTAGPYECEIWNSGSASRSDPVTLNLLHGPDL
	PRIFPSVTSYYSGENLDLSCFADSNPPAQYSWTINGKFQLSGQKLFIPQITPKHNGLY
	ACSARNSATGEESSTSLTIRVIAPPGLGTFAFNNPT
	SEQ ID NO: 45	990 bp
NOV18b,	AGATCTATGCACGCAGCAGAGATCATGGGGCCCCTCTCAGCCCCTCCCTGCACAGAGC
225029377 DNA
Sequence	ACATCAAATGGAAGGGGCTCCTGCTCACAGCATTACTTTTAAACTTCTGGAACTTGCC
	TACCACTGCCCAAGTCATGATTGAAGCCCAGCCACCCAAAGTGTCCGAGGGGAAGCAT
	GTTCTTCTACTTGTCCAAATCAGGGACCTCTACCATTACATTACATCATATGTAGTAG
	ACGGTCAATAAATTATATATGGACCGGCATACAGTGGACGAAGAACAGTATATTCCAA
	TGCATCCCTGCTGATCCAGAATGTCACCCGGCAGGACGCAGGATCCTACACCTTACAC
	ATCATAAGCGAGGTGATGGGACTAGAGGAGTAAACTGGATATTTCACCTTCACCTTAT
	ACCTGGAGACTCCCAAGCCCTCCATCTCCAGCAGCAACTTAAACCCCAGGGAGGCCAT
	GGAGACTGTGATCTTAACCTGTAATCCTGAGACTCCGGACGCAAGCTACCTGTGGTGG
	ATGAATGGTCAGAGCCTCCCTATGACTCATAGGATGCAGCTGTCTGAAACCAACAGGA
	CCCTCTTTCTATTTGGTGTCACAAGTATACTGCGGGACCCTATGAAAAATGTGATATG
	GAACTCAGGCAAGTGCCAGCCGCAGTGACCCAGTCACCCTGATCTCCTCCATGGTCCA
	GACCTCCCCAGAATTTTCCCTTCAGTCACCTCTTACTATTCAGGAGAGkACCTCGACT
	TGTCCTGCTTCGCAGACTCTAAACCCACCAGCACAGTATTCTTGGACATTAAATGAAA
	GTTTCAGCTATCAGGACAAAGCTCTTTATCCCTCAGATTACTCCAAGCATAAAATGGG
	CTCTATGCTTGCTCTGCTCGTAACTCAGCCACTGGCGAGGAAAGCTCCACATCCTTGA
	CAATCGGAGTCATTGCTCCTCCAGGATTAGGAACTTTTGCTTTCAATAATCCAACGCT
	CGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 46	330 aa	MW at 36399.9 kD
NOV18b,	RSMHAAEIMGPLSAPPCTEHIKWKGLLLTALLLNFWNLPTTAQVMIEAQPPKVSEGKD
225029377
Protein Sequence	VLLLVQIRDLYHYITSYVVDGQIIIYGPAYSGRETVYSNASLLIQNVTREDAGSYTLH
	IIKRGDGTRGVTGYFTFTLYLETPKPSISSSNLNPREAMETVILTCNPETPDASYLWW
	MNGQSLPMTHRMQLSETNRTLFLFGVTKYTAGPYECEIWNSGSASRSDPVTLNLLHGP
	DLPRIFPSVTSYYSGENLDLSCFADSNPPAQYSWTINGKFQLSGQKLFIPQITPKHNG
	YACSARNSATGEESSTSLTIGVIAPPGLGTFAFNITPTLE

[0424] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 18B.

TABLE 18B
Comparison of NOV18a against NOV18b.
			Identities/
	Protein	NOV18a Residues/	Similarities for
	Sequence	Match Residues	the Matched Region
	NOV18b	1 . . . 326	317/326 (97%)
		3 . . . 328	317/326 (97%)

[0425] Further analysis of the NOV18a protein yielded the following properties shown in Table 18C.

TABLE 18C
Protein Sequence Properties NOV18a
PSort     0.4500 probability located in cytoplasm;
analysis: 0.2390 probability located in
          lysosome (lumen); 0.2113 probability
          located in microbody (peroxisome);
          0.1000 probability located in
          mitochondrial matrix space
SignalP   Cleavage site between residues 41 and 42
analysis:

[0426] 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
ABG18511	Novel human diagnostic protein	1 . . . 322	321/337 (95%)	0.0
	#18502 - Homo sapiens, 355 aa.	18 . . . 354	321/337 (95%)
	[WO200175067-A2, 11 OCT.
	2001]
ABG18511	Novel human diagnostic protein	1 . . . 322	321/337 (95%)	0.0
	#18502 - Homo sapiens, 355 aa.	18 . . . 354	321/337 (95%)
	[WO200175067-A2, 11 OCT.
	2001]
AAY57912	Human transmembrane protein	7 . . . 325	260/334 (77%)	e−147
	HTMPN-36 - Homo sapiens, 335	1 . . . 334	278/334 (82%)
	aa. [WO9961471-A2, 02 DEC.
	1999]
AAM93561	Human polypeptide, SEQ ID NO:	7 . . . 311	223/320 (69%)	e−125
	3333 - Homo sapiens, 324 aa.	1 . . . 320	252/320 (78%)
	[EP1130094-A2, 05 SEP. 2001]
AAM93510	Human polypeptide, SEQ ID NO:	7 . . . 311	223/320 (69%)	e−125
	3229 - Homo sapiens, 326 aa.	1 . . . 320	252/320 (78%)
	[EP1130094-A2, 05 SEP. 2001]

[0427] 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
Q15242	Pregnancy-specific beta-1-	7 . . . 322	315/331 (95%)	0.0
	glycoprotein precursor - Homo	1 . . . 331	315/331 (95%)
	sapiens (Human), 332 aa.
Q8TCD9	Pregnancy specific beta-1-	7 . . . 326	287/335 (85%)	e−165
	glycoprotein 2 - Homo sapiens	1 . . . 335	295/335 (87%)
	(Human), 335 aa.
P11465	Pregnancy-specific beta-1-	7 . . . 326	285/335 (85%)	e−164
	glycoprotein 2 precursor (PSBG-2)	1 . . . 335	295/335 (87%)
	(Pregnancy-specific beta-1
	glycoprotein E) (PS-beta-E) - Homo
	sapiens (Human), 335 aa.
C27658	pregnancy-specific beta-1	7 . . . 326	285/336 (84%)	e−163
	glycoprotein E precursor - human,	1 . . . 336	295/336 (86%)
	336 aa.
O75237	PSGIIA-c - Homo sapiens (Human),	7 . . . 313	261/322 (81%)	e−147
	335 aa.	1 . . . 322	274/322 (85%)

[0428] PFam analysis indicates that the NOV18a protein contains the domains shown in the Table 18F.

TABLE 18F
Domain Analysis of NOV18a
			Identities/
			Similarities
	Pfam	NOV18a Match	for the	Expect
	Domain	Region	Matched Region	Value
	ig	245 . . . 294	16/53 (30%)	7.9e−08
			34/53 (64%)

Example 19

[0429] 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: 47	7347 bp
NOV19a,	ATGCAGAAGGAGCTGGGCATTGTGCCTTCCTGCCCTGCCATGAAGAGCCCCAGGCCCC
CG132541-01
DNA Sequence	ACCTCCTGCTACCATTGCTGCTGCTGCTGCTGCTGCTGCTGGGGGCTGGGGTGCCAGG
	TGCCTGGGGTCAGGCTGGGAGCCTGGACTTGCAGATTGATGAGGAGCAGCCAGCGGGT
	ACACTGATTGGCGACATCAGTGCGGCGCTTCCGGCAGGCAcGGCAGCTCCTCTCATGT
	ACTTCATCTCTGCCCAAGAGGGCAGCGGCGTGGGCACAGACCTGGCCATTGACGAACA
	CAGTGGGGTCGTCCGTACAGCCCGTGTCTTGGACCGTGAGCAGCGGGACCGCTACCGC
	TTCACTGCAGTCACTCCTGATGGTGCCACCGTAGAAGTTACAGTGCGAGTCGCTGACA
	TCAACGACCATGCTCCAGCCTTCCCACAGGCTCGGGCTGCCCTGCAGGTACCTGAGCA
	TACAGCTTTTGGCACCCGCTACCCACTGGAGCCTGCTCGTGATGCAGATGCTGGGCGT
	CTGGGAACCCAGGGCTATGCGCTATCTGGTGATGGGGCTGGAGAGACCTTCCGGCTGG
	AGACACGCCCCGGTCCAGATGGGACTCCAGTACCTGAGCTGGTAGTTACTGGGAAACT
	GGACCGAGAGAACCGCTCACACTATATGCTACAGCTGGAGGCCTATGATGGTGGTTCA
	CCCCCCCGGAGGGCCCAGGCCCTGCTGGACGTGACACTGCTGGACATCAATGACCATG
	CCCCGGCTTTCAATCAGAGCCGCTACCATGCTGTGGTGTCTGAGAGCCTGGCCCCTGG
	CAGTCCTGTCTTGCAGGTGTTCGCATCTGATGCCGATGCTGGTGTCAATGGGGCTGTG
	ACTTACGAGATCAACCGGAGGCAGAGCGAGGGTGATGGACCCTTCTCCATCGACGCAC
	ACACGGGGCTGCTGCAGTTAGAGCGGCCACTGGACTTTGAGCAGCGGCGGGTCCATGA
	ACTGGTGGTGCAAGCACGAGATGGTGGGGCTCACCCTGAGCTGGGCTCGGCCTTTGTG
	ACTGTGCATGTGCGAGATGCCAATGACAATCAGCCCTCCATGACTGTCATCTTTCTCA
	GTGCAGATGGCTCCCCCCAAGTGTCTGAGGCCGCCCCACCTGGACAGCTCGTTGCTCG
	CATCTCTGTGTCAGACCCAGATGATGGTGACTTTGCCCATGTCAATGTGTCCCTGGAA
	GGTGGAGAGGGCCACTTTGCCCTAAGCACCCAAGACAGCGTCATCTATCTGGTGTGTG
	GCTCGGCGGCTGGATCGAGAGGAGAGGGATGCCTATAACTTGAGGGTTACAGCCAC
	AGACTCAGGCTCACCTCCACTGCGGGCTGAGGCTGCCTTTGTGCTGCACGTCACTGAT
	GTCAACGACAATGCACCTGCCTTTGACCGCCAGCTCTACCGACCTGAGCCCCTGCCTG
	AGGTTGCGCTGCCTGGCAGCTTTGTAGTGCGGGTGACTGCTCGGGATCCTGACCAAGG
	CACCAATGGTCAGGTCACTTATAGCCTAGCCCCTGGCGCCCACACCCACTCGTTCTCC
	ATTGACCCCACCTCAGGCATTATCACTACGGCTGCCTCACTGGACTATGAGTTGGAAC
	CTCAGCCACAGCTGATTGTGGTGGCCACAGATGGTCGCCTGCCCCCTCTAGCCTCCTC
	TGCCACAGTTAGCGTGGCCCTGCAAGATGTGAATGATAATGAGCCCCAATTCCAGAGG
	ACTTTCTACAATGCCTCACTGCCTGAGGGCACCCAGCCTGGAACTTGCTTCCTGCAGG
	TGACAGCCACAGACGCGGATAGTGGCCCATTTGGCCTCCTCTCCTATTCCTTGGGTGC
	TGGACTTGGGTCCTCCGGATCTCCCCCATTCCGCATTGATGCCCACAGCGGTGATGTG
	TGCACAACCCGGACCCTGGACCGTGACCAGGGGCCCTCAAGCTTTGACTTCACAGTGA
	CAGCTGTGGATGGGGGAGGCCTCAAGTCCATCGTATATGTGAAGGTGTTTCTGTCAGA
	CGAGAATGACAACCCTCCTCAGTTTTATCCACGGGAGTATGCTGCCAGTATPAGTGCC
	CAGAGTCCACCAGGCACAGCTGTGCTGAGGTTGCGTGCCCATGACCCTGACCAGGGAT
	CCCATGGGCGACTCTCCTACCATATCCTGGCTGGCAACAGCCCCCCACTTTTTACCTT
	GGATGAGCAATCAGGTCTGTTGACAGTAGCCTGGCCCTTGGCCAGACGGGCCAATTCT
	GTGGTGCAGCTGGAGATCGGGGCTGAGGACGGAGGTGGCCTACAGGCAGAACCCAGTG
	CCCGAGTGGACATCAGCATTGTGCCTGGAACCCCCACACCACCCATATTTGAGCAACT
	ACAGTATGTTTTTTCTGTGCCAGAGGATGTGGCACCAGGCACCAGTGTGGGCATAGTC
	CAGGCACACAACCCACCAGGTCGCTTGGCACCTGTGACCCTTTCCCTATCAGGTCGGG
	AAATCCCCGAGGACTCTTCTCCCTAGATGCGGTATCAGGACTGTTGCAACACTTCCCC
	TCTGGACCGGGAGCTACTGGGACCAGTGTTGGAGCTGGAGGTGCGAGCAGGCAGTGGA
	GTGCCCCCAGCTTTCGCTGTAGCTCGCGTGCGTGTGCTGCTGGATGATGTGAATGACA
	ACTCCCCTGCCTTTCCTGCACCTGAAGACACGGTATTGCTACCACCAAACACTGCCCC
	AGGGACTCCCATCTATACACTGCGGGCTCTTGACCCCGACTCAGGTGTTAACAGTCGA
	GTCACCTTTACCCTGCTTGCTGGGGGTGGTGGAGCCTTCACCGTGGACCCCACCACAG
	GCCATGTACGGCTTATGAGGCCTCTGGGGCCCTCAGGAGGGCCAGCCCATGAGCTGGA
	GCTGGAGGCCCGGGATGGGGGCTCCCCACCACGCACCAGCCACTTTCGACTACGGGTG
	GTGGTACAGGATGTGGGAACCCGTCGGCTGGCTCCCCGATTCAACAGCCCTACCTACC
	GTGTGGACCTGCCCTCAGGCACCACTGCTGGAACTCAGGTCCTGCAAGTGCAGGCCCA
	AGCACCAGATGGGGGCCCTATCACCTATCACCTTGCAGCAGAGGGAGCAAGTAGCCCC
	TTTGGCCTGGAGCCACAGAGTGGGTGGCTATGGGTGCGGGCAGCACTACACCGTGAGG
	CCCAGGAATTGTACATACTGAAGGTAATGGCAGTGTCTGGGTCCAAAGCTGAGTTGGG
	GCAGCAGACAGGCACAGCCACCGTGAGGGTCAGCATCCTCAACCAGAATGAACACAGT
	CCCCGCTTGTCTGAGGATCCCACCTTCCTGGCTGTGGCTGAGAACCAGCCCCCAGGGA
	CCAGCGTGGGCCGAGTCTTTGCCACTGACCGAGACTCAGGACCCAATGGACGTCTGAC
	CTACAGCCTGCAACAGCTGTCTGAAGACAGCAAGGCCTTCCGCATCCACCCCCAGACT
	GGTGAGGTGACCACACTCCAAACCCTGGACCGTGAGCAGCAGAGCAGCTATCAGCTCC
	TGGTGCAGGTGCAGGATGGAGGGAGCCCACCCCGCAGCACCACAGGCACTGTCCATGT
	TGCAGTGCTTGACCTCAACGACAACAGCCCCACGTTCCTGCAGGCTTCAGGAGCTGCT
	GGTGGGGGCCTCCCTATACAGGTACCAGACCGCGTGCCTCCAGGAACACTGGTGACGA
	CTCTGCAGGCGAAGGATCCAGATGAGGGGGAGAATGGGACCATCTTCTACACGCTAAC
	TGGTCCTGGCTCAGAGCTTTTCTCTCTGCACCCTCACTCAGGGGAGCTGCTCACTGCA
	GCTCCCCTGATCCGAGCAGAGCGGCCCCACTATGTGCTGACACTGAGTGCTCATGACC
	AAGGCAGCCCTCCTCGAAGTCCCAGCCTCCAGCTGCTGGTGCAGGTACTTCCCTCAGC
	TCGCTTGGCCGAGCCGCCCCCAGATCTCGCAGAGCGGGACCCAGCGGCACCAGTGCCT
	GTCGTGCTGACGGTGACAGCAGCTGAGGGACTGCGGCCCGGCTCTCTGTTGGGCTCGG
	TGGCAGCGCCAGAGCCCGCGGGTCTGCGTGCACTCACCTACACACTGGTGGGCGGTGC
	CGATCCCGAGGGCACCTTCGCGCTGGATGCGGCCTCAGGGCGCTTGTACCTGGCGCCG
	CCCCTGGACTTCGAAGCTGGCCCGCCGTGGCGCGCGCTCACGGTACGCGCTGAGGGGC
	CGGGAGGCGCGGGCGCGCGGCTGCTGCGAGTGCAGGTGCAAGTGCAGCACGACAATGA
	GCATGCGCCCGCCTTTGCGCGCGACCCGCTGGCGCTGGCGCTGCCAGAGAACCCGGAG
	CCCGGCGCAGCGCTGTACACTTTCCGCGCGTCGGACGCCGACGGCCCCGGCCCCAATA
	GCGACGTGCGCTACCGCCTGCTGCGCCAGGAGCCGCCCGTGCCGGCGCTTCGCCTGGA
	CGCGCGCACCGGGGCGCTCAGCGCTCCGCGCGGCCTGGACCGAGAGACCACTCCCGCG
	CTGCTGCTGCTGGTGGAAGCCACCGACCGGCCCGCCAACGCCAGCCGCCGTCGTGCAG
	CGCGCGTTTCAGCGCGCCTCTTCGTCACGGATGAGAATGACAACGCGCCTGTCTTCGC
	CTCGCCGTCACGCGTGCGCCTCCCAGAGGACCAGCCGCCTGGGCCCGCGGCCCTGCAC
	GTGGTAGCCCGGGACCCGGATCTGGGCGAGGCTGCACGCGTGTCCTATCGGCTGGCAT
	CTGGCGGGGACGGCCACTTCCCGCTGCACTCAAGCACTCGTGCGCTGTCCGTGGTGCG
	GCCGTTCGACCGCGAACAACGAGCTGAGCACGTACTGACAGTGGTGGCCTCAGACCAC
	GGCTCCCCGCCGCGCTCGACCACGCAGGTCCTGACCGTCAGTGTCGCTGACGTCAACG
	ACGAGGCGCCTACTTTCCAGCAGCAGGAGTACAGCGTCCTCTTGCGTGAGAACAACCC
	TCCTGCCACATCTCTGCTCACCCTGCGAGCAACCGACCCCCACGTGGGTGCCAACGGG
	CAAGTGACTTATGGAGGCGTCTCTAGCGAAAGCTTTTCTCTGGATCCTGACACTCGTG
	TTCTCACGACTCTTCGGGCCCTGGATCGAGAGGAACAGGAGGAGATCAACCTGACAGT
	GTATGCCCAGGACAGGGGCTCACCTCCTCAGTTAACGCATGTCACTGTTCGAGTGGCT
	GTGGAGGATGAGAATGACCATGCACCAACCTTTGGGAGTGCCCATCTCTCTCTGGAGG
	TGCCTGAGGGCCAGGACCCCCAGACCCTTACCATGCTTCGGQCCTCTGATCCAGATGT
	GGGAGCCAATGGGCAGTTGCAGTACCGCATCCTAGATGGGGACCCATCAGGAGCCTTT
	GTCCTAGACCTTGCTTCTGGAGAGTTTGGCACCATGCGGCCACTAGACAGAGAACTGG
	AGCCAGCTTTCCAGCTGAGGATAGAGGCCCGGGATGGAGGCCAGCCAGCTCTCAGTGC
	AACACGCTGCTTTTGACAGTGACAGTGCTGGATGCCAATGACCATGCTCCAGCCTCCT
	GTGCCTGCCTACTCGTGGAGGTGCCGGAGGATGTGCCTGCAGGGACCCTGCTGCTCAC
	AGCTACAGGCTCATGACCCTGATGCTGGAGCTAATGGCCATGTGACCTACTACCTGGC
	CGCCGGTACAGCAGGAGCCTTCCTGCTGGAGCCCAGCTCTGGAGAACTGCGCACAGCT
	CCAGCCTTGGACAGAGAACAGTGTCCCAGCTACACCTTTTCTGTGAGTGCAGTGGATG
	GTGCAGCTGCTGGGCCCCTAAGCACCACAGTGTCTGTCACCATCACGGTGCGCGATGT
	CAATGACCATGCACCCACCTTCCCCACCAGTCCTCTGCGCCTACGTCTGCCCCGCCCA
	GGCCCCAGCTTCAGTACCCCAACCCTGGCTCTGGCCACACTGAGAGCTGAAGATCGTC
	ATGCTGGTGCCAATGCTTCCATTCTGTACCGGCTGGCAGGCACACCACCTCCTGGCAC
	TACTGTGGACTCTTACACTGGTGAAATCCGCGTGGCCCGCTCTCCTGTAGCTCTAGGC
	CCCCGAGATCGTGTCCTCTTCATTGTGGCCACTGATCTTGGCCGTCCAGCTCGCTCTG
	CCACTGGTGTCATCATTGTTGGACTGCAGGGGGAAGCTGAGCGTGGACCCCGCTTTCC
	CCGGGCTAGCAGTGAGGCTACGATTCGTGAGAATGCGCCCCCAGGTACTCCTATTGTC
	TCCCCCAGGGCCGTCCATGCAGGAGGCACAAATGGACCCATCACCTACAGCATTCTCA
	GTGGGAATGAGAAAGGGACATTCTCCATCCAGCCTAGTACAGGTGCCATCACAGTTCG
	CTCAGCAGAGGGGCTAGACTTCGAGGTGAGTCCACGGCTGCGACTGGTGCTGCAGGCA
	CTTGGAGGGGCCCCTGCTGCAGGTGGAGGCGGATGACCTGGATCAAGGCTCTGGAGGA
	ACAATGCTCCCCGTTTCCTGCGGCCCCATTATGTGGCCTTCCTTCCTGAGTCCCGGCC
	CTTGGAGGGGCCCCTGCTGCAGGTGGAGGCGGATGACCTGGATCAAGGCTCTGGAGGA
	CAGATTTCCTACAGTCTGGCTGCATCCCAGCCGGCACGTGGATTGTTCCACGTAGACC
	CACCACAGGCACTATCACTACCACAGCCATCCTGGACCGTGAGATCTGGGCTGAAAAC
	ACGGTTGGTGCTGATGGCCACAGACAGAGGGAGCCCAGCCCTGGTGGGCTCAGCTACC
	TTGACGGTGATGGTCATCGACACCAATGACAATCGCCCCACCATCCCCCAACCCTGGG
	AGCTCCGAGTGTCAGAAGATGGCAIGCCATGTGTGGCAGGTGCGCTGACAGCCATTGT
	GGCCGGCGAGCAGGAGCTCCGTGGCAGCTATAACTGGGACTACCTGCTGAGCTGGTGC
	CATCAGCACCAACCACTGGCCAGTGTCTTCACAGAGATCGCTCGGCTCAAGGATGAAG
	CTCGGCCATGTCCCCCAGCTCCCCGTATCGACCCACCACCCCTCATCACTGCCGTGGC
	CCACCCAGGAGCCAAGTCTGTGCCCCCCAAGCCAGCAAACACAGCTGCAGCCCGGGCC
	ATCTTCCCACCAGCTTCTCACCGCTCCCCCATCAGCCGTGAAGGCTCCCTGTCCTCAG
	CTGCCATGTCCCCCAGCTTCTCACCCTCTCTGTCTCCTCTGGCTGCTCGCTCACCCGT
	TGTCTCACCAATTGGGGTGGCCCAGGGTCCCTCAGCCTCAGCACTCAGCGCAGAGTCT
	GGCCTGGAGCCACCTGATGACACGGAGCTGCACATCTAG
	ORF Start: ATG at 1	ORF Stop: TAG at 7345
	SEQ ID NO: 48	2448 aa	MW at 258115.8 kD
NOV19a,	MQKELGIVPSCPGMKSPRPHLLLPLLLLLLLLLGAGVPGAWGQAGSLDLQIDEEQPAG
CG132541-01
Protein Sequence	TLIGDISAGLPAGTAAPLMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDREQRDRYR
	PTAVTPDGATVEVTVRVADINDHAPAFPQARAALQVPEHTAFGTRYPLEPARDADAGR
	LGTQGYALSGDGAGETFRLETRPGPDGTPVPELVVTGELDRENRSHYMLQLEAYDGGS
	PPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGVNGAV
	TYEINRRQSEGDGPFSIDAHTCLLQLERPLDFEQRRVHELVVQARDGGAHPELGSAFV
	TVHVRDANDNQPSMTVIFLSADGSPQVSEAAPPGQLVARISVSDPDDGDFAHVNVSLE
	GGEGHFALSTQDSVIYLVCVARRLDREERDAYNLRVTATDSGSPPLRAEAAFVLHVTD
	VNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGAHTHWFS
	IDPTSGIITTAASLDYELEPQPQLIVVATDGGLPPLASSATVSVALQDVNDNEPQFQR
	TFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGSSGSPPFRIDAHSGDV
	CTTRTLDRDQGPSSFDFTVTAVDGGGLKSMVYVKVFLSDENDNPPQFYPREYAASISA
	QSPRGTAVLRLRAHDPDQGSHGRLSYHILAGNSPPLFTLDEQSCLLTVAWPLARRANS
	VVQLEIGAEDGGGLQAEPSARVDISIVRGTPTPPIFEQLQYVFSVPEDVAPGTSVGIV
	QAHNPPGRLAPVTLSLSGGDPRGLFSLDAVSGLLQTLRPLDRELLGPVLELEVRAGSG
	VPPAFAVARVRVLLDDVNDNSPAFPAPEDTVLLPPNTAPGTPIYTLRALDPDSGVNSR
	VTETLLAGGGGAFTVDPTTGHVRLMRPLGPSGGRAHELELEARDGGSPPRTSHFRLRV
	VVQDVGTRGLAPRFNSPTYRVDLPSGTTAGTQVLQVQAQAPDGGPITYHLAAEGASSP
	FGLEPQSGWLNTRAALDREAQELYILKVMAVSGSKAELGQQTGTATVRVSILNQNEHS
	PRLSEDPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQT
	GEVTTLQTLDREQQSSYQLLVQVQDGGSPPRSTTGTVHVAVLDLNDNSPTFLQASGAA
	GGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHSGELLTA
	APLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSARLAEPPPDLAERDPAAPVP
	VVLTVTAAEGLRPGSLLGSVAAPEPAGVGALTYTLVGGADPEGTFALDAASCRLYLAR
	PLDFEAGPPWRALTVRAEGPGGAGARLLRVQVQVQDENEHAPAFARDPLALALPENPE
	PGAALYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPA
	LLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALH
	VVARDPDLGEAARVSYRLASGGDGHFRLHSSTGALSVVRPLDREQRAEHVLTVVASDH
	GSPPRSATQVLTVSVADVNDEApTFQQQEYSVLLRENNPPGTSLLTLRATDPDVGAGI
	AQVTYGGVSSESFSLDPDTGVLTTLRALDREEQEEINLTVYAQDRGSPPQLTHVTVRV
	VEDENDHAPTFGSAHLSLEVPEGQDPQTLTMLRASDPDVGANGQLQYRILDGDPSCAF
	VLDLASGEFGTMRPLDREVEPAFQLRIERDGGQPALSATLLLTVTVLDANDHIAPAFP
	VPAYSVEVPEDVPAGTLLLQLQAHDPDAGANGIVTYYLGAGTAGAFLLEPSSGELRTA
	AALDREQCPSYTPSVSAVDGAAAGPLSTTVSVTITVRDVNDHAPTFPTSPLRLRLPRP
	GPSFSTPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALG
	PRDRVLFIVATDLGRPARSATGVIIVGLQGEAERGPRFPPASSEATIRENAPPGTPIV
	SPPAVHAGGTNGPITYSILSGNEKGTFSIQPSTGAITVRSAEGLDFEVSPRLRLVLQA
	ESGGAFAFTVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEAADLDQGSGG
	QISYSLAASQPARGLFHVDPTTGTITTTAILDREIWAETRLVLAATDRGSPALVGSAT
	LTVMVIDTNDNRPTIPQPWELRVSEDGKPCVAGALTAIVAGEEELRGSYNWDYLLSW
	HQHQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAPGAKSVPPKPANTAAARA
	IFPPASHRSPISREGSLSSVASPSFSPSLSPLAARSPVVSPIGVAQGPSASALSAES
	GLEPPDDTELHI
	SEQ ID NO: 49	10759 bp
NOV19b,	GCGGGGGGAGGGGAGGGGAGGGGAGGGGGCGCGGGGCCGCGGCAGCGGACCTCGCATC
CG132541-02
DNA Sequence	CTCGGCGGGGCGGCTGTGCAGGAGGCGGCGCCCGGGCGTCAGCGGACGGACCGATCGA
	CGGCCAAGGGCGCGCGGACCGACGGCGGCTGCCCGGAGGGGATCGCGGGCCTCCGAGA
	CAGCCACTGCGGACGATGCGCGGCCCCAGGCCCCGCGCGAGCGGGCGCTGCCCGGGGG
	GCTGACCGCGGCCCGACGGCGCCCCAGCACCGGGCGAGGGAGCCCGCGTCGCGCGGAG
	GTCAGGGAGCCTGAGCTGGAGCCAGGGCCCCAGTGGGACCTGACCCAAAGTCTGAGGT
	CAAGCTCGGCCCAGAGCCTGGCCTGGAGCTGGAGCCCACAGCACAGCTGGACTACCCT
	TGTCATGCAGAAGGAGCTGGGCATTGTGCCTTCCTGCCCTGGCATGAAGAGCCCCAGG
	CCCCACCTCCTGCTACCATTGCTGCTGCTGCTGCTGCTGCTGCTGGGGGCTGGGGTGC
	CAGGTGCCTGGGGTCAGGCTGGGAGCCTGCACTTGCACATTGATGAGGAGCAGCCAGC
	GGGTACACTGATTGGCGACATCAGTGCGGGGCTTCCGGCAGGCACCGCAGCTCCTCTC
	ATGTACTTCATCTCTGCCCAAGAGCGCAGCGGCGTGGGCACAGACCTGGCCATTGACG
	AACACAGTGGGGTCGTCCGTACAGCCCGTGTCTTGGACCGTGAGCAGCGGGACCGCTA
	CCGCTTCACTCCAGTCACTCCTGATGGTGCCACCGTAGAAGTTACAGTGCGAGTGGCT
	GACATCAACGACCATGCTCCAGCCTTCCCACAGOCTCGGGCTGCCCTGCAGGTACCTG
	AGCATACAGCTTTTGGCACCCGCTACCCACTGGAGCCTGCTCGTGATGCAGATGCTCG
	GCGTCTGGGAACCCAGGGCTATGCGCTATCTGGTGATGGGGCTGGAGAGACCTTCCGG
	CTGGAGACACGCCCCGGTCCAGATGGGACTCCAGTACCTGAGCTGGTAGTTACTGGGG
	AACTGGACCGAGAGAACCGCTCACACTATATGCTACAGCTGGAGGCCTATGATGGTGG
	TTCACCCCCCCGCACGGCCCAGGCCCTGCTGGACGTGACACTGCTGGACATCAATGAC
	CATGCCCCGGCTTTCAATCAGAGCCGCTACCATGCTGTGGTGTCTGAGAGCCTGGCCC
	CTGGCAGTCCTGTCTTGCAGGTGTTCGCATCTGATGCCGATGCTGGTGTCAATGGGGC
	TGTGACTTACGAGATCAACCGCAAGGCAGAGCGAGGGTGATGGACCCTTCTCCATCGAC
	GCACACACGGCGCTGCTGCAGTTAGAGCGGCCACTGGACTTTGAGCAGCGGCGGGTCC
	ATGAACTGGTGGTGCAAGCACGAGATGGTGGGGCTCACCCTGAGCTGGGCTCGGCCTT
	TGTGACTGTGCATGTGCGAGATGCCAATGACAATCAGCCCTCCATGACTGTCATCTTT
	CTCAGTGCAGATGGCTCCCCCCAAGTGTCTGAGGCCGCCCCACCTGGACAGCTCGTTG
	CTCGCATCTCTGTGTCAGACCCAGATGATGGTGACTTTGCCCATGTCAATGTGTCCCT
	GGAAGGTGGAGAGGGCCACTTTGCCCTAAGCACCCAAGACAGCGTCATCTATCTGGTG
	TGTGTGGCTCGGCGGCTGGATCGAGAGGAGAGGGATGCCTATAACTTGAGGCTTACAG
	CCACAGACTCAGGCTCACCTCCACTGCGGGCTGAGGCTGCCTTTGTGCTGCACGTCAC
	TGATGTCAACGACAATGCACCTGCCTTTGACCGCCAGCTCTACCGACCTGAGCCCCTG
	CCTGAGGTTGCGCTGCCTGGCAGCTTTGTAGTGCGGGTGACTGCTCGGGATCCTGACC
	AAGGCACCAATGGTCAGGTCACTTATAGCCTAGCCCCTGGCGCCCACACCCACTGGTT
	CTCCATTGACCCCACCTCAGGCATTATCACTACGGCTGCCTCACTGGACTATGAGTTG
	GAACCTCAGCCACAGCTGATTGTGGTGGCCACAGATGGTGGCCTGCCCCCTCTAGCCT
	CCTCTGCCACAGTTAGCGTGGCCCTGCAAGATGTGATGAATAATGAGCCCCAATTCCA
	GAGGACTTTCTACAATGCCTCACTGCCTGAGGGCACCCAGCCTGGIACTTGCTTCCTG
	CAGGTGACAGCCACAGACGCGGATAGTGCCCCATTTGGCCTCCTCTCCTATTCCTTGG
	GTGCTGGACTTGGGTCCTCCGGATCTCCCCCATTCCGCATTGATGCCCATAGCGCTGA
	TGTGTGCACAACCCGGACCCTGGACCCTGACCAGGGGCCCTCAAGCTTTGACTTCACA
	GTGACAGCTGTGGATGGGGGAGGCCTCAAGTCCATGGTATATGTGAAGGTGTTTCTGT
	CAGACGAGAATGACAACCCTCCTCAGTTTTATCCACGGGAGTATGCTGCCAGTATAAG
	TGCCCAGAGTCCACCAGGCACAGCTGTGCTGAGGTTGCGTGCCCATGACCCTCACCAG
	GGATCCCATGGGCGACTCTCCTACCATATCCTGGCTGGCAACAGCCCCCCACTTTTTA
	CCTTGGATGAGCAATCAGGGCTGTTGACAGTAGCCTGGCCCTTGGCCAGACGGGCAAA
	TTCTGTGGTGCAGCTGGAGATCGGGGCTGAGGACGGAGGTGGCCTACAGGCAGAACCC
	AGTGCCCGAGTGGACATCAGCATTGTGCCTGGAACCCCCACACCACCCATATTTGAGC
	ACTACAGTATGTTTTTTCTGTGCCAGAGGATGTGGCACCAGGCACCAGTGTGGCACAT
	AGTCCAGGCACACAACCCACCAGGTCGCTTGGCACCTGTGACCCTTTCCCTATCAGGT
	GGGGATCCCCGAGGACTCTTCTCCCTAGATGCGGTATCAGGACTGTTGCAAACACTTC
	GCCCTCTGGACCCGGAGCTACTGGGACCAGTGTTGGAGCTGGAGGTGCGAGCAGGCAG
	TGGAGTGCCCCCAGCTTTCGCTGTAGCTCGGGTGCGTGTGCTGCTGGATGATGTGAAT
	GACAACTCCCCTGCCTTTCCTGCACCTGAAGACACGGTATTGCTACCACCAAACACTG
	CCCCAGGGACTCCCATCTATACACTGCGGGCTCTTGACCCCGACTCAGGTGTTAACAG
	TCGAGTCACCTTTACCCTGCTTGCTGGGGGTGGTGGAGCCTTCACCGTGGACCCCACC
	ACAGGCCATGTACGGCTTATGAGGCCTCTGGGGCCTCAGGACAGGCCAGCCCATGAGC
	TGGAGCTGGAGGCCCGGGATGGGGGCTCCCCACCACGCACCAGCCACTTTCGACTACG
	GGTGGTGGTACAGGATGTGGGAACCCGTGGGCTGGCTCCCCGATTCAACAGCCCTACC
	TACCGTCTGGACCTGCCCTCAGGCACCACTGCTGGAACTCAGGTCCTGCAAGTGCAGG
	CCCAAGCACCAGATGGGGGCCCTATCACCTATCACCTTGCACCAGAGGGAGCAAGTAG
	CCCCTTTGGCCTGGAGCCACAGAGTGGGTGGCTATGGGTGCGGGCAGCACTAGACCGT
	GAGGCCCAGGAATTGTACATACTGAAGGTAZTGGCAGTGTCTGGGTCCAAAGCTGAGT
	TGGGGCAGCAGACAGGCACAGCCACCGTGAGGGTCAGCATCCTCAACCAGAATGAACA
	CAGTCCCCGCTTGTCTGAGGATCCCACCTTCCTGGCTGTGGCTGAGAACCAGCCCCCA
	GGGACCAGCGTGGGCCGAGTCTTTGCCACTGACCGAGACTCAGGACCCAATGGACGTC
	TGACCTACAGCCTGCAACAGCTGTCTGAA\GACAGCAAGGCCTTCCGCATCCACCCCCA
	GACTGGAGAAGTGACCACACTCCAAACCCTGGACCGTGAGCAGCAGAGCAGCTATCAG
	CTCCTGGTGCAGGTGCAGGATGGAGGGAGCCCACCCCGCAGCACCACAGGCACTGTGC
	ATGTTGCAGTGCTTGACCTCAACGACAACAGCCCCACGTTCCTGCAGGCTTCAGGAGC
	TGCTGGTGGGGGCCTCCCTATACAGGTACCAGACCGCGTGCCTCCAGGAACACTGGTG
	ACGACTCTGCAGGCGAAGGATCCAGATGAGGGGCAGAATGGGACCATCTTGTACACGC
	TAACTGGTCCTGGCTCAGAGCTTTTCTCTCTGCACCCTCACTCAGGGGAGCTGCTCAC
	TGCAGCTCCCCTGATCCGAGCACAGCGGCCCCACTATGTGCTGACACTGAGTGCTCAT
	GACCAAGGCAGCCCTCCTCGAAGTGCCAGCCTCCAGCTGCTGGTGCAGGTGCTTCCCT
	CAGCTCGCTTGGCCGAGCCGCCCCCAGATCTCGCAGAGCGGGACCCAGCGGCACCAGT
	GCCTGTCGTGCTGACGGTGACAGCAGCTGAGGGACTGCGGCCCGGCTCTCTGTTGGGC
	TCGGTGGCAGCGCCAGAGCCCGCGCGTGTGGGTGCACTCACCTACACACTGGTGGGCG
	GTGCCGATCCCGAGGGCACCTTCGCGCTGGATGCGGCCTCAGGGCGCTTGTACCTGGC
	GCGGCCCCTGGACTTCGAAGCTGGCCCGCCGTGGCGCGCGCTCACGGTACGCGCTGAG
	GGGCCGGGAGGCGCCGGCGCGCGGCTGCTGCGAGTGCAGGTGCAAGTGCAGGACGAGA
	ATGAGCATGCGCCCGCCTTTGCGCGCGACCCGCTGGCGCTGGCGCTGCCAGAGAACCC
	GGAGCCCGGCGCAGCGCTGTACACTTTCCGCGCGTCGGACGCCGACGGCCCCGGCCCC
	AATAGCGACGTGCGCTACCGCCTGCTGCGCCACGAGCCGCCCGTGCCGGCGCTTCGCC
	TGGACGCGCGCACCGGGGCGCTCAGCGCTCCGCGCGGCCTGGACCGAGAGACCACTCC
	CGCGCTGCTGCTGCTGGTGGAAGCCACCGACCGGCCCGCCAACGCCAGCCQCCGTCGT
	GCAGCGCGCGTTTCAGCGCGCGTCTTCGTCACGGATGAGAATGACAACGCGCCTGTCT
	TCGCCTCGCCGTCACGCGTGCGCCTCCCAGAGGACCAGCCGCCTGGGCCCGCGGCCCT
	GCACGTGGTAGCCCGGGACCCGGATCTGGGCGAGGCTGCACGCGTGTCCTATCCGCTG
	GCATCTGGCGGGGACGGCCACTTCCGGCTGCACTCAAGCACTGGAGCGCTGTCCGTGG
	TGCGGCCGTTGGACCGCGAACAACGAGCTGAGCACGTACTGACAGTGGTGGCCTCAGA
	CCACGGCTCCCCGCCGCGCTCGGCCACGCAGGTCCTGACCGTCAGTGTCGCTGACGTC
	AACGACGAGGCGCCTACTTTCCAGCAGCAGGAGTACAGCGTCCTCTTGCGTGAGAACA
	ACCCTCCTGGCACATCTCTGCTCACCCTGCGAGCAACCGACCCCGACGTGGGGGCCAA
	CGGGCAAGTGACTTATGGAGGCGTCTCTAGCGAAAGCTTTTCTCTGGATCCTGACACT
	GGTGTTCTCACGACTCTTCGGGCCCTGGATCGAGAGGAACAGGAGGAGATCAACCTGA
	CAGTGTATGCCCAGGACAGGGGCTCACCTCCTCAGTTAACGCATGTCACTGTTCGAGT
	GGCTGTGGAGGATGAGAATGACCATGCACCAACCTTTGGGAGTGCCCATCTCTCTCTG
	GAGGTGCCTGAGGGCCAGGACCCCCAGACCCTTACCATGCTTCGGGCCTCTGATCCAG
	ATGTGGGAGCCAATGGGCAGTTGCAGTACCGCATCCTAGATGGGGACCCATCAGGAGC
	CTTTGTCCTAGACCTTGCTTCTGGAGACTTTGGCACCATGCGGCCACTAGACAGAGAA
	GTGGAGCCAGCTTTCCAGCTGAGGATAGACCCCCGGGATGGAGGCCAGCCAGCTCTCA
	GTGCCACGCTGCTTTTGACAGTGACAGTGCTGGATGCCAATGACCATGCTCCACCCTT
	TCCTGTGCCTGCCTACTCGGTGGAGGTGCCGGAGGATGTGCCTGCAGGGACCCTGCTG
	CTGCAGCTACAGGCTCATGACCCTGATGCTGGAGCTAATGGCCATGTGACCTACTACC
	TGGGCGCCGGTACACCAGGAGCCTTCCTGCTGGAGCCCAGCTCTGGAGAACTGCGCAC
	AGCTGCAGCCTTGGACAGAGAACAGTGTCCCAGCTACACCTTTTCTGTGAGTGCAGTG
	GATGGTGCAGCTGCTGGGCCCCTAAGCACCACAGTGTCTGTCACCATCACGGTGCGCG
	ATGTCAATGACCATGCACCCACCTTCCCACCAGTCCTCTGCGCCTACGTCTGCCCCGA
	CCCAGGCCCCAGCTTCAGTACCCCAACCCTGGCTCTGGCCACACTGAGAGCTGAAGAT
	CGTGATGCTGGTGCCAATGCTTCCATTCTGTACCGGCTGGCAGGCACACCACCTCCTG
	GCACTACTGTGGACTCTTACACTGGTGAAATCCGCGTGGCCCGCTCTCCTGTAGCTCT
	AGGCCCCCGAGATCGTGTCCTCTTCATTGTGGCCACTGATCTTGGCCGTCCAGCTCGC
	TCTGCCACTGGTGTGATCATTGTTGGACTGCAGGGGGAAGCTGAGCGTGGACCCCGCT
	TTCCCCGGCCTAGCAGTGAGOCTACGATTCGTGAGAATGCGCCCCCAGGGACTCCTAT
	TGTCTCCCCCAGGGCCGTCCATGCAGGAGGCACAAATGGACCCATCACCTACAGCATT
	CTCAGTGGGAATGAGAAAGGGACATTCTCCATCCAGCCTAGTACAGGTGCCATCACAG
	TTCGCTCAGCAGAGGGGCTAGACTTCGAGGTGAGTCCACGCCTGCGACTGGTGCTGCA
	GGCAGAGAGTGGAGGAGCCTTTGCCTTCACTGTGCTGACCCTGACCCTGCAAGATGCC
	AACGACAATGCTCCCCGTTTCCTGCGGCCCCATTATGTGGCCTTCCTTCCTGAGTCCC
	GGCCCTTGGAGGGGCCCCTGCTGCAGGTGGAGGCGGATGACCTGGATCAAGGCTCTGG
	AGGACAGATTTCCTACAGTCTGCCTGCATCCCAGCCGGCACGTGGATTGTTCCACGTA
	GACCCAACCACAGGCACTATCACTACCACAGCCATCCTGGACCGTOAGATCTGGGCTG
	AAACACGGTTGGTGCTGATGGCCACAGACAGAGGGAGCCCAGCCCTGGTGGGCTCAGC
	TACCTTGACGGTGATGGTCATCGACACCAATGACAATCGCCCCACCATCCCCCAACCC
	TGGGAGCTCCGAGTGTCAGAAGATGCGTTATTGGGCTCAGAGATTGCACAGGTAACAG
	GGkATGATGTGGACTCAGGACCCGTGCTGTGGTATGTGCTAAGCCCATCTGGGCCCCA
	GGATCCCTTCAGTGTTGGCCGCTATGGAGGCCGTGTCTCCCTCACGGGGCCCCTGGAC
	TTTGAGCAGTGTGACCGCTACCAGCTGCAGCTGCTGGCACATGATGGGCCTCATGAGG
	GCCGTGCCAACCTCACAGTCCTTGTGGAGGATGTCAATCACAATGCACCTGCCTTCTC
	ACAGAGCCTCTACCAGGTAATGCTGCTTGAGCACACACCCCCAGGCAGTGCCATTCTC
	TCCGTCTCTGCCACTGATCGGGACTCAGGTGCCAACGGTCACATTTCCTACCACCTGG
	CTTCCCCTGCCGATGGCTTCAGTGTTGACCCCAACAATGGGACCCTGTTCACAATAGT
	GGGAACAGTGGCCTTGGGCCATGACGGGTCAGGAGCAGTGGATGTGGTGCTGGAAGCA
	CGAGACCACGGGGCTCCAGGCCGGGCAGCACGAGCCACAGTGCACGTGCAGCTGCAGG
	ACCAGAACGACCACGCCCCGAGCTTCACATTGTCACACTACCGTGTGGCTGTGACTGA
	AGACCTGCCCCCTGGCTCCACTCTGCTCACCCTGGAGGCTACAGATGCTGATCGAAGC
	CGCAGCCATGCCGCTGTGGACTACAGCATCATCAGTGGCAACTGGGGCCGAGTCTTCC
	AGCTGGAACCCAGGCTGGCTGAGGCTGGGGAGAGTGCTGGACCAGGCCCCCGGGCACT
	GGGCTGCCTGGTGTTGCTTGAACCTCTAGACTTTGAAAGCCTGACACAGTACAATCTA
	ACAGTGGCTGCAGCTGACCGTGGGCAGCCACCCCAAAGCTCAGTCGTGCCAGTCACTG
	TCACTGTACTAGATGTCAATGACAACCCACCTGTCTTTACCCGAGCATCCTACCGTGT
	GACAGTACCTGAGGACACACCTGTTGGAGCTGAGCTGCTGCATGTAGAGGCCTCTGAC
	GCTGACCCTGGCCCTCATGGCCTCGTGCGTTTCACTGTCAGCTCAGGCGACCCATCAG
	GGCTCTTTGAGCTGGATGAGAGCTCAGGCACCTTGCGACTGGCCCATGCCCTGGACTG
	TGAGACCCAGGCTCGACATCAGCTTGTAGTACAGGCTGCTGACCCTGCTGGTGCACAC
	TTTGCTTTGGCACCAGTGACAATTGAGGTCCAGGATGTGAATGATCATGGCCCAGCCT
	TCCCACTGAACTTACTCAGCACCAGCGTGGCCGAGAATCAGCCTCCAGGCACTCTCGT
	GACCACTCTGCATGCAATCGACGGGGATGCTGGGGCTTTTGGGAGGCTCCGTTACAGC
	CTGTTGGAGGCTGGGCCAGGACCTGAGGGCCGTGAGGCATTTGCACTGAACAGCTCAA
	CAGGGGAGTTGCGTGCGCGAGTGCCCTTTGACTATGAGCACACAGAAAGCTTCCGGCT
	GCTGGTGGGTGCTGCTGATGCTGGGAATCTCTCAGCCTCTGTCACTGTGTCGGTGCTA
	GTGACTGGAGAGGATGAGTATGACCCTGTATTTCTGGCACCAGCTTTCCACTTCCAAG
	TGCCCGAAGGTGCCCGGCGTGGCCACAGCTTGGGTCACGTCCAGGCCACAGATGAGGA
	TGGGGGTGCCGATGGCCTGGTTCTGTATTCCCTTGCCACCTCTTCCCCCTATTTTGGT
	ATTAACCAGACTACAGGAGCCCTGTACCTGCGGGTGGACAGTCGGGCACCAGGCAGCG
	GAACAGCCACCTCTGGGGGTGGGGGCCGGACCCGGCGGGAAGCACCACGGGAGCTGAG
	GCTGGAGGTGATAGCACCGGGCCCTCTGCCTGGTTCCCGGAGTGCCACAGTGCCTGTG
	ACCGTGGATATCACCCACACCGCACTGGGCCTGGCACCTGACCTCAACCTGCTATTAG
	TAGGGGCCGTGGCAGCCTCCTTGGGAGTTGTGGTGGTGCTTGCACTGGCACCCCTGGT
	CCTAGGACTTGTTCGCGCCCGTAGCCGCAAGGCTGAGGCAGCCCCTGGCCCAATGTCA
	CAGGCAGCACCCCTAGCCAGTGACTCACTGCAGkAZCTGGGCCGGGAGCCACCTAGTC
	CACCACCCTCTGAGCACCTCTATCACCAGACTCTTCCCAGCTATGGTGGGCCAGGAGC
	TGGAGGACCCTACCCCCCTGGTGGCTCCTTGGACCCTTCACATTCAAGTGGCCGAGGA
	TCAGCAGAGGCTGCAGAGGATGATGAGATCCGCATGATCAATGAGTTCCCCCGTGTGG
	CCAGTGTGGCCTCCTCTCTGGCTCCCCGTGGCCCTGACTCAGGCATCCAGCAGGATGC
	AGATGGTCTGAGTGACACATCCTGCGAACCACCTGCCCCTGACACCTGGTATAAGGCC
	CGAAAGGCAGGGCTGCTGCTGCCAGGTGCAGGAGCCACTCTCTACAGAGAGGAGGGGC
	CCCCAGCCACTGCCACAGCCTTCCTGGGGGGCTGTGGCCTGAGCCCTGCACCCACTGG
	GGACTATGGCTTCCCAGCAGATGGCAAGCCATGTGTGGCAGGTGCGCTGACAGCCATT
	GTGGCCGGCGAGGAGGAGCTCCGTGGCAOCTATAACTGGGACTACCTGCTGAGCTGGT
	CCCCTCAGTTCCAACCACTGGCCAGTGTCTTCACAGAGATCGCTCGGCTCAAGGATGA
	AGCTCGGCCATGTCCCCCAGCTCCCCGTATCGACCCACCACCCCTCATCACTGCCGTG
	GCCCACCCAGGAGCCAAGTCTGTGCCCCCCAAGCCAGCAAACACAGCTGCAGCCCGGG
	CCATCTTCCCACCAGCTTCTCACCGCTCCCCCATCAGCCATGAAGGCTCCCTGTCCTC
	AGCTGCCATGTCCCCCAGCTTCTCACCCTCTCTGTCTCCTCTGGCTGCTCGCTCACCC
	GTTGTCTCACCATTTGCGGTGGCCCAGGGTCCCTCAGCCTCAGCACTCAGCGCAGAGT
	CTGGCCTGGAGCCACCTGATGACACGGAGCTGCACATCTAGCTGTCAGCCCAGGCTGG
	CCCGACCTGGGATGCGCACAGTGTCCCCAACGCAGGCCCCACTCTCAAGCCTGCCCTG
	GGCAGCCTCGGACTATGACTGGCTACGGGGAGGCCACCACCAGGCCCCAGCTCTCCAC
	CCTGAACTCCCCAGCCCCCTCAGAGTACTAGGACCACAGAAGCCCTGTTGCTCACTGA
	CCTGTGACCAGGTCCAATGTGGGGAGAAATATGAAGGAGGTAGCAGCCCTGGGTTCTC
	CTCAGTGAGGGATCCCTGCCCTGCACCAGCACCCTGAGATCGACCTGAGACTTTATTT
	ATTGGGGGTAGGGGGATGGAGGAGGTCCCTCCAAkCATGTTTGGACCCAGCTCCTTTGG
	GTTCCACTGACACCCCTGCCCCTGCCCCTGCCCAGAACCAAGTGCCATTTCTCACTCT
	GGAGCCTTAATAAACTGCAATTTGTATCC
	ORF Start: ATG at 411	ORF Stop: TAG at 10305
	SEQ ID NO: 50	3298 aa	MW at 346176.3 kD
NOV19b,	MQKELGIVPSCPGMKSPRPHLLLPLLLLLLLLLGAGVPGAWGQAGSLDLQIDEEQPAG
CG132541-02
Protein Sequence	TLIGDISAGLPAGTAAPLMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDREQRDRYR
	FTAVTPDGATVEVTVRVADINDHAPAFPQARAALQVPEHTAFGTRYPLEPARDADAGR
	LGTQGYALSGDGAGETFRLETRPGPDGTPVPELVVTGELDRENRSHYMLQLEAYDGGS
	PPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLARGSPVLQVFASDADAGVNGAV
	TYEINRRQSEGDGPFSIDAHTGLLQLERPLDFEQRRVHELVVQARDGGAHPELGSAFV
	TVHVRDANDNQPSMTVIFLSADGSPQVSEAAPRGQLVARISVSDPDDGDFAHVNTSLE
	GGEGHFALSTQDSVIYLVCVARRLDREERDAYNLRVTATDSGSPPLRAEAAFVLHVTD
	VNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGAHTHWFS
	IDPTSGIITTAASLDYELEPQPQLITVATDGGLPPLASSATVSVALQDVNDNEPQFQR
	TFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGSSGSPPFRIDAHSGDV
	CTTRTLDRDQGPSSFDFTVTAVDGGGLKSAVYVKVFLSDENDNPPQFYPREYAASISA
	QSPPGTAVLRLRAHDPDQGSHGRLSYHILAGNSPPLFTLDEQSGLLTVAWPLARRANS
	VVQLEIGAEDGGGLQAEPSARVDISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGIV
	QAHNPPGRLAPVTLSLSGGDPRGLFSLDAVSGLLQTLRPLDRELLGPVLELEVRAGSG
	VPPAFAVARVRVLLDDVNDNSPAFPAPEDTVLLPPNTAPGTPIYTLRALDPDSGVNSR
	VTFTLLAGGGGAFTVDPTTGHVRLMRPLGPSGGPAHELELEARDGGSPPRTSHFRLRV
	VVQDVGThGLAPRFNSPTYRVDLPSGTTAGTQVLQVQAQAPDGGPITYHLAAEGASSP
	FGLEPQSGWLWVRAALDREAQELYILKVMAVSGSKAELGQQTGTATVRVSILNQNEHS
	PRLSEDPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQT
	GEVTTLQTLDREQQSSYQLLVQVQDGGSPPRSTTGTVHVAVLDLNDNSPTFLQASGAA
	GGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHSGELLTA
	APLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSARLAEPPPDLAERDPAAPVP
	VVLTVTAAEGLRPCSLLGSVAAPEPAGVGALTYTLVGGADPEGTFALDAASGRLYLAR
	PLDFEAGPPWRALTVRAEGPGGAGARLLRVQVQVQDENEHAPAFARDPLALALPENPE
	PGAALYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPA
	LLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALH
	VVARDPDLGEAARVSYRLASGGDGHFRLHSSTGALSVVRPLDREQRAEHVLTVVASDH
	GSPPRSATQVLTVSVADVNIDEAPTFQQQEYSVLLRENPPGTSLLTLRATDPDVGANG
	QVTYGGVSSESFSLDPDTGVLTTLRALDREEQEEINLTVYAQDRGSPPQLTHVTVRVA
	VEDENDHAPTFGSAHLSLEVPEGQDPQTLTMLRASDPDVGANGQLQYRILDGDPSGAF
	VLDLASGEFGTMRPLDREVEPAFQLRIEARDGGQPALSATLLLTVTVLDANDHAPAFP
	VPAYSVEVPEDVPAGTLLLQLQAHDPDAGANGHVTYYLGAGTAGAFLLEPSSGELRTA
	AALDREQCPSYTFSVSAVDGAAAGPLSTTVSVTITVRDVNDHAPTFPTSPLRLRLPRP
	GPSFSTPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALG
	IPRDRVLFIVATDLGRPARSATGVIIVGLQGEAERGPRFPRASSEATIRENAPPGTPV
	SPRAVHAGGTNGPITYSILSGNEKGTFSIQPSTGAITVRSAEGLDFEVSPRLRLVLQA
	ESGGAFAFTVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEADDLDQGSGG
	IQISYSLAASQPARGLFHVDPTTGTITTTAILDREIWAETRLVLMATDRGSPALVGST
	LTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQD
	PFSVGRYGGRVSLTGPLDFEQCDRYQLQLLAHDGPHEGRANLTVLVEDvNDNAPAFSQ
	SLYQVMLLEHTPPGSAILSVSATDRDSGANGHISYHLASPADCFSVDPNNGTLFTIVG
	TVALGHDGSGAVDVVLEARDHGAPGRAARATVHVQLQDQNDHAPSFTLSHYRVAVTED
	LPPGSTLLTLEATDADGSRSHAAVDYSILSGNWGRVFQLEPRLAEAGESAGPGPRALG
	CLVLLEPLDFESLTQYNLTVAAADRGQPPQSSVVPVTVTVLDVNDNPPVFTRASYRVT
	VPEDTPVGAELLHVEASDADPCPHGLVRFTVSSGDPSGLFELDESSGTLRLAHALDCE
	TQARHQLVVQADPAGAHFALAPVTIEVQDVNIDHGPAFPLNLLSTSVAENQPPGTLVT
	TLHAIDGDAGAFGRLPYSLLEAGPGPEGREAFALNSSTGELRARVPFDYEHTESFRLL
	VGAADAGNLSASVTVSVLVTGEDEYDPVFLAPAFHFQVPEGARRGHSLGHTQATDEDG
	GADGLVLYSLATSSPYFGTNQTTGALYLRVDSRAPGSGTATSGGGGRTRREAPRELRL
	EVIARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVL
	GLVRARSRKAEAAPGPMSQAAPLASDSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAG
	GPYPRGCSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDAD
	GLSDTSCEPPAPDTWYKGRKAGLLLRGAGATLYREEGPPATATAFLGCCGLSPAPTGD
	YGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEA
	RPCPPAPRIDPPPLITAVAHPGAKSVPPKPANTAAkARAIFPPASHRSPISHEGSLSS
	AMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSAESGLEPPDDTELHI

[0430] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 19B.

TABLE 19B
Comparison of NOV19a against NOV19b.
			Identities/
	Protein	NOV19a Residues/	Similarities for the
	Sequence	Match Residues	Matched Region
	NOV19b	1 . . . 2318	2162/2318 (93%)
		1 . . . 2314	2166/2318 (93%)

[0431] Further analysis of the NOV19a protein yielded the following properties shown in Table 19C.

TABLE 19C
Protein Sequence Properties NOV19a
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 43 and 44
analysis:

[0432] 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
ABB05430	Human dachsous protein SEQ ID	1 . . . 2318	2297/2318 (99%)	0.0
	NO: 2 - Homo sapiens, 3298 aa.	1 . . . 2314	2301/2318 (99%)
	[JP2001327295-A, 27 NOV. 2001]
AAU74825	Human REPTR 8 protein - Homo	14 . . . 2318	2158/2305 (93%)	0.0
	sapiens, 3217 aa. [WO200198354-	1 . . . 2233	2170/2305 (93%)
	A2, 27 DEC. 2001]
ABB66499	Drosophila melanogaster	25 . . . 2304	875/2445 (35%)	0.0
	polypeptide SEQ ID NO 26289 -	7 . . . 2400	1269/2445 (51%)
	Drosophila melanogaster, 3503 aa.
	[WO200171042-A2, 27 SEP.
	2001]
AAU77406	Human NOV2 protein, homologue	14 . . . 611	590/598 (98%)	0.0
	of cadherin proteins - Homo	1 . . . 591	590/598 (98%)
	sapiens, 602 aa.
	[WO200206329-A2, 24 JAN.
	2002]
ABB59831	Drosophila melanogaster	46 . . . 2302	728/2419 (30%)	0.0
	polypeptide SEQ ID NO 6285 -	68 . . . 2410	1098/2419 (45%)
	Drosophila melanogaster, 5147 aa.
	[WO200171042-A2, 27 SEP.
	2001]

[0433] 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
Q96JQ0	Protocadherin 16 precursor	1 . . . 2318	2297/2318 (99%)	0.0
	(Cadherin 19) (Cadherin fibroblast	1 . . . 2314	2301/2318 (99%)
	1) - Homo sapiens (Human), 3298
	aa.
Q24292	DACHSOUS protein precursor	25 . . . 2304	871/2445 (35%)	0.0
	(ADHERIN) - Drosophila	7 . . . 2400	1267/2445 (51%)
	melanogaster (Fruit fly), 3503 aa.
IJFFTM	cadherin-related tumor suppressor	46 . . . 2302	730/2419 (30%)	0.0
	precursor - fruit fly (Drosophila	68 . . . 2410	1097/2419 (45%)
	melanogaster), 5147 aa.
P33450	Cadherin-related tumor suppressor	46 . . . 2302	728/2419 (30%)	0.0
	precursor (Fat protein) -	68 . . . 2410	1098/2419 (45%)
	Drosophila melanogaster (Fruit
	fly), 5147 aa.
Q99PF4	Cadherin 23 precursor	150 . . . 2300	668/2243 (29%)	0.0
	(Otocadherin) - Mus musculus	40 . . . 2199	1007/2243 (44%)
	(Mouse), 3354 aa.

[0434] PFam analysis indicates that the NOV19a protein contains the domains shown in the Table 19F.

TABLE 19F
Domain Analysis of NOV19a
		Identities/
		Similarities
Pfam	NOV19a Match	for the	Expect
Domain	Region	Matched Region	Value
cadherin	47 . . . 134	24/110 (22%)	6.8e−05
		61/110 (55%)
cadherin	148 . . . 246	35/111 (32%)	2.9e−09
		69/111 (62%)
cadherin	260 . . . 353	39/109 (36%)	1.3e−22
		69/109 (63%)
cadherin	371 . . . 463	33/107 (31%)	5.6e−14
		71/107 (66%)
cadherin	478 . . . 569	39/107 (36%)	1.4e−23
		72/107 (67%)
cadherin	583 . . . 676	38/110 (35%)	2.7e−16
		71/110 (65%)
cadherin	690 . . . 781	32/107 (30%)	7.1e−16
		67/107 (63%)
cadherin	795 . . . 885	33/107 (31%)	1.2e−11
		69/107 (64%)
cadherin	899 . . . 989	32/107 (30%)	7e−16
		70/107 (65%)
cadherin	1005 . . . 1096	30/107 (28%)	1.8e−14
		67/107 (63%)
cadherin	1110 . . . 1202	44/108 (41%)	7.6e−33
		78/108 (72%)
cadherin	1222 . . . 1312	36/107 (34%)	7.2e−21
		71/107 (66%)
cadherin	1337 . . . 1427	22/108 (20%)	0.0045
		62/108 (57%)
cadherin	1441 . . . 1537	34/108 (31%)	8.9e−08
		66/108 (61%)
cadherin	1550 . . . 1640	39/107 (36%)	8.5e−31
		78/107 (73%)
cadherin	1654 . . . 1742	42/107 (39%)	2.7e−27
		76/107 (71%)
cadherin	1756 . . . 1846	38/107 (36%)	1.8e−19
		71/107 (66%)
cadherin	1860 . . . 1951	39/107 (36%)	2.1e−28
		77/107 (72%)
cadherin	1974 . . . 2059	27/110 (25%)	0.017
		69/110 (63%)
cadherin	2073 . . . 2162	33/109 (30%)	3e−14
		70/109 (64%)
cadherin	2176 . . . 2268	43/108 (40%)	2.7e−20
		67/108 (62%)

Example 20

[0435] 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:51	3400 bp
NOV20a,	GAATTCTTAGTTGTTTTCTTTAGAAGAACATTTCTAGGGAATAATACAAGAAGATTTA
CC132888-02
DNA Sequence	GGAATCATTGAAGTTATAAATCTTTGGAATGAGCAAACTCAGAATGGTGCTACTTGAA
	CACTCTGGATCTGCTGACTTCAGAAGACATTTTGTCAACCTGAGTCCCTTCACCATTA
	CTGTGGTCTTACTTCTCAGTGCCTGTTTTGTCACCAGTTCTCTTGGAGGAACAGACAA
	GGAGCTGAGGCTAGTGGATGGTGAAAACAAGTGTAGCGGGAGAGTGGAAGTGAAAGTC
	CAGGAGGAGTGGGGAACGGTGTGTAATAATGGCTGGAGCATGGAAGCGGTCTCTGTGA
	TTTGTAACCAGCTGGGATGTCCAACTGCTATCAAAGCCCCTGGATGGGCTAATTCCAG
	TGCAGGTTCTGGACGCATTTGGATGGATCATGTTTCTTGTCGTGGGAATGAGTCAGCT
	CTTTGGGATTGCAAACATGATGGATGGGGAAAGCATAGTAACTGTACTCACCAACAAG
	ATGCTGGAGTGACCTGCTCAGATCGATCCAATTTGGAAATGAGGCTGACGCGTGGAGG
	GAATATGTGTTCTGGAAGAATAGAGATCAAATTCCAAGGACGGTGGGGAACAGTGTGT
	GATGATAACTTCAACATAGATCATGCATCTGTCATTTGTAGACAACTTGAATGTGGAA
	GTGCTGTCAGTTTCTCTGGTTCATCTAATTTTGGAGAAGGCTCTGGACCAATCTGGTT
	TGATGATCTTATATGCAACGGAAATGAGTCAGCTCTCTGGAACTGCAAACATCAAGGA
	TGGGGAAAGCATAACTGTGATCATGCTGAGGATGCTGGAGTGATTTGCTCAAAGGGAG
	CAGATCTGAGCCTGAGACTGGTAGATCGAGTCACTGAATGTTCAGGAAGATTAGAAGT
	GAGATTCCAAGGAGAATGGGGGACAATATGTGATGACGGCTGGGACAGTTACGATGCT
	GCTGTGGCATGCAAGCAACTGGGATGTCCkACTGCCGTCACAGCCATTGGTCGAGTTA
	ACGCCAGTAAGGGATTTGGACACATCTGGCTTGACAGCGTTTCTTGCCAGGGACATGA
	ACCTGCTGTCTGGCAATGTAAACACCATGAATGGGGAAAGCATTATTGCAATCACAAT
	GAAGATGCTGGCGTGACATGTTCTGATGGATCAGATCTGGAGCTAAGACTTAGAGGTG
	GAGGCAGCCGCTGTGCTGGGACAGTTGAGGTGGAGATTCAGAGACTGTTAGGGAACGT
	CTGTGACAGAGGCTGGGGACTGAAAGAAGCTGATGTGGTTTGCAGGCAGCTGGGATGT
	GGATCTGCACTCAAAACATCTTATCAAGTGTACTCCAAAATCCAGGCAACAAACACAT
	GGCTGTTTCTAAGTAGCTGTAACGGAAATGPAACTTCTCTTTGGGACTGCAAGAACTG
	GCAATGGGGTGGACTTACCTGTGATCACTATGAAGAAGCCAAAATTACCTGCTCAGCC
	CACAGGGAACCCAGACTGGTTGGAGGGGACATTCCCTGTTCTGGACGTGTTGAAGTGA
	AGCATGGTGACACGTGGGGCTCCATCTGTCATTCGGACTTCTCTCTGGAAGCTGCCAG
	CGTTCTATGCAGGGAATTACAGTGTGGCACAGTTGTCTCTATCCTGGGGGGAGCTCAC
	TTTGGAGAGGGAAATGGACAGATCTGGGCTGAAGAATTCCAGTGTGAGGGACATGAGT
	CCCATCTTTCACTCTGCCCAGTAGCACCCCGCCCAGAAGGAACTTGTAGCCACAGCAG
	GGATGTTGGAGTAGTCTGCTCAAGATACACAGAAATTCGCTTGGTGAATGGCAAGACC
	CCGTGTGAGGGCAGAGTGGAGCTCAAAACGCTTGGTGCCTGGGGATCCCTCTGTAACT
	CTCACTGGGACATAGAAGATGCCCATGTTCTTTGCCAGCAGCTTAAATGTGGAGTTGC
	CCTTTCTACCCCAGGAGGAGCACGTTTTGGAAAAGGAAATGGTCAGATCTGGAGGCAT
	ATGTTTCACTGCACTGGGACTGAGCAGCACATGGGAGATTGTCCTGTAACTGCTCTAG
	GTGCTTCATTATGTCCTTCAGAGCAAGTGGCCTCTGTAATCTGCTCAGGAAACCAGTC
	CCAAACACTGTCCTCGTGCAATTCATCGTCTTTGGGCCCAACAAGGCCTACCATTCCA
	GAAGAAAGTGCTGTGGCCTGCATAGAGAGTGGTCkACTTCGCCTGGTAAATGGAGGAG
	GTCGCTGTGCTGGGAGAGTAGACATCTATCATCAGCGCTCCTGGGGCACCATCTGTGA
	TGACAGCTGGGACCTGAGTGATGCCCACGTGGTTTGCAGACAGCTGGGCTGTGGAGAG
	GCCATTAATGCCACTGGTTCTGCTCATTTTGGGGAAGGAACAGGGCCCATCTGGCTGG
	ATGAGATGAAATGCAATGGAAAACAATCCCGCATTTGGCAGTGCCATTCACACGGCTG
	GGGGCAGCAAAATTGCAGGCACAAGGAGGATGCGGGAGTTATCTGCTCAGAATTCATG
	TCTCTGAGACTGACCAGTGAAGCCAGCAGAGAGGCCTGTGCAGGGCGTCTGGAAGTTT
	TTTACAATGGAGCTTGGGGCACTGTTGGCAAGAGTAGCATGTCTGAAACCACTGTGGG
	TGTGGTGTGCAGGCAGCTGGGCTGTGCAGACAAAGGGAAAATCAACCCTGCATCTTTA
	GACAAGGCCATGTCCATTCCCATGTGGGTGGACAATGTTCAGTGTCCAAAAGGACCTG
	ACACGCTGTGGCAGTGCCCATCATCTCCATGGGAGAAGAGACTGGCCAGCCCCTCGGA
	GGAGACCTGGATCACATGTGACAACAAGATAAGACTTCAGGAAGGACCCACTTCCTGT
	TCTGGACGTGTGGAGATCTGGCATGGAGGTTCCTGGGGGACAGTGTGTGATGACTCTT
	GGGACTTGGACGATGCTCAGGTGGTGTGTCAACAACTTGGCTGTGGTCCAGCTTTGAA
	AGCATTCAAAGAAGCAGAGTTTGGTCAGGGGACTGGACCGATATGGCTCAATGAAGTG
	AAGTCCAAAGGGAATGAGTCTTCCTTGTGGGATTGTCCTGCCAGACGCTGGGGCCATA
	GTGAGTGTGGGCACAAGGAAGACGCTGCAGTGAATTGCACAGATATTTCAGTGCAGAA
	AACCCCACAAAAAGCCACAACAGTTTCCTCAAGAGGAGAGAACTTAGTCCACCAAATT
	CAATACCGGGAGATGAATTCTTGCCTGAATGCAGATGATCTGGACCTAATGAATTCCT
	CAGGAGGCCATTCTGAGCCACACTGAAAAGGAAAATGGGAATTTATAACCCAGTGAGT
	TCAGCCTTTAAGATACCTTGATGAAGACCTGGAGTA
	ORF Start: ATG at 87	ORF Stop: TGA at 3330
	SEQ ID NO:52	1081 aa	MW at 117107.8 kD
NOV20a,	MSKLRMVLLEDSGSADFRRHFVNLSPFTITVVLLLSACFVTSSLGGTDKELRLVDGEN
CG132888-02
CG132888-02	KCSGRVEVKVQEEWGTVCNNGWSMEAVSVICNQLGCPTAIKAPGWANSSAGSGRIWMD
Protein Sequence
	HVSCRGNESALWDCKHDGWGKHSNCTHQQDAGVTCSDGSNLEMRLTRGGNMCSGRIEI
	KFQGRWGTVCDDNFNIDHASVICRQLECGSAVSPSGSSNFGEGSGPIWFDDLICNGNE
	SALWNCKHQGWGKHNCDHAEDAGVICSKGADLSLRLVDGVTECSGRLEVRFQGEWGTI
	CDDGWDSYDAAVACKQLGCPTAVTAIGRVNASKGFGHIWLDSVSCQGHEPAVWQCKHH
	EWGKHYCNHNEDAGVTCSDGSDLELRLRGGGSRCAGTVEVEIQRLLGKVCDRGWGLKE
	ADVVCRQLGCGSALKTSYQVYSKIQATNTWLFLSSCNGNETSLWDCKNWQWGGLTCDH
	YEEAKITCSAHREPRLVGGDIPCSGRVEVKHGDTWGSICDSDFSLEAASVLCRELQCG
	TVVSILGGAHFGEGNGQIWAEEFQCEGHESHLSLCPVAPRPEGTCSHSRDVGVVCSRY
	TEIRLVNGKTPCEGRVELKTLGAWGSLCNSHWDIEDAHVLCQQLKCGVALSTPGGARF
	GKGNGQIWRHMFHCTGTEQHMGDCPVTALGASLCPSEQVASVICSGNQSQTLSSCNSS
	SLGPTRPTIPEESAVACIESGQLRLVNCGGRCAGRVEIYHEGSWGTICDDSSDLSDAH
	VVCRQLGCGEAINATGSAHFGEGTGPIWLDEMKCNGKESRIWQCHSHGWGQQNCRHKE
	DAGVICSEFMSLRLTSEASREACAGRLEVFYNGAWGTVGKSSMSETTVGVVCRQLGCA
	DKGKINPASLDKANSIPMWVDNVQCPKGPDTLWQCPSSPWEKRLASPSEETWITCDNK
	IRLQEGPTSCSGRVEIWHGGSWGTVCDDSWDLDDAQVVCQQLGCGPALKAFKEAEFGQ
	GTGPIWLNEVKCKGNESSLWDCPARRWGHSECGHKEDAAVNCTDISVQKTPQKATTVS
	SRGENLVHQIQYREMNSCLNADDLDLMNSSGGHSEPH

[0436] Further analysis of the NOV20a protein yielded the following properties shown in Table 20B.

TABLE 20B
Protein Sequence Properties NOV20a
PSort     0.6500 probability located in plasma membrane; 0.5658 probability located in
analysis: mitochondrial inner membrane; 0.3635 probability located in microbody
          (peroxisome); 0.3000 probability located in Golgi body
SignalP   Cleavage site between residues 46 and 47
analysis:

[0437] 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 20C.

TABLE 20C
Geneseq Results for NOV20a
		NOV20a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAM41280	Human polypeptide SEQ ID NO	1 . . . 1081	1081/1121 (96%)	0.0
	6211 - Homo sapiens, 1124 aa.	4 . . . 1124	1081/1121 (96%)
	[WO200153312-A1, 26 JUL.
	2001]
AAM41279	Human polypeptide SEQ ID NO	1 . . . 1081	1081/1121 (96%)	0.0
	6210 - Homo sapiens, 1124 aa.	4 . . . 1124	1081/1121 (96%)
	[WO200153312-A1, 26 JUL.
	2001]
AAM39493	Human polypeptide SEQ ID NO	1 . . . 1081	1081/1121 (96%)	0.0
	2638 - Homo sapiens, 1121 aa.	1 . . . 1121	1081/1121 (96%)
	[WO200153312-A1, 26 JUL.
	2001]
AAB66039	Human TANGO 234 mature	46 . . . 1067	586/1057 (55%)	0.0
	protein - Homo sapiens, 1413 aa.	324 . . . 1379	737/1057 (69%)
	[WO200077239-A2, 21 DEC.
	2000]
AAB66040	Human TANGO 234 extracellular	46 . . . 1034	575/989 (58%)	0.0
	domain - Homo sapiens, 1319 aa.	324 . . . 1311	722/989 (72%)
	[WO200077239-A2, 21 DEC.
	2000]

[0438] 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 20D.

TABLE 20D
Public BLASTP Results for NOV20a
		NOV20a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q07898	M130 antigen precursor - Homo	6 . . . 1081	1076/1116 (96%)	0.0
	sapiens (Human), 1116 aa.	1 . . . 1116	1076/1116 (96%)
Q07900	M130 antigen cytoplasmic variant	6 . . . 1075	1070/1110 (96%)	0.0
	2 precursor - Homo sapiens	1 . . . 1110	1070/1110 (96%)
	(Human), 1156 aa.
Q07899	M130 antigen cytoplasmic variant	6 . . . 1079	1070/1114 (96%)	0.0
	1 precursor - Homo sapiens	1 . . . 1114	1070/1114 (96%)
	(Human), 1151 aa.
Q99MX8	Macrophage hemoglobin	5 . . . 1075	804/1108 (72%)	0.0
	scavenger receptor CD163	5 . . . 1108	911/1108 (81%)
	precursor - Mus musculus
	(Mouse), 1121 aa.
Q9NR16	Scavenger receptor cysteine-rich	46 . . . 1067	585/1057 (55%)	0.0
	type 1 protein M160 precursor -	364 . . . 1419	736/1057 (69%)
	Homo sapiens (Human), 1453 aa.

[0439] PFam analysis indicates that the NOV20a protein contains the domains shown in the Table 20E.

TABLE 20E
Domain Analysis of NOV20a
			Identities/
			Similarities
	Pfam	NOV20a Match	for the	Expect
	Domain	Region	Matched Region	Value
	SRCR	54 . . . 152	43/115 (37%)	2.2e−30
			80/115 (70%)
	SRCR	162 . . . 259	46/114 (40%)	9.6e−34
			79/114 (69%)
	SRCR	269 . . . 366	47/114 (41%)	2.4e−35
			80/114 (70%)
	SRCR	376 . . . 473	43/114 (38%)	7.4e−24
			73/114 (64%)
	SRCR	481 . . . 578	52/114 (46%)	2e−39
			87/114 (76%)
	SRCR	586 . . . 683	41/114 (36%)	2.4e−29
			78/114 (68%)
	SRCR	722 . . . 819	53/114 (46%)	9.4e−45
			89/114 (78%)
	SRCR	829 . . . 926	35/114 (31%)	3.2e−17
			69/114 (61%)
	SRCR	932 . . . 1029	51/114 (45%)	2.1e−37
			80/114 (70%)

Example 21

[0440] 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: 53	4308 bp
NOV21a,	ATGGGGAAGAGAGGCATGATGAGAGATCTCTGTGGCTTGTGTGTGCCAAGGTCACCAC
CG133159-01
DNA Sequence	TGGAAACTCTCAAGGACAATACCTGTGTCTCCTCCAAGGCCCATCCCTCGTGCCTAAC
	ACAGTTCCTGGCAGAGACCAGAAACTCCTTTGACTGTTGTGAACCTGATGAGGTCCCT
	GATCACTGTCCAGGGCCGCCAGGCTCCAAGCACAGGGCCCGGCCAGCCCCGGATCCCC
	CTCCCCTCTTCGATGACACAAGCGGTGGTTATTCCAGCCAGCCCGGGGGATACCCAGC
	CACAGGAGCAGACGTGGCCTTCAGTGTCAACCACTTGCTTGGGGACCCAATGCCCAAT
	GTGGCTATCGCCTATGGCAGCTCCATCGCATCCCATGGGAAGGACATGGTGCACAAGG
	AGCTGCACCGTTTTGTGTCTGTGAGCAAACTCAAGTATTTTTTTGCTGTGGACACAGC
	CTACGTGGCCAAGAAGCTAGGGCTGCTGGTCTTCCCCTACACACACCAGAACTGGGAA
	GTGCAGTACAGTCGTCATGCTCCTCTGCCCCCCCGGCAAGACCTCAACGCCCCTGACC
	TCTATATCCCCAGCGTGCTCTGTTATCCCTTCTTCCAAGAAGCCTTTCCTGACCCCCT
	GAGCAAGTGGTGGCTCCCTTCTGGGTTCCCACAACTGCCTGTCCACATGGCATTTTTC
	AGGCTGCCCACACATACAGCTGACTCTTCTCTGTCCTGTTGGCTGCACAGGGCCAGGC
	CCATCGTGGACACCCAGGCGATGGCCTTCATTACTTACGTGCTCCTGGCTGGGATGGC
	ACTGGGCATTCAGAAAAGGTTCTCCCCGGAGGTGCTGGGCCTGTGTGCAAGCACAGCG
	CTGGTGTGGGTGGTGATGGAGGTGCTGGCCCTGCTCCTGGGCCTCTACCTGGCCACCG
	TGCGCAGTGACCTGAGCACCTTTCACCTGCTGGCCTACAGTGGCTACAAATACGTGGG
	AATGATCCTCAGTGTGCTCACGGGGCTGCTGTTCGGCAGCGATGGCTACTACGTGGCG
	CTGGCCTGGACCTCATCGGCGCTCATGTACTTCATTGTGCGCTCTTTGCGGACAGCAG
	CCCTGGGCCCCGACAGCATGGGGGGCCCCGTCCCCCGGCAGCGTCTCCAGCTCTACCT
	GACTCTGGGAGCTGCAGCCTTCCAGCCCCTCATCATATACTGGCTGACTTTCCACCTG
	GTCCGGCAGCTGCTACCCTCACCTCCAGAGGTGGTAGAAGAGGAGGGGGATGTTGAGG
	CCCAGGGTCACCCACTCTGCTGCACACAGAAACATCAGACAGAAGACGCCGTGGATGC
	AGTATTCTGGGACCACCAGCTGGGGGATGACTACCTGTTTAAGCTGCTTTTGATTGGC
	GACTCAGGCGTGGGCAAGTCATGCCTGCTCCTGCGGTTTGCTGATGACACGTACACAG
	AGAGCTACATCAGCACCATCGGGGTGGACTTCAAGATCCGAACCATCGAGCTGGATGG
	CAAAACTATCAAACTTCAGATCTGGGACACAGCGGCCCAGGAACGGTTCCGGACCATC
	ACTTCCAGCTACTACCGGGGGGCTCATGGCATCATCGTGGTGTATGACGTCACTGACC
	AGATTCACAAGTGCCAGTTCCGGCCCGGCCATTGTTCkAGGCCCTTGAGATTTAACTG
	CGAACAAGGTGGGGGTGGCTCTGGCATTCTACTGACGGAAACAGACAATAAACTTGCA
	TACAGAACCACCGTGACTTTAGGAGTGATAAGGTCAATGCTTCCAATAGAGTTGGAGC
	AAGTGCGCCAQAAGCTGCTGCAGCTGCTCCGCACCTACTCACCCAGCGCCCAGGTCAA
	GCGGCTCCTGCAGGCCTGCAAGCTGCTCTACATGGCCCTGAGGACCCAGCAAGGGGAG
	GGCGCGGGTGCCGACGAGTTCCTGCCTCTGCTGAGCCTCGTCTTGGCCCACTGTGACC
	TTCCTGACCTGCTGCTGGAGGCCGAGTACATGTCGGAGCTGCTGGAGCCCAGCCTGCT
	TACTGGAGAGGGTCGCTACTACCTGACCAGCCTCTCTGCCAGCCTGGCCCTGCTGAGT
	GGCCTGGGTCAGGCCCACACCCTCCCACTGAGCCCCGTGCAGGAGCTACGGCGCTCCC
	TCAGCCTCTGGGAGCAGCGCCGCCTCCCTGCCACCCACTGCTTCCAGCACCTCCTCCG
	AGTAGCCTATCAGGATCCCAGCAGTGGCTGCACCTCCAAGACCCTGGCCGTGCCCCCA
	GAGGCCTCGATTGCCACCCTGAACCAGCTCTGTGCCACCAAGTTCCGAGTGACCCAGC
	CCAACACTTTTCGCCTCTTCCTGTACAAGGAGCAGGGCTACCACCGCCTGCCCCCTGG
	GGCCCTGGCCCACAGGCTGCCCACCACTGGCTACCTCGTCTACCGCCGGGCAGAGTGG
	CCTGAGACCCAGGGGGCTGTGACAGAGGAGGAGGGCAGTGGGCAGTCAGAGGCAAGAA
	GCAGAGGGGAGGAGCAAGGGTGCCAGGGAGATGGGGATCCTGGGGTCAAAGCCAGCCC
	CAGGGACATTCGGGAACAGTCTGAGACAACTGCTGAAGGGGGCCAGGAGTTTGAGTGG
	CTGCCCTTCGGCTCTGTGGCCGCTGTGCAGTGCCAGGCTGGCAGGGGAGCCTCTCTGC
	TCTGCGTGAAGCAGCCTGAGGGAGGTGTGGGCTGGTCACGGGCTGGGCCCCTGTGCCT
	GGGGACTGGCTGCAGCCCTGACAACGGGGGCTGCGAACACGAATGTGTGGAGGAGGTG
	GATGGTCACGTGTCCTGCCGCTGCACTGAGGGCTTCCGGCTGGCAGCAGACGGGCGCA
	GTTGCGAGGACCCCTGTCCCCAGGCTCCGTGCGAGCAGCAGTGTGAGCCCGGTGGGCC
	ACAAGGCTACAGCTGCCACTGTCGCCTGGGTTTCCGGCCAGCGGAGGATGATCCGCAC
	CGCTGTGTGGACACAGATGAGTGCCAGATTGCCGGTGTGTGCCAGCAGATGTGTGTCA
	ACTACGTTGGTGGCTTCGAGTGTTATTGTAGCGAGGGACATGAGCTGGAGGCTGATGG
	CATCAGCTGCAGCCCTGCAGGGGCCATGGGTGCCCAGGCTTCCCAGGACCTCGGAGAT
	GAGTTGCTGGATGACGGCGAGGATGAGGAAGATGAAGACGAGGCCTGGAACGCCTTCA
	ACGGTGGCTGGACGGAGATGCCTGGGATCCTGTGGATGGAGCCTACGCAGCCGCCTGA
	CTTTGCCCTGGCCTATAGACCGAGCTTCCCAGAGGACAGAGAGCCACAGATACCCTAC
	CCGGAGCCCACCTGGCCACCCCCGCTCAGTGCCCCCAGGGTCCCCTACCACTCCTCAG
	TGCTCTCCGTCACCCGGCCTGTGGTGGTCTCTGCCACGCATCCCACACTGCCTTCTGC
	CCACCAGCCTCCTGTGATCCCTGCCACACACCCAGCTTTGTCCCGTGACCACCAGATC
	CCCGTGATCGCAGCCAACTATCCACATCTGCCTTCTGCCTACCAACCCGGTATTCTCT
	CTGTCTCTCATTCAGCACAGCCTCCTGCCCACCAGCCCCCTATGATCTCAACCAAATA
	TCCGGAGCTCTTCCCTGCCCACCAGTCCCCCATGTTTCCAGACACCCGGGTCGCTGGC
	ACCCAGACCACCACTCATTTGCCTGGAATCCCACCTAACCATGCCCCTCTGGTCACCA
	CCCTCGGTGCCCAGCTACCCCCTCAAGCCCCAGATGCCCTTGTCCTCAGAACCCAGGC
	CACCCAGCTTCCCATTATCCCAACTGCCCAGCCCTCTCTGACCACCACCTCCAGGTCC
	CCTGTGTCTCCTGCCCATCAAATCTCTGTGCCTGCTGCCACCCAGCCCGCAGCCCTCC
	CCACCCTCCTGCCCTCTCAGAGCCCCACTAACCAGACCTCACCCATCAGCCCTACACA
	TCCCCATTCCAAAGCCCCCCAAATCCCAAGGGAAGATGGCCCCAGTCCCAAGTTGGCC
	CTGTGGCTGCCCTCACCAGCTCCCACAGCAGCCCCAACAGCCCTGGGGGAGGCTGGTC
	TTGCCGAGCACAGCCAGAGGGATGACCGGTGGCTGCTGGTGGCACTCCTGGTGCCAAC
	GTGTGTCTTTTTGGTGGTCCTGCTTGCACTGGGCATCGTGTACTGCACCCGCTGTGGC
	CCCCATGCACCCAACAAGCGCATCACTGACTGCTATCGCTGGGTCATCCATGCTGGGA
	GCAAGAGCCCAACAGAACCCATGCCCCCCAGGGGCAGCCTCACAGGGGTGCAGACCTG
	CAGAACCAGCGTGTGA
	ORF Start: ATG at 1	ORF Stop: TGA at 4306
	SEQ ID NO:54	1435 aa	MW at 156118.8 kD
NOV21a,	MGKRGMMRDLCGLCVPRSPVETLKDNTCVSSKAHPSCLTQFLAETRNSFDCCEPDEVP
CG133159-01
Protein Sequence	DHCPGPPGSKHRARAAPDPPPLFDDTSCGYSSQPGGYPATGADVAFSVNHLLGDPMAN
	VAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQNWE
	VQYSRDAPLPPRQDLNAPDLYIPSVLCYPFFQEAFPDPLSKWWLPSGFPQLPVHMAFF
	RLPTHTADSSLSCWLHRARPIVDTQAMAFITYVLLAGMALGIQKRFSPEVLGLCASTA
	LVWVVMEVLALLLGLYLATVRSDLSTFHLLAYSGYKYVGMILSVLTGLLFCSDGYYVA
	LAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGAAAFQPLIIYWLTFHL
	VRQLLPSPPEVVEEEGDVEAQGHPLCCTQKHQTEEAVDGVFWDHQLGDDYLFKLLLIG
	DSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTI
	TSSYYRGAHGIIVVYDVTDQTHKCQFRPGHCSRPLRFNCEQGGGGSGILVTETDNKLA
	YRTTVTLGVIRSMLPIELEQVRQKLLQLLRTYSPSAQVKRLLQACKLLYMALRTQEGE
	GAGADEFLPLLSLVLAHCDLPELLLEAEYMSELLEPSLLTGEGGYYLTSLSASLALLS
	GLGQAHTLPLSPVQELRRSLSLWEQRRLPATHCFQHLLRVAYQDPSSGCTSKTLAVPP
	EASIATLNQLCATKFRVTQPNTFGLFLYKEQGYHRLPPGALAHRLPTTGYLVYRRAEW
	PETQGAVTEEEGSGQSEARSRGEEQGCQGDGDAGVKASPRDIREQSETTAEOGQEFEW
	LPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLGTGCSPDNGGCEHECVEEV
	DGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPH
	RCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLGD
	ELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDFALAYRPSFPEDREPQIPY
	PEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRDHQI
	PVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAG
	TQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRS
	PVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLA
	LWLPSPAPTAAPTALGEAGLAEHSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCG
	PHAPNKRITDCYRWVIHAGSKSPTEPMPPRGSLTGVQTCRTSV

[0441] Further analysis of the NOV21a protein yielded the following properties shown in Table 21B.

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

[0442] 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	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB90732	Human Tumour Endothelial	867 . . . 1435	569/569 (100%)	0.0
	Marker polypeptide SEQ ID NO	189 . . . 757	569/569 (100%)
	196 - Homo sapiens, 757 aa.
	[WO200210217-A2, 07 FEB.
	2002]
ABB90721	Human Tumour Endothelial	867 . . . 1435	569/569 (100%)	0.0
	Marker polypeptide SEQ ID NO	189 . . . 757	569/569 (100%)
	177 - Homo sapiens, 757 aa.
	[WO200210217-A2, 07 FEB.
	2002]
AAM25557	Human protein sequence SEQ ID	941 . . . 1435	489/495 (98%)	0.0
	NO: 1072 - Homo sapiens, 494 aa.	2 . . . 494	489/495 (98%)
	[WO200153455-A2, 26 JUL.
	2001]
AAB93749	Human protein sequence SEQ ID	1003 . . . 1435	432/433 (99%)	0.0
	NO: 13411 - Homo sapiens, 433	1 . . . 433	432/433 (99%)
	aa. [EP1074617-A2, 07 FEB
	2001]
AAM93967	Human stomach cancer expressed	1003 . . . 1435	432/433 (99%)	0.0
	polypeptide SEQ ID NO 2 - Homo	1 . . . 433	432/433 (99%)
	sapiens, 433 aa. [WO200109317-
	A1, 08 FEB. 2001]

[0443] 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	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9HCU0	Tumor endothelial marker 1	867 . . . 1435	569/569 (100%)	0.0
	precursor (Endosialin protein) -	189 . . . 757	569/569 (100%)
	Homo sapiens (Human), 757 aa.
Q96KB6	CDNA FLJ14384 fis, clone	1003 . . . 1435	432/433 (99%)	0.0
	HEMBA1002150 - Homo sapiens	1 . . . 433	432/433 (99%)
	(Human), 433 aa.
Q91ZV1	Endosialin - Mus musculus	867 . . . 1435	431/586 (73%)	0.0
	(Mouse), 765 aa.	189 . . . 765	469/586 (79%)
Q91V98	Tumor endothelial marker 1	867 . . . 1435	430/586 (73%)	0.0
	precursor (Endosialin) - Mus	189 . . . 765	468/586 (79%)
	musculus (Mouse), 765 aa.
Q96CC8	Hypothetical 84.1 kDa protein -	595 . . . 866	271/272 (99%)	e−154
	Homo sapiens (Human), 783 aa.	489 . . . 760	272/272 (99%)

[0444] PFam analysis indicates that the NOV21a protein contains the domains shown in the Table 21E.

TABLE 21E
Domain Analysis of NOV21a
		Identities/
		Similarities
Pfam	NOV21a Match	for the	Expect
Domain	Region	Matched Region	Value
arf	445 . . . 619	40/202 (20%)	0.0036
		102/202 (50%)
ras	459 . . . 628	69/210 (33%)	1.6e−30
		131/210 (62%)
VPS9	595 . . . 700	51/107 (48%)	2.7e−50
		97/107 (91%)
RA	730 . . . 811	22/113 (19%)	9.8e−17
		70/113 (62%)
EGF	913 . . . 949	13/47 (28%)	4.6e−06
		31/47 (66%)
TIL	936 . . . 994	19/74 (26%)	0.17
		40/74 (54%)
EGF	994 . . . 1028	13/47 (28%)	0.00035
		26/47 (55%)

Example 22

[0445] 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: 55	1902 bp
NOV22a,	CCCCAGTGCGGCCGGGGCGCGGGTTCGAGCTGCTGCTCGGCAAGCCTGGGTGTCTAGG
CG133508-01
DNA Sequence	GCATGAGCGGAGTGTGGGGGGCCGGCGGGCCTCGGTGCCAGGAGGCGCTCGCGGTCCT
	CGCCTCGCTGTGCCGGGCCCGGCCGCCCCCTCTCGGGCTGGACGTGGAGACTTGTCGG
	AGCTTCGAGCTGCAGCCCCCAGAGCGGAGTCCCAGCGCGGCAGGCGCAGGCACCTCTG
	TCAGCCTCCTCGCAGTTGTAGTTATTGTGTGTGGCGTGGCCCTGGTGGCAGTTTTTCT
	CTTTCTCTTTTGGAAGCTGTGCTGGATGCCCTGGAGGAACAAGGAGGCCTCCAGTCCC
	TCTTCTGCTAATCCCCCCTTGGAAGCCCTCCAGAGCCCCACCTTCAGAGGCAACATGG
	CGGACAAGCTGAAGGACCCCAGCACCCTGGGCTTCCTGGAGGCCGCCGTGAAGATCAG
	CCACACGTCCCCAGATATCCCACCTGAGGTGCAGATGTCGGTCAAGGAGCACATCATG
	CGTCACACCCGGCTGCAGCGGCAAACTACACAGCCAGCGTCATCCACCAGGCACACGT
	CCTTCAAGCGCCACCTGCCAAGGCAGATGCATGTCTCCAGTGTAGACTATGGCAATGA
	GCTTCCACCAGCAGCAGAGCAGCCCACCAGCATTGGCCGCATCAAGCCTGAGCTCTAC
	AAGCAGAAGTCGGTGGATGGGGAGGATGCCAAGTCTGAGGCCACCAAGAGCTGCGGGA
	AGATCAACTTCAGCCTACGCTACGATTACGAGACCGAGACCCTGATTGTGCGTATCCT
	GAAGGCTTTTGACCTCCCTGCCAAGGACTTTTGTGGAAGCTCTGACCCTTATGTCAAG
	ATCTACCTCCTGCCTGACCGCAAATGCAAGCTGCAGACCCGGGTGCACCGCAAGACCC
	TGAACCCCACCTTTGATGAGAACTTCCACTTCCCTGTGCCCTATGAGGAGCTGGCTGA
	CCGCAAGCTGCATCTCAGTGTCTTCGACTTTGACCGCTTCTCCCGCCATGACATGATT
	GGCGAGGTCATCCTGGACAACCTCTTTCAGGCCTCTGACCTGTCTCGGGAAACCTCCA
	TCTGGAAGGATATCCAATATGCCACAAGTGAAAGCGTGGACTTGGGAGAGATCATGTT
	CTCCCTTTGCTACCTGCCCACTGCAGGCAGGCTCACCCTCACAGTGATTAAGTGTCGG
	AACCTCAAGGCGATGGACATCACAGGCTATTCAGATCCCTATGTGAAAGTGTCCTTGC
	TCTGTGATGGGCGGAGGCTGAACAAGAAGAAAACAACCATAAACAAAAACACTCTCAA
	TCCTGTCTACAATGAGGCCATCATCTTTGACATTCCCCCGGAAAACATGGATCAAGTC
	AGCCTGCTCATCTCAGTCATGGACTATGATCGAGTGGGCCACAATGAGATCATAGGAG
	TCTGTCGTGTGGGGATCACTGCTGAAGGCCTGGGCAGGGACCACTGGAACGAGATGCT
	GGCATACCCCCGGAAGCCCATCGCACACTGGCACTCCTTGGTGGAGGTAAAGAAATCC
	TTCAAAGAGGGAAACCCTCGGTTGTGATTTCATTCACGTCCATGCCGCAAGCAGAGAG
	ACTGCCACCTGGAGTTAGGATGGCAGGCCCGAGCTGCTAGCTTCGACAGTGAGAGCTC
	GTGCCCATCTCCGAAACCACCTCCAACACCATGAGATGTGCAGCCAAATAACACAAAT
	GGGACTCAGCAATGTTCTCTTTGCACTTGTTCAACCGTCTAAACAGTGTTGTGCAGTC
	GCAGTGGCGGCAGCAGCGGCAGCCGTCCGTCACTCCAGAGTCTTACCTGCTCCTGTGT
	AGGTCAAAGCTGAGACACTTGTCATGTGGTCAGATCTGTCTTAGTC
	ORF Start: ATG at 61	ORF Stop: TGA at 1591
	SEQ ID NO:56	510 aa	MW at 57324.3 kD
NOV22a	MSGVWGAGGPRCQEALAVLASLCRARPPPLGLDVETCRSFELQPPERSPSAAGAGTSV
CG133508-01
Protein Sequence	SLLAVVVIVCGVALVAVFLFLFWKLCWMPWRNKEASSPSSANPPLEALQSPSFRGNMA
	DKLKDPSTLGFLEAAVKISHTSPDIPAEVQMSVKEHIMRHTRLQRQTTEPASSTRHTS
	FKRHLPRQMHVSSVDYGNELPPAAEQPTSIGRIKPELYKQKSVDGEDAKSEATKSCCK
	INFSLRYDYETETLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTL
	NPTFDENFHFPVPYEELADRKLHLSVFDFDRFSRHDMIGEVILDNLFEASDLSRETSI
	WKDIQYATSESVDLGEIMFSLCYLPTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLL
	CDGRRLKKKKTTIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNETIGV
	CRVGITAEGLGRDHWNEMLAYPRKPIAHWHSLVEVKKSFKEGNPRL
	SEQ ID NO: 57	675 bp
NOV22b,	GGATCCCTGATTGTGCGTATCCTGAAGGCTTTTGACCTCCCTGCCAAGGACTTTTGTG
225171562 DNA
Sequence	GAAGCTCTGACCCTTATGTCAAGATCTACCTCCTGCCTGACCGCAAATGCAAGCTGCA
	GACCCGGGTGCACCGCAAGACCCTGAACCCCACCTTTGATGAGAACTTCCACTTCCCT
	GTGCCCTATGAGGAGCTGGCTGACCGCAAGCTGCATCTCAGTGTCTTCGACTTTGACC
	GCTTCTCCCGCCATGACATGATTGGCGAGGTCATCCTGGACAACCTCTTTGAGGCCTC
	TGACCTGTCTCGGGPAACCTCCATCTGGAAGGATATCCAATATGCCACAAGTGAAAGC
	GTGGACTTGGGAGAGATCATGTTCTCCCTTTGCTACCTGCCCACTGCAGGCAGGCTCA
	CCCTCACAGTGATTAAGTGTCGGAACCTCAAGGCGATGGACATCACAGGCTATTCAGA
	TCCCTATGTGAAAGTGTCCTTGCTCTGTGATGGGCGGAGGCTGAAGAAGAAGAAAACA
	ACCATAAAGAAAAACACTCTCAATCCTGTCTACAATGAGGCCATCATCTTTGACATTC
	CCCCGGAAAACATGGATCAAGTCAGCCTGCTCATCTCAGTCATGGACTATGATCGAGT
	GGGCCACAATGAGATCATAGGAGTCTGTCGTCTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 58	225 aa	MW at 25902.6 kD
NOV22b,	GSLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTLNPTFDENFHFP
225171562
Protein Sequence	VPYEELADRKLHLSVFDFDRFSRHDMTGEVILDNLFEASDLSRETSIWKDIQYATSES
	VDLGEIMFSLCYLRTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLLCDGRRLKKKKT
	TIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNEIIGVCRLE

[0446] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 22B.

TABLE 22B
Comparison of NOV22a against NOV22b.
			Identities/
	Protein	NOV22a Residues/	Similarities for
	Sequence	Match Residues	the Matched Region
	NOV22b	245 . . . 467	210/223 (94%)
		2 . . . 224	212/223 (94%)

[0447] Further analysis of the NOV22a protein yielded the following properties shown in Table 22C.

TABLE 22C
Protein Sequence Properties NOV22a
PSort     0.6760 probability located in plasma membrane; 0.1000
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 26 and 27
analysis:

[0448] 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 22D.

TABLE 22D
Geneseq Results for NOV22a
		NOV22a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU19715	Human novel extracellular matrix	82 . . . 510	428/429 (99%)	0.0
	protein, Seq ID No 365 - Homo	33 . . . 461	429/429 (99%)
	sapiens, 461 aa. [WO200155368-
	A1, 02 AUG. 2001]
AAU87165	Novel central nervous system	82 . . . 421	339/340 (99%)	0.0
	protein #75 - Homo sapiens, 412 aa.	33 . . . 372	340/340 (99%)
	[WO200155318-A2, 02 AUG. 2001]
ABB05693	Human cell	12 . . . 510	261/580 (45%)	e−127
	signaling/communication protein	10 . . . 583	340/580 (58%)
	clone amy2_2o13 - Homo sapiens,
	590 aa. [WO200198454-A2, 27
	DEC. 2001]
AAE17499	Human secretion and trafficking	12 . . . 510	261/580 (45%)	e−127
	protein-8 (SAT-8) - Homo sapiens,	10 . . . 583	340/580 (58%)
	590 aa. [WO200202610-A2, 10
	JAN. 2002]
AAU19714	Human novel extracellular matrix	230 . . . 500	179/272 (65%)	e−105
	protein, Seq ID No 364 - Homo	10 . . . 281	218/272 (79%)
	sapiens, 295 aa. [WO200155368-
	A1, 02 AUG. 2001]

[0449] 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 22E.

TABLE 22E
Public BLASTP Results tor NOV22a
		NOV22a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9R0N8	Synaptotagmin VI - Mus	1 . . . 510	493/511 (96%)	0.0
	musculus (Mouse), 511 aa.	1 . . . 511	498/511 (96%)
Q62746	Synaptotagmin VI - Rattus	1 . . . 510	490/511 (95%)	0.0
	norvegicus (Rat), 511 aa.	1 . . . 511	498/511 (96%)
Q9QUK7	Synaptotagmin VIDELTATM2 -	86 . . . 510	413/426 (96%)	0.0
	Mus musculus (Mouse), 426 aa.	1 . . . 426	416/426 (96%)
Q9R0N4	Synaptotagmin X (SytX) - Mus	12 . . . 499	331/499 (66%)	0.0
	musculus (Mouse), 523 aa.	13 . . . 501	390/499 (77%)
Q925B8	Synaptotagmin 10 - Rattus	12 . . . 499	330/499 (66%)	0.0
	norvegicus (Rat), 523 aa.	13 . . . 501	390/499 (78%)

[0450] PFam analysis indicates that the NOV22a protein contains the domains shown in the Table 22F.

TABLE 22F
Domain Analysis of NOV22a
			Identities/
			Similarities for
	Pfam	NOV22a Match	the Matched	Expect
	Domain	Region	Region	Value
	C2	246 . . . 332	45/97 (46%)	5.2e−35
			77/97 (79%)
	C2	378 . . . 466	44/97 (45%)	7.3e−37
			78/97 (80%)

Example 23

[0451] 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: 59	1751 bp
NOV23a,	CGGGAGCCTCTCCCTGAGGGGCACCGCGTTCTTCAGGAGCTGGGCCTCCAGTGCGGCG
CG133548-01
DNA Sequence	CGATGTCAGGCGCGGTGACAGCTCTGTGAGTCCGAGGCCGCGGCGTGTGGCTGGGCGG
	CTGCGGGGCCTGACCGGTCCGCTCATGGTGCCGCCACGACGCCATCGCGGGGCAGGAA
	GGCCAGGGGTGCTGAGTTCTTCACCTCCTTTTAGACTGAGATCTGCCAAGTTTTCCGG
	CATTGCTCTTGAGGATCTCAGAAGGGCTCTTAAGACAAGACTGCAAATGGTGTGTGTA
	TTTGTCATGAACCGAATGAATTCCCAGAACAGTGGTTTCACTCACCGCAGGCGAATGG
	CTCTTGGGATTGTTATTCTTCTGCTTGTTGATGTGATATGGGTTGCTTCCTCTGAACT
	TACTTCGTATGTTTTTACCCAGTACAACAAACCATTCTTCAGCACCTTTGCAAAAACA
	TCTATGTTTGTTTTGTACCTTTTGGGCTTTATTATTTGGAAGCCATGCAGACAACAGT
	GTACAAGAGGACTTCGCGGAAAGCATGCTGCTTTTTTTGCAGATGCTGAAGGTTACTT
	TCCTGCTTGCACAACAGATACAACTATGAATAGTTCTTTGAGTGAACCTCTGTATGTG
	CCTGTGAAATTCCATGATCTTCCAAGTGAAAAACCTGAGAGCACAAACATTGATACTG
	AAAAAAGTCCCAAAAAGTCTCGTGTGAGGTTCAGTAATATCATGGAGATTCGACAGCT
	TCCGTCAAGTCATGCATTGGAAGCAAAGTTGTCTCGCATGTCATATCCTGTGAAAGAA
	CAAGAATCCATACTGAAAACTGTGGGGAAACTTACTGCAACTCAAGTAGCGAAAATTA
	GCTTTTTTTTTTGCTTTGTGTGGTTTTTGGCAAATTTGTCATATCAAGAAGCACTTTC
	AGACACACAAGTTGCTATAGTTAATATTTTATCTTCAACTTCCGGTCTTTTTACCTTA
	ATCCTTGCTGCAGTATTTCCAAGTAACAGTGGAGATAGATTTACCCTTTCTAAACTAT
	TAGCTGTAATTTTAAGCATTGGAGGCGTTGTACTGGTAAACCTGGCAGGGTCTGAAAA
	ACCTGCTGGAACAGACACAGTAGGTTCCATTTGGTCTCTTGCTGGAGCCATGCTCTAT
	GCTGTCTATATTGTTATGATTAAGAGAAAAGTAGATAGAGAAGACAAGTTGGATATTC
	CAATGTTCTTTGGTTTTCTAGGTTTGTTTAATCTGCTGCTCTTATGGCCAGGTTTCTT
	TTTACTTCATTATACTGGATTTGAGQACTTCGAGTTTCCCAATAAAGTAGTATTAATC
	TGCATTATCATTAATGGCCTTATTGGAACAGTACTCTCAGAGTTCCTGTGGTTGTGGG
	GCTGCTTTCTTACCTCATCATTGATAGGCACACTTGCACTAAGCCTTACAATACCTCT
	GTCCATAATAGCTGACATGTGTATGCAAAAGGTACAGTTTTCTTGGTTATTTTTTGCA
	GGAGCTATCCCTGTATTTTTTTCATTTTTTATTGTAACTCTCCTATGCCATTATAATA
	ATTGGGATCCTGTGATGGTGGGAATCAGAAGAATATTTGCTTTTATATGCAGAAAACA
	TCGAATTCAGAGGCTTCCAGAAGACAGCGAACAGTGTGAGAGTCTCATTTCTATGCAC
	AGTGTTTCTCAGGAGGATGGAGCTAGTTAGCTGTCTGTTGTCTGTAGCCCAGGTTTGT
	ATGTGAGCTGG
	ORF Start: ATG at 141	ORF Stop: TAG at 1710
	SEQ ID NO: 60	523 aa	MW at 58872.3 kD
NOV23a,	MVPPRRHRGAGRPGVLSSSPPFRLRSAKFSGIALEDLRRALKTRLQMVCVFVMNRMNS
CG133548-01
Protein Sequence	QNSGFTQRRRMALGIVILLLVDVIWVASSELTSYVFTQYNKPFFSTFAKTSMFVLYLL
	GFIIWKPWRQQCTRCLRGKHAAFFADAEGYFAACTTDTTMNSSLSEPLYVPVKFHDLP
	SEKPESTNIDTEKSPKKSRVRFSNIMEIRQLRSSHALEAKLSRMSYPVKEQESILKTV
	GKLTATQVAKISFFFCFVWFLANLSYQEALSDTQVAIVNILSSTSGLFTLILAAVFPS
	NSGDRFTLSKLLAVILSIGGVVLVNLAGSEKPAGRDTVGSIWSLAGAMLYAVYIVMIK
	RKVDREDKLDIPMFFGFVGLFNLLLLWPGFFLLHYTGFEDFEFPNKVVLMCIIINGLI
	GTVLSEFLWLWGCFLTSSLIGTLALSLTIPLSIIADMCMQKVQFSWLFFAGAIPVFPS
	FFIVTLLCHYNNWDPVMVGIRRIFAFICRKHRIQRVPEDSEQCESLISMHSVSQEDGA
	SEQ ID NO:61	1607 bp
NOV23b,	CGGGAGCCTCTCCCTGAGGCiAGCACCGCGTTCTTCAGGAGCTGGGCCTCCAGTGCGGCG
CG133548-02
DNA Sequence	CGATGTCAGGCGCGGTGACAGCTCTGTGAGTCCGAGGCCGCGGCGTGTGGCTGGGCGG
	CTGCGGGGCCTGACCGGTCCGCTCATGGTGCCGCCACGACGCCATCGCGGGGCAGGAA
	GGCCAGGGATGCTGAGTTCTTCACCTCCTTTTAGACTGAGATCTGCCAAGTTTTCCGG
	CATTGCTCTTGAGGATCTCAGAAGGGCTCTTAAGACAAGACTGCAAATGGTGTGTGTA
	TTTGTCATGACCGATGAATTCCCAGAACAGTGGTTTCACTCAGCGCAGGCGAAAATGG
	CTCTTGGGATTGTTATTCTTCTGCTTGTTGATGTGATATGGGTTGCTTCCTCTGAACT
	TACTTCGTTTGCAGATGCTGAAGGTTACTTTGCTGCTTGCACAACAGATACAACTATC
	AATAGTTCTTTGAGTGAACCTCTGTATGTGCCTGTGAAATTCCATGATCTTCCAAGTG
	AAAAACCTGAGAGCACAAACATTGATACTGAAAAAAGTCCCAAAAAGTCTCGTGTGAG
	GTTCAGTAATATCATGGAGATTCGACAGCTTCCGTCAACTCATGCATTGGAAGCAAAC
	TTGTCTCGCATGTCATATCCTGTGPAAGAACAAGAATCCATACTGAAAACTGTGGGGA
	AACTTACTGCAACTCAAGTAGCGAAAATTAGCTTTTTTTTTTGCTTTGTGTGGTTTTT
	GGCAAATTTGTCATATCAAGAAGCACTTTCAGACACACAAGTTGCTATAGTTAATATT
	TTATCTTCAACTTCCGGTCTTTTTACCTTAATCCTTGCTGCAGTATTTCCAAGTAACA
	GTGGAGATAGATTTACCCTTTCTAAACTATTAGCTGTAATTTTAAGCATTGGAGGCGT
	TGTACTGGTAAACCTGGCAGGGTCTGAAAAACCTGCTGGAAGAGACACAGTAGGTTCC
	ATTTGGTCTCTTGCTGGAGCCATGCTCTATGCTGTCTATATTGTTATGATTAAGAGAA
	AAGTAGATAGAGAAGACAAGTTGGATATTCCAATGTTCTTTGGTTTTGTAGGTTTGTT
	TAATCTGCTGCTCTTATGGCCAGGTTTCTTTTTACTTCATTATACTGGATTTGAGGAC
	TTCGAGTTTCCCAATAAAGTAGTATTAATGTGCATTATCATTAATGGCCTTATTGGAA
	CAGTACTCTCAGAGTTCCTGTGGTTGTCGGCCTGCTTTCTTACCTCATCATTGATAGG
	CACACTTGCACTAAGCCTTACAATACCTCTGTCCATAATAGCTGACATGTGTATGCAA
	AAGGTACAGTTTTCTTCGTTATTTTTTGCAGGAGCTATCCCTGTATTTTTTTCATTTT
	TTATTGTAACTCTCCTATGCCATTATAATAATTGGGATCCTGTGATGGTGGGAATCAG
	AAGAATATTTGCTTTTATATGCAGAAAACATCGAATTCAGAGGGTTCCAGAAGACAGC
	GAACAGTGTGAGAGTCTCATTTCTATGCACAGTGTTTCTCAGGAGGATGGAGCTAGTT
	AGCTGTCTGTTGTCTGTAGCCCAGGTTTGTATGTGAGCTGG
	ORF Start: ATG at 141	ORF Stop: TAG at 1566
	SEQ ID NO: 62	475 aa	MW at 53094.6 kD
NOV23b,	MVPPRRHRGAGRPGVLSSSPPFRLRSAKFSGIALEDLRRALKTRLQMVCVFVMNRMNS
CG133548-02
Protein Sequence	QNSGFTQRRRMALGIVILLLVDVIWVASSELTSFADAEGYFAACTTDTTMNSSLSEPL
	YVPVKFHDLPSEKPESTNIDTEKSPKKSRVRFSNIMEIRQLPSSHALEAKLSRMSYPV
	KEQESILKTVGKLTATQVAKISFFFCFVWFLANLSYQEALSDTQVAIVNILSSTSGLF
	TLILAAVPPSNSGDRFTLSKLLAVILSIGGVVLVNLAGSEKPAGRDTVGSIWSLAGAM
	LYAVYIVMIKRKVDREDKLDIPMFFGFVGLFNLLLLWPGFFLLHYTGFEDFEFPNKVV
	LMCIIINGLIGTVLSEFLWLWGCFLTSSLIGTLALSLTIPLSIIADMCMQKVQFSWLF
	FAGAIPVFFSFFIVTLLCHYNNWDPVMVGIRRIFAPICRKHRIQRVPEDSEQCESLIS
	MHSVSQEDGAS

[0452] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 23B.

TABLE 23B
Comparison of NOV23a against NOV23b.
			Identities/
			Similarities for
	Protein	NOV23a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV23b	15 . . . 523	431/509 (84%)
		15 . . . 475	431/509 (84%)

[0453] Further analysis of the NOV23a protein yielded the following properties shown in Table 23C.

TABLE 23C
Protein Sequence Properties NOV23a
PSort     0.6000 probability located in plasma membrane; 0.4000
analysis: probability located in Golgi body; 0.3000 probability
          located in endoplasmic reticulum (membrane); 0.3000
          probability located in microbody (peroxisome)
SignalP   No Known Signal Sequence Indicated
analysis:

[0454] 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 23D.

TABLE 23D
Geneseq Results for NOV23a
		NOV23a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU12294	Human PRO6097 polypeptide	1 . . . 523	522/523 (99%)	0.0
	sequence - Homo sapiens, 523 aa.	1 . . . 523	523/523 (99%)
	[WO200140466-A2, 07 JUN. 2001]
AAE21623	Human gene 14 encoded secreted	1 . . . 523	520/523 (99%)	0.0
	protein, SEQ ID NO: 95 - Homo	1 . . . 523	521/523 (99%)
	sapiens, 523 aa. [WO200222654-
	A1, 21 MAR. 2002]
AAE21622	Human gene 14 encoded secreted	1 . . . 523	520/523 (99%)	0.0
	protein, SEQ ID NO: 94 - Homo	19 . . . 541	521/523 (99%)
	sapiens, 541 aa. [WO200222654-
	A1, 21 MAR. 2002]
AAE21611	Human gene 14 encoded secreted	56 . . . 523	465/468 (99%)	0.0
	protein HOSDW58, SEQ ID NO: 83 -	1 . . . 468	466/468 (99%)
	Homo sapiens, 468 aa.
	[WO200222654-A1, 21 MAR. 2002]
AAB58385	Lung cancer associated polypeptide	187 . . . 523	336/337 (99%)	0.0
	sequence SEQ ID 723 - Homo	1 . . . 337	337/337 (99%)
	sapiens, 337 aa. [WO200055180-
	A2, 21 SEP. 2000]

[0455] 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 23E.

TABLE 23E
Public BLASTP Results for NOV23a
		NOV23a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q8WV83	Similar to RIKEN cDNA	1 . . . 523	522/523 (99%)	0.0
	1300003P13 gene - Homo sapiens	1 . . . 523	523/523 (99%)
	(Human), 523 aa.
Q8R314	RIKEN cDNA 1300003P13 gene -	1 . . . 523	492/524 (93%)	0.0
	Mus musculus (Mouse), 524 aa.	1 . . . 524	508/524 (96%)
Q9DBK9	1300003P13Rik protein - Mus	1 . . . 523	491/524 (93%)	0.0
	musculus (Mouse), 524 aa.	1 . . . 524	508/524 (96%)
Q9H7D8	CDNA: FLJ21013 fis, clone	156 . . . 523	366/368 (99%)	0.0
	CAE05223 - Homo sapiens	1 . . . 368	367/368 (99%)
	(Human), 368 aa.
Q9H6P8	CDNA: FLJ22004 fis, clone	10 . . . 247	234/238 (98%)	e−130
	HEP06871 - Homo sapiens	4 . . . 241	236/238 (98%)
	(Human), 244 aa.

[0456] PFam analysis indicates that the NOV23a protein contains the domains shown in the Table 23F.

TABLE 23F
Domain Analysis of NOV23a
			Identities/
			Similarities for
	Pfam	NOV23a Match	the Matched	Expect
	Domain	Region	Region	Value
	DUF6	338 . . . 470	19/136 (14%)	0.082
			92/136 (68%)

Example 24

[0457] 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:63	5964 bp
NOV24a,	GCTGACCACAACATGGCTGCGGCGCCTGGGCTGCTCGTCTGGCTGCTCGTGCTCCGGC
CG133569-01
DNA Sequence	TGCCCTGGCGGGTGCCGGGCCAGCTGGACCCCAGCACTGGCCGGCGGTTCTCGGAGCA
	CAAACTCTGCGCGGACGACGAATGCAGCGTGTTAATGTACCGCGGTGAGGCTCTTGAA
	GATTTCACAGGCCCGGATTGTCGTTTTGTGAATTTTAAAAAAGGTGATCCTGTATATG
	TTTTGGATATTTTCCAAAAGATTTAATCCAGGTAGTTCATGAATATACCAAAGAAGAG
	CTACAAGTTCCAACAGATGAGACGGATTTTGTTTGTTTTGATGGAGGAAGAGATGATT
	TTCATAATTATAATGTAGAAGAACTTTTAGGGTTTTTGGAACTGTACAATTCTGCAGC
	TACAGATTCTGAGAAAGCTGTAGAAAAAACTTTACAGGATATGGAAAAAAACCCTGAA
	TTATCTAAGGAAAGGGAACCTGAACCTGAACCAGTAGAAGCCAACTCAGAGGAAAGTG
	ATAGTGTATTCTCAGAAAACACTGAGGATCTTCAGQAACAGTTTACAACTCAGAAGCA
	CCACTCCCATGCAAACAGCCAAGCAAATCATGCTCAGGGAGAGCAGGCTTCATTTGAA
	TCTTTTGAAGAAATGCTGCAAGATAACTAAAGTGCCAGAAAGTGAAAACAACAAAAAA
	CCAGCAATAGTTCTCAGGTCTCAAATGAACAGGATAAGATTGATGCCTATAAAATTTT
	GAAAAAAGAAATGACTCTAGACTTGAAAACCAAATTTGGCTCAACAGCTGATGCACTT
	GTATCTGATGATGAGACAACCAGACTCGTTACTTCATTAGAAGATCATTTTGATGAGG
	AATTGGATACTGAGTATTATGCAGTTGGAAAGGAAGATGAGGAGAACCAAGAAGACTT
	TGATGAGTTGCCATTACTTACCTTTACAGATGGGGAAGATATAAAAACTCCAGCAAAG
	TCTGGCGTTGAGAAATATCCAACAGATAAAAGAGCAGAAATTCATGAAGAGGACAAGG
	TTCAGCTAACTGTGCCCCCTGGCATCAAAAATGATGATAAAAATATACTAACAACCTG
	GGGGGACACTATCTTCTCTATTGTCACAGGAGGTGAAGAAACAAGAGATACGATGGAT
	TTAGAGAGCTCTAGTTCAGAGGAAGAAAAAGAAGATGATGATGATGCATTAGTCCCAG
	ATAGCAAACAGGGGAAACCACAGTCAGCAACAGATTATAGTGACCCTGACAATGTAGA
	TGATGGTCTTTTTATTGTAGACATTCCTAACAAAATAATGACAAGAAGTAAACGCAAA
	GAACATCACATTAAAGGAAAAGGGAGGGGAGTTCAGGAATCCAAGAGGGGCCTGGTAC
	AAGATAAGACAGAATTAGAGGATGAAAATCAAGAAGGCATGACTGTGCACAGTTCTGT
	TCACAGCAATAACCTCAACTCTATGCCAGCTGCTGAAAAGGGTAAACACACATTAAAA
	TCAGCTTATGATGATACAGAAAATGACCTAAAAGGAGCAGCTATTCATATCTCAAAAG
	GAATGCTCCACGAAGAAAAGCCTGGAGAGCAGATTTTGGAAGGTGGCTCAGAGAGTGA
	ATCTGCACAGAAAGCTGCAGGGAATCAAATGAATGACAGAAAGATTCAACAGGAATCC
	CTGGGTAGTGCACCACTCATGGGAGATGACCACCCTAACGCATCCAGAGACAGTGTGG
	AGGGAGACGCTTTGGTAAATGGGGCCAAACTGCACACGCTTTCAGTGGAGCATCAACG
	TGAGGAATTGAAAGAGGAATTAGTTCTTAAAACTCAAAACCAACCTAGATTCTCCTCT
	CCAGATGAGATTGATTTGCCCAGAGAACTGGAAGACGAGGTTCCCATTCTGGGAAGAA
	ATCTTCCCTGGCAACAAGAAAGAGATGTGGCTGCCACAGCCAGTAAGCAAATGAGTGA
	GAAGATAAGGCTCTCTGAGCGAGAAGCCAAAGAGGACTCCTTGGATGAAGAGTTTTTT
	CATCACAAGGCAATGCAGGGCACAGAGGTAGGACAGACAGACCAAACTGACAGCACAG
	GAGGACCAGCTTTCCTTTCTAAGTAGAIXGAGGATGATTATCCCTCTGAAGAACTACT
	AGAGGATGAAAACGCTATAAATGCAAAACGGTCTAAAGAAAAAAACCCTGGGAATCAG
	GGCAGGCAGTTTGATGTTAATCTCCAAGTCCCTGACAGAGCAGTTTTAGGGACCATTC
	ATCCAGATCCAGAAATTGAAGAAAGCAAGCAAGkAACTAGTATGATTTTGGATAGCGA
	AAAAACAAGTGAGACTGCTGCCAAAGGGGTCAACACAGGAGGCAGGGAACCAAATACA
	ATGGTGGAAAAAGAACGCCCTCTGGCAGATAAGAAAGCACAGAGACCATTTGAACGAA
	GTGACTTTTCTGACAGCATAAAAATTCAGACTCCAGAATTAGGTGAAGTGTTTCAGAA
	TAAAGATTCTGATTATCTGAAGAACGACAACCCTGAGGAACATCTGAAGACCTCAGGG
	CTTGCAGGGGAGCCTGAGGGAGAACTCTCAAAAGAGGACCATGAGAACACAGAGAAGT
	ACATGGGCACAGAAAGCCAGGGGTCTGCTGCTGCAGAACCTGAAGATGACTCGTTCCA
	CTGGACTCCACATACAAGTGTAGAGCCAGGGCATAGTGACAAGAGGGAGGACTTACTT
	ATCATAAGCAGCTTCTTTAAAGAACAACAGTCTTTGCAGCGGTTCCAGAAGTACTTTA
	ATGTCCATGAGCTGGAAGCCTTGCTACAAGAAATGTCATCAAAACTGAAGTCAGCGCA
	GCAGGAGAGCCTGCCCTATAATATGGAAAAAGTCCTAGATAAGGTCTTCCGTGCTTCT
	GAGTCACAAATTCTGAGCATAGCAGAAAAAATGCTTGATACTCGTGTGGCTGAAAATA
	GAGATCTGGGAATGAACGAAAATAACATATTTGAAGAGGCTGCAGTGCTTGATGACAT
	TCAAGACCTCATCTATTTTGTCAGGTACAAGCACTCCACAGCAGAGGAGACAGCCACA
	CTCGTCATCGCACCACCTCTAGAGGAAGGCTTGGGTGGAGCAATGGAAGAGATGCAAC
	CACTGCATGAAGATAATTTCTCACGAGAGAAGACAGCAGAACTTAATGTGCAGGTTCC
	TGAAGAACCCACCCACTTGGACCAACGTGTGATTGGGGACACTCATGCCTCAGAAGTG
	TCACAGAAGCCAAATACTGAGAAAGACCTGGACCCAGGGCCAGTTACAACAGAAGACA
	CTCCTATGGATGCTATTGATGCAAACAAGCAACCAGAGACAGCCGCCGAAGAGCCGGC
	AAGTGTCACACCTTTGGAAAACGCAATCCTTCTAATATATTCATTCATGTTTTATTTA
	ACTAAGTCGCTAGTTGCTACATTGCCTGATGATGTTCAGCCTGGGCCTGATTTTTATG
	GACTGCCATGGAAACCTGTATTTATCACTGCCTTCTTGGGAATTGCTTCGTTTGCCAT
	TTTCTTATGGAGAACTGTCCTTGTTGTGAAGGATAGAGTATATCAAGTCACGGAACAG
	CAAATTTCTGAGAAGTTGAAGACTATCATGAAAGAAAATACAGAACTTGTACAAAAAT
	TGTCAATTATGAACAGAAGATCAAGGAATCAJAAAGAACATGTTCAGGAAACCAGGAA
	ACAAAATATGATTCTCTCTGATGAAGCAATTAAATATAAGGATAAAATCAAGACACTT
	GAAAAAAATCAGGAAATTCTGGATGACACAGCTAAAAATCTTCGTGTTATGCTAGAAT
	CTGAGAGAGAACAGAATGTCAAGAATCAGGACTTGATATCAGAAAACAAGAAATCTAT
	AGAGAAGTTAAAGGATGTTATTTCAATGAATGCCTCAGAGTTTTCAGAGGTTCAGATT
	GCACTTAATGAAGCTAAGCTTAGTGPAGAGAAGGTGAAGTCTGAATGCCATCGGGTTC
	AAGAAGAAAATGCTAGGCTTAAGAAGAAAAAAGAGCAGTTGCAGCAGGAAATCGAAGA
	CTGGAGTAAATTACATGCTGAGCTCAGTGAGCAAATCAAATCATTTGAGAAGTCTCAG
	AAAGATTTGGAAGTAGCTCTTACTCACAAGGATGATAATATTAATGCTTTGACTAACT
	GAATTACACAGTTGAATCTGTTAGAGTGTGAATCTGAATCTGAGGGTCAAAATAAAGG
	TGGAAATGATTCAGATGAATTAGCAAATGGAGAACTGGGAGGTGACCGGAATGAGAAG
	ATGAAAAATCAAATTAAGCAGATGATGGATGTCTCTCGGACACAGACTGCAATATCGG
	TAGTTGAAGAGGATCTAAAGCTTTTACAGCTTAAGCTAAGAGCCTCCGTGTCCACTAA
	ATGTAACCTGGAAGACCAGGTAAAGAAATTGGAAGATGACCGCPACTCACTACAAGCT
	GCCAAAGCTGGACTGGAAGATGAATGCAAAACCTTGAGGCAGAAAGTGGAGATTCTGA
	ATGAGCTCTATCAGCAGAAGGAGATGGCTTTGCAAAAGAAGCTGAGTCAAGAAGAGTA
	TGAACGGCAAGAAAGAGAGCACAGGCTGTCAGCTGCAGATGAAAAGGCAGTTTCGGCT
	GCACAGGAAGTAAAAACTTACAAGCGGAGAATTGAAGAAATGGAGGATCAATTACAGA
	AGACAGAGCGGTCATTTAAAAACCAGATCGCTACCCATGAGAAGAAAGCTCATGAAAA
	CTGGCTCAAAGCTCGTGCTGCAGAAAGAGCTATAGCTGAAGAGAAAAGGGAAGCTGCC
	AATTTGAGACACAAATTATTAGAATTAACACAAAACATGGCAATGCTGCAAGAAGAAC
	CTGTGATTGTAAAACCAATGCCAGGAAAACCAAATACACAAAACCCTCCACCCACAGC
	TCCTCTGAGCCAGAATGGCTCTTTTCGCCCATCCCCTGTGAGTGGTGGAGAATGCTCC
	CCTCCATTGACAOTGOAOCCACCCGTGAGACCTCTCTCTGCTACTCTCAATCGPAGAG
	ATATGCCTAGAAGTGAATTTGGATCAGTCGACCOGCCTCTACCTCATCCTCGATGGTC
	AGCTGAGGCATCTGGGAAACCCTCTCCTTCTGATCCAGGATCTGGTACAGCTACCATG
	ATGAACAGCAGCTCAAGAGGCTCTTCCCCTACCAGGGTACTCGATGAAGGCAAGGTTA
	ATATGGCTCCAAAAOGOCCCCCTCCTTTCCCAGGAGTCCCTCTCATGAGCACCCCCAT
	GGGAGGCCCTGTACCACCACCCATTCOATATGGACCACCACCTCAGCTCTGCGGACCT
	TTTGGGCCTCGGCCACTTCCTCCACCCTTTGGCCCTGGTATGCGTCCACCACTAGGCT
	TAAGAGAATTTGCACCAGGCGTTCCACCAGGAAGACGGGACCTGCCTCTCCACCCTCG
	GGGATTTTTACCTGGACACGCACCATTTAGACCTTTAGGTTCACTTGGCCCAAGAGAG
	TACTTTATTCCTGGTACCCGATTACCACCCCCAACCCATGGTCCCCAGGAATACCCAC
	CACCACCTOCTGTAAGAGACTTACTGCCGTCAGGCTCTAGAGATGAGCCTCCACCTGC
	CTCTCAGAGCACTAGCCAGGACTGTTCACAOGCTTTAAAACAGAGCCCATAAAACTAT
	GACCTCTGAGGTTTCATTGGAAAGAAAGTGTACTGTGCATTATCCATTACAGTAAAGG
	ATTTCATTGGCTTCAAAATCCAAAAGTTTATTTTAAAAGGTTTGTTGTTAGAACTAAG
	CTGCCTTGGCAGTGTGCATTTTTGAGCCAAACAATTCAAAAATGTCATTTCTTCCCTA
	AATAAAAATCACCTTTTAAGCTAAAAAGAAAAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 13	ORF Stop: TAA at 5734
	SEQ ID NO: 64	1907 aa	MW at 213668.2 kD
NOV24a,	MAAAPGLLVWLLVLRLRWRVPGQLDPSTGRRFSEHKLCADDECSVLMYRGEALEDFTG
CG133569-01
Protein Sequence	PDCRFVNFKKGDPVYVYYKLARGWPEVWAGSVGRTFGYFPKDLIQVVHEYTKEELQVP
	TDETDFVCFDGGRDDFHNYNMEELLGFLELYNSAATDSEKAVEKTLQDMEKNPELSKE
	REPEPEPVEANSEESDSVFSENTEDLQEQFTTQKHHSHANSQANHAQGEQASFESFEE
	MLQDKLKVPESENNKTSNSSQVSNEQDKIDAYKLLKKEMTLDLKTKFGSTADALVSDD
	ETTRLVTSLEDDFDEELDTEYYAVGKEDEENQEDFDELPLLTFTDGEDMKTPAKSGVE
	KYPTDKEQNSNEEDKVQLTVPPGIKNDDKNILTTWGDTIFSIVTGGEETRDTMDLESS
	SSEEEKEDDDDALVPDSKQGKPQSATDYSDPDNVDDGLFIVDIPKTNNDKEVNAEHHI
	KGKGRGVQESKRGLVQDKTELEDENQEGMTVHSSVHSNNLNSMPAAEKGKDTLKSAYD
	DTENDLKGAAIHISKGMLHEEKPGEQILECGSESESAQKAAGNQMNDRKIQQESLGSA
	PLMGDDHPNASRDSVEGDALVNGAKLHTLSVEHQREELKEELVLKTQNQPRFSSPDEI
	DLRRELEDEVPILGRNLPWQQERDVAATASKQMSEKIRLSEGEAKEDSLDEEFFHHKA
	MQGTEVGQTDQTDSTGGPAFLSKVEEDDYPSEELLEDENAINAKRSKEKNPGNQGRQF
	DVNLQVPDRAVLGTIHPDPEIEESKQETSMILDSEKTSETAAKGVNTGGREPNTMVEK
	ERPLADKKAQRPFERSDFSDSTKIQTPELGEVFQNKDSDYLKNDNPEEHLKTSGLAGE
	PEGELSKEDHENTEKYMGTESQGSAAAEPEDDSFHWTPHTSVEPGHSDKREDLLIISS
	FFKEQQSLQRFQKYFNVHELEALLQEMSSKLKSAQQESLPYNMEKVLDKVFRASESQI
	LSIAEKMLDTRVAENRDLGMNENNIFEEAAVLDDIQDLIYFVRYKHSTAEETATLVMA
	PPLEEGLCGAMEEMQPLHEDNFSREKTAELNVQVPEEPTHLDQRVIGDTHASEVSQKP
	NTEKDLDPGPVTTEDTPMDAIDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKSL
	VATLPDDVQPGPDFYGLPWKPVFTTAFLGIASFAIFLWRTVLVVKDRVYQVTEQQISE
	KLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQ
	EILDDTAKNLRVMLESEREQNVKNQDLTSENKKSIEKLKDVISMNASEFSEVQIALNE
	AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE
	VALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ
	IKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAG
	LEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEV
	KTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRH
	KLLELTQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLT
	VEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSDPGSGTATMMNSS
	SRGSSPTRVLDEGKVNMAPKGPPPFPGVPLMSTPMGGPVPPRIRYGPPPQLCGPFGPR
	PLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIP
	GTRLPPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQDCSQALKQSP
	SEQ ID NO: 65	4985 bp
NOV24b,	GCTGACCACAACATGGCTGCGGCGCCTGGGCTCCTCGTCTGGCTGCTCGTGCTCCGGC
CG133569-02
DNA Sequence	TGCCCTGGCGGGTGCCGGGCCAGCTGGACCCCACCACTGGCCGGCGGTTCTCGGAGCA
	CAAACTCTGCGCGGACGACGAATGCAGCGTGTTAATGTACCCCCGTGAGGCTCTTGAA
	GATTTCACAGGCCCGGATTGTCGTTTTGTGAATTTTAAAAAAGGTGATCCTGTATATG
	TTTACTATAAACTGGCAAGAGGATGGCCTGAAGTTTGGGCTGGAAGTGTAGGACGCAC
	TTTTGGATATTTTCCAAAAGATTTAATCCAGGTAGTTCATGAATATACCAAAGAAGAG
	CTACAAGTTCCAACAGATGAGACGGATTTTGTTTGTTTTGATGGAGGAAGAGATGATT
	TTCATAATTATAATGTAGAAGAACTTTTAGGGTTTTTGGAACTGTACAATTCTGCAGC
	TACAGATTCTGAGAAAGCTGTAGAAAAAACTTTACAGGATATGGAAAAAAACCCTGAA
	TTATCTAAGGAAAGGGAACCTGAACCTGAACCAGTAGAAGCCAACTCAGAGGAAAGTG
	ATAGTGTATTCTCAGAAAACACTGAGGATCTTCACGAACAGTTTACAACTCAGAAGCA
	CCACTCCCATGCAAACAGCCAAGCAAATCATGCTCAGGGAGAGCAGGCTTCATTTGAA
	TCTTTTGAAGAAATGCTGCAAGATAAAACTAAAAAGTGCCAGAAAGTGAACAACAAAA
	CCAGCAATAGTTCTCAGGTCTCAAATGAACAGGATAAGATTGATGCCTATAAACTTTT
	GAAAAAAGAAATGACTCTAGACTTGAAAACCAAATTTGGCTCAACAGCTGATGCACTT
	GTATCTGATGATGAGACAACCAGACTCGTTACTTCATTAGAAGATGATTTTGATGAGG
	AATTGGATACTGAGTATTATGCAGTTGGAGGAAGATGAGGAGAAACCAAGAAAGACTT
	TGATGAGTTGCCATTACTTACCTTTACAGATGGGGAAGATATGAAAACTCCAGCAAAG
	TCTGGCGTTGAGAAATATCCAACAGATAAGAGCAGAAATTCAAATGAAGAGGACAAGG
	TTCAGCTAACTGTGCCCCCTGGCATCAAAAATGATGATAAAAATATACTAACAACCTG
	GGGGGACACTATCTTCTCTATTGTCACAGGAGGTGAAGAAACAAGAGATACGATGGAT
	TTAGAGAGCTCTAGTTCAGAGGAAGAAAAAGAAGATGATGATGATGCATTAGTCCCAG
	ATAGCAAACAGGGGAAACCACAGTCAGCAACAGATTATAGTGACCCTGACAATGTAGA
	TGATGGTCTTTTTATTGTAGACATTCCTAAAACAAATAATGACAAAGAAGTAAACGCA
	GAACATCACATTAAAGGAAAAGAAACGGGAGTTCACGAATCCAAGAGGGGCCTGGTAC
	AAGATAAGACAGAATTAGAGGATGAAAATCAAGAAGGCATGACTGTGCACAGTTCTGT
	TCACAGCAATAACCTCAACTCTATGCCAGCTGCTGAAAAGGGTAAAGACACATTAAAA
	TCAGCTTATGATGATACAGAAAATGACCTAAAAGGAGCAGCTATTCATATCTCAAAAG
	GAATGCTCCACGAAGAAAAGCCTGGAGAGCAGATTTTGGAAGGTGGCTCAGAGAGTGA
	ATCTGCACAGAAAGCTGCAGGGAATCAAATGAATGACAGAAAGATTCAACAGGAATCC
	CTCGGTAGTGCACCACTCATGGGACATGACCACCCTAACGCATCCAGAGACAGTGTGG
	AGGGAGACGCTTTGGTAAATCGCGCCAAACTGCACACGCTTTCAGTGGAGCATCAACG
	TGAGGAATTGPAAGAGGAATTAGTTCTTAAAACTCAAAACCAACCTAGATTCTCCTCT
	CCAGATGAGATTGATTTGCCCAGAGAACTGGAAGACGAGGTTCCCATTCTGGGAAGAA
	ATCTTCCCTGGCAACAAGAAAGAGATGTGGCTGCCACAGCCAGTAAGCAAATGAGTGA
	GAAGATAAGGCTCTCTGAGGGAGAAGCCAAAGAGGACTCCTTGGATGAAGAGTTTTTT
	CATCACAAGGCAATGCAGGGCACAGAGGTAGGACAGACACACCAAACTGACAGCACAG
	GAGGACCAGCTTTCCTTTCTAAAGTAGAAGAGGATGATTATCCCTCTGAAGAACTACT
	AGAGGATGAAAACGCTATAAATGCAAAACGGTCTAAGAAAAAAAACCCTGGGAATCAG
	GGCAGGCAGTTTGATGTTAATCTGCAAGTCCCTGACAGAGCAGTTTTAGGGACCATTC
	ATCCAGATCCAGAAATTGAAGAAAGCAAGCAAGAAACTAGTATGATTTTGGATAGCGA
	AAAAACAAGTGAGACTGCTGCCAAAGGGGTCAACACAGGAGGCAGGGAACCAAATACA
	ATGGTGGAAAAAGAACGCCCTCTGGCAGATAAGAAAGCACAGAGACCATTTGAACGAA
	GTGACTTTTCTGACAGCATAAAAATTCAGACTCCAGAATTAGGTGAAGTGTTTCAGAA
	TAAAGATTCTGATTATCTGAAGAACGACAACCCTGAGGAACATCTGAAGACCTCAGGG
	CTTGCAGGGGAGCCTGAGGGAGAACTCTCAAAAGAGGACCATGAGAACACAGAGAAGT
	ACATCGGCACAGAAAGCCAGGGGTCTGCTGCTGCAGAACCTGAAGATGACTCGTTCCA
	CTGGACTCCACATACAAGTGTAGAGCCAGGGCATAGTGACAAGAGGGAGGACTTACTT
	ATCATAAGCAGCTTCTTTAAAGAACAACAGTCTTTGCAGCGGTTCCAGAAGTACTTTA
	ATGTCCATGAGCTGGAAGCCTTGCTACAAGAAATGTCATCAAAACTGAAGTCAGCGCA
	GCAGGAGAGCCTGCCCTATAATATGGAAAAAGTCCTAGATAAGGTCTTCCGTGCTTCT
	GAGTCACAAATTCTGAGCATAGCAGAAAAAATGCTTGATACTCGTGTGGCTGAAAATA
	GAGATCTGGGAATGAACGAAAATAACATATTTGAAGAGGCTGCAGTGCTTGATGACAT
	TCAAGACCTCATCTATTTTGTCAGGTACAAGCACTCCACAGCAGAGGAGACAGCCACA
	CTGGTGATGGCACCACCTCTAGAGGAAGGCTTGGGTGGAGCAATGGAAGAGATGCAAC
	CACTGCATGAAGATAATTTCTCACGAGAGAAGACAGCAGAACTTAATGTGCAGGTTCC
	TGAAGAACCCACCCACTTCGACCAACGTGTGATTGGGGACACTCATGCCTCAGAAGTG
	TCACAGAAGCCAAATACTGAGAAAGACCTGGACCCAGGGCCAGTTACAACAGAACACA
	CTCCTATGGATGCTATTGATGCAAACAAGCAACCAGAGACAGCCGCCGAAGAGCCGGC
	AAGTGTCACACCTTTGGAAAACGCAATCCTTCTAATATATTCATTCATGTTTTATTTA
	ACTAAGTCGCTAGTTGCTACATTGCCTGATGATGTTCACCCTGGGCCTGATTTTTATG
	GACTGCCATCGAAACCTGTATTTATCACTGCCTTCTTGGGAATTGCTTCGTTTGCCAT
	TTTCTTATGGAGAACTGTCCTTGTTGTGAAGGATAGAGTATATCAAGTCACGGAACAG
	CAAATTTCTGAGAAGTTGAAGACTATCATGAAAGAAAATACAGAACTTGTACAAAAAT
	TGTCAAATTATGAACAGAAGATCAAGGAATCAAAGAAACATGTTCAGGAAACCAGGAA
	ACAAAATATGATTCTCTCTGATGAAGCAATTAAATATAAGGATAAAATCAAGACACTT
	GAAAAAAATCAGGAAATTCTGGATGACACAGCTAAAAATCTTCGTGTTATGCTAGAAT
	CTGAGAGAGAACAGAATGTCAAGAATCAGGACTTGATATCAGAAAACAAGAAATCTAT
	AGAGAAGTTAAAGGATGTTATTTCAATGAATGCCTCAGAGTTTTCAGAGGTTCAGATT
	GCACTTAATGAAGCTAAGCTTAGTGAAGAGAAGGTGAAGTCTGAATGCCATCGGGTTC
	AAGAAGAAAATGCTAGGCTTAAGAAGAAAAAAGAGCAGTTGCAGCAGGAAATCGAAGA
	CTGGAGTAAATTACATGCTGAGCTCAGTGAGCAAATCAAATCATTTGAGAAGTCTCAG
	AAAGATTTGGAAGTAGCTCTTACTCACAAGGATGATAATATTAATGCTTTGACTAACT
	GCATTACACAGTTGAATCTGTTAGAGTGTGAATCTGAATCTGAGGGTCAAAATAAAGG
	TGGAAATGATTCAGATGAATTAGCAAATGGAGAAGTGGGAGGTGACCGGAATGAGAAG
	ATGAAAAATCAAATTAAGCAGATGATGGATGTCTCTCGGACACAGACTGCAATATCGG
	TAGTTGAAGAGGATCTAAAGCTTTTACAGCTTAAGCTAAGAGCCTCCGTGTCCACTCC
	TCCACCCTTTGGCCCTGGTATGCGTCCACCACTAGGCTTAAGAGAATTTGCACCAGGC
	GTTCCACCAGGAAGACGGGACCTGCCTCTCCACCCTCGGGGATTTTTACCTGGACACG
	CACCATTTAGACCTTTAGGTTCACTTGGCCCAAGAGAGTACTTTATTCCTGGTACCCG
	ATTACCACCCCCAACCCATGGTCCCCAGGAATACCCACCACCACCTGCTGTAAGAGAC
	TTACTGCCGTCAGGCTCTAGAGATGAGCCTCCACCTGCCTCTCAGAGCACTAGCCAGG
	ACTGTTCACAGGCTTTAAAACAGAGCCCATAAAACTATGACCTCTGAGGTTTCATTGG
	AAAGAAAGTGTACTGTGCATTATCCATTACAGTAAAGGATTTCATTGGCTTCAAAATC
	CAAAAGTTTATTTTAAAAGGTTTGTTGTTAGAACTAAGCTGCCTTGGCAGTGTGCATT
	TTTGAGCCAAACAATTCAAAAATGTCATTTCTTCCCTAAATAAAAATCACCTTTT
	ORF Start: ATG at 13	ORF Stop: TAA at 4786
	SEQ ID NO: 66	1591 aa	MW at 178733.8 kD
NOV24b,	MAAAPGLLVWLLVLRLPWRVPGQLDPSTGRRFSEHKLCADDECSVLMYRGEALEDFTG
CG133569-02
Protein Sequence	PDCRFVNFKKGDRVYVYYKLARGWPEVWAGSVGRTFGYPPKDLIQVVHEYTKEELQVP
	TDETDFVCFDGGRDDFHNYNVEELLGFLELYNSAATDSEKAVEKTLQDMEKNPELSKE
	REPEPEPVEANSEESDSVFSENTEDLQEQFTTQKHHSHANSQANHAQGEQASFESFEE
	MLQDKLKVPESENNKTSNSSQVSNEQDKIDAYKLLKKEMTLDLKTKFGSTADALVSDD
	ETTRLVTSLEDDFDEELDTEYYAVGKEDEENQEDFDELPLLTFTDGEDMKTPAKSGVE
	KYPTDKEQNSNEEDKVQLTVPPGIKNDDKNILTTWGDTIFSIVTGGEETRDTMDLESS
	SSEEEKEDDDDALVPDSKQGKPQSATDYSDPDNVDDGLFIVDIPKTNNDKEVNAEHHI
	KGKGRGVQESKRGLVQDKTELEDENQEGMTVHSSVHSNNLNSMPAAEKGKDTLKSAYD
	DTENDLKGAAIHISKGMLHEEKPGEQILEGGSESESAQKAAGNQMNDRKIQQESLGSA
	PLMGDDHPNASRDSVEGDALVNGAKLHTLSVEHQREELKEELVLKTQNQPRFSSPDEI
	DLPRELEDEVPILGRNLPWQQERDVAATASKQMSEKIRLSEGEAKEDSLDEEFFHHKA
	MQGTEVGQTDQTDSTGGPAFLSKVEEDDYPSEELLEDENAINAKRSKEKNPGNQGRQP
	DVNLQVPDRAVLGTIHPDPEIEESKQETSMILDSEKTSETAAKGVNTGGREPNTMVEK
	ERPLADKKAQRPFERSDFSDSIKIQTPELGEVFQNKDSDYLKNDNPEEHLKTSGLAGE
	PEGELSKEDHENTEKYMGTESQGSAAAEPEDDSFHWTPHTSVEPGHSDKREDLLIISS
	FFKEQQSLQRFQKYFNVHELEALLQEMSSKLKSAQQESLPYNMEKVLDKVFRASESQI
	LSIAEKMLDTRVAENRDLGMNENNIFEEAAVLDDIQDLIYFVRYKHSTAEETATLVMK
	PPLEEGLGGAMEEMQPLHEDNFSREKTAELNVQVPEEPTHLDQRVIGDTHASEVSQKP
	NTEKDLDPGPVTTEDTPMDAIDANKQPETAAEEPASVTPLENAILLIYSFMPYLTKSL
	VATLPDDVQPGPDFYGLPWKPVFITAFLGIASFAIFLWRTVLVVKDRVYQVTEQQISE
	KLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQ
	EILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNE
	AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE
	VALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ
	IKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTPPPFGPGMRPPLGLREFAPGVPPG
	RRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPTHGPQEYPPPPAVRDLLPS
	GSRDEPPPASQSTSQDCSQALKQSP

[0458] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 24B.

TABLE 24B
Comparison of NOV24a against NOV24b.
			Identities/
			Similarities for
	Protein	NOV24a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV24b	23 . . . 1484	1386/1462 (94%)
		23 . . . 1484	1386/1462 (94%)

[0459] Further analysis of the NOV24a protein yielded the following properties shown in Table 24C.

TABLE 24C
Protein Sequence Properties NOV24a
PSort     0.4600 probability located in plasma membrane; 0.1080
analysis: probability located in nucleus; 0.1000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 23 and 24
analysis:

[0460] 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/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAM25602	Human protein sequence SEQ ID	715 . . . 1907	1191/1193 (99%)	0.0
	NO: 1117 - Homo sapiens, 1193	1 . . . 1193	1193/1193 (99%)
	aa. [WO200153455-A2, 26 JUL.
	2001]
AAU32407	Novel human secreted protein	715 . . . 1907	1186/1194 (99%)	0.0
	#2898 - Homo sapiens, 1194 aa.	1 . . . 1194	1186/1194 (99%)
	[WO200179449-A2, 25 OCT.
	2001]
AAU29319	Human PRO polypeptide	1 . . . 492	489/492 (99%)	0.0
	sequence #296 - Homo sapiens,	1 . . . 491	491/492 (99%)
	499 aa. [WO200168848-A2, 20
	SEP. 2001]
AAG73911	Human colon cancer antigen	1325 . . . 1798	474/474 (100%)	0.0
	protein SEQ ID NO: 4675 -	1 . . . 474	474/474 (100%)
	Homo sapiens, 487 aa.
	[WO200122920-A2, 05 APR.
	2001]
AAY70210	Human TANGO 130 protein -	1 . . . 410	409/410 (99%)	0.0
	Homo sapiens, 410 aa.	1 . . . 410	410/410 (99%)
	[WO200012762-A1, 09 MAR.
	2000]

[0461] 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
		NOV24a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q92580	KIAA0268 protein - Homo sapiens	715 . . . 1907	1192/1193 (99%)	0.0
	(Human), 1193 aa (fragment).	1 . . . 1193	1192/1193 (99%)
O15320	Meningioma-expressed antigen	1158 . . . 1871	233/790 (29%)	1e−71
	6/11 (MEA6) (MEA11) - Homo	20 . . . 783	381/790 (47%)
	sapiens (Human), 804 aa.
Q14083	C219-reactive peptide - Homo	1306 . . . 1441	136/136 (100%)	9e−71
	sapiens (Human), 136 aa	1 . . . 136	136/136 (100%)
	(fragment).
Q96SG9	BA500G10.2 (Novel protein	1158 . . . 1900	217/812 (26%)	1e−66
	similar to meningioma expressed	34 . . . 822	371/812 (44%)
	antigen 6 (MEA6) and 11
	(MEA 11)) - Homo sapiens
	(Human), 825 aa (fragment).
O95046	WUGSC: H_DJ0988G15.3 protein	1160 . . . 1873	214/781 (27%)	2e−62
	(DJ1005H11.2)	22 . . . 775	368/781 (46%)
	(WUGSC: H_DJ0988G15.3
	protein) - Homo sapiens (Human),
	777 aa.

[0462] PFam analysis indicates that the NOV24a protein contains the domains shown in the Table 24F.

TABLE 24F
Domain Analysis of NOV24a
			Identities/
			Similarities for
	Pfam	NOV24a Match	the Matched	Expect
	Domain	Region	Region	Value
	SH3	48 . . . 105	16/61 (26%)	0.026
			34/61 (56%)

Example 25

[0463] 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: 67	1153 bp
NOV25a,	ATGCTGCCGTGGCTTCTTGTCTTCTCTGCTCTGGGTCTCCAGGCCTGGGGTGATTCCT
CG133858-01
DNA Sequence	CCTGGAACAAAACACAAGCTAAACAGGTATCAGAGGGGCTCCAGTACCTATTTGAGAA
	CATCTCCCAGCTCACTCAAAAAGGCCTCCCCACAGATGTCTCCACCACGGTCTCCCGC
	AAGGCATGGGGGGCAGAAGCTGTTGGCTGCAGTATTCAGCTGACCACGCCAGTGAATC
	TCCTTGTTATACACCATGTCCCTGGACTGGAGTGTCACGACCAGACAGTCTGCAGCCA
	GAGACTGCGGGAACTGCAGGCCCATCATGTCCACAACAACAGTGGGTGTGATGTGGCC
	TACAACTTCCTGGTTGGGGATGATGGCAGGGTGTATGAAGGTGTTGGCTGGAATATCC
	AAGGAGTGCACACCCAAGGCTACAACAACATCTCCCTGGGCTTTGCCTTCTTCGGCAC
	TAAGAAAGGCCACAGTCCCAGCCCTGCTGCCCTGTCGGCCATGGAAAACCTAATCACC
	TATGCTGTCCAGAAGCGCCACCTGTCATCCAGTTATGTTCAGCCACTTCTTGTGAAAG
	GCGAGAACTGCCTGGCCCCTCGGCAGAAGACAAGCCTGAAGAAGGCTTGCCCCGGCGT
	TGTCCCACGGTCTGTGTGGGGAGCCAGGGAGACCCACTGTCCCAGGATGACTCTCCCA
	GCGAAGTATGGCATCATTATCCACACTGCCGGGAGGACCTGCAACATTTCTGATGAGT
	GCCGCCTGCTGGTCCGGGACATCCAGTCTTTCTACATAGACAGGCTCAAGTCATGCGA
	CATTGGTTATAACTTCCTGGTGGGCCAGGATGGCGCCATTTATGAAGGGGTGGGCTGC
	AATGTCCAAGGCTCCTCCACCCCTGGCTACGATGACATTGCCCTGGGCATTACCTTCA
	TGGGCACCTTCACAGGTATACCACCCAATGCTGCAGCACTAGAGGCAGCCCAAGACCT
	GATCCAGTGTGCCATGGTCAAAGGGTACCTGACTCCCAACTACCTGCTGGTGGGCCAC
	AGTGATGTGGCCCGAACCTTGTCTCCTGGGCAGGCTTTATACAACATCATCAGCACCT
	GGCCTCATTTCAAGCACTGTGGACAAGAAGCCACGGCAGCATAAGGGCGAT
	ORF Start: ATG at 1	ORF Stop: TAA at 1144
	SEQ ID NO: 68	381 aa	MW at 41393.7 kD
NOV25a,	MLPWLLVFSALGLQAWGDSSWNKTQAKQVSEGLQYLFENISQLTEKGLPTDVSTTVSR
CG133858-01
Protein Sequence	KAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVA
	YNFLVGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLIT
	YAVQKGHLSSSYVQPLLVKGENCLAPRQKTSLKKACPGVVPRSVWGARETHCPRMTLP
	AKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVGW
	NVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGH
	SDVARTLSPGQALYNIISTWPHFKHCGQEATAA

[0464] Further analysis of the NOV25a protein yielded the following properties shown in Table 25B.

TABLE 25B
Protein Sequence Properties NOV25a
PSort     0.5500 probability located in lysosome (lumen); 0.3700
analysis: probability located in outside; 0.1000 probability located
          in endoplasmic reticulum (membrane); 0.1000 probability
          located in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 18 and 19
analysis:

[0465] 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 25C.

TABLE 25C
Geneseq Results for NOV25a
		NOV25a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB53272	Human polypeptide #12 - Homo	1 . . . 373	368/373 (98%)	0.0
	sapiens, 369 aa.	1 . . . 369	369/373 (98%)
	[WO200181363-A1, 01 NOV.
	2001]
AAE00693	Human full length granulocyte	1 . . . 373	368/373 (98%)	0.0
	peptide homolog Zgpa1 protein #2 -	1 . . . 369	369/373 (98%)
	Homo sapiens, 369 aa.
	[WO200129224-A2, 26 APR. 2001]
AAE00692	Human full length granulocyte	1 . . . 373	370/375 (98%)	0.0
	peptide homolog Zgpa1 protein #1 -	1 . . . 375	371/375 (98%)
	Homo sapiens, 375 aa.
	[WO200129224-A2, 26 APR. 2001]
AAY96963	Wound healing tissue peptidoglycan	1 . . . 373	349/373 (93%)	0.0
	recognition protein-like protein -	1 . . . 368	352/373 (93%)
	Homo sapiens, 368 aa.
	[WO200039327-A1, 06 JUL. 2000]
ABB53271	Human polypeptide #11 - Homo	153 . . . 373	217/221 (98%)	e−127
	sapiens, 241 aa. [WO200181363-	21 . . . 241	218/221 (98%)
	A1, 01 NOV. 2001]

[0466] 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 25D.

TABLE 25D
Public BLASTP Results for NOV25a
		NOV25a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q96LB8	Peptidoglycan recognition	1 . . . 373	373/373 (100%)	0.0
	protein-I-beta precursor - Homo	1 . . . 373	373/373 (100%)
	sapiens (Human), 373 aa.
CAC38715	Sequence 7 from Patent	1 . . . 373	368/373 (98%)	0.0
	WO0129224 - Homo sapiens	1 . . . 369	369/373 (98%)
	(Human), 369 aa.
CAC38714	Sequence 4 from Patent	1 . . . 373	370/375 (98%)	0.0
	WO0129224 - Homo sapiens	1 . . . 375	371/375 (98%)
	(Human), 375 aa.
Q9HD75	Hypothetical 40.0 kDa protein -	1 . . . 373	349/373 (93%)	0.0
	Homo sapiens (Human), 368 aa.	1 . . . 368	352/373 (93%)
Q96LB9	Peptidoglycan recognition	2 . . . 373	231/372 (62%)	e−136
	protein-I-alpha precursor - Homo	4 . . . 341	268/372 (71%)
	sapiens (Human), 341 aa.

[0467] PFam analysis indicates that the NOV25a protein contains the domains shown in the Table 25E.

TABLE 25E
Domain Analysis of NOV25a
			Identities/
			Similarities
	Pfam	NOV25a Match	for the	Expect
	Domain	Region	Matched Region	Value
No Significant Matches Found

Example 26

[0468] 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: 69	1182 bp
NOV26a,	GTCCTGGGACCACATGGGGACGCTGCCATGGCTTCTTGCCTTCTTCATTCTGGGTCTC
CG134100-01
DNA Sequence	CAGGCTTGGGGTTCTCCTGGAGTGAGACCCAAGCCAGAGCCTTGTCCCAGAGGCTTAT
	GGACCTGTTTGTCAGCATCTCACAGTTCATTCACAAGGGTCGCAATGATACTCCCACC
	ATCGTCTCCCGCAAGGAGTGGGGGGCAAGACCGCTCGCCTGCAGGGCCCTGCTGACCC
	TGCCTGTGGCCTACATCATCACAGACCAGCTCCCAGGGATGCAGTGCCAGCAGCAGAG
	CGTTTGCAGCCAGATGCTGCGGGGGTTGCAGTCCCATTCCGTCTACACCATAGGCTGG
	TGCGACGTGGCCTACAACTTCCTGGTTGGGGATGATGGCAGGGTGTATGAAGGTGTTG
	GCTGGAACATCCAAGGCTTGCACACCCAGGGCTACAACAACATTTCCCTGGGCATCGC
	CTTCTTTGGCAATAAGATAAGCAGCAGTCCCAGCCCTGCTGCCTTATCAGCTGCAGAG
	GGTCTGATCTCCTATGCCATCCAGAAGGGTCACCTGTCGCCCAGGTATATTCAGCCAC
	TTCTTCTGAAAGAAGAGACCTGCCTGGACCCTCAACATCCAGTGATGCCCAGGAAGGT
	TTGCCCCAACATCATCAAACGATCTGCTTGGGAAGCCAGAGAGACACACTGCCCTAAA
	ATGAACCTCCCAGCCAAATATGTCATCATCATCCACACCGCTGGCACAAGCTGCACTG
	TATCCACAGACTGCCAGACTGTCGTCCGAAACATACAGTCCTTTCACATGGACACACG
	GAACTTTTGTGACATTGGATATCACTTCCTGGTGGGCCAGGATGGTGGCGTGTATGAA
	GGGGTTGGATGGCACATCCAAGGCTCTCACACTTATGGATTCAACGATATTGCCCTAG
	GAATTGCCTTCATCGGCTACTTTGTAGAAAAGCCTCCAAATGCTGCAGCGCTGGAGGC
	GGCCCAGGACCTGATCCAGTGTGCCGTGGTTGAGGGGTACCTGACTCCAAACTACCTG
	CTGATGGGCCACAGTGACGTGGTCAACATCCTGTCCCCTGGGCAGGCTTTGTATAACA
	TCATCAGCACCTGGCCTCATTTCAAGCACTGAAGGAGGCCCCACTCCCTTTGAGACTG
	CCCTCCCTCCCCTGCTGGGTCT
	ORF Start: ATG at 28	ORF Stop: TGA at 1132
	SEQ ID NO: 70	368 aa	MW at 40515.0kD
NOV26a,	MASCLLHSGSPGLGFSWSETQARGLSQRLMDLFVSISQFIHKGRNDTPTIVSRKEWGA
CG134100-01
Protein Sequence	RPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLV
	GDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFGNKISSSPSPAALSAAECLISYAIQK
	GHLSPRYIQPLLLKEETCLDPQHPVMPRKVCPNIIKRSAWEARETHCPKMNLPAKYVI
	IIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGS
	HTYGFNDIALGIAFIGYFVEKRPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVN
	ILSPGQALYNIISTWPHFKH
	SEQ ID NO: 71	1087 bp
NOV26b,	GTCCTGGGACCACATGGGGACGCTGCCATGGCTTCTTOCCTTCTTCATTCTGGGTCTC
CG134100-02
DNA Sequence	CAGGCTTGGGATACTCCCACCATCGTCTCCCGCAAGGAGTGGGGGGCAAGACCGCTCG
	CCTGCAGGGCCCTGCTGACCCTGCCTGTGGCCTACATCATCACAGACCAGCTCCCAGG
	GATGCAGTGCCAGCAGCAGAGCOTTTGCAGCCAGATGCTGCCGGGGTTGCAGTCCCAT
	TCCGTCTACACCATAGGCTGGTGCGACGTGGCGTACAACTTCCTGGTTGGGGATGATG
	GCAGGGTGTATGAAGGTGTTGGCTGGAACATCCAAGGCTTGCACACCCAGGGCTACAA
	CAACATTTCCCTGGGCATCGCCTTCTTTGGCAATAAGATAAGCAGCAGTCCCAGCCCT
	GCTGCCTTATCAGCTGCAGAGGGTCTGATCTCCTATGCCATCCAGAAGGGTCACCTGT
	CGCCCAGGTATATTCAGCCACTTCTTCTGAAAGAAGAGACCTGCCTGGACCCTCAACA
	TCCAGTGATGCCCAGGAAGGTTTGCCCCAACATCATCAAACGATCTGCTTGGGAAGCC
	AGAGAGACACACTGCCCTAAAATGAACCTCCCAGCCAAATATGTCATCATCATCCACA
	CCGCTGGCACAAGCTGCACTGTATCCACAGACTGCCAGACTGTCGTCCGAAACATACA
	GTCCTTTCACATCGACACACGGAACTTTTGTGACATTGGATATCACTTCCTGGTGGGC
	CAGGATGGTGGCGTGTATGAAGGGGTTGGATGGCACATCCAACGCTCTCACACTTATG
	GATTCAACGATATTGCCCTAGGAATTGCCTTCATCGGCTACTTTGTAGAAAAGCCTCC
	AAATGCTGCAGCGCTGGAGGCGGCCCAGGACCTGATCCAGTGTGCCGTGGTTGAGGGG
	TACCTGACTCCAAACTACCTGCTGATGGGCCACAGTGACGTGGTCAACATCCTGTCCC
	CTGGGCACGCTTTGTATAACATCATCAGCACCTGGCCTCATTTCAAGCACTGAAGGAC
	GCCCCACTCCCTTTGAGACTGCCCTCCCTCCCCTGCTGGGTCT
	ORF Start: ATG at 14	ORF Stop: TGA at 1037
	SEQ ID NO: 72	341 aa	MW at 37640.9kD
NOV26b,	MGTLPWLLAFFILGLQAWDTPTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQ
CG134100-02
Protein Sequence	QQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISL
	GIAFFGNKISSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLLLKEETCLDPQHPVMP
	RKVCPNIIKRSAWEARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHM
	DTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAA
	LEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQALYNIISTWPHFKH

[0469] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 26B.

TABLE 26B
Comparison of NOV26a against NOV26b.
			Identities/
	Protein	NOV26a Residues/	Similarities for
	Sequence	Match Residues	the Matched Region
	NOV26b	46 . . . 368	299/323 (92%)
		19 . . . 341	299/323 (92%)

[0470] Further analysis of the NOV26a protein yielded the following properties shown in Table 26C.

TABLE 26C
Protein Sequence Properties NOV26a
PSort     0.4500 probability located in cytoplasm;
analysis: 0.3239 probability located in microbody
          (peroxisome); 0.2643 probability
          located in lysosome (lumen); 0.1000
          probability located in mitochondrial
          matrix space
SignalP   No Known Signal Sequence Indicated
analysis:

[0471] 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 26D.

TABLE 26D
Geneseq Results for NOV26a
		NOV26a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAE00692	Human full length granulocyte	16 . . . 368	231/356 (64%)	e−139
	peptide homolog Zgpa1 protein #1 -	20 . . . 375	276/356 (76%)
	Homo sapiens, 375 aa.
	[WO200129224-A2, 26 APR.
	2001]
ABB53272	Human polypeptide #12 - Homo	16 . . . 368	230/353 (65%)	e−138
	sapiens, 369 aa. [WO200181363-	20 . . . 369	274/353 (77%)
	A1, 01 NOV. 2001]
AAE00693	Human full length granulocyte	16 . . . 368	230/353 (65%)	e−138
	peptide homolog Zgpa1 protein #2 -	20 . . . 369	274/353 (77%)
	Homo sapiens, 369 aa.
	[WO200129224-A2, 26 APR.
	2001]
AAY76124	Human secreted protein encoded by	46 . . . 269	224/224 (100%)	e−133
	gene 1 - Homo sapiens, 244 aa.	19 . . . 242	224/224 (100%)
	[WO9958660-A1, 18 NOV. 1999]
AAY96962	Keratinocyte peptidoglycan	46 . . . 269	224/224 (100%)	e−133
	recognition protein-like protein -	19 . . . 242	224/224 (100%)
	Homo sapiens, 243 aa.
	[WO200039327-A1, 06 JUL. 2000]

[0472] 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 26E.

TABLE 26E
Public BLASTP Results for NOV26a
		NOV26a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q96LB9	Peptidoglycan recognition	46 . . . 368	322/323 (99%)	0.0
	protein-I-alpha precursor - Homo	19 . . . 341	322/323 (99%)
	sapiens (Human), 341 aa.
Q96LB8	Peptidoglycan recognition	16 . . . 368	232/354 (65%)	e-139
	protein-I-beta precursor - Homo	20 . . . 373	275/354 (77%)
	sapiens (Human), 373 aa.
CAC38714	Sequence 4 from Patent	16 . . . 368	231/356 (64%)	e-138
	WO0129224 - Homo sapiens	20 . . . 375	276/356 (76%)
	(Human), 375 aa.
CAC38715	Sequence 7 from Patent	16 . . . 368	230/353 (65%)	e-138
	WO0129224 - Homo sapiens	20 . . . 369	274/353 (77%)
	(Human), 369 aa.
Q9HD75	Hypothetical 40.0 kDa protein -	16 . . . 368	221/353 (62%)	e-126
	Homo sapiens (Human), 368 aa.	20 . . . 368	263/353 (73%)

[0473] PFam analysis indicates that the NOV26a protein contains the domains shown in the Table 26F.

TABLE 26F
Domain Analysis of NOV26a
			Identities/
			Similarities for
	Pfam	NOV26a Match	the Matched	Expect
	Domain	Region	Region	Value
No Significant Matches Found

Example 27

[0474] 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:73	2195 bp
NOV27a,	TTTGTTCCTAACAGATTTCTTGCGACAAGGAAACCCGCAGTCTTCCGCTTCCGGTTGC
CG134403-01
DNA Sequence	TCTGTTGCCATACTAACCCCACCCATAACAGCCGTGGTGGTTATGGCTGGCCTGAGCG
	GCGCGCAGATCCCCGACGGGGAGTTCACCGCGGTCGTGTACCGCCTCATCCGCAATGC
	ACGCTACGCCGAGGCGGTGCAGCTGCTGGGCGGAGAACTGCACCGGAGCCCTAGGAGC
	CGCGCCGGCCTGTCGCTGCTAGGCTACTGCTACTACCGCCTGCAGGAGTTCGCGCTGG
	CGGCCGAGTGCTATGAGCAGCTGGGCCAGCTGCACCCGGAACTGGAGCAGTACCGCCT
	GTACCAGGCCCAGGCCCTGTACAAGGCCTGCCTTTATGCGGAGGCCACCCGGGTCGCC
	TTCCTTCTCCTGGATAACCCCGCCTACCACAGCCGGGTCCTCCGCCTGCAAGCTGCTA
	TCAAGTACAGCGAGGGCGATCTGCCAGGGTCCAGGAGCCTGGTAGAGCAGCTGCCGAG
	TAGGGAAGGGGGAGAGGAPAGTGGGGCCGAGAATCAGACCGATGGCCAGATCAACCTG
	GGTTGTTTGCTCTACAAGGAGGGACAGTATGAAGCTGCATGCTCCAAGTTTTTTGCCG
	CCCTGCAGGCCTCCGGCTACCAGCCTGACCTTTCCTACAACCTGGCTTTGGCCTATTA
	CAGCAGCCGACACTATCCTTCAGCACTGAAGCATATCGCTGAGATTATTGAGCGTGGC
	ATCCGCCAGCACCCTGAGCTAGGTGTCGGCATGACCACTGAGGGCATTGATGTTCGCA
	GTGTTCGCAACACCTTAGTCCTCCATCAGACTGCTCTGGTGGAAGCCTTCAACCTTAA
	GGCAGCTATAGAATACCAACTGAGAAACTATGAGGCAGCTCAAGAAGCCCTCACTCAC
	ATGCCACCCAGGGCAGAGGAAGAGTTGGACCCTGTGACCCTACACAACCAGGCACTAA
	TGAACATGGATGCCAGGCCTACAGAAGGGTTTGAAAAGCTACACTTTTTGCTCCAACA
	GAATCCCTTTCCTCCAGAGACTTTTGGCAACCTGTTGCTGCTCTACTGTAAATATGAG
	TATTTTGACCTGCCAGCAGATGTCCTGGCACAAAATGCCCATTTGATTTATAAGTTCC
	TCACACCCTATCTCTATGACTTCTTGGACGCTGTGATCACTTGCCAGACAGCTCCTGA
	AGAGGCTTTCATTAACCTTGATGGGCTAGCAGGGATGCTGACTGACCTCCTCCGGAAA
	CTTACCATACAAGTACAGGAAGCAAGACACAATAGAGATGATGAAGCTATCAAAAAGG
	CAGTGAATGAATATGATGAAACCATGGAGAAATACATTCCTGTGTTGATGGCTCAGGC
	AAAAATCTACTGGAATCTTGAAAATTATCCAATGGTGGAAAAGATCTTCCGCAAATCT
	GTGGAATTCTGTAACGACCATGATGTGTGGAAGTTGAATGTGGCTCATGTTCTGTTCA
	TGCAGGAAAACAAATACAAGAAGCCATTGGTTTCTATGAACCCATAGTCAAGAAAACA
	TTATGATAACATCCTCAATGTCAGTGCTATTGTACTGGCTAATCTCTGTGTTTCCTAT
	ATTATGACAAGTCAAAATGAAGAXGCAGAGGAGTTGATGAGGAAGATTGAAAAGGAGG
	AAGAGCAGCTCTCTTATGATGACCCAGATAAGAAAATGTACCATCTCTGCATTGTGAA
	TTTGGTGATACGAACTCTTTATTGTGCCAAAGGAAATTATGACTTTGGTATTTCTCGA
	GTTATCAAAAGCTTGGAACCTTACAACAAAAAGCTGGGAACAGACACCTGGTATTATG
	CCAAAAGATGCTTCCTGTCCTTGTTAGAAAACATGTCAAAACACACAATCATGCTTCG
	TCATAGTGTTATTCAAGAATGTGTCCAGTTTCTAGAACACTGTGAACTTCATCGCAGA
	AACATACCTGCTGTTATTGAACAACCCCTGGAAGAAGAAAGAATGCATGTTGGAAAGA
	ATACAGTCACATATGAGTCTAGGCAGTTAAAAGCTTTCATTTATGAGATTATAGGATC
	GAATATATAGTAATAGCTGATAGTGGCATTTATCAAATGGCTTTCTTATGTAAATTTG
	CATCGCTTTATTTACCCTTTGGCATCTTTATATTTGTTACATGTTGAAC
	ORF Start: ATG at 101 ORF	Stop: TAG at 2096
	SEQ ID NO: 74	665 aa	MW at 76098.0 kD
NOV27a,	MAGLSGAQIPDGEFTAVVYRLIRNARYAEAVQLLGGELQRSPRSRAGLSLLGYCYYRL
CG134403-01
Protein Sequence	QEFALAAECYEQLGQLHPELEQYRLYQAQALYKACLYAEATRVAFLLLDNPAYHSRVL
	RLQAAIKYSEGDLPGSRSLVEQLPSREGGEESGGENETDGQINLGCLLYKEGQYEAAC
	SKFFAALQASCYQPDLSYNLALAYYSSRQYASALKHIAEIIERGIRQHPELGVGMTTE
	GIDVRSVGNTLVLHQTALVEAFNLKAAIEYQLRNYEAAQEALTDMPPRAEEELDPVTL
	HNQALMNMDARPTEGFEKLQFLLQQNPFPPETFGNLLLLYCKYEYFDLAADVLAENAH
	LIYKFLTPYLYDFLDAVITCQTAPEEAFIKLDGLAGMLTEVLRKLTIQVQEARHNRDD
	EAIKKAVNEYDETMEKYIPVLMAQAKIYWNLENYPMVEKIPRKSVEFCNDHDVWKLNV
	AHVLPMQENKYKEATGFYEPIVKKHYDNILNVSAIVLANLCVSYIMTSQNEEAEELMR
	KIEKEEEQLSYDDPDKKMYHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYNKKLGT
	DTWYYAKRCFLSLLENMSKHTIMLRDSVIQECVQFLEHCELHGRNIPAVIEQPLEEER
	MHVGKNTVTYESRQLKALIYEIIGWNI

[0475] Further analysis of the NOV27a protein yielded the following properties shown in Table 27B.

TABLE 27B
Protein Sequence Properties NOV27a
PSort     0.8500 probability located in endoplasmic
analysis: reticulum (membrane); 0.6640 probability
          located in plasma membrane; 0.3000
          probability located in microbody
          (peroxisome); 0.1000 probability located
          in mitochondrial inner membrane
SignalP   No Known Signal Sequence Indicated
analysis:

[0476] 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 27C.

TABLE 27C
Geneseq Results for NOV27a
		NOV27a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAM39821	Human polypeptide SEQ ID NO	1 . . . 640	636/640 (99%)	0.0
	2966 - Homo sapiens, 843 aa.	60 . . . 699	637/640 (99%)
	[WO200153312-A1, 26 JUL. 2001]
AAM41607	Human polypeptide SEQ ID NO	356 . . . 664	293/309 (94%)	e−173
	6538 - Homo sapiens, 310 aa.	1 . . . 309	302/309 (96%)
	[WO200153312-A1, 26 JUL. 2001]
ABB61288	Drosophila melanogaster	22 . . . 660	301/648 (46%)	e−157
	polypeptide SEQ ID NO 10656 -	18 . . . 646	424/648 (64%)
	Drosophila melanogaster, 652 aa.
	[WO200171042-A2, 27 SEP. 2001]
AAB94836	Human protein sequence SEQ ID	385 . . . 664	266/280 (95%)	e−156
	NO: 16004 - Homo sapiens, 281 aa.	1 . . . 280	273/280 (97%)
	[EP1074617-A2, 07 FEB. 2001]
ABB48602	Listeria monocytogenes protein	59 . . . 317	57/260 (21%)	2e−04
	#1306 - Listeria monocytogenes,	14 . . . 237	102/260 (38%)
	417 aa. [WO200177335-A2, 18
	OCT. 2001]

[0477] 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 27D.

TABLE 27D
Public BLASTP Results for NOV27a
		NOV27a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q96NE6	CDNA FLJ30990 fis, clone	1 . . . 665	635/665 (95%)	0.0
	HLUNG1000037 - Homo sapiens	1 . . . 638	635/665 (95%)
	(Human), 638 aa.
Q9CY00	2510042P03Rik protein - Mus	1 . . . 665	615/665 (92%)	0.0
	musculus (Mouse), 664 aa.	1 . . . 664	642/665 (96%)
Q99J38	Similar to RIKEN cDNA	1 . . . 665	598/665 (89%)	0.0
	2510042P03 gene - Mus musculus	1 . . . 664	632/665 (94%)
	(Mouse), 664 aa.
Q9D2H0	4930506L13Rik protein - Mus	1 . . . 617	558/617 (90%)	0.0
	musculus (Mouse), 616 aa.	1 . . . 616	586/617 (94%)
Q9VK41	CG5142 protein - Drosophila	22 . . . 660	301/648 (46%)	e−157
	melanogaster (Fruit fly), 652 aa.	18 . . . 646	424/648 (64%)

[0478] PFam analysis indicates that the NOV27a protein contains the domains shown in the Table 27E.

TABLE 27E
Domain Analysis of NOV27a
			Identities/
			Similarities for
	Pfam	NOV27a Match	the Matched	Expect
	Domain	Region	Region	Value
	TPR	45 . . . 78	10/34 (29%)	0.97
			22/34 (65%)

Example 28

[0479] 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:75	1165 bp
NOV28a,	CCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCATCCTAGTCCTG
CG135049-01
DNA Sequence	TGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCTCTGCTCTCCC
	GGGGCTCCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGCGGGATATTAA
	CAAAGACAGAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAAACCACGCCCAGGAA
	TACAGACGGGGTGGCCTGGGATCTCTGTTCTATCTTACACTGGATGTGCTAGAGACTG
	ACTGCCATGTGCTCAGAAAGAAGGCATGGCAAGACTGTGGAATGAGGATATTTTTTGA
	ATCAGTTTATGGTCAATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTC
	TATTTAGCTGCTTATAACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGA
	CGTGCCCGGACTGCCCAGGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGA
	GGCTGCCACCGAGTCTCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCT
	CTCTTCAAAGTCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTGTGGG
	AATACTTAATTAAAGAATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCA
	GTCCTCCGACTCTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGG
	GAAAAGTTTGTCTCTGTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAA
	GTGAAAACTCTGCTGTTAACCAGAAACCTACAAACCTTCCCAAGGTGGAAGAATCCCA
	GCAGAAAAACACCCCCCCAACAGACTCCCCCTCCAAAGCTGGGCCAAGAGGATCTGTC
	CAATATCTTCCTGACTTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCT
	TTCCTGTGCATCTGGACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTT
	CCTCTTCCTGGAGCCTATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAA
	GCACGCACTGCTGAGTGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGC
	CATGA
	ORF Start: ATG at 17	ORF Stop: TGA at 1163
	SEQ ID NO: 76	382 aa	MW at 42077.4 kD
NOV28a,	MGLLLPLALCILVLCCGAMSPRQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD
CG135049-01
Protein Sequence	GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLETDCHVLRKKAWQDCGMRIFFESVYGQ
	CKAIFYMNNPSRVLYLAAYNCTLRPVSKKKIYMTCPDCPGSIPTDSSNHQVLEAATES
	LAKYNNENTSKQYSLFKVTPASSQWVVGPSYLWEYLIKESPCTKSQASSCSLQSSDSV
	PVGLCKGSLTRTHWEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTP
	PTDSPSKAGPRGSVQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEP
	MEEKLVVLPFPKEKARTAECPGPAQNASPLVLPP
	SEQ ID NO: 77	1303 bp
NOV28b,	GTAACAAAACCGCTCAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAG
CG135049-02
DNA Sequence	CTCCACAAACTGACCCATCCTGGGCCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCC
	CTGGCACTCTGCATCCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCAA
	TCAACCCCTCGGCTCTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGC
	AGGCTTTGCCCTGCGGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTC
	AACCGAGTGAACGACGCCCAGGAATACAGACCGGGTGGCCTGGGATCTCTGTTCTATC
	TTACACTGGATGTGCTAGACTGTGGAATGAGGATATTTTTTGAATCAGTTTATGGTCA
	ATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTCTATTTAGCTGCTTAT
	AACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGACGTGCCCTGACTGCC
	CAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACCGAGTC
	TCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCTCTCTTCAAAGTCACC
	AGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTGGAATACTTAATTAAAG
	AATCACCATCTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGACTCTGT
	GCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTGTCTCT
	GTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTCTGCTG
	TTAACCAGAAACCTACAAACCTTCCCAAGGTGGAAGAATCCCAGCAGAAAAACACCCC
	CCCAACACACTCCCCCTCCAAAGCTGGGCCAAGAGGATCTGTCCAATATCTTCCTGAC
	TTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCATCTGG
	ACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTGGAGCC
	TATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTGCTGAG
	TGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCATGAGAATCACACA
	GAGTCTTCTGTAGGGGTATGGTGCGCCGCATGACATGGGAGGCGATGCGGACGATGGA
	CAGAGACAGAGCGTGCACACGTAGAGT
	ORF Start: ATG at 99	ORF Stop: TGA at 1206
	SEQ ID NO: 78	369 aa	MW at 40458.6 kD
NOV28b,	MGLLLPLALCILVLCCGAIVISPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD
CG135049-02
Protein Sequence	GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLDCGMRIFFESVYGQCKAIFYMNNPSRVAA
	LYLAAYNCTLRPVSKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYAA
	SLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTH
	WEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGS
	VQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKE
	KARTAECPGPAQNASPLVLPP
	SEQ ID NO: 79	1970 bp
NOV28c	GTAACAAAACCGCTCAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAG
CG135049-03
DNA Sequence	CTCCACAAACTGACCCATCCTGGGCCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCC
	CTGGCACTCTGCATCCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCC
	TCAACCCCTCGGCTCTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGC
	AGGCTTTGCCCTGCGGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTC
	AACCGAGTGAACGACGCCCAGGAATACAGACGGGGTGGCCTGGGATCTCTGTTCTATC
	TTACACTGGATGTGCTAGACTGTGGAATGAGGATATTTTTTGAATCAGTTTATGGTCA
	ATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTCTATTTAGCTGCTTAT
	AACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGACGTGCCCTGACTGCC
	CAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACCGAGTC
	TCTTGCGAAATACAACAATGAGAACACATCCAAAGCAGTATTCTCTCTTCAAGTCACC
	AGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTGGAATACTTAATTAAAG
	AATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGACTCTGT
	GCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTGTCTCT
	GTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTCTGCTG
	TTAACCAGAAACCTACAAACCTTCCCAAGGTGGAAGAATCCCAGCAGAAAAATACCCC
	CCCAACAGACTCCCCCTCCAAACCTGGGCCAAGAGGATCTGTCCAATATCTTCCTGAC
	TTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCATCTGG
	ACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTGGAGCC
	TATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTGCTGAG
	TGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCATGAGAATCACACA
	GAGTCTTCTCTAGGGGTATGGTGCGCCGCATGACATGGGAGGCGATGGGGACGATGGA
	CAGAGACAGAGCGTGCACACGTAGAGTACCAGGGGAAGGAGCAGACCCATCCTGGGCC
	TTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCATCCTAGTCCTGTG
	CTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCTCTGCTCTCCCCG
	GGCTGCAATCACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGGCGGGATATTAAC
	AAAGACAGAAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAACGACGCCCAGGAAT
	ACAGACGGGGTGGCCTGGGATCTCTGTTCTATCTTACACTGGATGTGCTAGAGACTGA
	CTGCCATGTGCTCAGAAAGAAGGCATGGCAAGACTGTGGAATGAGGATATTTTTTGAA
	TCAGTTTATGGTCAATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTCT
	ATTTAGCTGCTTATAACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGAC
	GTGCCCTGACTGCCCAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAG
	GCTGCCACCGAGTCTCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCTC
	TCTTCAAAGTCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTGTGG
	ORF Start: ATG at 99	ORF Stop: TGA at 1206
	SEQ ID NO:80	1369 aa	MW at 40458.6 kD
NOV28c,	MCLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD
CG135049-03
Protein Sequence	GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLDCGMRIFFESVYGQCKAIFYMNNPSRV
	LYLAAYNCTLRPVSKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYHNENTSKQY
	SLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTH
	WEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGS
	VQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKE
	KARTAECPGPAQNASPLVLPP
	SEQ ID NO:81	1427 bp
NOV28d,	AAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAGCTCCACiAACTGAC
CG135049-04
DNA Sequence	CCATCCTGGGCCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCAT
	CCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCT
	CTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGC
	GGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAACGA
	CGCCCAGGAATACAGACGGGCAATTTCAAAAAAAAAGATTTACATGACGTGCCCTGAC
	TGCCCAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACCG
	AGTCTCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCTCTCTTCAAAGT
	CACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTGGAATACTTAATT
	AAAGAATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGACT
	CTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTGT
	CTCTGTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTCT
	GCTGTTAACCAGAAACCTACAACCTTCCCAAGGTGGAAAGAATCCCAGCAGAAAAACA
	CCCCCCCAACAGACTCCCCCTCCkAAGCTGGGCCAAGACGATCTGTCCAATATCTTCC
	TGACTTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCAT
	CTGGACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTGG
	AGCCTATGGAGGAGAAGCTGGTCGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTGC
	TGAGTGCCCACGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCATGAGAATCA
	CACAGAGTCTTCTGTAGGGGTATGGTGCGCCGCATGACATCGGAGGCGATGGGGACGA
	TGGACAGAGACAGAGCGTGCACACGTAGAGTGGCTAGTGAAGGACCCCTTTTTGACTC
	TTCTTGGTCTCAGCATGTTGACTGGGATTGGAAATAATGAGACTGAGCCCTCGGCTTG
	GGCTGCACTCTACCCT2TACACTGCCTTGTACCCTGAGCTGCATCACCTCCTAAACTG
	AGCAGTCTCATACCATGGAGAGATGCCTCTCTTATGTCTTCAGCCACTCACTTATAAA
	GATACTTATCTTTTCAGCAGTATATATGTGCTGAAATCTCAGCATGAAAGCATTGCAT
	GAGTAAGATACTTTCCCTAAAAAAAAAAAAAAAAA
	ORF Start: ATG at 85	ORF Stop: TGA at 1036
	SEQ ID NO: 82	317 aa	MW at 34555.7 kD
NOV28d,	MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD
CG135049-04
Protein Sequence	GYVLRLNRVNDAQEYRRAISKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNE
	NTSKQYSLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKG
	SLTRTHWEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSK
	AGPRGSVQYLPDLDDKNSQEKGPQEAFPVHLDLTThPQGETLDISFLFLEPMEEKLVV
	LPFPKEKARTAECPGPAQNASPLVLPP
	SEQ ID NO: 83	1544 bp
NOV28e,	AAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAGCTCCACAAACTGAC
CG135049-05
DNA Sequence	CCATCCTGGGCCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCAT
	CCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTCGCCCTCAACCCCTCGGCT
	CTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGC
	GGGATATTAACAAAGACAGAAAGGATGGCTATCTGCTGAGACTCAACCGAGTGAACGA
	CGCCCAGGAATACAGACGGGGTGGCCTGGGATCTCTGTTCTATCTTACACTGGATGTG
	CTAGAGACTGACTGCCATGTGCTCAGAAAGAAGGCATGGCAAGACTGTGGAATGAGGA
	TATTTTTTGAATCAGCATCAACAGTTTCAAAAAAAAAGATTTACATGACGTGCCCTGA
	CTGCCCAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACC
	GAGTCTCTTGCGAAATACAACATGAGAACACATCCAAGCAGTATTCTCTCTTCAAAAG
	TCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTCGAATACTTAAT
	TAAAGAATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGAC
	TCTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTG
	TCTCTGTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTC
	TGCTGTTAACCAGAAACCTACAAACCTTCCCkAGGTGGAAGAATCCCAGCAGAAAAAC
	ACCCCCCCAACAGACTCCCCCTCCAAAGCTGGGCCAAGAGGATCTGTCCAATATCTTC
	CTGACTTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCA
	TCTGGACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTG
	GAGCCTATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTG
	CTGAGTGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCATGAGAATC
	ACACAGAGTCTTCTGTAGGGGTATGGTGCGCCGCATGACATGGGAGGCGATGGGGACG
	ATGGACAGAGACAGAGCGTGCACACGTAGAGTGGCTAGTGAAGGACGCCTTTTTGACT
	CTTCTTGGTCTCAGCATGTTGACTGGGATTGGAAATAATGAGACTGAGCCCTCGGCTT
	GGGCTGCACTCTACCCTGTACACTGCCTTGTACCCTGAGCTGCATCACCTCCTAAACT
	GAGCAGTCTCATACCATGGAGAGATGCCTCTCTTATGTCTTCAGCCACTCACTTATAA
	AGATACTTATCTTTTCAGCAGTATATATGTGCTGAAATCTCAGCATGAAAGCATTGCA
	TGAGTAAAGATACTTTCCCTAAAAAAAAAAAAAAAA
	ORF Start: ATG at 85	ORF Stop: TGA at 1153
	SEQ ID NO: 84	356 aa	MW at 38961.8 kD
NOV28e,	MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD
CG135049-05
Protein Sequence	GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLETDCHVLRKKAWQDCGMRIFPESASTV
	SKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYSLFKVTRASSQWV
	VGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTHWEKFVSVTCDFFE
	SQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGSVQYLPDLDDKNSQ
	EKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKEKARTAECPGPAQN
	ASPLVLPP
	SEQ ID NO: 85	1511 bp
NOV28f,	AAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAGCTCCACAAACTGAC
CG135049-06
DNA Sequence	CCATCCTGGGCCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCAT
	CCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCT
	CTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGC
	GGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAACGA
	CGCCCAGGAATACAGACGGGTTTATGGTCAATGCAAAGCAATATTTTATATGAACAAC
	CCAAGTAGAGTTCTCTATTTAGCTGCTTATAACTGTACTCTTCGCCCAGTTTCAAAAA
	AAAAGATTTACATGACGTGCCCTGACTGCCCAAGCTCCATACCCACTGACTCTTCCAA
	TCACCAAGTGCTGGAGGCTGCCACCGAGTCTCTTGCGAAATACAACAATGAGAACACA
	TCCAAGCAGTATTCTCTCTTCAAAGTCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCC
	CTTCTTACTTTGTGGAATACTTAATTAAAGAATCACCATGTACTAAATCCCAGGCCAG
	CAGCTGTTCACTTCAGTCCTCCGACTCTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTG
	ACTCGAACACACTGGGAAAAGTTTGTCTCTCTGACTTGTGACTTCTTTGAATCACAGG
	CTCCAGCCACTGGAAGTGAAAACTCTGCTGTTAACCAGAAACCTACAAACCTTCCCAA
	GGTGGAAGAATCCCAGCAGAAAAACACCCCCCCAACAGACTCCCCCTCCAAAGCTGGG
	CCAAGAGGATCTGTCCAATATCTTCCTGACTTGGATGATAAAAATTCCCAGGAAAAGG
	GCCCTCAGGAGGCCTTTCCTGTGCATCTGGACCTAACCACGAATCCCCACGGAGAAAC
	CCTGGATATTTCCTTCCTCTTCCTGGAGCCTATGGAGGAGAAGCTGGTGGTCCTGCCT
	TTCCCCAAAGAAAAAGCACGCACTGCTGAGTGCCCAGGGCCAGCCCAGAATGCCAGCC
	CTCTTGTCCTTCCGCCATGAGAATCACACAGAGTCTTCTGTAGGGCTATGGTCCCCCG
	CATGACATGGGAGGCGATGGGGACGATGGACAGAGACAGAGCGTGCACACGTAGAGTG
	GCTAGTGAAGGACGCCTTTTTGACTCTTCTTGGTCTCAGCATGTTGACTGGCATTGGA
	AATAATGAGACTCAGCCCTCGGCTTGGGCTGCACTCTACCCTGTACACTGCCTTCTAC
	CCTGAGCTGCATCACCTCCTAAACTGAGCAGTCTCATACCATCGACAGATGCCTCTCT
	TATGTCTTCAGCCACTCACTTATAAAGATACTTATCTTTTCAGCAGTATATATGTGCT
	GAAATCTCAGCATGAAAGCATTGCATGAGTAAAGATACTTTCCCTAAAAAAAAAAAAA
	AAA
	ORF Start: ATG at 85	ORF Stop: TGA at 1120
	SEQ ID NO: 86	345 aa	MW at 37822.5 kD
NOV28f,	MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD
CG135049-06
Protein Sequence	GYVLRLNRVNDAQEYRRVYCQCKAIFYMNNPSRVLYLAAYNCTLRPVSKKKIYMTCPD
	CPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYSLFKVTRASSQWVVGPSYFVEYLI
	KESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTHWEKFVSVTCDFFESQAPATGSENS
	AVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGSVQYLPDLDDKNSQEKGPQEAFPVH
	LDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKEKARTAECPGPAQNASPLVLPP

[0480] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 28B.

TABLE 28B
Comparison of NOV28a against NOV28b through NOV28f.
			Identities/
			Similarities for
	Protein	NOV28a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV28b	17 . . . 382	337/366 (92%)
		17 . . . 369	337/366 (92%)
	NOV28c	17 . . . 382	337/366 (92%)
		17 . . . 369	337/366 (92%)
	NOV28d	140 . . . 382	225/243 (92%)
		75 . . . 317	226/243 (92%)
	NOV28e	17 . . . 382	321/366 (87%)
		17 . . . 356	321/366 (87%)
	NOV28f	17 . . . 382	313/366 (85%)
		17 . . . 345	313/366 (85%)

[0481] Further analysis of the NOV28a protein yielded the following properties shown in Table 28C.

TABLE 28C
Protein Sequence Properties NOV28a
PSort     0.8200 probability located in outside; 0.1900
analysis: probability located in lysosome (lumen); 0.1000
          probability located in endoplasmic reticulum
          (membrane); 0.1000 probability located
          in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 19 and 20
analysis:

[0482] 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
AAB75368	Human secreted protein #27 -	1 . . . 382	379/382 (99%)	0.0
	Homo sapiens, 382 aa.	1 . . . 382	379/382 (99%)
	[WO200100806-A2, 04 JAN. 2001]
AAB25782	Human secreted protein SEQ ID	1 . . . 382	379/382 (99%)	0.0
	#94 - Homo sapiens, 382 aa.	1 . . . 382	379/382 (99%)
	[WO200037491-A2, 29 JUN. 2000]
AAW88491	Human liver clone HP01263-	1 . . . 382	379/382 (99%)	0.0
	encoded transmembrane protein -	1 . . . 382	379/382 (99%)
	Homo sapiens, 382 aa.
	[WO9855508-A2, 10 DEC. 1998]
AAB51346	Human HS-glycoprotein-like	1 . . . 382	378/382 (98%)	0.0
	protein sequence SEQ ID NO: 5 -	1 . . . 382	379/382 (98%)
	Homo sapiens, 382 aa.
	[JP2000300275-A, 31 OCT. 2000]
AAB51347	Bovine HS-glycoprotein-like	10 . . . 381	245/377 (64%)	e−141
	protein sequence SEQ ID NO: 6 -	1 . . . 377	289/377 (75%)
	Bos taurus, 378 aa. [JP2000300275-
	A, 31 OCT. 2000]

[0483] 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
CAC24999	Sequence 43 from Patent	1 . . . 382	379/382 (99%)	0.0
	WO0100806 precursor - Homo	1 . . . 382	379/382 (99%)
	sapiens (Human), 382 aa.
Q9UGM5	Fetuin-B precursor (IRL685)	1 . . . 382	377/382 (98%)	0.0
	(16G2) - Homo sapiens (Human),	1 . . . 382	378/382 (98%)
	382 aa.
Q9QXC1	Fetuin-B precursor (IRL685) -	1 . . . 382	246/397 (61%)	e−135
	Mus musculus (Mouse), 388 aa.	1 . . . 388	297/397 (73%)
Q9QX79	Fetuin-B precursor (IRL685) -	1 . . . 377	238/388 (61%)	e−129
	Rattus norvegicus (Rat), 378 aa.	1 . . . 378	295/388 (75%)
Q9D763	2310011017Rik protein - Mus	61 . . . 382	208/334 (62%)	e−115
	musculus (Mouse), 325 aa.	1 . . . 325	254/334 (75%)

[0484] PFam analysis indicates that the NOV28a protein contains the domains shown in the Table 28F.

TABLE 28F
Domain Analysis of NOV28a
			Identities/
			Similarities for
	Pfam	NOV28a Match	the Matched	Expect
	Domain	Region	Region	Value
	cystatin	37 . . . 104	23/68 (34%)	5.4e−13
			52/68 (76%)
	cystatin	155 . . . 254	32/112 (29%)	6e−10
			70/112 (62%)

Example 29

[0485] 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: 87	2973 bp
NOV29a,	CGCCCCGGGCTGGCGATGCTGCGCCGCCCCGCTCCCGCGCTGGCCCCGGCCGCCCGGC
CG54912-02
DNA Sequence	TGCTGCTGGCCGGGCTGCTGTGCGGCGGCGGGGTCTGGGCCGCGCGAGTTAACAAGCA
	CAAGCCCTGGCTGGAGCCCACCTACCACGGCATAGTCACAGAGAACGACAACACCGTA
	CTCCTCGACCCCCCACTGATCGCGCTGGATAAAGATGCGCCTCTGCGATTTGCAGAGA
	GTTTTGAGGTGACAGTCACCAAAGAAGGTGAGATTTGTGGATTTAATTCACGCGCAAA
	GAATGTCCCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGC
	TCCAAAGAGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCT
	ATGATTGTGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGT
	TCATATTCAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTAC
	AAAGCCACGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGG
	ATGCCGACTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGA
	CGTGCCCTTTACTGTTGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTAC
	GGGAAAGAACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAG
	CCACAGAAGATGTTTTGGTGAAGATCAGCATTAAGCCCACCTGCACCCCTGGGTGGCA
	AGGATGGAACAACAGGATTGAGTATGAGCCGGGCACCGGCGCGTTGGCCGTCTTTCCA
	AATATCCACCTGCAGACATGTGACGAGCCAGTCGCCTCAGTACAGGCCACAGTGGAGC
	TAGAAACCAGCCACATAGGGAAAGGCTGCGACCGAGACACCTACTCAGAGAAGTCCCT
	CCACCGGCTCTGTGGTGCGGCCGCGGGCACTGCCGAGCTGCTGCCATCCCCGAGTGGA
	TCCCTCAACTGGACCATGGOCCTGCCCACCGACAATGGCCACCACAGCGACCAGGTGT
	TTGAGTTCAACGGCACCCAGGCAGTGAGGATCCCGGATGGCCTCGTGTCGGTCAGCCC
	CAAAGAGCCGTTCACCATCTCGGTGTGGATGAGACATGGGCCATTCGGCAGGAAGAAG
	GAGAGAATTCTTTGCAGTTCTGATAAAACAGATATGAATCGGCACCACTACTCCCTCT
	ATGTCCACGGGTGCCGGCTGATCTTCCTCTTCCGTCAGGATCCTTCTGAGGAGAAGAA
	ATACAGACCTGCAGAGTTCCACTGGAAGTTGAATCAGGTCTGTGATGAGGAATGGCAC
	CACTACGTCCTCAATGTAGAATTCCCGAGTCTGACTCTCTATGTGGATGGCACGTCCC
	ACGAGCCCTTCTCTGTGACTGAGGATTACCCGCTCCATCCATCCAAGATAGAAACTCA
	GCTCGTGGTGGGGGCTTGCTGGCAAGAGTTTTCAGGAGTTGAAAATGACAATGAAACT
	GAGCCTGTGACTGTGGCCTCTGCAGGTGGCGACCTGCACATGACCCAGTTTTTCCGAG
	GCAATCTGGCTGGCTTAACTCTCCGTTCCGGGAAACTCGCGGATAACAAGGTGATCGA
	CTGTCTGTATACCTGCAAGGAGGGGCTGGACCTGCAGGTCCTCGAAGACAGTGGCAGA
	GGCGTGCAGATCCAAGCACACCCCAGCCAGTTGGTATTGACCTTGGAGGGAGAAGACC
	TCGGGGAATTGGATAAGGCCATGCAGCACATCTCGTACCTGAACTCCCGGCAGTTCCC
	CACGCCCGGAATTCGCAGACTCAAATCACCAGCACAATCAAGTGTTTTAAACGAGGCC
	ACCTGCATTTCGGTCCCCCCGGTAGATGGCTACGTGATGGTTTTACAGCCCGAGGAGC
	CCAAGATCAGCCTGAGTGGCGTCCACCATTTTGCCCGAGCAGCTTCTGAATTTGAAAG
	CTCAGAAGCCGTGTTCCTTTTCCCTGAGCTTCGCATCATCAGCACCATCACGAGAGAA
	GTGGAGCCTGAAGGGGACGGGGCTGAGGACCCCACAGTTCAAGAATCACTGGTGTCCG
	AGGAGATCGTGCACGACCTGGATACCTGTGAGGTCACGGTGGAGGGAGAGGAGCTGAA
	CCACGAGCAGGAGAGCCTGGAGGTGGACATGGCCCGCCTGCAGCAGAAGGGCATTGAA
	GTGAGCAGCTCTGAACTGGGCATGACCTTCACAGGCGTGGACACCATGGCCAGCTACG
	AGGAGGTTTTGCACCTGCTGCGCTATCGGAACTGGCATGCCAGGTCCTTCCTTGACCG
	GAAGTTTAAGCTCATCTGCTCAGAGCTGAATGGCCGCTACATCAGCAACGAATTTAAG
	GTGGAGGTGAATGTAATCCACACGGCCAACCCCATGGAACACGCCAACCACATGGCTG
	CCCAGCCACAGTTCGTGCACCCGGAACACCGCTCCTTTGTTGACCTGTCAGGCCACAA
	CCTGGCCAACCCCCACCCGTTCGCAGTCGTCCCCAGCACTGCGACAGTTGTGATCGTG
	GTGTGCGTCAGCTTCCTGGTGTTCATGATTATCCTGGGGGTATTTCGGATCCGGGCCG
	CACATCGGCGGACCATGCGGGATCAGGACACCGGGAAGGAGAACGAGATGGACTGGGA
	CGACTCTGCCCTGACCATCACCGTCAACCCCATGGAGACCTATGAGGACCAGCACAGC
	AGTGAGGAGGAGGACGAAGAGGAAGAGGAAGAGGAAGCGAGGACGGCGIAAGAAGAGG
	ATGACATCACCAGCGCCGAGTCGGAGAGCAGCGAGGAGGAGGAGGGGGAGCAGGGCGA
	CCCCCAGAACGCAACCCGGCAGCAGCAGCTGGAGTGGGATGACTCCACCCTCAGCTAC
	TGACCCGTGCCCCCG
	ORF Start: ATG at 16	ORF Stop: TGA at 2959
	SEQ ID NO:88	981 aa	MW at 109791.7 kD
NOV29a,	MLRRPAPALAPAARLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPP
CG54912-02
Protein Sequence	LIALDKDAPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKL
	DCELQKDYSFTTQAYDCGKGPDGTNVKKSHKATVHIQVNDVNEYAPVFKEKSYKATVI
	EGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVPFTVDAAGYIKNTEKLNYGKEHQ
	YKLTVTAYDCGKKRATEDVLVKISIKPTCTPGWQGWNNRIEYEPGTGALAVFPNIHLE
	TCDEPVASVQATVELETSHIGKGCDRDTYSEKSLHRLCGAAAGTAELLPSPSGSLNWT
	MGLPTDNGHDSDQVFEFNGTQAVRIPDGVVSVSPKEPFTISVWMRHGPFGRKKETILC
	SSDKTDMNRHHYSLYVHGCRLIFLFRQDPSEEKKYRPAEFHWKLNQVCDEEWHHYVLN
	VEFPSVTLYVDGTSHEPFSVTEDYPLHPSKIETQLVVGACWQEFSGVENDNETEPVTV
	ASAGGDLHMTQFFRGNLAGLTLRSGKLADKKVIDCLYTCKEGLDLQVLEDSGRGVQIQ
	AHPSQLVLTLECEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISV
	PPVDGYVMVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEG
	DGAEDPTVQESLVSEEIVHDLDTCEVTVEGEELNHEQESLEVDMARLQQKGIEVSSSE
	LGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNEFKVEVNV
	IHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSF
	LVFMIILGVFRIRAAHRRTMRDQDTGKENEMDWDDSALTITVNPMETYEDQHSSEEEE
	EEEEAAEESEDGEEEDDITSAESESSEEEEGEQGDPQNATRQQQLEWDDSTLSY
	SEQ ID NO: 89	672 bp
NOV29b,	AGATCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG
207601301 DNA
Sequence	TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA
	TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC
	CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG
	AGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCTATGATTG
	TGGGAAGGGACCTGATGGCACCAACGTGATAAAGTCTCATAAAGCAACTGTTCATATT
	CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTACAAAGCCA
	CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA
	CTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC
	TTTACTGTCGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTACGGGAAAG
	AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA
	AGATGTTTTGGTGAAGATCAGCATTAAGCTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO 90	224 aa	MW at 25130.3 kD
NOV29b,	RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV
207601301
Protein Sequence	PFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVIKSHKATVHI
	QVNDVNEYAPVFKEKSYKATVIEGKQYDSTLRVEAVDADCSPQFSQICSYEIITPDVP
	FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE
	SEQ ID NO: 91	672 bp
NOV29c,	AGATCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG
207601309 DNA
Sequence	TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA
	TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC
	CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG
	AGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCTATGATTG
	TGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGTTCATATT
	CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTACAAAGCCA
	CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA
	CTGCTCCCCTCAGTTTAGCCACATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC
	TTTACTGTTGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTACGGGAAAG
	AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA
	AGATGTTTTGGTGAAGATCAGCATTAAGCTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 92	224 aa	MW at 25145.3 kD
NOV29c,	RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV
207601309
Protein Sequence	PFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHI
	QVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQTCSYEIITPDVP
	FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE
	SEQ ID NO: 93	702 bp
NOV29d	AGATCTGCGCCAGTTAACAAGCACAAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG
207601313 DNA
Sequence	TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA
	TGCGCCTCTGCGATTTGCAGAGAGTTTTGAGGTGACAGTCACCAAAGAAGGTGAGATT
	TGTGGATTTAAAATTCACGGGCAGAATGTCCCCTTTGATCCAGTGGTAGTGGATAAAT
	CCACTGGTGAGGGAGTCATTCGCTCCAAAGAGAAACTGGACTGTGAGCTGCAGAAAGA
	CTATTCATTCACCATCCAGGCCTGTGGTTGTGGGAAGGGACCTGATGGCACCAACGTG
	AAAAAGTCTCATAAAGCAACTGTTCATATTCAGGTGAACGACGTGAATGAGTACGCGC
	CCGTGTTCAAGGAGAAGTCCTACAAAGCCACGGTCATCGAGGGGAACCAGTACGACAG
	CATTTTGAGGGTGGAGGCCGTGGATGCCGACTGCTCCCCTCAGTTCAGCCAGATTTGC
	AGCTACGAAATCATCACTCCAGACGTGCCCTTTACTGTTGACAAAGATGGTTATATAA
	AAAACACAGAGAAATTAAACTACGGGAAAGAACATCAATATAAGCTGACCGTCACTGC
	CTATGACTGTGGGAAAAAAAGAGCCACAGAAGATGTTTTGGTGAAGATCAGCATTAAG
	CTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 94	234 aa	MW at 26177.4 kD
NOV29d,	RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAESFEVTVTKEGEI
207601313
Sequence	CGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQACGCGKGPDGTNV
	KKSHKATVHIQVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQIC
	SYEIITPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIK
	LE
	SEQ ID NO: 95	672 bp
NOV29e,	AGATCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG
207601331 DNA
Sequence	TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA
	TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC
	CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG
	AGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCTATGATTG
	TGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGTTCATATT
	CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAGGTCCTACAAAGCCA
	CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA
	CTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC
	TTTACTGTTGACAAAGATGGTTATATAAAAAACACACAGAAATTAAACTACGGGAAAG
	AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA
	AGATGTTTTGGTGAAGATCAGCATTAAGCTCCAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO:96	224 aa	MW at 25173.3 kD
NOV29e,	RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV
207601331
Protein Sequence	PFDAVVVDKSTGEGVTRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHI
	QVNDVNEYAPVFKERSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVP
	FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE
	SEQ ID NO: 97	672 bp
NOV29f,	AGATCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGACCCCACCTACCACGGCATAG
207639332 DNA
Sequence	TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA
	TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC
	CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG
	AGAAACTGGACTGTGAGCTGCACAAAGGCTATTCATTCACCATCCAGGCCTATGATTG
	TGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGTTCATATT
	CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTACAAAGCCA
	CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA
	CTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC
	TTTACTGTTGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTACGGGAAAG
	AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA
	AGATGTTTTGGTGAAGATCAGCATTAAGCTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 98	224 aa	MW at 25087.2 kD
NOV29f,	RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV
207639332
Protein Sequence	PFDAVVVDKSTGEGVIRSKEKLDCELQKGYSFTIQAYDCGKGPDGTNVKKSHKATVHI
	QVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVP
	FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE

[0486] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 29B.

TABLE 29B
Comparison of NOV29a against NOV29b through NOV29f.
			Identities/
			Similarities for
	Protein	NOV29a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV29b	28 . . . 258	219/231 (94%)
		2 . . . 222	220/231 (94%)
	NOV29c	28 . . . 258	220/231 (95%)
		2 . . . 222	221/231 (95%)
	NOV29d	28 . . . 258	228/231 (98%)
		2 . . . 232	229/231 (98%)
	NOV29e	28 . . . 258	219/231 (94%)
		2 . . . 222	221/231 (94%)
	NOV29f	28 . . . 258	219/231 (94%)
		2 . . . 222	220/231 (94%)

[0487] Further analysis of the NOV29a protein yielded the following properties shown in Table 29C.

TABLE 29C
Protein Sequence Properties NOV29a
PSort     0.4600 probability located in plasma membrane; 0.1030
analysis: probability located in microbody (peroxisome); 0.1000
          probability located in endoplasmic reticulum
          (membrane); 0.1000 probability located in endoplasmic
          reticulum (lumen)
SignalP   Cleavage site between residues 29 and 30
analysis:

[0488] 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 29D.

TABLE 29D
Geneseq Results for NOV29a
		NOV29a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAB93107	Human protein sequence SEQ ID	646 . . . 981	335/336 (99%)	0.0
	NO: 11970 - Homo sapiens, 336 aa.	1 . . . 336	336/336 (99%)
	[EP1074617-A2, 07 FEB. 2001]
AAU19843	Human novel extracellular matrix	50 . . . 331	270/282 (95%)	e−158
	protein, Seq ID No 493 - Homo	5 . . . 276	270/282 (95%)
	sapiens, 276 aa. [WO200155368-
	A1, 02 AUG. 2001]
AAW95631	Homo sapiens secreted protein gene	15 . . . 408	246/405 (60%)	e−146
	clone hj968_2 - Homo sapiens, 428	8 . . . 400	301/405 (73%)
	aa. [WO9856805-A1, 17 DEC.
	1998]
AAU91129	Human secreted protein sequence	514 . . . 949	198/444 (44%)	e−114
	#49 - Homo sapiens, 467 aa.	17 . . . 456	309/444 (69%)
	[WO200218412-A1, 07 MAR.
	2002]
AAB58434	Lung cancer associated polypeptide	514 . . . 944	195/444 (43%)	e−113
	sequence SEQ ID 772 - Homo	17 . . . 456	305/444 (67%)
	sapiens, 467 aa. [WO200055180-
	A2, 21 SEP. 2000]

[0489] 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 29E.

TABLE 29E
Public BLASTP Results for NOV29a
		NOV29a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
O94985	KIAA0911 protein - Homo	1 . . . 981	981/981 (100%)	0.0
	sapiens (Human), 981 aa.	1 . . . 981	981/981 (100%)
Q9EPL2	Calsyntenin-1 protein precursor -	1 . . . 981	907/981 (92%)	0.0
	Mus musculus (Mouse), 979 aa.	1 . . . 979	948/981 (96%)
Q9DDD3	Calsyntenin-1 protein - Gallus	31 . . . 981	818/952 (85%)	0.0
	gallus (Chicken), 948 aa	1 . . . 948	891/952 (92%)
	(fragment).
AAH29027	Hypothetical 83.0 kDa protein -	235 . . . 981	683/747 (91%)	0.0
	Mus musculus (Mouse), 745 aa	1 . . . 745	718/747 (95%)
	(fragment).
Q9H4D0	Calsyntenin-2 - Homo sapiens	28 . . . 981	528/968 (54%)	0.0
	(Human), 955 aa.	34 . . . 955	707/968 (72%)

[0490] PFam analysis indicates that the NOV29a protein contains the domains shown in the Table 29F.

TABLE 29F
Domain Analysis of NOV29a
			Identities/
			Similarities for
	Pfam	NOV29a Match	the Matched	Expect
	Domain	Region	Region	Value
	cadherin	42 . . . 155	30/127 (24%)	0.071
			72/127 (57%)
	cadherin	169 . . . 258	28/108 (26%)	0.0034
			61/108 (56%)

Example 30

[0491] 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: 99	24 bp
NOV30a,	TTTGAGCAAAACAGAAGACAGCCC
CG56315-03 DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 100	8 aa	MW at 1074.2kD
NOV30a,	FEQNRRQP
CG56315-03 Protein Sequence
	SEQ ID NO: 101	24 bp
NOV30b,	TTTGAGTGCAACAGGAGACAGCCC
CG56315-04 DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 102	8 aa	MW at 1049.2kD
NOV30b,	FECNRRQP
CG56315-04 Protein Sequence
	SEQ ID NO: 103	24 bp
NOV30c,	TTTGAGCAAAACAGTAGACAGCCC
CG56315-05 DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 104	8 aa	MW at 1005.1kD
NOV30c,	FEQNSRQP
CG56315-05 Protein Sequence
	SEQ ID NO: 105	24 bp
NOV30d,	TTTGAGTGCAACAGTAGACAGCCC
CG56315-06 DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 106	8 aa	MW at 980.1kD
NOV30d,	FECNSRQP
CG56315-06 Protein Sequence
	SEQ ID NO: 107	24 bp
NOV30e,	TTTGAGCAAAACAGTAGACAGGCC
CG56315-07 DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 108	8 aa	MW at 979.0kD
NOV30e,	FEQNSRQA
CG56315-07 Protein Sequence
	SEQ ID NO: 109	24 bp
NOV30f,	TTTGAGTGCAACAGTAGACAGGCC
CG56315-08 DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 110	8 aa	MW at 954.0kD
NOV30f,	FECNSRQA
CG56315-08 Protein Sequence

[0492] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 30B.

TABLE 30B
Comparison of NOV30a against NOV3Ob through NOV30f.
			Identities/
			Similarities for
	Protein	NOV30a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV30b	No Significant Alignment Found.
	NOV30c	1 . . . 8	7/8 (87%)
		1 . . . 8	7/8 (87%)
	NOV30d	No Significant Alignment Found.
	NOV30e	No Significant Alignment Found.
	NOV30f	No Significant Alignment Found.

[0493] Further analysis of the NOV30a protein yielded the following properties shown in Table 30C.

TABLE 30C
Protein Sequence Properties NOV30a
PSort analysis:
SignalP analysis: No Known Signal Sequence Indicated

[0494] 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 30D.

TABLE 30D
Geneseq Results for NOV30a
		NOV30a	Identities/
	Protein/	Residues/	Similarities for
Geneseq	Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
No Significant Matches Found

[0495] 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 30E.

TABLE 30E
Public BLASTP Results for NOV30a
		NOV30a	Identities/
Protein		Residues/	Similarities for
Accession	Protein/	Match	the Matched	Expect
Number	Organism/Length	Residues	Portion	Value
No Significant Matches Found

[0496] PFam analysis indicates that the NOV30a protein contains the domains shown in the Table 30F.

TABLE 30F
Domain Analysis of NOV30a
			Identities/
			Similarities for
		NOV30a	the Matched	Expect
	Pfam Domain	Match Region	Region	Value
No Significant Matches Found

Example 31

[0497] 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: 115	2628 bp
NOV31a,	ACCGTGCCTCTGCGGCCTGCGTGCCCGGAGTCCCCGCCTGTGTCGTCTCTGTCGCCGT
CG56326-01
DNA Sequence	CCCCGTCTCCTGCCAGGCGCGGAGCCCTGCGAGCCGCGGGTGGGCCCCAOGCGCGCAG
	ACATGGGCTGCTCCGCCAAAGCGCGCTGGGCTGCCGGGGCGCTGGGCGTCGNGGGGCT
	ACTGTGCGCTGTGCTCGGCGCTGTCATGATCGTGATGGTGCNGTCGCTCATCAAGCAG
	CAGGTCCTTAAGAACGTCCGCATCGACCCCAGTAGCCTGTCCTTCAACATGTGGAAGG
	AGATCCCTATCCCCTTCTATCTCTCCGTCTACTTCTTTGACGTCATGAACCCCAGCGA
	GATCCTGAAGGGCGAGAAGCCGCAGGTGCGGGAGCCCGGGCCCTACGTCTACAGGGAG
	TTCAGGCACAAAAGCAACATCACCTTCAACAACAACGACACCGTGTCCTTCCTCGAGT
	ACCGCACCTTCCAGTTCCAGCCCTCCAAGTCCCACGGCTCGGAGAGCGACTACATCGT
	CATGCCCAACATCCTGGTCTTGGGTGCGGCGGTGATGATGGAGAATAAGCCCATGACC
	CTGAAGCTCATCATGACCTTGGCATTCACCACCCTCGGCGAACGTGCCTTCATGAACC
	GCACTGTGGGTGAGATCATGTGGGGCTACAAGGACCCCCTTGTGAATCTCATCAACAA
	GTACTTTCCAGGCATGTTCCCCTTCAAGGACAAGTTCGGATTATTTGCTGAGCTCAAC
	AACTCCGACTCTGGGCTCTTCACGGTGTTCACGGGGGTCCAGAACATCAGCAGGATCC
	ACCTCGTGGACAAGTGGAACGGGCTGAGCAAGGTTGACTTCTGGCATTCCGATCAGTG
	CAACATGATCAATGGAACTTCTGGGCAAATGTGGCCGCCCTTCATGACTCCTGAGTCC
	TCGCTGGAGTTCTACAGCCCGGAGGCCTGCCGATCCATGAAGCTAATGTACAAGGAGT
	CAGGGGTGTTTGAAGGCATCCCCACCTATCGCTTCGTGGCTCCCAAAACCCTGTTTGN
	CAACGGGTCCATCTACCCACCCAACGAAGGCTTCTGCCCGTGCCTGGAGTCTGGAATT
	CAGAACGTCAGCACCTGCAGGTTCAGTGCCCCCTTGTTTCTCTCCCATCCTCACTTCC
	TCAACGCCGACCCGGTTCTGGCAGAAGNGGTGACTNNCCTGCACNCTAACCAGGAGGC
	ACACTCCTTGTTCCTGGACATCCACCCGGTCACGGGAATCCCCATGAACTGCTCTGTG
	AAACTGCAGCTGAGCCTCTACATGAAATCTGTCGCAGGCATTGGACAAACTGGGAAGA
	TTGAGCCTGTGGTCCTGCCGCTGCTCTGGTTTGCACAGAGCGGGGCCATGGAGGGGGA
	GACTCTTCACACATTCTACACTCAGCTGGTGTTGATGCCCAAGGTGATGCACTATGCC
	CAGTACGTCCTCCTGGCGCTGGGCTGCGTCCTGCTGCTGGTCCCTGTCATCTGCCAAA
	TCCGGAGCCAAGAGAAATGCTATTTATTTTGGAGTAGTAGTAAAAAGGGCTCAAAGGA
	TAAGGAGGCCATTCAGGCCTATTCTGAATCCCTGATGACATCAGCTCCCAAGGGCTCT
	GTGCTGCAGGAAGCAAAACTGTAGGCTCCTGAGGACACCGTGAGCCAGCCAGGCCTGG
	CCGCTGGGCCTGACCGGCCCCCCAGCCCCTACACNCCGCTTCTCCCGGACTCTCCCAG
	CAGACAGCCCCCCAGCCCCACAGCCTGAGCCTCCCAGCTGCCATGTCCCTGTTGCACA
	CCTGCACACACGCCCTGGCACACATACACACATGCGTGCAGGCTTGTGCAGACACTCA
	GGGATGGAGCTGCTGCTGAAGGGACTTGTAGGGAGAGGCTCGTCAACAACCACTGTTC
	TGGAACGTTCTCTCCACGTGGCCCACAGGCCTGACCACAGGGGCTGTGGGTCCTGCGT
	CCCCTTCCTCGGGTGAGCCTGGCCTGTCCCGTTCAGCCGTTGGGCCCAGGCTTCCTCC
	CCTCCAACGTGAAACACTGCAGTCCCGGTGTGGTGGCTCCCCATGCAGGACGGGCCAG
	GCTGGGAGTGCCGCCTTCCTGTGCCAAATTCAGTGGGGACTCAGTGCCCAGGCCGTGG
	CCACGAGCTTTGGCCTTGGTCTACCTGCCAGGCCAGGCAAAGCGCCTTTACACAGGCC
	TCGGAAAACAATGGAGTGAGCACAAGATGCCCTGTGCAGCTGCCCGAGGGTCTCCGCC
	CACCCCGGCCGGACTTTGATCCCCCCGAAGTCTTCACAGGCACTCCATCGGGTTGTCT
	GGCGCCCTTTTCCTCCAGCCTAAACTGACATCATCCTATGGACTGAGCCGGCCACTTT
	GGCCGAAGTGGCCGCAGGCTGTGCCCCCGAGCTGCCCCCACCCCCTCACAGGGTCCCT
	CAGATTATAGGTGCCCAGGCTGAGGTGAAGAGGCCTGGGGGCCCTGCCTTCCGGCCGC
	TCCTGGACCCTGGGGCAAACCTGTGACCCTTTTCTACTGGAATAGAAATGAGTTTTAT
	CATCTTTGAAAAATAATTCACTCTTGAAGTAATAAACGTTTAAAAAAATGGGAAAAAA
	AAAAAAAAAAAAAAAAAA
	ORF Start: at 218	ORF Stop: at 1745
	SEQ ID NO: 116	509 aa	MW at 56449.3kD
NOV31a,	MGCSAKARWAAGALGVXGLLCAVLGAVMIVMVXSLIKQQVLKNVRIDPSSLSFNMWKE
CG56326-01
Protein Sequence	IPIPFYLSVYFFDVMNPSEILKGEKPQVREPGPYVYREFRHKSNITFNNNDTVSFLEY
	RTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNR
	TVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIH
	LVDKWNGLSKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKES
	GVFEGIPTYRFVAPKTLFXNGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFL
	NADPVLAEXVTXLHXNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKI
	EPVVLPLLWFAESGAMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQI
	RSQEKCYLFWSSSKKGSKDKEAIQAYSESLMTSAPKGSVLQEAKL
	SEQ ID NO: 117	1248bp
NOV31b,	AGATCTCTCATCAAGCAGCAGGTCCTTAAGAACGTGCCCATCGACCCCAGTAGCCTGT
175070268 DNA
Sequence	CCTTCAACATGTGGAAGGAGATCCCTATCCCCTTCTATCTCTCCGTCTACTTCTTTGA
	CGTCATGAACCCCAGCGAGATCCTGAAGGGCGAGAAGCCGCAGGTGCGGGAGCGCGGG
	CCCTACGTGTACAGGGAGTTCAGGCACAAAAGCAACATCACCTTCAACAACAACGACA
	CCGTGTCCTTCCTCGAGTACCGCACCTTCCAGTTCCAGCCCTCCAAGTCCCACGGCTC
	GGAGAGCGACTACATCGTCATGCCCAACATCCTGGTCTTGGGTGCGGCGGTGATGATG
	GAGAATAAGCCCATGACCCTGAAGCTCATCATGACCTTGGCATTCACCACCCTCGGCG
	AACGTGCCTTCATGAACCGCACTGTGGGTGAGATCATGTGGGGCTACAAGGACCCCCT
	TGTGAATCTCATCAACAAGTACTTTCCAGGCATGTTCCCCTTCAAGGACAAGTTCGGA
	TTATTTGCTGAGCTCAACAACTCCGACTCTGGGCTCTTCACGGTGTTCACGGGGGTCC
	AGAACATCAGCAGGATCCACCTCGTGGACAAGTGGAACGGGCTGAGCAAGGTTGACTT
	CTGGCATTCCGATCAGTGCAACATGATCAATGGAAGTTCTGGGCAAATGTGGCCGCCC
	TTCATGACTCCTGAGTCCTCGCTGGAGTTCTACAGCCCGGAGGCCTGCCGATCCATGA
	AGCTAATGTACAAGGAGTCAGGGGTGTTTGAAGGCATCCCCACCTATCGCTTCGTGGC
	TCCCAAAACCCTGTTTGCCAACGGGTCCATCTACCCACCCAACGAAGGCTTCTGCCCG
	TGCCTGGAGTCTGGAATTCAGAACGTCAGCACCTGCAGGTTCAGTGCCCCCTTGTTTC
	TCTCCCATCCTCACTTCCTCAACGCCGACCCGGTTCTGGCAGAAGCGGTGACTGGCCT
	GCACCCTAACCAGGAGGCACACTCCTTGTTCCTGGACATCCACCCGGTCACGGGAATC
	CCCATGAACTGCTCTGTGAAACTGCAGCTGAGCCTCTACATGAAATCTGTCGCAGGCA
	TTGGACAAACTGGGAAGATTGAGCCTGTGGTCCTGCCGCTGCTCTGGTTTGCAGAGAG
	CGGGGCCATGGAGGGCGAGACTCTTCACACATTCTACACTCAGCTGGTGTTGATGCCC
	AAGGTGATGCACTATGCCCAGTACGTCGAC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 118	416 aa	MW at 47303.3kD
NOV31b,	RSLIKQQVLKNVRIDPSSLSFNMWKEIPIPFYLSVYFFDVMNPSEILKGEKPQVRERG
175070268
Protein Sequence	PYVYREFRHKSNITFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMM
	ENKPMTLKLIMTLAFTTLCERAFMNRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFG
	LFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCNMINCTSGQMWPP
	FMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYRFVAPKTLFANGSIYPPNEGFCP
	CLESGIQNXTSTCRFSAPLFLSHPHFLNADPVLAEAVTGLHPNQEAHSLFLDIHPVTGI
	PMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESGAJAEGETLHTFYTQLVLMP
	KVMHYAQYVD

[0498] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 31B.

TABLE 31B
Comparison of NOV31a against NOV31b.
			Identities/
			Similarities for
	Protein	NOV31a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV31b	34 . . . 447	409/414 (98%)
		2 . . . 415	409/414 (98%)

[0499] Further analysis of the NOV31a protein yielded the following properties shown in Table 31C.

TABLE 31C
Protein Sequence Properties NOV31a
PSort     0.5644 probability located in microbody (peroxisome);
analysis: 0.4600 probability located in plasma membrane;
          0.1000 probability located in endoplasmic reticulum
          (membrane); 0.1000 probability located in endoplasmic
          reticulum (lumen)
SignalP   Cleavage site between residues 35 and 36
analysis:

[0500] 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 31D.

TABLE 31D
Geneseq Results for NOV31a
		NOV31a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAW97900	Human SR-BI class B scavenger -	1 . . . 509	503/509 (98%)	0.0
	Homo sapiens, 509 aa.	1 . . . 509	503/509 (98%)
	[WO9902736-A2, 21 JAN. 1999]
AAW97899	Human SR-BI class B scavenger -	1 . . . 509	502/509 (98%)	0.0
	Homo sapiens, 509 aa.	1 . . . 509	502/509 (98%)
	[WO9902735-A2, 21 JAN. 1999]
ABB12012	Human SR-BI class B scavenger	1 . . . 509	501/509 (98%)	0.0
	homologue, SEQ ID NO: 2382 -	24 . . . 532	501/509 (98%)
	Homo sapiens, 532 aa.
	[WO200157188-A2, 09 AUG.
	2001]
AAY49573	Human CLA-1 protein sequence -	1 . . . 509	501/509 (98%)	0.0
	Homo sapiens, 509 aa.	1 . . . 509	501/509 (98%)
	[WO9950454-A2, 07 OCT. 1999]
ABG22317	Novel human diagnostic protein	1 . . . 509	485/514 (94%)	0.0
	#22308 - Homo sapiens, 537 aa.	24 . . . 537	490/514 (94%)
	[WO200175067-A2, 11 OCT. 2001]

[0501] 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 31E.

TABLE 31E
Public BLASTP Results for NOV31a
			Identities/
Protein			Similarities for
Accession		NOV31a Residues/	the Matched	Expect
Number	Protein/Organism/Length	Match Residues	Portion	Value
Q14016	CLA-1 - Homo sapiens (Human),	1 . . . 509	501/509 (98%)	0.0
	509 aa.	1 . . . 509	501/509 (98%)
Q8WTV0	Similar to CD36 antigen (collagen	1 . . . 467	460/467 (98%)	0.0
	type I receptor, thrombospondin	1 . . . 467	460/467 (98%)
	receptor)-like 1 - Homo sapiens
	(Human), 552 aa.
Q8SQC1	High density lipoprotein receptor	1 . . . 509	437/509 (85%)	0.0
	SR-BI - Sus scrofa (Pig), 509 aa.	1 . . . 509	474/509 (92%)
O18824	Scavenger receptor class B type 1 -	1 . . . 509	418/509 (82%)	0.0
	Bos taurus (Bovine), 509 aa.	1 . . . 509	462/509 (90%)
Q60417	HaSR-BI - Cricetulus griseus	1 . . . 509	409/509 (80%)	0.0
	(Chinese hamster), 509 aa.	1 . . . 509	455/509 (89%)

[0502] PFam analysis indicates that the NOV31a protein contains the domains shown in the Table 31F.

TABLE 31F
Domain Analysis of NOV31a
		Identities/
Pfam	NOV31a	Similarities for
Domain	Match Region	the Matched Region	Expect Value
CD36	5 . . . 445	213/567 (38%)	3.6e−227
		410/567 (72%)

Example 32

[0503] 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: 119	1284 bp
NOV32a,	ATGCATCTTATCGACTACCTGCTCCTCCTGCTGGTTCGACTACTGGCCCTTTCTCATG
CG56711-01
DNA Sequence	GCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGCAGAT
	TCTGGAGACAGGTGGGGGCTCCCCCAGCCTCPAGATAGCCCCTGCCAATGCTGACTTT
	GCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTTTTCT
	CCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCACACAG
	CCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTCCGAT
	GTCCATAGGGGCTTCCACCACCTCCTGCACACTCTGAACCTCCCCGGCCATGGGCTGG
	AAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAAAATT
	CCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTACGAC
	ACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGGAAGA
	TTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATTACAT
	TTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAAAGAC
	TTTTATGTTGATGAGAACACAACACTCCGGGTGCCCATGATGCTGCAGGACCAGGAGC
	ATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATTACAA
	AGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGATTGAA
	GAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACPACTTGTTGCGGAAGAGGAATT
	TTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATGTATT
	AGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGACTTA
	TCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCCACCT
	TGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCAAATT
	CTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGTGGTG
	ATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCCACGA
	AACCATAG
	ORF Start: ATG at 1	ORF Stop: TAG at 1282
	SEQ ID NO: 120	427 aa	MW at 48469.3kD
NOV32a,	MHLIDYLLLLLVGLLALSHGQLHVEHDGESCSNSSHQQILETGGGSPSLKIAPANADF
CG56711-01
Protein Sequence	AFRFYYLIASETPGKNIFFSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESD
	VHRGFQHLLHTLNLPGHGLETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYD
	TVGTIQLINDHVKKETRGKIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKD
	FYVDENTTVRVPMMLQDQEHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIE
	EVLTPEMLMRWNNLLRKRNFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADL
	SGITKQQKLEASKSFHKATLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVV
	IFSTSTQSVLFLGKVVDPTKP
	SEQ ID NO: 121	1233 bp
NOV32b,	GGATCCCAGCTGCACGTTGAGCATGATCGTGAGAGTTGCAGTAACAGCTCCCACCAGC
166280659 DNA
Sequence	AGATTCTGGAGACAGGTGAGGCCTCCCCCAGCCTGAAGATAGCCCCTGCCAATGCTGA
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTC
	CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCPA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CCACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT
	ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA
	AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGACGCATCCAAAAGTTTCCACAAGGCC
	ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA
	AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGACTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 122	411 aa	MW at 46775.1kD
NOV32b,	GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280659
Protein Sequence	FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG
	LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KTVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGTTKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF
	SEQ ID NO: 123	1233 bp
NOV32c,	GGATCCCAGCTGCACGTTCAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC
166280667 DNA
166280667 DNA	AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA
Sequence
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGACCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCAGCCAGATCCTTGAGGGCCTGGCCTTCAACCTCACCGAGCTGTCTGAGTC
	CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT
	ACATTTACTTCAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCGAGGG
	AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCCGTGCTACGGATGGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC
	ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA
	AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 124	411 aa	MW at 46775.1kD
NOV32e,	GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280667
Protein Sequence	FSPLSISAAYANLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG
	LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF
	SEQ ID NO: 125	1233 bp
NOV32d,	GGATCCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC
166280670 DNA
Sequence	AGATTCTGGACACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCAGCCAGATCCTTGAGGGCCTGCGCTTCAACCTCACCGAGCTGTCTGAGTC
	CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT
	ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA
	AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC
	ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA
	AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 126	411 aa	MW at 46775.1kD
NOV32d,	GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280670
Protein Sequence	FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG
	LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF
	SEQ ID NO: 127	1233 bp
NOV32e,	GGATCCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC
166280673 DNA
Sequence	AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCACCCAGATCCTTGAGCGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTC
	CGATGTCCATAGGCCCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGCGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGCACGTCTTGATGGTGCTGGTGAATT
	ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA
	AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATCATGCTGCAGGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACCGATGGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGCCTGGGCTTCACGGATCTGTTCTCCAAGTGCGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC
	ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA
	AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGACTCTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 128	411 aa	MW at 46775.1kD
NOV32e,	GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280673
Protein Sequence	FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRCFQHLLHTLNLPGHG
	LETRVOSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF
	SEQ ID NO: 129	1233 bp
NOV32f,	GGATCCCAGCTGCACGTTGAGCATGATCGTCAGAGTTGCAGTAACAGCTCCCACCAGC
166280680 DNA
Sequence	AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTCAGTC
	CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTCAAGTTCCTTGCAA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGCTGAATT
	ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA
	AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCACGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC
	AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGOCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 130	411 aa	MW at 46775.1kD
NOV32f,	GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280680
Protein Sequence	FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG
	LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF
	SEQ ID NO: 131	1233 bp
NOV32g,	GGATCCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC
166280703 DNA
Sequence	AGATTCTGCAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCAGCCAGATCCTTGAGGGCCTCCGCTTCAACCTCACCGAGCTGTCTGAGTC
	CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT
	ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA
	AGACTTTTATGTTGATGAGAACACAACACTCCGGGTGCCCATGATGCTGCAGGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATCGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCPAGTGGGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC
	ACCTTGGACGTGGATGAGGCTGGCACCGACGCTGCAGCAGCCACCAGCTTCGCGATCA
	AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 132	411 aa	MW at 46775.1kD
NOV32g,	GSQLHVEHDCESCSNSSHQQTLETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280703
Protein Sequence	FSPLSISAAYAMLSLGACSHSRSQILEGLCFNLTELSESDVHRGFQHLLHTLNLPGHG
	LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPNMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFATKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF
	SEQ ID NO: 133	1233 bp
NOV32h,	GGATCCCAGCTGCACGTTGAGCATGATGGTGAGACTTGCAGTAACAGCTCCCACCAGC
166280730 DNA
Sequence	AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA
	CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT
	TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC
	ACAGCCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTC
	CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG
	CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA
	AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA
	CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG
	AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT
	ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA
	AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG
	GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT
	ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT
	TGAAGAGGTTCTGACTCCAGAGATGCTAATGACGTGGAACAACTTGTTGCGGAAGAGG
	AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG
	TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA
	CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC
	ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA
	AATTCTTCTCTGCCCAGACGAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT
	GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC
	ACGAAACCAGAATTC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 134	411 aa	MW at 46775.1kD
NOV32h,	GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF
166280730
Protein Sequence	FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG
	LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG
	KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ
	EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR
	NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA
	TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP
	TKPEF

[0504] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 32B.

TABLE 32B
Comparison of NOV32a against NOV32b through NOV32h.
			Identities/
			Similarities for
	Protein	NOV32a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV32b	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)
	NOV32c	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)
	NOV32d	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)
	NOV32e	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)
	NOV32f	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)
	NOV32g	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)
	NOV32h	21 . . . 427	387/407 (95%)
		3 . . . 409	387/407 (95%)

[0505] Further analysis of the NOV32a protein yielded the following properties shown in Table 32C.

TABLE 32C
Protein Sequence Properties NOV32a
PSort     0.7809 probability located in outside; 0.4253 probability
analysis: located in lysosome (lumen); 0.2787 probability located
          in microbody (peroxisome); 0.1000 probability located
          in endoplasmic reticulum (membrane)
SignalP   Cleavage site between residues 21 and 22
analysis:

[0506] 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
AAE15747	Human protease inhibitor (PI)	1 . . . 427	425/427 (99%)	0.0
	4 (kallistatin) protein - Homo	1 . . . 427	426/427 (99%)
	sapiens, 427 aa.
	[WO200179227-A2, 25 OCT.
	2001]
AAM02223	Peptide #905 encoded by probe	1 . . . 216	215/216 (99%)	e−120
	for measuring human breast	1 . . . 216	215/216 (99%)
	gene expression - Homo
	sapiens, 216 aa.
	[WO200157270-A2, 09 AUG.
	2001]
AAM26911	Peptide #948 encoded by probe	1 . . . 216	215/216 (99%)	e−120
	for measuring placental gene	1 . . . 216	215/216 (99%)
	expression - Homo sapiens,
	216 aa. [WO200157272-A2,
	09 AUG. 2001]
AAM14496	Peptide #930 encoded by probe	1 . . . 216	215/216 (99%)	e−120
	for measuring cervical gene	1 . . . 216	215/216 (99%)
	expression - Homo sapiens,
	216 aa. [WO200157278-A2,
	09 AUG. 2001]
AAM66622	Human bone marrow expressed	1 . . . 216	215/216 (99%)	e−120
	probe encoded protein SEQ ID	1 . . . 216	215/216 (99%)
	NO: 26928 - Homo sapiens,
	216 aa. [WO200157276-A2,
	09 AUG. 2001]

[0507] 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
Q96BZ5	Hypothetical 48.5 kDa protein -	1 . . . 427	426/427 (99%)	0.0
	Homo sapiens (Human), 427 aa.	1 . . . 427	426/427 (99%)
P29622	Kallistatin precursor (Kallikrein	1 . . . 427	425/427 (99%)	0.0
	inhibitor) (Protease inhibitor 4) -	1 . . . 427	426/427 (99%)
	Homo sapiens (Human), 427 aa.
P97569	Kallistatin - Rattus norvegicus	1 . . . 425	241/425 (56%)	e−132
	(Rat), 423 aa.	1 . . . 422	312/425 (72%)
O46519	Alpha-1-antitrypsin - Equus	4 . . . 426	202/427 (47%)	9e−97
	caballus (Horse), 421 aa.	5 . . . 420	273/427 (63%)
O54760	Alpha-1-antitrypsin-like protein	4 . . . 426	201/427 (47%)	4e−96
	CM55-SI precursor - Tamias	5 . . . 412	269/427 (62%)
	sibiricus (Siberian chipmunk)
	(Asian chipmunk), 413 aa.

[0508] PFam analysis indicates that the NOV32a protein contains the domains shown in the Table 32F.

TABLE 32F
Domain Analysis of NOV32a
			Identities/
			Similarities for
	Pfam	NOV32a Match	the Matched	Expect
	Domain	Region	Region	Value
	serpin	48 . . . 424	193/397 (49%)	1.6e−171
			317/397 (80%)

Example 33

[0509] 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: 135	24 bp
NOV33a,	TTTGTCCAAAACAGGCTGCAGCCG
CG57658-02
DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 136	8 aa	MW at 1001.2 kD
NOV33a,	FVQNRLQP
CG57658-02
Protein Sequence
	SEQ ID NO: 137	24 bp
NOV33b,	TTTGTCTGCAACAGGCTGCAGCCG
CG57658-03
DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 138	8 aa	MW at 976.2 kD
NOV33b,	FVCNRLQP
CG57658-03
Protein Sequence
	SEQ ID NO: 139	24 bp
NOV33c,	TTTGTCCAAAACACGCTGCAGCCG
CG57658-04
DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 140	8 aa	MW at 946.1 kD
NOV33c,	FVQNTLQP
CG57658-04
Protein Sequence
	SEQ ID NO: 141	24 bp
NOV33d,	TTTGTCTGCAACACGCTGCAGCCG
CG57658-05
DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 142	8 aa	MW at 921.1 kD
NOV33d,	FVCNTLQP
CG57658-05
Protein Sequence
	SEQ ID NO: 143	24 bp
NOV33e,	TTTGTCCAAAACACGCTGCAGGCG
CG57658-06
DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 144	8 aa	MW at 920.0 kD
NOV33e,	FVQNTLQA
CG57658-06
Protein Sequence
	SEQ ID NO: 145	24 bp
NOV33f,	TTTGTCTGCAACACGCTGCAGGCG
CG57658-07
DNA Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 146	8 aa	MW at 895.0 kD
NOV33f,	FVCNTLQA
CG57658-07
Protein Sequence

[0510] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 33B.

TABLE 33B
Comparison of NOV33a against NOV33b through NOV33f.
			Identities/
		NOV33a Residues/	Similarities for
	Protein Sequence	Match Residues	the Matched Region
	NOV33b	No Significant Alignment Found.
	NOV33c	1 . . . 8	7/8 (87%)
		1 . . . 8	7/8 (87%)
	NOV33d	No Significant Alignment Found.
	NOV33e	No Significant Alignment Found.
	NOV33f	No Significant Alignment Found.

[0511] Further analysis of the NOV33a protein yielded the following properties shown in Table 33C.

TABLE 33C
Protein Sequence Properties NOV33a
PSort analysis:
SignalP analysis: No Known Signal Sequence Indicated

[0512] 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/
	Protein/Organism/	Residues/	Similarities
Geneseq	Length	Match	for the	Expect
Identifier	[Patent #, Date]	Residues	Matched Region	Value
No Significant Matches Found

[0513] 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
		NOV33a	Identities/
Protein		Residues/	Similarities
Accession	Protein/Organism/	Match	for the	Expect
Number	Length	Residues	Matched Portion	Value
No Significant Matches Found

[0514] PFam analysis indicates that the NOV33a protein contains the domains shown in the Table 33F.

TABLE 33F
Domain Analysis of NOV33a
			Identities/
			Similarities
	Pfam	NOV33a Match	for the	Expect
	Domain	Region	Matched Region	Value
No Significant Matches Found

Example 34

[0515] 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: 149	72 bp
NOV34a,	CAGGAGACACGGAACGCCAAGGGC
CG57664-02	CACGCGCAGATTTACCGAGTGAAC
DNA	CTGCGGACCCTGCTCCGCTATTAC
Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 150	24 aa	MW at 2964.4 kD
NOV34a,	QETRNAKGHAQIYRVNLRTLLRYY
CG57664-02
Protein
Sequence

[0516] Further analysis of the NOV34a protein yielded the following properties shown in Table 34B.

TABLE 34B
Protein Sequence Properties NOV34a
PSort     0.8500 probability located in lysosome (lumen); 0.5392
analysis: probability located in nucleus; 0.1000 probability
          located in mitochondrial matrix space; 0.0000
          probability located in endoplasmic reticulum (membrane)
SignalP   No Known Signal Sequence Indicated
analysis:

[0517] 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 34C.

TABLE 34C
Geneseq Results for NOV34a
		NOV34a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length [Patent	Match	the Matched	Expect
Identifier	#, Date]	Residues	Region	Value
AAM23917	Rhesus monkey EST encoded	1 . . . 24	24/24 (100%)	3e−07
	protein SEQ ID NO: 1442 - Macaca	125 . . . 148	24/24 (100%)
	mulatta, 153 aa. [WO200154477-
	A2, 02 AUG. 2001]
AAB58652	Murine class I H-2 protein #5 - Mus	1 . . . 24	16/24 (66%)	0.025
	musculus, 311 aa. [US6153408-A,	62 . . . 85	20/24 (82%)
	28 NOV. 2000]
AAY52891	Murine class I molecule H-2D-d	1 . . . 24	16/24 (66%)	0.025
	peptide SEQ ID NO: 69 - Mus sp,	62 . . . 85	20/24 (82%)
	311 aa. [US5976551-A, 02 NOV.
	1999]
AAY68237	Murine class I molecule protein SEQ	1 . . . 24	16/24 (66%)	0.025
	ID NO: 69 - Mus sp, 311 aa.	62 . . . 85	20/24 (82%)
	[US6011146-A, 04 JAN. 2000]
AAB58650	Murine class I H-2 protein #3 - Mus	3 . . . 24	16/22 (72%)	0.043
	musculus, 350 aa. [US6153408-A,	64 . . . 85	19/22 (85%)
	28 NOV. 2000]

[0518] 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 34D.

TABLE 34D
Public BLASTP Results for NOV34a
		NOV34a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q30714	MHC class I antigen Mamu B*06 -	1 . . . 24	19/24 (79%)	0.004
	Macaca mulatta (Rhesus macaque),	18 . . . 41	20/24 (83%)
	294 aa.
Q95H92	Similar to histocompatibility 2, Q	1 . . . 24	17/24 (70%)	0.010
	region locus 7 - Mus musculus	89 . . . 112	21/24 (86%)
	(Mouse), 332 aa.
Q31152	MHC class I Q4 beta-2-	1 . . . 24	17/24 (70%)	0.010
	microglobulin (Qb-1) - Mus	83 . . . 106	21/24 (86%)
	musculus (Mouse), 326 aa
	(fragment).
Q9QYQ3	A1h - Rattus norvegicus (Rat), 346	1 . . . 24	17/24 (70%)	0.013
	aa (fragment).	62 . . . 85	20/24 (82%)
Q951L1	MHC class I antigen - Felis	1 . . . 24	17/24 (70%)	0.017
	silvestris catus (Cat), 62 aa	34 . . . 57	20/24 (82%)
	(fragment).

[0519] PFam analysis indicates that the NOV34a protein contains the domains shown in the Table 34E.

TABLE 34E
Domain Analysis of NOV34a
		Identities/
		Similarities
	NOV34a Match	for the
Pfam Domain	Region	Matched Region	Expect Value
MHC_I	1 . . . 24	16/24 (67%)	6.1e−07
		24/24 (100%)

Example 35

[0520] 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: 153	72 bp
NOV35a,	CGGAACACACAGATCTGCAAGGCC
CG57668-02	CAAGCACGGACTGAACGAGAGAAC
DNA	CTGCGGATCGCGCTCCGCTACTAC
Sequence
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 154	24 aa	MW at 2967.4 kD
NOV35a,	RNTQICKAQARTERENLRIALRYY
CG57668-02
Protein
Sequence

[0521] Further analysis of the NOV35a protein yielded the following properties shown in Table 35B.

TABLE 35B
Protein Sequence Properties NOV35a
PSort     0.8191 probability located in mitochondrial
analysis: intermembrane space; 0.5581 probability located in
          mitochondrial matrix space; 0.5500 probability located
          in nucleus; 0.3285 probability located in lysosome
          (lumen)
SignalP   No Known Signal Sequence Indicated
analysis:

[0522] 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/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length [Patent	Match	the Matched	Expect
Identifier	#, Date]	Residues	Region	Value
AAM05915	Peptide #4597 encoded by probe for	1 . . . 24	24/24 (100%)	5e−07
	measuring breast gene expression -	51 . . . 74	24/24 (100%)
	Homo sapiens, 79 aa.
	[WO200157270-A2, 09 AUG. 2001]
AAM18309	Peptide #4743 encoded by probe for	1 . . . 24	24/24 (100%)	5e−07
	measuring cervical gene expression -	51 . . . 74	24/24 (100%)
	Homo sapiens, 79 aa.
	[WO200157278-A2, 09 AUG. 2001]
AAM70472	Human bone marrow expressed	1 . . . 24	24/24 (100%)	5e−07
	probe encoded protein SEQ ID NO:	51 . . . 74	24/24 (100%)
	30778 -Homo sapiens, 79 aa.
	[WO200157276-A2, 09 AUG. 2001]
AAW33794	Peptide B2702.60-84 tested for	1 . . . 23	19/23 (82%)	3e−04
	immunomodulating activity -	3 . . . 25	22/23 (95%)
	Synthetic, 25 aa. [WO9744351-A1,
	27 NOV. 1997]
AAR83090	HLA-B2702 CTL modulating	1 . . . 23	19/23 (82%)	3e−04
	peptide (B2702.60-84) - Synthetic,	3 . . . 25	22/23 (95%)
	25 aa. [WO9526979-A1, 12 OCT.
	1995]

[0523] 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		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Values
CAB22750	HLA-H PROTEIN - Homo sapiens	1 . . . 24	24/24 (100%)	1e−06
	(Human), 90 aa (fragment).	62 . . . 85	24/24 (100%)
HLHU12	MHC class I histocompatibility	1 . . . 24	23/24 (95%)	3e−06
	antigen HLA alpha chain precursor	83 . . . 106	24/24 (99%)
	(clone pHLA 12.4) - human, 359
	aa.
CAB66931	Gogo-H protein - Gorilla gorilla	1 . . . 24	23/24 (95%)	3e−06
	(gorilla), 359 aa (fragment).	83 . . . 106	24/24 (99%)
CAB22754	HLA-H PROTEIN - Homo sapiens	1 . . . 24	23/24 (95%)	3e−06
	(Human), 90 aa (fragment).	62 . . . 85	24/24 (99%)
CAB22753	HLA-H PROTEIN - Homo sapiens	1 . . . 24	23/24 (95%)	3e−06
	(Human), 90 aa (fragment).	62 . . . 85	24/24 (99%)

[0524] PFam analysis indicates that the NOV35a protein contains the domains shown in the Table 35E.

TABLE 35E
Domain Analysis of NOV35a
		Identities/
		Similarities
	NOV35a Match	for the
Pfam Domain	Region	Matched Region	Expect Value
MHC_I	1 . . . 24	13/24 (54%)	0.00021
		23/24 (96%)

Example 36

[0525] The NOV36 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 36A.

TABLE 36A
NOV36 Sequence Analysis
	SEQ ID NO: 157	72 bp
NOV36a,	GAGGAGACACGGAACACCAAGGCCC
CG59256-02	ACGCACAGACTGACAGAATGAACCT
DNA	GCAGACCCTGCGCGGCTACTAC
Sequence
	QRF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 158	24 aa	MW at 2897.2 kD
NOV36a,	EETRNTKAHAQTDRMNLQTLRGYY
CG59256-02
Protein
Sequence

[0526] Further analysis of the NOV36a protein yielded the following properties shown in Table 36B.

TABLE 36B
Protein Sequence Properties NOV36a
PSort     0.8169 probability located in lysosome (lumen); 0.6500
analysis: probability located in cytoplasm; 0.1000 probability
          located in mitochondrial matrix space; 0.0000
          probability located in endoplasmic reticulum (membrane)
SignalP   No Known Signal Sequence Indicated
analysis:

[0527] 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/
		Residues/	Similarities for
Geneseq	Protein/Organism/	Match	the Matched	Expect
Identifier	Length [Patent #, Date]	Residues	Region	Value
AAU79455	HLA-G recombinant protein 2 -	1 . . . 24	24/24 (100%)	2e−07
	Homo sapiens, 234 aa.	93 . . . 116	24/24 (100%)
	[WO200222784-A2, 21 MAR.
	2002]
AAU79454	HLA-G recombinant protein 1 -	1 . . . 24	24/24 (100%)	2e−07
	Homo sapiens, 326 aa.	93 . . . 116	24/24 (100%)
	[WO200222784-A2, 21 MAR.
	2002]
AAU79450	HLA-G alpha1 domain protein -	1 . . . 24	24/24 (100%)	2e−07
	Homo sapiens, 92 aa.	64 . . . 87	24/24 (100%)
	[WO200222784-A2, 21 MAR.
	2002]
AAM48340	Human leukocyte antigen,	1 . . . 24	24/24 (100%)	2e−07
	HLA-G7 - Homo sapiens, 116	86 . . . 109	24/24 (100%)
	aa. [WO200196564-A2, 20
	DEC. 2001]
AAM02055	Peptide #737 encoded by probe	1 . . . 24	24/24 (100%)	2e−07
	for measuring human breast	61 . . . 84	24/24 (100%)
	gene expression - Homo
	sapiens, 89 aa. [WO200157270-
	A2, 09 AUG. 2001]

[0528] 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		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
CAD20672	Sequence 7 from Patent	1 . . . 24	24/24 (100%)	3e−07
	WO0196564 - Homo sapiens	86 . . . 109	24/24 (100%)
	(Human), 116 aa.
Q31611	B2 microglobulin - Homo sapiens	1 . . . 24	24/24 (100%)	3e−07
	(Human), 246 aa.	86 . . . 109	24/24 (100%)
Q8WLP2	MHC-G protein - Homo sapiens	1 . . . 24	24/24 (100%)	3e−07
	(Human), 165 aa (fragment).	52 . . . 75	24/24 (100%)
Q8WLS1	HLA-G histocompatibility	1 . . . 24	24/24 (100%)	3e−07
	antigen, class I, G - Homo sapiens	86 . . . 109	24/24 (100%)
	(Human), 338 aa.
Q95391	HLA-G - Homo sapiens(Human),	1 . . . 24	24/24 (100%)	3e−07
	182 aa (fragment).	62 . . . 85	24/24 (100%)

[0529] PFam analysis indicates that the NOV36a protein contains the domains shown in the Table 36E.

TABLE 36E
Domain Analysis of NOV36a
			Identities/
			Similarities for
	Pfam	NOV36a	the Matched	Expect
	Domain	Match Region	Region	Value
	MHC_I	1 . . . 24	13/24 (54%)	2.1e−05
			23/24 (96%)

Example 37

[0530] 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: 161	555 bp
NOV37a,	ATGCACAGCCACCGCGACTTCCAGCCGGTGCTCCACCTGGTTGCGCTCAACAGCCCCC
CG59437-01
DNA Sequence	TGTCAGGCGGCATGCGGGGCATCCGCGGGGCCGACTTCCAGTGCTTCCAGCAGGCGCG
	GGCCGTGGGGCTGGCGGGCACCTTCCGCGCCTTCCTGTCCTCGCGCCTGCACGACCTG
	TACAGCATCGTGCGCCGTGCCGACCGCGCAGCCGTGCCCATCGTCAACCTCAAGGACG
	AGCTGCTGTTTCCCAGCTGGGAGGCTCTGTTCTCAGGCTCTGAGGGTCCGCTGAAGCC
	CGGGGCACGCATCTTCTCCTTTAACGGCAAGGACGTCCTGACCCACCCCACCTGGCCC
	CAGAAGAGCGTGTGGCATGGCTCGGACCCCAACGGGCGCAGGCTGACCGAGAGCTACT
	GTGAGACGTGGCGGACGGAGGCTCCCTCGGCCACGGGCCAGGCCTACTCGCTGCTGGG
	GGGCAGGCTCCTGGGGCAGAGTGCCGCGAGCTGCCATCACGCCTACATCGTGCTATGC
	ATTGAGAACAGCTTCATGACTGCCTCCPAGTAG
	ORF Start: ATG at 1	ORF Stop: TAG at 553
	SEQ ID NO: 162	184 aa	MW at 20246.8kD
NOV37a,	MHSHRDPQPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDL
CG59437-01
Protein Sequence	YSIVRRADRAAVPIVNLKDELLFPSWEALFSGSEGPLKPGARTFSFNGKDVLTHPTWP
	QKSVWHGSDPNGRRLTESYCETWRTEAPSATGQAYSLLGGRLLGQSAASCHHAYIVLC
	IENSFMTASK
	SEQ ID NO: 163	482 bp
NOV37b,	GGATCCGGCATGCGGGGCATCCGCGGGGCCGACTTCCAGCGCTTCCACCAGGCGCGGA
170108827 DNA
Sequence	AGGTGCCCGCCAGCCCCACGGCCCGCGCCTGCAGGACCTGTACAGCATCGTGCGCCGT
	GCCGACCGCGCAGCCGTGCCCATCGTCAACCTCAAGGACGAGCTGCTGTTTCCCAGCT
	GGGAGGCCCTGTTCTCAGGCTCTGAGGGTCCGCTGAAGCCCGGGGCACGCATCTTCTC
	CTTTGACGGCAAGGACGTCCTGAGGCACCCCACCTGGCCCCAGAAGAGCGTGTGGCAT
	GGCTCGGACCCCAACGGGCCCAGGCTGACCGAGAGCTACTGTGAGACGTGGCGGACGG
	AGGCTCCCTCGGCCACGGGCCAGCCCTCCTCGCTGCTGGGGGGCAGGCTCCTGGGGCA
	GAGTGCCGCGAGCTGCCATCACGCCTACATCGTGCTCTGCATTGAGAACAGCTTCATG
	ACTGCCTCCAAGCTCGAG
	ORF Start: at 3	ORF Stop: end of sequence
	SEQ ID NO: 164	160 aa	MW at 17488.6kD
NOV37b,	IRHAGHPRGRLPALPAGAEGARQPHGPRLQDLYSIVRRADRAAVPIVNLKDELLFPSW
170108827
Protein Sequence	EALFSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTE
	APSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFMTASKLE
	SEQ ID NO: 165	480 bp
	NOV37c,	GGATCCGGCATGCGGGGCATCCGCGGGGCCGACTTCCAGTGCTTCCAGCAGGCGCGGA
	170108863 DNA
	Sequence	AGGTGCCCGCCAGCCCCACGGCCCGCGCCTGCAGGACCTGTACAGCATCGTGCGCCGT
		GCCGACCGCGCAGCCGTGCCCATCGTCAACCTCAAGGACGAGCTGCTQTTTCCCAGCT
		GGGAGGCTCTGTTCTCAGGCTGAGGGTCCGCTGAAGCCCGGGGCACCCATCTTCTCCT
		TTGACCGCAAGGACGTCCTGAGGCACCCCACCTCGCCCCAGAAGAGCGTGTGGCATGG
		CTCGGACCCCAACGGGCGCAGGCTGACCGAGAGCTACTGTGAGACGTGGCGGACGGAG
		GCTCCCTCGGCCACGGGCCAGGCCTCCTCCCTGCTGGGGGGCAGGCTCCTGGCGCAGA
		GTCCCGCGAGCTGCCATCACGCCTACATCGTGCTCTGCATTGAGAACAGCTTCATGAC
		TGCCTCCAAGCTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 166	160 aa	MW at 17082.1kD
NOV37c,	GSGMRGIRGADFQCFQQARKVPASPTARACRTCTASCAVPTAQPCPSSTSRTSCCFPA
170108863
Protein Sequence	GRLCSQAEGPLKPGARIFSFDGKDVLRHRTWPQKSVWHGSDPNGRRLTESYCETWRTE
	APSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFNTASKLE

[0531] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 37B.

TABLE 37B
Comparison of NOV37a against NOV37b and NOV37c.
		Identities/
		Similarities for
Protein	NOV37a Residues/	the Matched
Sequence	Match Residues	Region
NOV37b	54 . . . 184	111/131 (84%)
	28 . . . 158	112/131 (84%)
NOV37c	23 . . . 184	95/162 (58%)
	3 . . . 158	99/162 (60%)

[0532] Further analysis of the NOV37a protein yielded the following properties shown in Table 37C.

TABLE 37C
Protein Sequence Properties NOV37a
PSort     0.7480 probability located in microbody (peroxisome);
analysis: 0.2213 probability located in lysosome (lumen); 0.1000
          probability located in mitochondrial matrix space;
          0.0000 probability located in endoplasmic reticulum
          (membrane)
SignalP   No Known Signal Sequence Indicated
analysis:

[0533] 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 37D.

TABLE 37D
Geneseq Results for NOV37a
		NOV37a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent#, Date]	Residues	Region	Value
AAU76689	Synthetic plasmid pEnd-HR#1 FPD	2 . . . 184	180/183 (98%)	e−103
	fusion protein sequence - Chimeric -	93 . . . 275	181/183 (98%)
	Mus sp, 275 aa. [WO200210372-
	A1, 07 FEB. 2002]
AAU76688	Human collagen XVIII 1alpha NCI	2 . . . 184	180/183 (98%)	e−103
	domain protein sequence - Homo	128 . . . 310	181/183 (98%)
	sapiens, 310 aa. [WO200210372-
	A1, 07 FEB. 2002]
AAM49503	Human endostatin protein - Homo	2 . . . 184	180/183 (98%)	e−103
	sapiens, 183 aa. [CN1177005-A,	1 . . . 183	181/183 (98%)
	25 MAR. 1998]
AAM48895	Human endostatin protein - Homo	2 . . . 184	180/183 (98%)	e−103
	sapiens, 183 aa. [WO200193897-	1 . . . 183	181/183 (98%)
	A2, 13 DEC. 2001]
AAB49379	Human endostatin SEQ ID NO: 2 -	2 . . . 184	180/183 (98%)	e−103
	Homo sapiens, 183 aa.	1 . . . 183	181/183 (98%)
	[WO200067771-A1, 16 NOV.
	2000]

[0534] 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 37E.

TABLE 37E
Public BLASTP Results for NOV37a
		NOV37a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
A53019	collagen alpha 1(XVIII) chain -	2 . . . 184	180/183 (98%)	e−103
	human, 684 aa (fragment).	502 . . . 684	181/183 (98%)
AAM52249	Multi-functional protein MFP -	2 . . . 184	180/183 (98%)	e−103
	Homo sapiens (Human), 261 aa.	79 . . . 261	181/183 (98%)
Q8WX15	Collagen XVIII - Homo sapiens	2 . . . 184	180/183 (98%)	e−103
	(Human), 187 aa (fragment).	5 . . . 187	181/183 (98%)
P39060	Collagen alpha 1(XVIII) chain	2 . . . 184	180/183 (98%)	e−103
	precursor [Contains: Endostatin] -	1334 . . . 1516	181/183 (98%)
	Homo sapiens(Human), 1516 aa.
B56101	collagen alpha 1(XVIII) chain	2 . . . 182	152/181 (83%)	4e−88
	precursor, long splice form -	1591 . . . 1771	168/181 (91%)
	mouse, 1774 aa.

[0535] PFam analysis indicates that the NOV37a protein contains the domains shown in the Table 37F.

TABLE 37F
Domain Analysis of NOV37a
			Identities/
			Similarities for
	Pfam	NOV37a	the Matched	Expect
	Domain	Match Region	Region	Value
No Significant Matches Found

Example 38

[0536] 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: 167	678 bp
NOV38a,	GCTGCTGCAGTTGCCATGGTACAAGGGATGGGTTGTGGATTAGAGTTGGCATACTTGG
CG59739-01
DNA Sequence	CAGCCCGCTGCTTGATGAATGCAGCCAACAGCTGGGGGTTGGCGTGAAGGATACTAAG
	CACCTGTCGCTGCTGCAGTTGCCATGGTGACAAGGGTTGCTGGCACAAGGATCTGCAA
	CAAGCTGGCAGCTAGAATTCAGCGGCCGCTGAATTCTAGCTTCAACTTCACTACTTCT
	GTAGTCTCATCTTGAGTAAAAGAGAACCCAGCCAACTATGAAGTTCCTTGTCTTTGCC
	TTCATCTTGGCTCTCATGGTTTCCATGATTGGAGCTGATTCATCTGAAGAGAAATTTT
	TGCGTAGAATTGGAAGATTCGGTTATGGGTATGGCCCTTATCAGCCAGTTCCAGAACA
	ACCACTATACCCACAACCATACCAACCACAATACCAACAATATACCTTTTAATATCAT
	CAGTAACTGCAGGACATGATTATTGAGGCTTGATTGGCAAATACGACTTCTACATCCA
	TATTCTCATCTTTCATACCATATCACACTACTACCACTTTTTGAAGAATCATCAAAGA
	GCAATGCAAATGAAAAACACTATAATTTACTGTATACTCTTTGTTTCAGGATACTTGC
	CTTTTCAATTGTCACTTGATCATATAATTGCATTTAAACT
	ORF Start: ATG at 270	ORF Stop: TAA at 456
	SEQ ID NO: 168	62 aa	MW at 7304.4kD
NOV38a,	MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQ
CG59739-01
Protein Sequence	QYTF
	SEQ ID NO: 169	141 bp
NOV38 b,	GGATCCGATTCATCTGAAGAGAAATTTTTGCGTAGAATTGGAAGATTCGGTTATGGGT
169679148 DNA
Sequence	ATGGCCCTTATCAGCCAGTTCCAGAACAACCACTATACCCACAACCATACCAACCACA
	ATACCAACAATATACCTTTCTCGAG
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 170	47 aa	MW at 5606.1kD
NOV38b	GSDSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTFLE
169679148
Protein Sequence

[0537] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 38B.

TABLE 38B
Comparison of NOV38a against NOV38b.
	NOV38a	Identities/
	Residues/	Similarities
Protein	Match	for the
Sequence	Residues	Matched Region
NOV38b	18 . . . 38	20/21 (95%)
	1 . . . 21	21/21 (99%)

[0538] Further analysis of the NOV38a protein yielded the following properties shown in Table 38C.

TABLE 38C
Protein Sequence Properties NOV38a
PSort     0.8200 probability located in outside;
analysis: 0.3016 probability located in microbody
          (peroxisome); 0.1000 probability located
          in endoplasmic reticulum (membrane);
          0.1000 probability located in endoplasmic
          reticulum (lumen)
SignalP   Cleavage site between residues 20 and 21
analysis:

[0539] 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 38D.

TABLE 38D
Genesq Results for NOV38a
		NOV38a	Identities/
		Residues/	Similarities
Genesp	Protein/Organism/Length [Patent	Match	for the	Expect
Identifier	#, Date]	Residues	Matched Region	Value
AAY94527	Human statherin protein - Homo	1 . . . 62	62/62 (100%)	9e−32
	sapiens, 62 aa. [WO200024779-A1	1 . . . 62	62/62 (100%)
	04 MAY 2000]
AAB42456	Human ORFX ORF2220	3 . . . 62	54/67 (80%)	2e−24
	polypeptide sequence SEQ ID	16 . . . 82	56/67 (82%)
	NO: 4440 - Homo sapiens, 82 aa.
	[WO200058473-A2, 05 OCT. 2000]
AAG80022	Strathin homologue peptide	33 . . . 47	15/15 (100%)	0.002
	fragment - Unidentified, 15 aa.	1 . . . 15	15/15 (100%)
	[DE10017249-A1, 11 OCT. 2001]
AAW90168	BK-RiV plant stratherin peptide	33 . . . 47	15/15 (100%)	0.002
	fragment homologue - Unknown, 15	1 . . . 15	15/15 (100%)
	aa. [EP889053-A2, 07 JAN. 1999]
AAU90983	Transplant media associated	1 . . . 25	17/25 (68%)	0.033
	antimicrobial peptide #19 - Homo	1 . . . 25	20/25 (80%)
	sapiens, 51 aa. [WO200209738-A1,
	07 FEB. 2002]

[0540] 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 38E.

TABLE 38E
Public BLASTP Results for NOV38a
			Identities/
		NOV38a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
P02808	Statherin precursor - Homo sapiens	1 . . . 62	62/62 (100%)	2e−31
	(Human), 62 aa.	1 . . . 62	62/62 (100%)
P02809	Statherin precursor - Macaca	1 . . . 60	38/61 (62%)	6e−14
	fascicularis (Crab eating macaque)	1 . . . 61	39/61 (63%)
	(Cynomolgus monkey), 61 aa.
P14709	Statherin - Macaca arctoides (Stump-	20 . . . 60	30/42 (71%)	6e−10
	tailed macaque), 42 aa.	1 . . . 42	31/42 (73%)
P15515	Histatin 1 precursor (Histidine-rich	1 . . . 25	17/25 (68%)	0.015
	protein 1) (Post-PB protein) (PPB)	1 . . . 25	21/25 (84%)
	[Contains: Histatin 2] - Homo sapiens
	(Human), 57 aa.
P15516	Histatin 3 precursor (Histidine-rich	1 . . . 25	17/25 (68%)	0.075
	protein 3) (PB) (Basic histidine-rich	1 . . . 25	20/25 (80%)
	protein) [Contains: Histatins 4 to 12] -
	Homo sapiens (Human), 51 aa.

[0541] PFam analysis indicates that the NOV38a protein contains the domains shown in the Table 38F.

TABLE 38F
Domain Analysis of NOV38a
			Identities/
			Similarities
		NOV38a	for the
	Pfam	Match	Matched	Expect
	Domain	Region	Region	Value
No Significant Matches Found

Example 39

[0542] 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: 171	72 bp
NOV39a,	CTACAGACACTGGGCGCCAAGGCCCAGGCACAGACTGACCGAGTGAACCTGCGGACCC
CG94630-02
DNA Sequence	TGCTCCGCTACTAC
	ORF Start: at 1	ORF Stop: end of sequence
	SEQ ID NO: 172	24 aa	MW at 2793.2kD
NOV39a.	LQTLGAKAQAQTDRVNLRTLLRYY
CG94630-02
Protein Sequence

[0543] Further analysis of the NOV39a protein yielded the following properties shown in Table 39B.

TABLE 39B
Protein Sequence Properties NOV39a
PSort     0.8500 probability located in lysosome
analysis: (lumen); 0.7847 probability located in
          mitochondrial intermembrane space;
          0.4500 probability located in cytoplasm;
          0.4488 probability located in
          mitochondrial matrix space
SignalP   No Known Signal Sequence Indicated
analysis:

[0544] 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 39C.

TABLE 39C
Geneseq Results for NOV39a
			Identities/
		NOV39a	Similarities
		Residues/	for the
Geneseq	Protein/Organism/Length [Patent #,	Match	Matched	Expect
Identifier	Date]	Residues	Region	Value
AAP70155	Sequence encoded by genomic DNA	2 . . . 24	16/23 (69%)	0.17
	encoding human histocompatibility	87 . . . 109	19/23 (82%)
	antigen HLA-B 27 - Homo sapiens,
	362 aa. [EP226069-A, 24 JUN. 1987]
AAM23917	Rhesus monkey EST encoded protein	2 . . . 24	16/23 (69%)	0.22
	SEQ ID NO: 1442 - Macaca mulatta,	126 . . . 148	17/23 (73%)
	153 aa. [WO200154477-A2, 02 AUG.
	2001]
AAU79455	HLA-G recombinant protein 2 - Homo	2 . . . 24	14/23 (60%)	0.85
	sapiens, 234 aa. [WO200222784-A2,	94 . . . 116	17/23 (73%)
	21 MAR. 2002]
AAU79454	HLA-G recombinant protein 1 - Homo	2 . . . 24	14/23 (60%)	0.85
	sapiens, 326 aa. [WO200222784-A2,	94 . . . 116	17/23 (73%)
	21 MAR. 2002]
AAU79450	HLA-G alpha1 domain protein -	2 . . . 24	14/23 (60%)	0.85
	Homo sapiens, 92 aa.	65 . . . 87	17/23 (73%)
	[WO200222784-A2, 21 MAR. 2002]

[0545] 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 39D.

TABLE 39D
Public BLASTP Results for NOV39a
			Identities/
		NOV39a	Similarities
Protein		Residues/	for the
Accession		Match	Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q30175	MHC class I HLA-J antigen -	1 . . . 24	24/24 (100%)	4e−06
	Homo sapiens (Human), 218 aa	85 . . . 108	24/24 (100%)
	(fragment).
Q8WW48	Hypothetical 28.9 kDa protein -	1 . . . 24	24/24 (100%)	4e−06
	Homo sapiens (Human), 264 aa	89 . . . 112	24/24 (100%)
	(fragment).
Q95533	Class I histocompatibility antigen -	3 . . . 24	18/22 (81%)	0.013
	Pan troglodytes (Chimpanzee), 137	29 . . . 50	18/22 (81%)
	aa (fragment).
Q9MXK1	MHC class I antigen - Pan	3 . . . 24	18/22 (81%)	0.013
	troglodytes (Chimpanzee), 362 aa.	88 . . . 109	18/22 (81%)
Q95430	MHC class I - Pongo pygmaeus	2 . . . 24	18/23 (78%)	0.017
	(Orangutan), 354 aa (fragment).	79 . . . 101	20/23 (86%)

[0546] PFam analysis indicates that the NOV39a protein contains the domains shown in the Table 39E.

TABLE 39E
Domain Analysis of NOV39a
			Identities/
		NOV39a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
	MHC_I	2 . . . 24	15/23 (65%)	7.1e−05
			21/23 (91%)

Example 40

[0547] 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: 175	1513 bp
NOV40a,	TCGCGATGCTGCTGCGCCTGTTGCTGGCCTGGGCGGCCGCAGGGCCCACACTGGGCCA
CG95205-02
DNA Sequence	GGACCCCTGGGCTGCTGAGCCCCGTGCCGCCTGCGGCCCCAGCAGCTGCTACGCTCTC
	TTCCCACGGCGCCGCACCTTCCTGGAGGCCTGGCGCGCCTGCCGCGAGCTGGGGGGCG
	ACCTGGCCACTCCTCGGACCCCCGAGGAGGCCCAGCGTGTGGACAGCCTGGTGGGTGC
	GGGCCCAGCCAGCCGGCTGCTGTGGATCGGCCTGCAGCGGCAGGCCCGGCAATGCCAG
	CTGCAGCGCCCACTGCGCGGCTTCACGTGGACCACAGGGGACCAGGACACGGCTTTCA
	CCAACTGGGCCCAGCCAGCCTCTGGAGGCCCCTGCCCGGCCCAGCGCTCTGTGGCCCT
	GGAGGCAAGTGGCGAGCACCGCTGGCTGGAGGGCTCGTGCACCCTGGCTGTCGACGGC
	TACCTGTGCCAGTTTGGCTTCGAGGGCGCCTGCCCGGCGCTGCAAGATGAGGCGGGCC
	AGGCCGGCCCAGCCGTGTATACCACGCCCTTCCACCTGGTCTCCACAGAGTTTGAGTG
	GCTGCCCTTCGGCTCTGTGGCCGCTGTGCAGTGCCAGGCTGGCAGGGGAGCCTCTCTG
	CTCTGCGTGAAGCAGCCTGAGGGAGGTGTGGGCTGGTCACGGGCTGGGCCCCTGTGCC
	TGGGGACTGGCTGCAGCCCTGACAACGGCGGCTGCGAACACGAATGTGTGGAGGAGGT
	GGATGGTCACGTGTCCTGCCGCTGCACTGAGGGCTTCCGGCTGGCAGCAGACGGGCGC
	AGTTGCGAGCACCCCTGTGCCCAGGCTCCGTGCGAGCAGCAGTGTGAGCCCGGTGGGC
	CACAAGGCTACAGCTGCCACTGTCGCCTCGGTTTCCGGCCAGCGGAGGATGATCCGCA
	CCGCTGTGTGGACACAGATGAGTGCCAGATTGCCGGTGTGTGCCAGCAGATGTGTGTC
	AACTACGTTGCTGGCTTCGAGTGTTATTGTAGCGAGGGACATGAGCTGGAGGCTCATG
	GCATCAGCTGCAGCCCTGCAGGGGCCATGGGTGCCCAGGCTTCCCAGGACCTCGGAGA
	TGAGTTGCTGGATGACGCGGAGGATGAGGAAGATGAAGACGAGGCCTGGAAGGCCTTC
	AACGGTGGCTGGACGGAGATGCCTGGGATCCTGTGGATGGAGCCTACGCAGCCGCCTG
	ACTTTGCCCTGGCCTATAGACCGAGCTTCCCAGAGGACAGAGAGCCACAGATACCCTA
	CCCGGAGCCCACCTGGCCACCCCCGCTGCCCAGCTGGACAGATGGCTTCCTGCTCCCC
	AGGCCCAGCCAGGGTCCTCTCTCAACCACTAGACTTGGCTCTCAGGAACTCTGCTTCC
	TGGCCCAGCGCTCGTGACCAAGGATACACCAAAGCCCTTAAGACCTCAGGGGGCGGGT
	GCTGGGGTCTTCTCCAATAAATGGGGTGTCACCCTTAAAAAAAAAAAAAAAAAAAAAA
	AAAAA
	ORF Start: ATG at 6	ORF Stop: TGA at 1407
	SEQ ID NO: 176	467 aa	MW at 50389.6kD
NOV40a,	MLLRLLLAWAAAGPTLGQDPWAAEPRAACGPSSCYALFPRRRTFLEAWRACRELGGDL
CG95205-02
Protein Sequence	ATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQLQRPLRGFTWTTGDQDTAFTN
	WAQPASGGPCPAQRCVALEASGEHRWLEGSCTLAVDGYLCQEGFEGACPALQDEAGQA
	GPAVYTTPFHLVSTEFEWLPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLG
	TGCSPDNGGCEHECVEEVDGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQ
	GYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGI
	SCSPAGAMGAQASQDLGDELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDF
	ALAYRPSFPEDREPQIPYPEPTWPPPLPSWTDGFLLPRPSQGPLSTTRLGSQELCFLA
	QRS

[0548] Further analysis of the NOV40a protein yielded the following properties shown in Table 40B.

TABLE 40B
Protein Sequence Properties NOV40a
PSort     0.3700 probability located in outside;
analysis: 0.1440 probability located in microbody
          (peroxisome); 0.1000 probability
          located in endoplasmic reticulum
          (membrane); 0.1000 probability located
          in endoplasmic reticulum (lumen)
SignalP   Cleavage site between residues 18 and 19
analysis:

[0549] 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
ABB90732	Human Tumour Endothelial Marker	1 . . . 433	433/433 (100%)	0.0
	polypeptide SEQ ID NO 196 -	1 . . . 433	433/433 (100%)
	Homo sapiens, 757 aa.
	[WO200210217-A2, 07 FEB. 2002]
ABB90721	Human Tumour Endothelial Marker	1 . . . 433	433/433 (100%)	0.0
	polypeptide SEQ ID NO 177 -	1 . . . 433	433/433 (100%)
	Homo sapiens, 757 aa.
	[WO200210217-A2, 07 FEB. 2002]
ABB90780	Mouse Tumour Endothelial Marker	1 . . . 433	382/433 (88%)	0.0
	polypeptide SEQ ID NO 291 - Mus	1 . . . 433	397/433 (91%)
	musculus, 765 aa. [WO200210217-
	A2, 07 FEB. 2002]
ABB90727	Mouse Tumour Endothelial Marker	1 . . . 433	382/433 (88%)	0.0
	polypeptide SEQ ID NO 190 - Mus	1 . . . 433	397/433 (91%)
	musculus, 765 aa. [WO200210217-
	A2, 07 FEB. 2002]
AAE05343	Mouse tumour endothelial marker I	3 . . . 464	388/469 (82%)	0.0
	precursor protein - Mus sp, 492 aa.	1 . . . 469	408/469 (86%)
	[WO200148192-A1, 05 JUL. 2001]

[0550] 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
Q9HCU0	Tumor endothelial marker I	1 . . . 433	433/433 (100%)	0.0
	precursor (Endosialin protein) -	1 . . . 433	433/433 (100%)
	Homo sapiens (Human), 757 aa.
Q91V98	Tumor endothelial marker I	1 . . . 433	382/433 (88%)	0.0
	precursor (Endosialin) - Mus	1 . . . 433	397/433 (91%)
	musculus (Mouse), 765 aa.
Q91ZV1	Endosialin - Mus musculus	1 . . . 433	382/433 (88%)	0.0
	(Mouse), 765 aa.	1 . . . 433	397/433 (91%)
Q96KB6	CDNA FLJ14384 fis, clone	325 . . . 433	109/109 (100%)	2e−64
	HEMBA1002150 - Homo sapiens	1 . . . 109	109/109 (100%)
	(Human), 433 aa.
THHUB	thrombomodulin precursor	2 . . . 352	147/375 (39%)	2e−54
	[validated] - human, 575 aa.	1 . . . 365	184/375 (48%)

[0551] PFam analysis indicates that the NOV40a protein contains the domains shown in the Table 40E.

TABLE 40E
Domain Analysis of NOV40a
			Identities/
		NOV40a	Similarities for
	Pfam	Match	the Matched	Expect
	Domain	Region	Region	Value
	Xlink	43 . . . 61	9/19 (47%)	0.034
			15/19 (79%)
	lectin_c	40 . . . 158	29/134 (22%)	8.4e−06
			80/134 (60%)
	sushi	176 . . . 230	15/66 (23%)	0.72
			39/66 (59%)
	EGF	235 . . . 271	13/47 (28%)	4.6e−06
			31/47 (66%)
	TIL	258 . . . 316	19/74 (26%)	0.17
			40/74 (54%)
	EGF	316 . . . 350	13/47 (28%)	0.00035
			26/47 (55%)

Example B

[0552] Sequencing Methodology and Identification of NOVX Clones

[0553] 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.

[0554] 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.

[0555] 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.

[0556] The laboratory screening was performed using the methods summarized below:

[0557] 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).

[0558] 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.

[0559] 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).

[0560] 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.

[0561] 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, traclea, 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.

[0562] 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.

[0563] 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

[0564] Quantitative Expression Analysis of Clones in Various Cells and Tissues

[0565] 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/5I (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).

[0566] 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.

[0567] 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.

[0568] 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.

[0569] 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.

[0570] 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.

[0571] 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.

[0572] Panels 1, 1.1, 1.2, and 1.3D

[0573] 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.

[0574] In the results for Panels 1, 1.1, 1.2 and 1.3D, the following abbreviations are used:

[0575] ca.=carcinoma,

[0576] *=established from metastasis,

[0577] met=metastasis,

[0578] s cell var=small cell variant,

[0579] non-s=non-sm=non-small,

[0580] squam=squamous,

[0581] pl. eff=pl effusion=pleural effusion,

[0582] glio=glioma,

[0583] astro=astrocytoma, and

[0584] neuro=neuroblastoma.

[0585] General_screening_panel_v1.4, v1.5 and v1.6

[0586] 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 arc as described for Panels 1, 1.1, 1.2, and 1.3D.

[0587] Panels 2D, 2.2, 2.3 and 2.4

[0588] 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.

[0589] HASS Panel v 1.0

[0590] 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.

[0591] ARDAIS Panel v 1.0

[0592] 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” arc 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.

[0593] Panel 3D, 3.1 and 3.2

[0594] 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 arc 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.

[0595] Panels 4D, 4R, and 4.1D

[0596] 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.).

[0597] 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, IFN 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.

[0598] 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 1-2 μg/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 2×106 cells/mil 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.

[0599] 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 100 ng/ml. Dendritic cells were also stimulated with anti-CD40 monoclonal antibody (Pharmingen) at 10 μg/ml for 6 and 12-14 hours.

[0600] 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 5.5×10−5M (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 pyrivate (Gibco), mercaptoethanol 5.5×10−5M (Gibco), and 10 mM Hepes (Gibco) and IL-2 for 4-6 days before RNA was prepared.

[0601] 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.

[0602] 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 105-106 cells/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 (1 μg/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 5.5×10−5M (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.

[0603] 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 5×105 cells/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.

[0604] For these cell lines and blood cells, RNA was prepared by lysing approximately 107 cells/ml using Trizol (Gibco BRL). Briefly, 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 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.

[0605] AI_comprehensive panel_v1.0

[0606] 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.

[0607] 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.

[0608] 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.

[0609] 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.

[0610] 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-lanti-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.

[0611] In the labels employed to identify tissues in the AI_comprehensive panel_v1.0 panel, the following abbreviations are used:

[0612] AI=Autoimmunity

[0613] Syn=Synovial

[0614] Normal=No apparent disease

[0615] Rep22 /Rep20 =individual patients

[0616] RA=Rheumatoid arthritis

[0617] Backus=From Backus Hospital

[0618] OA=Osteoarthritis

[0619] (SS)(BA)(MF)=Individual patients

[0620] Adj=Adjacent tissue

[0621] Match control=adjacent tissues

[0622] -M=Male

[0623] -F=Female

[0624] COPD=Chronic obstructive pulmonary disease

[0625] Panels 5D and 5I

[0626] 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.

[0627] 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:

[0628] Patient 2: Diabetic Hispanic, overweight, not on insulin

[0629] Patient 7-9: Nondiabetic Caucasian and obese (BMI>30)

[0630] Patient 10: Diabetic Hispanic, overweight, on insulin

[0631] Patient 11: Nondiabetic African American and overweight

[0632] Patient 12: Diabetic Hispanic on insulin

[0633] 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:

[0634] Donor 2 and 3 U: Mesenchymal Stem cells, Undifferentiated Adipose

[0635] Donor 2 and 3 AM: Adipose, AdiposeMidway Differentiated

[0636] Donor 2 and 3 AD: Adipose, Adipose Differentiated

[0637] 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.

[0638] 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.

[0639] In the labels employed to identify tissues in the 5D and 5I panels, the following abbreviations are used:

[0640] GO Adipose=Greater Omentum Adipose

[0641] SK=Skeletal Muscle

[0642] UT=Uterus

[0643] PL=Placenta

[0644] AD=Adipose Differentiated

[0645] AM=Adipose Midway Differentiated

[0646] U=Undifferentiated Stem Cells

[0647] Panel CNSD.01

[0648] 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.

[0649] 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.

[0650] In the labels employed to identify tissues in the CNS panel, the following abbreviations are used:

[0651] PSP=Progressive supranuclear palsy

[0652] Sub Nigra=Substantia nigra

[0653] Glob Palladus=Globus palladus

[0654] Temp Pole=Temporal pole

[0655] Cing Gyr=Cingulate gyrus

[0656] BA 4 =Brodman Area 4

[0657] Panel CNS_Neurodegeneration_V1.0

[0658] 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.

[0659] 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.

[0660] In the labels employed to identify tissues in the CNS_Neurodegeneration_V1.0 panel, the following abbreviations are used:

[0661] AD=Alzheimer's disease brain; patient was demented and showed AD-like pathology upon autopsy

[0662] Control=Control brains; patient not demented, showing no neuropathology

[0663] Control (Path)=Control brains; patient not demented but showing sever AD-like pathology

[0664] SupTemporal Ctx=Superior Temporal Cortex

[0665] Inf Temporal Ctx=Inferior Temporal Cortex

[0666] A. NOV1a and NOV1b (CG113254-01 and CG113254-02): Fibulin

[0667] Expression of gene CG113254-01 and CG113254-02 was assessed using the primer-probe sets Ag1294b, Ag746, Ag905, Ag4470 and Ag4726, described in Tables AA, AB, AC, AD and AE. Results of the RTQ-PCR runs are shown in Tables AF, AG, AH, AI, AJ, AK, AL and AM. Please note that CG113254-02 represents a full-length physical clone and is recognized only by two probes and primer sets: Ag4470 and Ag4726.

TABLE AA
Probe Name Ag1294b
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-cattggcagctacaagtgttc-3′	21	691	205
Probe	TET-5′-ctgtcgaactggcttccaccttcat-3′-	25	712	206
		TAMRA
Reverse	5′-cctccgacactcgtttacatc-3′	21	758	207

[0668]

TABLE AB
Probe Name Ag746
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gcattggcagctacaagtgt-3′	20	690	208
Probe	TET-5′-ctgtcgaactggcttccaccttcat-3′-	25	712	209
		TAMRA
Reverse	5′-cctccgacactcgtttacatc-3′	21	758	210

[0669]

TABLE AC
Probe Name Ag905
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-cattggcagctacaagtgttc-3′	21	691	211
Probe	TET-5′-ctgtcgaactggcttccaccttcat-3′-	25	712	212
Reverse	5′-cctccgacactcgtttacatc-3′	21	758	213

[0670]

TABLE AD
Probe Name Ag4470
				Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gcatcaggtgtacagaeattga-3′	22	510	214
Probe	TET-5′-cgaatgtgtaacctcctcctgcgag-3′-	25	532	215
		TAMRA
Reverse	5′-acaaacccaccttctgtgttc-3′	21	568	216

[0671]

TABLE AL
Probe Name Ag4726
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gtgtctgtctggctggaaac-3′	20	1497	217
Probe	TET-5′-tgcatctctcctgagtgtccttctgg-3′-	26	1523	218
	TAMRA
Reverse	5′-acaagtacaqcaatccgtctgt-3′	22	1567	219

[0672]

TABLE AF
AI_comprehensive panel_v1.0
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag1294b, Run	Ag4470, Run
Tissue Name	249007981	249008358
110967 COPD-F	6.6	3.0
110980 COPD-F	16.6	8.7
110968 COPD-M	3.9	3.4
110977 COPD-M	31.6	38.2
110989 Emphysema-F	45.1	31.4
110992 Emphysema-F	7.2	3.3
110993 Emphysema-F	5.8	5.5
110994 Emphysema-F	3.3	2.1
110995 Emphysema-F	2.0	15.4
110996 Emphysema-F	3.1	2.0
110997 Asthma-M	3.7	0.8
111001 Asthma-F	2.8	7.7
111002 Asthma-F	5.3	5.5
111003 Atopic Asthma-F	6.1	6.0
111004 Atopic Asthma-F	3.4	12.4
111005 Atopic Asthma-F	3.9	5.6
111006 Atopic Asthma-F	2.4	1.4
111417 Allergy-M	6.6	3.5
112347 Allergy-M	3.3	5.8
112349 Normal Lung-F	3.2	6.1
112357 Normal Lung-F	100.0	100.0
112354 Normal Lung-M	58.6	69.3
112374 Crohns-F	7.5	9.4
112389 Match Control Crohns-F	3.5	7.1
112375 Crohns-F	5.1	7.4
112732 Match Control Crohns-F	0.5	6.7
112725 Crohns-M	10.6	5.8
112387 Match Control Crohns-M	3.5	0.0
112378 Crohns-M	1.7	4.7
112390 Match Control Crohns-M	55.5	52.5
112726 Crohns-M	3.6	7.9
112731 Match Control Crohns-M	13.9	13.1
112380 Ulcer Col-F	13.7	13.2
112734 Match Control Ulcer Col-F	5.6	8.4
112384 Ulcer Col-F	3.9	2.8
112737 Match Control Ulcer Col-F	3.3	2.8
112386 Ulcer Col-F	0.0	0.0
112738 Match Control Ulcer Col-F	0.0	1.6
112381 Ulcer Col-M	4.2	9.4
112735 Match Control Ulcer Col-M	18.2	25.2
112382 Ulcer Col-M	4.2	7.6
112394 Match Control Ulcer Col-M	0.0	0.0
112383 Ulcer Col-M	12.2	6.6
112736 Match Control Ulcer Col-M	2.0	2.4
112423 Psoriasis-F	3.9	4.5
112427 Match Control Psoriasis-F	30.8	25.7
112418 Psoriasis-M	4.6	4.3
112723 Match Control Psoriasis-M	23.8	27.5
112419 Psoriasis-M	2.7	2.6
112424 Match Control Psoriasis-M	1.9	4.0
112420 Psoriasis-M	4.9	13.7
112425 Match Control Psoriasis-M	25.9	25.7
104689 (MF) OA Bone-Backus	12.9	7.3
104690 (MF) Adj “Normal” Bone-	3.7	1.2
Backus
104691 (MF) OA Synovium-Backus	6.9	11.3
104692 (BA) OA Cartilage-Backus	21.3	7.4
104694 (BA) OA Bone-Backus	6.6	2.0
104695 (BA) Adj “Normal” Bone-	2.3	5.3
Backus
104696 (BA) OA Synovium-Backus	5.7	6.3
104700 (SS) OA Bone-Backus	6.2	5.6
104701 (SS) Adj “Normal” Bone-	3.8	5.8
Backus
104702 (SS) OA Synovium-Backus	15.4	15.1
117093 OA Cartilage Rep7	18.0	12.2
112672 OA Bone5	90.1	97.3
112673 OA Synovium5	63.7	46.0
112674 OA Synovial Fluid cells5	32.3	32.5
117100 OA Cartilage Rep14	3.3	0.0
112756 OA Bone9	7.0	14.8
112757 OA Synovium9	12.2	17.4
112758 OA Synovial Fluid Cells9	3.9	5.2
117125 RA Cartilage Rep2	4.6	7.9
113492 Bone2 RA	2.4	1.5
113493 Synovium2 RA	1.1	0.0
113494 Syn Fluid Cells RA	1.4	0.0
113499 Cartilage4 RA	1.4	2.0
113500 Bone4 RA	0.5	1.7
113501 Synovium4 RA	1.7	2.3
113502 Syn Fluid Cells4 RA	1.8	0.7
113495 Cartilage3 RA	1.6	1.2
113496 Bone3 RA	1.1	2.3
113497 Synovium3 RA	0.0	0.0
113498 Syn Fluid Cells3 RA	0.6	0.8
117106 Normal Cartilage Rep20	4.5	5.7
113663 Bone3 Normal	6.7	0.9
113664 Synovium3 Normal	1.2	1.6
113665 Syn Fluid Cells3 Normal	0.9	3.3
117107 Normal Cartilage Rep22	1.3	3.5
113667 Bone4 Normal	11.8	8.7
113668 Synovium4 Normal	12.0	12.8
113669 Syn Fluid Cells4 Normal	10.7	24.3

[0673]

TABLE AG
CNS_neurodegeneration_v1.0
	Rel.	Rel.	Rel.
	Exp. (%)	Exp. (%)	Exp. (%)
	Ag1294b,	Ag4470,	Ag4726,
Tissue	Run	Run	Run
Name	206231468	224535165	224706360
AD 1 Hippo	11.2	13.7	11.6
AD 2 Hippo	22.5	22.2	23.5
AD 3 Hippo	4.7	6.3	0.0
AD 4 Hippo	8.7	10.7	15.2
AD 5 Hippo	37.6	35.1	35.6
AD 6 Hippo	100.0	95.9	100.0
Control 2 Hippo	28.7	15.8	21.9
Control 4 Hippo	30.4	23.7	40.3
Control (Path) 3 Hippo	6.9	0.0	3.6
AD 1 Temporal Ctx	16.3	15.0	26.1
AD 2 Temporal Ctx	31.6	14.8	25.2
AD 3 Temporal Ctx	3.8	2.6	5.6
AD 4 Temporal Ctx	10.9	23.7	36.1
AD 5 Inf Temporal Ctx	34.6	38.4	35.8
AD 5 Sup Temporal Ctx	19.6	29.7	55.9
AD 6 Inf Temporal Ctx	73.7	85.3	76.8
AD 6 Sup Temporal Ctx	81.2	100.0	97.9
Control 1 Temporal Ctx	1.2	7.7	5.1
Control 2 Temporal Ctx	15.5	28.5	42.9
Control 3 Temporal Ctx	5.9	16.7	18.4
Control 4 Temporal Ctx	7.9	14.5	17.2
Control (Path) 1 Temporal	41.8	32.3	43.5
Ctx
Control (Path) 2 Temporal	26.2	34.9	36.6
Ctx
Control (Path) 3 Temporal	1.5	2.8	11.4
Ctx
Control (Path) 4 Temporal	19.2	31.6	20.3
Ctx
AD 1 Occipital Ctx	15.8	17.8	17.4
AD 2 Occipital Ctx	0.0	0.0	0.0
(Missing)
AD 3 Occipital Ctx	1.2	7.9	3.6
AD 4 Occipital Ctx	17.8	11.3	7.9
AD 5 Occipital Ctx	8.7	9.3	17.6
AD 6 Occipital Ctx	12.3	20.3	30.8
Control 1 Occipital Ctx	0.0	5.8	3.0
Control 2 Occipital Ctx	27.4	36.3	34.6
Control 3 Occipital Ctx	5.4	9.4	2.8
Control 4 Occipital Ctx	6.7	10.7	15.4
Control (Path) 1 Occipital	56.3	54.7	85.3
Ctx
Control (Path) 2 Occipital	10.4	10.0	21.8
Ctx
Control (Path) 3 Occipital	1.2	0.0	0.0
Ctx
Control (Path) 4 Occipital	6.3	18.3	5.0
Ctx
Control 1 Parietal Ctx	6.4	7.4	9.7
Control 2 Parietal Ctx	39.5	33.2	55.9
Control 3 Parietal Ctx	4.4	9.6	11.2
Control (Path) 1 Parietal	17.6	22.4	45.4
Ctx
Control (Path) 2 Parietal	17.6	28.1	12.1
Ctx
Control (Path) 3 Parietal	0.0	2.2	4.2
Ctx
Control (Path) 4 Parietal	26.4	44.1	30.1
Ctx

[0674]

TABLE AH
General_screening_panel_v1.4
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag4470, Run	Ag4726, Run
Tissue Name	222655825	222842378
Adipose	4.8	3.3
Melanoma* Hs688(A).T	3.3	2.7
Melanoma* Hs688(B).T	3.1	2.7
Melanoma* M14	2.8	4.8
Melanoma* LOXIMVI	0.2	0.1
Melanoma* SK-MEL-5	0.8	0.4
Squamous cell carcinoma SCC-4	0.6	0.2
Testis Pool	5.5	4.3
Prostate ca.* (bone met) PC-3	3.0	1.6
Prostate Pool	1.1	0.5
Placenta	10.0	7.7
Uterus Pool	2.3	0.1
Ovarian ca. OVCAR-3	0.8	0.7
Ovarian ca. SK-OV-3	0.4	0.6
Ovarian ca. OVCAR-4	0.3	0.3
Ovarian ca. OVCAR-5	1.6	1.1
Ovarian ca. IGROV-1	0.5	1.4
Ovarian ca. OVCAR-8	0.9	0.7
Ovary	7.7	5.0
Breast ca. MCF-7	0.9	0.4
Breast ca. MDA-MB-231	1.2	0.5
Breast ca. BT 549	1.8	0.7
Breast ca. T47D	4.9	4.2
Breast ca. MDA-N	0.3	0.2
Breast Pool	2.4	0.8
Trachea	4.5	1.3
Lung	7.9	5.5
Fetal Lung	3.8	1.8
Lung ca. NCI-N417	3.9	3.6
Lung ca. LX-I	0.9	0.7
Lung ca. NCI-H146	0.8	0.8
Lung ca. SHP-77	2.3	0.3
Lung ca. A549	0.9	0.8
Lung ca. NCI-H526	2.9	2.1
Lung ca. NCI-H23	1.4	0.8
Lung ca. NCI-H460	2.2	1.2
Lung ca. HOP-62	2.0	0.5
Lung ca. NCI-H522	31.6	20.2
Liver	20.7	11.6
Fetal Liver	63.7	61.1
Liver ca. HepG2	100.0	100.0
Kidney Pool	11.2	6.7
Fetal Kidney	5.3	2.0
Renal ca. 786-0	1.6	1.7
Renal ca. A498	0.8	1.3
Renal ca. ACHN	2.2	2.5
Renal ca. UO-31	12.9	10.6
Renal ca. TK-10	54.0	41.8
Bladder	2.9	1.8
Gastric ca. (liver met.) NCI-N87	2.3	2.0
Gastric ca. KATO III	0.8	0.6
Colon ca. SW-948	0.5	0.6
Colon ca. SW480	3.3	0.7
Colon ca.* (SW480 met) SW620	16.2	12.8
Colon ca. HT29	0.0	0.1
Colon ca. HCT-116	4.4	3.7
Colon ca. CaCo-2	94.0	31.9
Colon cancer tissue	16.5	7.9
Colon ca. SW1116	0.6	1.0
Colon ca. Colo-205	0.0	0.0
Colon ca. SW-48	0.2	0.0
Colon Pool	2.6	1.0
Small Intestine Pool	10.8	4.9
Stomach Pool	2.4	3.4
Bone Marrow Pool	1.0	0.0
Fetal Heart	2.6	0.7
Heart Pool	1.7	0.7
Lymph Node Pool	2.7	2.6
Fetal Skeletal Muscle	2.3	1.6
Skeletal Muscle Pool	0.8	1.0
Spleen Pool	0.6	0.4
Thymus Pool	16.3	7.9
CNS cancer (glio/astro) U87-MG	5.7	6.4
CNS cancer (glio/astro) U-118-MG	2.7	1.6
CNS cancer (neuro; met) SK-N-AS	4.8	4.4
CNS cancer (astro) SF-539	0.0	0.2
CNS cancer (astro) SNB-75	5.2	4.4
CNS cancer (glio) SNB-19	0.5	1.1
CNS cancer (glio) SF-295	8.3	5.1
Brain (Amygdala) Pool	2.9	2.5
Brain (cerebellum)	5.9	7.3
Brain (fetal)	25.3	12.2
Brain (Hippocampus) Pool	3.7	1.9
Cerebral Cortex Pool	4.6	2.6
Brain (Substantia nigra) Pool	4.7	2.1
Brain (Thalamus) Pool	3.8	3.9
Brain (whole)	9.2	8.5
Spinal Cord Pool	3.6	1.9
Adrenal Gland	4.2	2.6
Pituitary gland Pool	0.8	0.6
Salivary Gland	1.0	0.9
Thyroid (female)	2.0	1.8
Pancreatic ca. CAPAN2	0.0	0.0
Pancreas Pool	3.0	1.1

[0675]

TABLE AI
Panel 1.2
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag746, Run	Ag746, Run
Tissue Name	115163442	119442272
Endothelial cells	12.3	5.9
Heart (Fetal)	0.0	0.0
Pancreas	0.0	0.0
Pancreatic ca. CAPAN 2	0.0	0.0
Adrenal Gland	0.0	0.2
Thyroid	0.1	0.0
Salivary gland	0.0	0.0
Pituitary gland	0.2	0.1
Brain (fetal)	2.4	16.0
Brain (whole)	0.0	0.3
Brain (amygdala)	0.0	0.0
Brain (cerebellum)	0.0	0.0
Brain (hippocampus)	0.0	0.0
Brain (thalamus)	0.0	0.0
Cerebral Cortex	0.0	0.0
Spinal cord	0.0	0.0
glio/astro U87-MG	0.0	0.0
glio/astro U-118-MG	0.0	0.0
astrocytoma SW1783	0.0	0.0
neuro*; met SK-N-AS	0.0	0.2
astrocytoma SF-539	0.0	0.0
astrocytoma SNB-75	0.0	0.0
glioma SNB-19	0.0	0.0
glioma U251	0.0	0.0
glioma SF-295	0.0	0.0
Heart	0.0	0.0
Skeletal Muscle	0.0	0.0
Bone marrow	0.0	0.0
Thymus	1.2	2.8
Spleen	0.0	0.0
Lymph node	0.0	0.0
Colorectal Tissue	0.0	0.0
Stomach	0.0	0.0
Small intestine	0.0	0.0
Colon ca. SW480	0.0	0.0
Colon ca.* SW620 (SW480 met)	1.1	1.9
Colon ca. HT29	0.0	0.0
Colon ca. HCT-116	0.0	0.0
Colon ca. CaCo-2	46.3	56.6
Colon ca. Tissue (ODO3866)	0.0	0.0
Colon ca. HCC-2998	0.0	0.0
Gastric ca.* (liver met) NCI-N87	0.0	0.0
Bladder	0.0	0.0
Trachea	0.0	0.0
Kidney	0.0	0.0
Kidney (fetal)	0.1	0.9
Renal ca. 786-0	0.0	0.0
Renal ca. A498	0.0	0.0
Renal ca. RXF 393	0.0	0.0
Renal ca. ACHN	0.0	0.0
Renal ca. UO-31	0.0	0.0
Renal ca. TK-10	0.0	0.0
Liver	32.8	51.2
Liver (fetal)	7.2	100.0
Liver ca. (hepatoblast) HepG2	100.0	94.0
Lung	0.0	0.0
Lung (fetal)	0.0	0.0
Lung ca. (small cell) LX-1	0.0	0.0
Lung ca. (small cell) NCI-H69	0.0	0.0
Lung ca. (s. cell var.) SHP-77	0.0	0.0
Lung ca. (large cell) NCI-H460	0.0	0.0
Lung ca. (non-sm. cell) A549	0.0	0.0
Lung ca. (non-s. cell) NCI-H23	0.0	0.0
Lung ca. (non-s. cell) HOP-62	0.0	0.0
Lung ca. (non-s. cl) NCI-H522	63.7	90.1
Lung ca. (squam.) SW 900	0.0	0.0
Lung ca. (squam.) NCI-H596	0.0	0.0
Mammary gland	0.7	3.6
Breast ca.* (pl. ef) MCF-7	0.0	0.0
Breast ca.* (pl. ef) MDA-MB-231	0.0	0.0
Breast ca.* (pl. ef) T47D	0.0	0.0
Breast ca. BT-549	0.0	0.0
Breast ca. MDA-N	0.0	0.0
Ovary	0.5	11.7
Ovarian ca. OVCAR-3	0.0	0.0
Ovarian ca. OVCAR-4	0.0	0.0
Ovarian ca. OVCAR-5	0.0	0.0
Ovarian ca. OVCAR-8	0.0	0.0
Ovarian ca. IGROV-1	0.0	0.0
Ovarian ca. (ascites) SK-OV-3	0.0	0.0
Uterus	0.0	0.0
Placenta	34.4	39.5
Prostate	0.0	0.0
Prostate ca.* (bone met) PC-3	0.0	0.0
Testis	1.0	3.5
Melanoma Hs688(A).T	0.0	0.0
Melanoma* (met) Hs688(B).T	0.0	0.0
Melanoma UACC-62	0.0	0.0
Melanoma M14	0.0	0.0
Melanoma LOX IMVI	0.0	0.0
Melanoma* (met) SK-MEL-5	0.0	0.0

[0676]

TABLE AJ
Panel 2D
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag746, Run	Ag746, Run
Tissue Name	147127131	148019631
Normal Colon	18.3	21.8
CC Well to Mod Diff (ODO3866)	16.5	21.7
CC Margin (ODO3866)	3.1	0.0
CC Gr.2 rectosigmoid (ODO3868)	0.0	0.8
CC Margin (ODO3868)	0.5	2.0
CC Mod Diff (ODO3920)	1.2	2.3
CC Margin (ODO3920)	1.3	2.6
CC Gr.2 ascend colon (ODO3921)	3.4	4.4
CC Margin (ODO3921)	1.3	0.0
CC from Partial Hepatectomy	8.4	1.9
(ODO4309) Mets
Liver Margin (ODO4309)	49.7	41.5
Colon mets to lung (OD04451-01)	0.3	5.3
Lung Margin (OD04451-02)	0.0	1.8
Normal Prostate 6546-1	9.1	12.1
Prostate Cancer (OD04410)	2.0	9.7
Prostate Margin (OD04410)	16.8	20.3
Prostate Cancer (OD04720-01)	13.5	14.4
Prostate Margin (OD04720-02)	14.0	22.4
Normal Lung 061010	6.8	11.7
Lung Met to Muscle (ODO4286)	1.8	0.7
Muscle Margin (ODO4286)	11.5	13.1
Lung Malignant Cancer (OD03126)	1.5	6.0
Lung Margin (OD03126)	4.8	2.4
Lung Cancer (OD04404)	4.2	2.3
Lung Margin (OD04404)	9.0	10.4
Lung Cancer (OD04565)	0.3	0.0
Lung Margin (OD04565)	0.4	0.3
Lung Cancer (OD04237-01)	10.7	11.1
Lung Margin (OD04237-02)	4.9	5.4
Ocular Mel Met to Liver (ODO4310)	10.5	11.9
Liver Margin (ODO4310)	22.4	32.8
Melanoma Mets to Lung (OD04321)	0.0	0.0
Lung Margin (OD04321)	0.6	0.0
Normal Kidney	5.3	5.3
Kidney Ca, Nuclear grade 2	39.8	43.8
(OD04338)
Kidney Margin (OD04338)	4.8	6.4
Kidney Ca Nuclear grade 1/2	3.0	0.3
(OD04339)
Kidney Margin (OD04339)	5.4	10.0
Kidney Ca, Clear cell type	18.2	19.2
(OD04340)
Kidney Margin (OD04340)	9.0	10.4
Kidney Ca, Nuclear grade 3	5.2	8.3
(OD04348)
Kidney Margin (OD04348)	6.9	4.7
Kidney Cancer (OD04622-01)	41.8	45.4
Kidney Margin (OD04622-03)	1.9	1.4
Kidney Cancer (OD04450-01)	9.2	6.2
Kidney Margin (OD04450-03)	10.2	9.0
Kidney Cancer 8120607	2.2	1.7
Kidney Margin 8120608	6.5	6.4
Kidney Cancer 8120613	2.2	0.7
Kidney Margin 8120614	6.3	3.0
Kidney Cancer 9010320	10.9	16.5
Kidney Margin 9010321	9.0	11.3
Normal Uterus	4.3	6.3
Uterus Cancer 064011	13.4	17.7
Normal Thyroid	9.1	14.9
Thyroid Cancer 064010	6.4	5.9
Thyroid Cancer A302152	4.4	5.1
Thyroid Margin A302153	12.0	22.1
Normal Breast	9.9	14.3
Breast Cancer (OD04566)	0.4	0.2
Breast Cancer (OD04590-01)	5.3	3.9
Breast Cancer Mets (OD04590-03)	4.0	10.4
Breast Cancer Metastasis (OD04655-05)	7.2	4.4
Breast Cancer 064006	5.2	3.3
Breast Cancer 1024	12.1	18.6
Breast Cancer 9100266	2.7	5.3
Breast Margin 9100265	5.0	5.8
Breast Cancer A209073	0.5	1.8
Breast Margin A209073	1.7	0.4
Normal Liver	39.5	47.0
Liver Cancer 064003	4.2	0.6
Liver Cancer 1025	66.4	74.2
Liver Cancer 1026	36.1	42.6
Liver Cancer 6004-T	100.0	100.0
Liver Tissue 6004-N	22.8	34.4
Liver Cancer 6005-T	39.2	35.4
Liver Tissue 6005-N	33.2	38.2
Normal Bladder	6.6	4.9
Bladder Cancer 1023	1.0	4.8
Bladder Cancer A302173	2.6	0.7
Bladder Cancer (OD04718-01)	0.0	0.7
Bladder Normal Adjacent	3.5	14.4
(OD04718-03)
Normal Ovary	50.7	47.3
Ovarian Cancer 064008	10.2	7.4
Ovarian Cancer (OD04768-07)	73.7	80.7
Ovary Margin (OD04768-08)	2.6	0.8
Normal Stomach	2.9	2.9
Gastric Cancer 9060358	0.0	1.1
Stomach Margin 9060359	2.4	0.3
Gastric Cancer 9060395	0.5	1.1
Stomach Margin 9060394	5.2	2.0
Gastric Cancer 9060397	3.4	7.0
Stomach Margin 9060396	1.4	0.0
Gastric Cancer 064005	1.3	6.0

[0677]

TABLE AK
Panel 4.1D
	Rel.	Rel.	Rel.
	Exp. (%)	Exp. (%)	Exp. (%)
	Ag1294b,	Ag4470,	Ag4726,
	Run	Run	Run
Tissue Name	200065765	191882058	204150067
Secondary Th1 act	15.3	21.8	8.4
Secondary Th2 act	7.2	14.9	0.4
Secondary Tr1 act	5.5	11.3	3.1
Secondary Th 1 rest	6.7	5.3	0.5
Secondary Th2 rest	1.0	1.8	2.6
Secondary Tr1 rest	1.3	2.3	0.5
Primary Th1 act	26.6	42.0	24.8
Primary Th2 act	34.2	37.6	19.8
Primary Tr1 act	40.3	42.3	27.9
Primary Th1 rest	0.3	1.1	0.0
Primary Th2 rest	0.5	1.3	0.0
Primary Tr1 rest	0.0	0.0	1.1
CD45RA CD4 lymphocyte	7.7	5.9	2.2
act
CD45RO CD4 lymphocyte	10.9	9.9	16.5
act
CD8 lymphocyte act	11.0	19.2	9.9
Secondary CD8	11.8	10.4	8.9
lymphocyte rest
Secondary CD8	4.7	4.5	1.9
lymphocyte act
CD4 lymphocyte none	0.0	0.6	0.0
2ry Th1/Th2/Tr1_anti-	1.7	4.9	2.5
CD95 CH11
LAK cells rest	0.0	1.1	1.4
LAK cells IL-2	3.1	3.5	1.7
LAK cells IL-2 + IL-	2.9	1.4	1.1
12
LAK cells IL-2 + IFN	0.5	0.0	1.3
gamma
LAK ceils IL-2 + IL-	0.5	2.3	1.1
18
LAK cells PMA/	1.0	3.3	4.2
ionomycin
NK Cells IL-2 rest	1.4	3.9	2.0
Two Way MLR 3 day	3.1	4.8	1.8
Two Way MLR 5 day	5.0	9.3	4.2
Two Way MLR 7 day	4.7	9.4	4.0
PBMC rest	0.6	0.0	0.0
PBMC PWM	11.5	20.6	9.9
PBMC PHA-L	7.2	18.3	14.1
Ramos (B cell) none	1.8	4.5	2.0
Ramos (B cell)	3.4	9.2	2.7
ionomycin
B lymphocytes PWM	20.2	20.3	17.6
B lymphocytes CD40L and	12.2	10.4	11.0
IL-4
EOL-1 dbcAMP	1.5	1.9	3.2
EOL-1 dbcAMP PMA/	1.1	2.7	0.5
ionomycin
Dendritic cells none	8.5	5.1	4.0
Dendritic cells LPS	6.4	6.7	5.9
Dendritic cells anti-	8.7	7.9	4.7
CD40
Monocytes rest	0.0	1.0	0.0
Monocytes LPS	1.1	1.6	2.2
Macrophages rest	8.8	13.0	4.8
Macrophages LPS	0.0	0.0	0.0
HUVEC none	10.1	18.3	8.5
HUVEC starved	7.6	11.5	11.4
HUVEC IL-1beta	5.6	11.1	10.2
HUVEC IFN gamma	21.9	29.9	11.3
HUVEC TNFalpha + IFN	3.5	4.5	1.1
gamma
HUVEC TNFalpha + IL4	31.2	45.7	19.1
HUVEC IL-11	17.7	28.3	20.7
Lung Microvascular EC	65.1	71.2	61.6
none
Lung Microvascular EC	34.4	27.7	30.4
TNFalpha + IL-1beta
Microvascular Dermal	42.3	38.4	29.9
EC none
Microvascular Dermal	16.7	24.1	7.6
EC TNFalpha + IL-
1beta
Bronchial epithelium	2.4	5.0	4.4
TNFalpha + IL-1beta
Small airway	1.7	6.6	4.2
epithelium none
Small airway	2.5	1.3	2.4
epithelium TNFalpha +
IL-1beta
Coronery artery SMC	9.0	10.3	2.1
rest
Coronery artery SMC	5.2	1.8	4.1
TNFalpha + IL-1beta
Astrocytes rest	2.1	1.4	0.8
Astrocytes TNFalpha +	2.2	3.1	1.2
IL-1beta
KU-812 (Basophil) rest	10.2	29.5	14.9
KU-812 (Basophil)	11.1	18.9	8.6
PMA/ionomycin
CCD1106	0.0	2.3	0.9
(Keratinocytes) none
CCD1106 (Keratinocytes)	0.6	0.0	0.0
TNFalpha + IL-1beta
Liver cirrhosis	6.8	10.2	6.0
NCI-H292 none	21.3	16.6	10.3
NCI-H292 IL-4	11.5	9.0	7.3
NCI-H292 IL-9	13.8	32.5	17.4
NCI-H292 IL-13	19.9	5.3	6.7
NCI-H292 IFN gamma	7.3	15.5	13.8
HPAEC none	20.4	37.9	28.9
HPAEC TNFalpha +	21.5	17.4	15.4
IL-1beta
Lung fibroblast none	23.5	22.7	15.7
Lung fibroblast TNF	8.8	11.7	9.2
alpha + IL-1 beta
Lung fibroblast IL-4	21.2	17.7	24.7
Lung fibroblast IL-9	16.8	36.1	18.2
Lung fibroblast IL-13	33.2	36.1	19.8
Lung fibrobast IFN	19.1	11.7	7.8
gamma
Dermal fibroblast	2.9	1.3	0.1
CCD1070 rest
Dermal fibroblast	0.0	0.8	0.2
CCD1070 TNF alpha
Dermal fibroblast	1.5	1.6	4.5
CCD1070 IL-1 beta
Dermal fibroblast IFN	45.1	5.4	32.8
gamma
Dermal fibroblast IL-4	100.0	100.0	100.0
Dermal Fibroblast rest	53.6	39.5	39.2
Neutrophils TNFa +	1.5	0.0	0.6
LPS
Neutrophils rest	10.2	0.5	0.1
Colon	1.5	0.5	1.6
Lung	1.7	0.7	1.3
Thymus	40.1	59.9	25.0
Kidney	1.5	0.7	0.0

[0678]

TABLE AL
Panel 4D
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag1294b, Run	Ag1294b, Run
Tissue Name	138944262	139408252
Secondary Th1 act	10.9	7.7
Secondary Th2 act	6.4	8.0
Secondary Tr1 act	11.3	9.3
Secondary Th1 rest	3.4	2.7
Secondary Th2 rest	1.5	2.5
Secondary Tr1 rest	1.4	2.0
Primary Th1 act	48.0	46.0
Primary Th2 act	38.7	27.7
Primary Tr1 act	72.2	55.5
Primary Th1 rest	3.1	2.3
Primary Th2 rest	1.0	0.8
Primary Tr1 rest	1.1	0.5
CD45RA CD4 lymphocyte act	2.9	1.8
CD45RO CD4 lymphocyte act	18.6	12.2
CD8 lymphocyte act	17.8	6.8
Secondary CD8 lymphocyte rest	6.8	6.0
Secondary CD8 lymphocyte act	5.5	4.1
CD4 lymphocyte none	0.0	0.2
2ry Th1/Th2/Tr1_anti-CD95 CH11	2.9	3.1
LAK cells rest	1.4	0.3
LAK cells IL-2	3.8	2.2
LAK cells IL-2 + IL-12	3.0	0.8
LAK ceils IL-2 + IFN gamma	2.0	1.7
LAK cells IL-2 + IL-18	0.5	0.2
LAK cells PMA/ionomycin	0.7	1.3
NK Cells IL-2 rest	0.7	0.7
Two Way MLR 3 day	1.1	2.5
Two Way MLR 5 day	2.5	2.8
Two Way MLR 7 day	4.5	5.0
PBMC rest	0.0	0.0
PBMC PWM	41.8	29.1
PBMC PHA-L	34.4	21.8
Ramos (B cell) none	4.7	2.4
Ramos (B cell) ionomycin	9.2	5.8
B lymphocytes PWM	51.8	51.4
B lymphocytes CD40L and IL-4	10.2	12.3
EOL-1 dbcAMP	0.3	0.2
EOL-1 dbcAMP PMA/ionomycin	0.4	1.8
Dendritic cells none	6.7	3.8
Dendritic cells LPS	4.7	3.1
Dendritic cells anti-CD40	6.0	5.6
Monocytes rest	0.0	0.0
Monocytes LPS	0.7	0.8
Macrophages rest	19.8	9.9
Macrophages LPS	0.7	0.5
HUVEC none	9.3	10.2
HUVEC starved	19.2	13.1
HUVEC IL-1beta	4.1	1.7
HUVEC IFN gamma	21.0	13.7
HUVEC TNF alpha + IFN gamma	2.8	0.6
HUVEC TNF alpha + IL4	30.8	25.7
HUVEC IL-11	11.6	7.3
Lung Microvascular EC none	24.1	20.0
Lung Microvascular EC TNFalpha +	8.0	12.2
IL-1beta
Microvascular Dermal EC none	64.6	45.7
Microvascular Dermal EC TNFalpha +	18.4	11.7
IL-1beta
Bronchial epithelium TNFalpha +	5.2	5.4
IL1beta
Small airway epithelium none	4.0	3.2
Small airway epithelium TNFalpha +	8.2	4.5
IL-1beta
Coronery artery SMC rest	5.8	6.3
Coronery artery SMC TNFalpha +	4.5	5.1
IL-1beta
Astrocytes rest	0.8	0.5
Astrocytes TNFalpha + IL-1beta	3.6	1.9
KU-812 (Basophil) rest	16.0	11.1
KU-812 (Basophil) PMA/ionomycin	12.3	9.5
CCD1106 (Keratinocytes) none	0.0	0.5
CCD1106 (Keratinocytes) TNFalpha +	0.7	0.4
IL-1beta
Liver cirrhosis	8.4	3.8
Lupus kidney	2.0	3.2
NCI-H292 none	21.9	25.7
NCI-H292 IL-4	15.7	12.3
NCI-H292 1L-9	20.6	14.7
NCI-H292 IL-13	8.3	5.7
NCI-H292 IFN gamma	5.1	8.2
HPAEC none	18.7	23.8
HPAEC TNFalpha + IL-1beta	11.9	12.9
Lung fibroblast none	15.7	13.5
Lung fibroblast TNF alpha + IL-1	6.9	4.7
beta
Lung fibroblast IL-4	25.0	16.6
Lung fibroblast IL-9	14.7	15.8
Lung fibroblast IL-13	40.3	32.5
Lung fibroblast IFN gamma	15.4	17.4
Dermal fibroblast CCD1070 rest	0.5	0.9
Dermal fibroblast CCD1070 TNF alpha	0.9	0.8
Dermal fibroblast CCD1070 IL-1 beta	0.6	0.6
Dermal fibroblast IFN gamma	32.1	18.4
Dermal fibroblast IL-4	100.0	100.0
IBD Colitis 2	0.0	0.0
IBD Crohn's	0.3	0.8
Colon	1.4	0.5
Lung	0.5	0.8
Thymus	2.9	4.3
Kidney	65.5	47.3

[0679]

TABLE AM
general oncology screening panel_v_2.4
                          Rel. Exp. (%)
                          Ag4470, Run
Tissue Name               260280484
Colon cancer 1            1.0
Colon NAT 1               0.3
Colon cancer 2            0.0
Colon NAT 2               0.3
Colon cancer 3            1.1
Colon NAT 3               0.0
Colon malignant cancer 4  2.2
Colon NAT 4               0.0
Lung cancer 1             0.4
Lung NAT 1                0.2
Lung cancer 2             58.2
Lung NAT 2                0.0
Squamous cell carcinoma 3 1.3
Lung NAT 3                46.3
Metastatic melanoma 1     28.9
Melanoma 2                1.4
Melanoma 3                0.3
Metastatic melanoma 4     26.2
Metastatic melanoma 5     16.3
Bladder cancer 1          0.3
Bladder NAT 1             0.0
Bladder cancer 2          1.0
Bladder NAT 2             0.1
Bladder NAT 3             0.0
Bladder NAT 4             1.1
Prostate adenocarcinoma 1 4.3
Prostate adenocarcinoma 2 1.5
Prostate adenocarcinoma 3 1.8
Prostate adenocarcinoma 4 4.4
Prostate NAT 5            1.0
Prostate adenocarcinoma 6 0.5
Prostate adenocarcinoma 7 0.2
Prostate adenocarcinoma 8 0.7
Prostate adenocarcinoma 9 1.7
Prostate NAT 10           0.6
Kidney cancer 1           9.5
Kidney NAT 1              3.7
Kidney cancer 2           100.0
Kidney NAT 2              2.2
Kidney cancer 3           71.7
Kidney NAT 3              1.9
Kidney cancer 4           75.8
Kidney NAT 4              0.9

[0680] AI_comprehensive panel_v1.0 Summary: Ag1294b/Ag4470 Two experiments with two different probe and primer sets 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.

[0681] CNS_neurodegeneration_v1.0 Summary: Ag1294b/Ag4470/Ag4726 Three 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.

[0682] General_screening_panel_v1.4 Summary: Ag4470/Ag4726 Two experiments with different probe and primer sets produce results that are in excellent agreement. 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.

[0683] 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.

[0684] Moderate expression is also seen in the fetal brain, placenta, and endothelial cells.

[0685] 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.

[0686] Panel 4.1D Summary: Ag1294b/Ag4470/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 expression 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.

[0687] 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-H1292 cells, acutely activated T cells, and activated B cells.

[0688] 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.

[0689] 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. Furthermore, therapeutic modulation of the expression or function of this gene product may be useful in the treatment of lung and kidney cancer.

[0690] B. NOV2a (CG122729-01): Novel SPTM Protein.

[0691] Expression of gene CG122729-01 was assessed using the primer-probe sets Ag1441, Ag1447 and Ag4533, described in Tables BA, BB and BC. Results of the RTQ-PCR runs are shown in Tables BD, BE and BF.

TABLE BA
Probe Name Ag1441
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-acttctacggtgacagaatgga-3′	22	2804	220
Probe	TET-5′-cctcatcaaaagcaccatcctggg-3′-	24	2847	221
	TAMRA
Reverse	5′-ctgtccaaagttgctgacaaac-3′	22	2871	222

[0692]

TABLE BB
Probe Name Ag1447
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gatcggagtaaggcctttaaaa-3′	22	1969	223
Probe	TET-5′-ctgctctttccaacccagcctgaag-3′-	25	1995	224
	TAMRA
Reverse	5′-cggggtatctccttagattgag-3′	22	2044	225

[0693]

TABLE 13L
Probe Name Ag433
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-ccaaatgaagacgtgaaagaaa-3′	22	757	226
Probe	TET-5′-accaagtttgagtgatgtccaacaca-3′-	26	792	227
	TAMRA
Reverse	5′-tctgcactgtcttctggatgt-3′	21	818	228

[0694]

TABLE BD
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%)
                               Ag4533, Run
Tissue Name                    224702760
AD 1 Hippo                     26.2
AD 2 Hippo                     2.2
AD 3 Hippo                     25.2
AD 4 Hippo                     16.3
AD 5 Hippo                     25.3
AD 6 Hippo                     100.0
Control 2 Hippo                48.3
Control 4 Hippo                29.1
Control (Path) 3 Hippo         8.6
AD 1 Temporal Ctx              9.2
AD 2 Temporal Ctx              30.4
AD 3 Temporal Ctx              12.9
AD 4 Temporal Ctx              25.9
AD 5 Inf Temporal Ctx          27.9
AD 5 Sup Temporal Ctx          43.5
AD 6 Inf Temporal Ctx          28.9
AD 6 Sup Temporal Ctx          58.6
Control 1 Temporal Ctx         17.1
Control 2 Temporal Ctx         18.4
Control 3 Temporal Ctx         12.2
Control 3 Temporal Ctx         16.8
Control (Path) 1 Temporal Ctx  17.4
Control (Path) 2 Temporal Ctx  13.0
Control (Path) 3 Temporal Ctx  3.2
Control (Path) 4 Temporal Ctx  19.9
AD 1 Occipital Ctx             5.1
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             13.7
AD 4 Occipital Ctx             26.4
AD 5 Occipital Ctx             12.8
AD 6 Occipital Ctx             7.3
Control 1 Occipital Ctx        19.2
Control 2 Occipital Ctx        27.2
Control 3 Occipital Ctx        13.6
Control 4 Occipital Ctx        14.9
Control (Path) 1 Occipital Ctx 24.5
Control (Path) 2 Occipital Ctx 5.0
Control (Path) 3 Occipital Ctx 2.0
Control (Path) 4 Occipital Ctx 15.6
Control 1 Parietal Ctx         17.3
Control 2 Parietal Ctx         40.9
Control 3 Parietal Ctx         6.1
Control (Path) 1 Parietal Ctx  17.7
Control (Path) 2 Parietal Ctx  12.7
Control (Path) 3 Parietal Ctx  3.7
Control (Path) 4 Parietal Ctx  26.1

[0695]

TABLE BE
General_screening_panel_v1.4
                                 Rel. Exp. (%)
                                 Ag4533, Run
Tissue Name                      222735045
Adipose                          13.9
Melanoma* Hs688(A).T             0.0
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    0.0
Testis Pool                      2.1
Prostate ca.* (bone met) PC-3    0.0
Prostate Pool                    1.9
Placenta                         3.4
Uterus Pool                      0.9
Ovarian ca. OVCAR-3              0.1
Ovarian ca. SK-OV-3              1.2
Ovarian ca. OVCAR-4              0.0
Ovarian ca. OVCAR-5              0.0
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.0
Ovary                            4.0
Breast ca. MCF-7                 0.1
Breast ca. MDA-MB-231            0.0
Breast ca. BT 549                0.0
Breast ca. T47D                  0.1
Breast ca. MDA-N                 0.0
Breast Pool                      10.4
Trachea                          13.1
Lung                             1.2
Fetal Lung                       21.6
Lung ca. NCI-N417                0.0
Lung ca. LX-1                    0.0
Lung ca. NCI-H146                0.2
Lung ca. SHP-77                  0.3
Lung ca. A549                    0.0
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 0.0
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  0.0
Lung ca. NCI-H522                0.0
Liver                            1.3
Fetal Liver                      11.9
Liver ca. HepG2                  0.0
Kidney Pool                      8.2
Fetal Kidney                     3.4
Renal ca. 786-0                  0.0
Renal ca. A498                   0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.0
Renal ca. TK-10                  0.0
Bladder                          25.3
Gastric ca. (liver met.) NCI-N87 0.2
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  0.0
Colon ca.* (SW480 met) SW620     0.3
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.0
Colon ca. CaCo-2                 0.2
Colon cancer tissue              13.6
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.0
Colon Pool                       12.2
Small Intestine Pool             4.3
Stomach Pool                     3.3
Bone Marrow Pool                 3.2
Fetal Heart                      2.9
Heart Pool                       2.5
Lymph Node Pool                  7.6
Fetal Skeletal Muscle            3.5
Skeletal Muscle Pool             0.7
Spleen Pool                      100.0
Thymus Pool                      32.1
CNS cancer (glio/astro) U87-MG   0.0
CNS cancer (glio/astro) U-118-MG 0.0
CNS cancer (neuro; met) SK-N-AS  0.0
CNS cancer (astro) SF-539        0.0
CNS cancer (astro) SNB-75        0.0
CNS cancer (glio) SNB-19         0.0
CNS cancer (glio) SF-295         0.3
Brain (Amygdala) Pool            6.7
Brain (cerebellum)               4.8
Brain (fetal)                    2.6
Brain (Hippocampus) Pool         8.2
Cerebral Cortex Pool             6.1
Brain (Substantia nigra) Pool    6.1
Brain (Thalamus) Pool            11.5
Brain (whole)                    12.0
Spinal Cord Pool                 15.5
Adrenal Gland                    9.2
Pituitary gland Pool             1.8
Salivary Gland                   6.9
Thyroid (female)                 1.7
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    7.7

[0696]

TABLE BF
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4533, Run
Tissue Name                      198383974
Secondary Th1 act                0.1
Secondary Th2 act                0.1
Secondary Tr1 act                0.1
Secondary Th1 rest               0.1
Secondary Th2 rest               0.1
Secondary Tr1 rest               0.1
Primary Th1 act                  0.1
Primary Th2 act                  0.4
Primary Tr1 act                  0.2
Primary Th1 rest                 0.3
Primary Th2 rest                 0.3
Primary Tr1 rest                 1.3
CD45RA CD4 lymphocyte act        3.6
CD45RO CD4 lymphocyte act        1.9
CD8 lymphocyte act               1.2
Secondary CD8 lymphocyte rest    0.5
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              1.4
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.1
LAK cells rest                   33.7
LAK cells IL-2                   2.2
LAK cells IL-2 + IL-12           3.6
LAK cells IL-2 + IFN gamma       3.3
LAK cells IL-2 + IL-18           4.0
LAK cells PMA/ionomycin          22.5
NK Cells IL-2 rest               3.6
Two Way MLR 3 day                20.4
Two Way MLR 5 day                12.2
Two Way MLR 7 day                4.1
PBMC rest                        6.9
PBMC PWM                         5.7
PBMC PHA-L                       10.7
Ramos (B cell) none              33.2
Ramos (B cell) ionomycin         41.2
B lymphocytes PWM                17.9
B lymphocytes CD40L and IL-4     100.0
EOL-1 dbcAMP                     20.0
EOL-1 dbcAMP PMA/ionomycin       52.5
Dendritic cells none             46.7
Dendritic cells LPS              26.1
Dendritic cells anti-CD40        53.6
Monocytes rest                   15.2
Monocytes LPS                    15.6
Macrophages rest                 42.0
Macrophages LPS                  12.4
HUVEC none                       0.0
HUVEC starved                    0.1
HUVEC IL-1beta                   0.0
HUVEC IFN gamma                  0.1
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.7
Lung Microvascular EC none       0.0
Lung Microvascular EC TNFalpha + 0.0
IL-1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  0.0
IL1beta
Small airway epithelium none     0.1
Small airway epithelium TNFalpha + 0.2
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha +   0.0
IL-1beta
Astrocytes rest                  0.1
Astrocytes TNFalpha + IL-1beta   0.0
KU-812 (Basophil) rest           0.1
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     0.0
CCD1106 (Keratinocytes) TNFalpha + 0.0
IL-1beta
Liver cirrhosis                  0.5
NCI-H292 none                    0.0
NCI-H292 IL-4                    0.0
NCI-H292 IL-9                    0.0
NCI-H292 IL-13                   0.0
NCI-H292 IFN gamma               0.0
HPAEC none                       0.0
HPAEC TNF alpha + IL-1beta       0.1
Lung fibroblast none             0.0
Lung fibroblast TNF alpha + IL-1 0.0
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.0
Lung fibroblast IL-13            0.0
Lung fibroblast IFN gamma        0.0
Dermal fibroblast CCD1070 rest   0:0
Dermal fibroblast CCD1070 TNF alpha 0.0
Dermal fibroblast CCD1070 IL-1 beta 0.1
Dermal fibroblast IFN gamma      0.2
Dermal fibroblast IL-4           1.8
Dermal Fibroblasts rest          0.6
Neutrophils TNFa + LPS           6.3
Neutrophils rest                 22.4
Colon                            3.0
Lung                             2.2
Thymus                           11.6
Kidney                           1.2

[0697] CNS_neurodegeneration_v1.0 Summary: Ag4533 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 levels in the brain. Please see Panel 1.4 for discussion of utility of this gene in the central nervous system.

[0698] General_screening_panel_v1.4 Summary: Ag4533 Highest expression of this gene is seen in the spleen (CT=28.4). In addition, low to moderate levels of expression are seen in all regions of the CNS examined, including the hippocampus, thalamus, substantia nigra, amygdala, cerebellum and cerebral cortex.

[0699] 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.

[0700] Panel 4.1D Summary: Ag4553 Highest expression of this gene is seen in CD40/IL-40 treated B lymphocytes (CT=27.3). In addition, prominent levels of expression are seen in dendritic cells, eosinophils, macrophages, monocytes, and PBMCs. 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.

[0701] C. NOV3a (CG122777-01): P-type Trefoil Domain Containing Protein

[0702] Expression of gene CG122777-01 was assessed using the primer-probe set Ag4528, described in Table CA. Results of the RTQ-PCR runs are shown in Tables CB and CC.

TABLE CA
Probe Name Ag4528
				SEQ ID
Primers	Sequences	Length	Start Position	No
Forward	5′-cagcatctgcttgttctggt-3′	20	302	229
Probe	TET-5′-gtgctgcatatgcccggtttcct-3′-	23	339	230
	TAMRA
Reverse	5′-gacggacttggacatgtcac-3′	20	373	231

[0703]

TABLE CB
General_screening_panel_v1.4
                                 Rel. Exp. (%)
                                 Ag4528, Run
Tissue Name                      222262771
Adipose                          0.0
Melanoma* Hs688(A).T             1.6
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    1.0
Testis Pool                      31.4
Prostate ca.* (bone met) PC-3    0.5
Prostate Pool                    0.0
Placenta                         0.0
Uterus Pool                      0.0
Ovarian ca. OVCAR-3              1.3
Ovarian ca. SK-OV-3              0.0
Ovarian ca. OVCAR-4              3.8
Ovarian ca. OVCAR-5              2.3
Ovarian ca. IGROV-1              1.2
Ovarian ca. OVCAR-8              3.7
Ovary                            0.4
Breast ca. MCF-7                 1.1
Breast ca. MDA-MB-231            0.4
Breast ca. BT 549                0.0
Breast ca. T47D                  8.7
Breast ca. MDA-N                 0.0
Breast Pool                      0.9
Trachea                          100.0
Lung                             0.0
Fetal Lung                       19.3
Lung ca. NCI-N417                0.0
Lung ca. LX-1                    2.9
Lung ca. NCI-H146                0.9
Lung ca. SHP-77                  0.4
Lung ca. A549                    5.5
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 4.2
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  9.5
Lung ca. NCI-H522                6.0
Liver                            0.0
Fetal Liver                      0.8
Liver ca. HepG2                  15.2
Kidney Pool                      0.0
Fetal Kidney                     0.0
Renal ca. 786-0                  2.1
Renal ca. A498                   0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  7.2
Renal ca. TK-10                  3.7
Bladder                          0.0
Gastric ca. (liver met.) NCI-N87 8.3
Gastric ca. KATO III             1.1
Colon ca. SW-948                 1.5
Colon ca. SW480                  1.5
Colon ca.* (SW480 met) SW620     0.3
Colon ca. HT29                   0.4
Colon ca. HCT-116                1.0
Colon ca. CaCo-2                 1.7
Colon cancer tissue              0.4
Colon ca. SW1116                 1.4
Colon ca. Colo-205               2.5
Colon ca. SW-48                  2.7
Colon Pool                       0.0
Small Intestine Pool             1.1
Stomach Pool                     0.5
Bone Marrow Pool                 0.0
Fetal Heart                      0.0
Heart Pool                       0.0
Lymph Node Pool                  0.3
Fetal Skeletal Muscle            0.5
Skeletal Muscle Pool             0.0
Spleen Pool                      0.0
Thymus Pool                      1.8
CNS cancer (glio/astro) U87-MG   1.3
CNS cancer (glio/astro) U-118-MG 4.0
CNS cancer (neuro; met) SK-N-AS  1.5
CNS cancer (astro) SF-539        2.2
CNS cancer (astro) SNB-75        1.9
CNS cancer (glio) SNB-19         1.2
CNS cancer (glio) SF-295         0.4
Brain (Amygdala) Pool            0.0
Brain (cerebellum)               1.2
Brain (fetal)                    0.4
Brain (Hippocampus) Pool         0.0
Cerebral Cortex Pool             0.0
Brain (Substantia nigra) Pool    0.6
Brain (Thalamus) Pool            0.0
Brain (whole)                    0.0
Spinal Cord Pool                 1.5
Adrenal Gland                    0.8
Pituitary gland Pool             6.7
Salivary Gland                   0.0
Thyroid (female)                 0.0
Pancreatic ca. CAPAN2            0.5
Pancreas Pool                    1.8

[0704]

TABLE CC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4528, Run
Tissue Name                      198361170
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.0
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        0.0
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.0
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              0.0
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   0.0
LAK cells IL-2                   0.0
LAK cells IL-2 + IL-12           0.0
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.0
LAK cells PMA/ionomycin          0.0
NK Cells IL-2 rest               0.0
Two Way MLR 3 day                0.0
Two Way MLR 5 clay               0.0
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.0
PBMC PHA-L                       0.0
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.0
EOL-1 dbcAMP                     2.2
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             0.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.0
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.0
Macrophages LPS                  0.0
HUVEC none                       0.0
HUVEC starved                    0.0
HUVEC IL-1beta                   0.0
HUVEC IFN gamma                  0.0
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.0
Lung Microvascular EC none       0.0
Lung Microvascular EC TNFalpha + 0.0
IL-1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  3.1
IL1beta
Small airway epithelium none     0.0
Small airway epithelium TNFalpha + 0.0
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha +   0.0
IL-1beta
Astrocytes rest                  0.0
Astrocytes TNFalpha + IL-1beta   5.3
KU-812 (Basophil) rest           0.0
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     3.1
CCD1106 (Keratinocytes) TNFalpha + 0.0
IL-1beta
Liver cirrhosis                  0.0
NCI-H292 none                    49.0
NCI-H292 IL-4                    45.1
NCI-H292 IL-9                    50.0
NCI-H292 IL-13                   7.7
NCI-H292 IFN gamma               20.3
HPAEC none                       0.0
HPAEC TNF alpha + IL-1 beta      0.0
Lung fibroblast none             2.6
Lung fibroblast TNF alpha + IL-1 3.3
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.0
Lung fibroblast IL-13            0.0
Lung fibroblast IFN gamma        0.0
Dermal fibroblast CCD1070 rest   0.0
Dermal fibroblast CCD1070 TNF alpha 0.0
Dermal fibroblast CCD1070 IL-1 beta 9.9
Dermal fibroblast IFN gamma      0.0
Dermal fibroblast IL-4           0.0
Dermal Fibroblasts rest          2.2
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 0.0
Colon                            0.0
Lung                             0.0
Thymus                           2.8
Kidney                           100.0

[0705] CNS_neurodegeneration_v1.0 Summary: Ag4528 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0706] General_screening_panel_v1.4 Summary: Ag4528 Highest expression of this gene is seen in the trachea (CT=30.5). Thus, expression of this gene could be used to differentiate between this sample and other samples on this panel and as a marker of this tissue. Low but significant levels of expression are also seen in testis, fetal lung and cell lines derived from gastric, renal, breast, liver and lung cancers.

[0707] Panel 4.1D Summary: Ag4528 This gene is only expressed at detectable levels in the kidney (CT=34). Thus, 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 glomerulonephiritis.

[0708] D. NOV4a (CG124229-01): Insulin Like Growth Factor Binding Protein 3

[0709] Expression of gene CG124229-01 was assessed using the primer-probe set Ag6776, described in Table DA. Results of the RTQ-PCR runs are shown in Tables DB, DC, DD and DE.

TABLE DA
Probe Name Ag6776
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-atatggtccctgccgtagag-3′	201	703	232
Probe	TET-5′-tgaatcacctgaagttcctcaatgtgc-3′-	27	738	233
	TAMRA
Reverse	5′-tgtacacccctgggactca-3′	19	765	234

[0710]

TABLE DB
AI_comprehensive panel_v1.0
                                 Rel. Exp. (%)
                                 Ag6776, Run
Tissue Name                      283839691
110967 COPD-F                    2.0
110980 COPD-F                    18.6
110968 COPD-M                    1.2
110977 COPD-M                    41.8
110989 Emphysema-F               14.0
110992 Emphysema-F               3.7
110993 Emphysema-F               1.4
110994 Emphysema-F               1.7
110995 Emphysema-F               9.5
110996 Emphysema-F               1.3
110997 Asthma-M                  2.5
111001 Asthma-F                  6.3
111002 Asthma-F                  8.1
111003 Atopic Asthma-F           7.9
111004 Atopic Asthma-F           6.3
111005 Atopic Asthma-F           4.2
111006 Atopic Asthma-F           0.6
111417 Allergy-M                 5.9
112347 Allergy-M                 0.1
112349 Normal Lung-F             0.1
112357 Normal Lung-F             4.6
112354 Normal Lung-M             9.9
112374 Crohns-F                  2.5
112389 Match Control Crohns-F    3.9
112375 Crohns-F                  2.5
112732 Match Control Crohns-F    0.5
112725 Crohns-M                  2.4
112387 Match Control Crohns-M    16.4
112378 Crohns-M                  0.2
112390 Match Control Crohns-M    25.7
112726 Crohns-M                  1.3
1112731 Match Control Crohns-M   12.0
112380 Ulcer Col-F               8.8
112734 Match Control Ulcer Col-F 1.4
112384 Ulcer Col-F               12.5
112737 Match Control Ulcer Col-F 0.6
112386 Ulcer Col-F               4.8
112738 Match Control Ulcer Col-F 0.8
112381 Ulcer Col-M               0.2
112735 Match Control Ulcer Col-M 0.5
112382 Ulcer Col-M               6.9
112394 Match Control Ulcer Col-M 2.8
112383 Ulcer Col-M               9.9
112736 Match Control Ulcer Col-M 5.1
112423 Psoriasis-F               1.5
112427 Match Control Psoriasis-F 100.0
112418 Psoriasis-M               2.4
112723 Match Control Psoriasis-M 0.3
112419 Psoriasis-M               4.0
112424 Match Control Psoriasis-M 6.5
112420 Psoriasis-M               35.8
112425 Match Control Psoriasis-M 79.6
104689 (MF) OA Bone-Backus       15.8
104690 (MF) Adj “Normal” Bone-Backus 11.0
104691 (MF) OA Synovium-Backus   1.7
104692 (BA) OA Cartilage-Backus  0.0
104694 (BA) OA Bone-Backus       4.2
104695 (BA) Adj “Normal” Bone-Backus 4.3
104696 (BA) OA Synovium-Backus   3.6
104700 (SS) OA Bone-Backus       3.2
104701 (SS) Adj “Normal” Bone-Backus 7.5
104702 (SS) OA Synovium-Backus   3.7
117093 OA Cartilage Rep7         17.7
112672 OA Bone5                  21.8
112673 OA Synovium5              9.2
112674 OA Synovial Fluid cells5  12.7
117100 OA Cartilage Rep14        2.8
112756 OA Bone9                  1.7
112757 OA Synovium9              0.2
112758 OA Synovial Fluid Cells9  1.3
117125 RA Cartilage Rep2         1.8
113492 Bone2 RA                  0.6
113493 Synovium2 RA              0.3
113494 Syn Fluid Cells RA        0.5
113499 Cartilage4 RA             0.6
113500 Bone4 RA                  0.6
113501 Synovium4 RA              0.4
113502 Syn Fluid Cells4 RA       0.4
113495 Cartilage3 RA             0.4
113496 Bone3 RA                  0.5
113497 Synovium3 RA              0.3
113498 Syn Fluid Cells3 RA       0.6
117106 Normal Cartilage Rep20    2.0
113663 Bone3 Normal              0.0
113664 Synovium3 Normal          0.0
113665 Syn Fluid Cells3 Normal   0.1
117107 Normal Cartilage Rep22    2.7
113667 Bone4 Normal              24.1
113668 Synovium4 Normal          31.6
113669 Syn Fluid Cells4 Normal   36.1

[0711]

TABLE DC
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%) Ag6776,
Tissue Name                    Run 278368013
AD 1 Hippo                     16.6
AD 2 Hippo                     26.8
AD 3 Hippo                     11.3
AD 4 Hippo                     4.6
AD 5 Hippo                     83.5
AD 6 Hippo                     100.0
Control 2 Hippo                32.1
Control 4 Hippo                14.3
Control (Path) 3 Hippo         44.8
AD 1 Temporal Ctx              26.8
AD 2 Temporal Ctx              30.6
AD 3 Temporal Ctx              9.2
AD 4 Temporal Ctx              14.3
AD 5 Inf Temporal Ctx          45.4
AD 5 Sup Temporal Ctx          41.5
AD 6 Inf Temporal Ctx          55.9
AD 6 Sup Temporal Ctx          80.1
Control 1 Temporal Ctx         2.4
Control 2 Temporal Ctx         25.3
Control 3 Temporal Ctx         23.5
Control 3 Temporal Ctx         8.2
Control (Path) 1 Temporal Ctx  40.6
Control (Path) 2 Temporal Ctx  31.0
Control (Path) 3 Temporal Ctx  52.9
Control (Path) 4 Temporal Ctx  23.5
AD 1 Occipital Ctx             13.5
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             13.8
AD 4 Occipital Ctx             19.6
AD 5 Occipital Ctx             61.6
AD 6 Occipital Ctx             48.6
Control 1 Occipital Ctx        3.6
Control 2 Occipital Ctx        87.7
Control 3 Occipital Ctx        35.6
Control 4 Occipital Ctx        13.4
Control (Path) 1 Occipital Ctx 43.5
Control (Path) 2 Occipital Ctx 7.5
Control (Path) 3 Occipital Ctx 56.6
Control (Path) 4 Occipital Ctx 10.9
Control 1 Parietal Ctx         4.1
Control 2 Parietal Ctx         26.1
Control 3 Parietal Ctx         16.4
Control (Path) 1 Parietal Ctx  37.9
Control (Path) 2 Parietal Ctx  25.5
Control (Path) 3 Parietal Ctx  69.3
Control (Path) 4 Parietal Ctx  28.5

[0712]

TABLE DD
General_screening_panel_v1.6
                                 Rel. Exp. (%) Ag6776,
Tissue Name                      Run 277729935
Adipose                          2.0
Melanoma* Hs688(A).T             68.8
Melanoma* Hs688(B).T             41.8
Melanoma* M14                    0.7
Melanoma* LOXIMVI                1.1
Melanoma* SK-MEL-5               0.2
Squamous cell carcinoma SCC-4    0.5
Testis Pool                      0.3
Prostate ca.* (bone met) PC-3    0.8
Prostate Pool                    0.9
Placenta                         10.2
Uterus Pool                      1.3
Ovarian ca. OVCAR-3              4.1
Ovarian ca. SK-OV-3              11.4
Ovarian ca. OVCAR-4              10.0
Ovarian ca. OVCAR-5              0.0
Ovarian ca. IGROV-1              2.9
Ovarian ca. OVCAR-8              0.4
Ovary                            0.7
Breast ca. MCF-7                 0.7
Breast ca. MDA-MB-231            0.6
Breast ca. BT 549                1.7
Breast ca. T47D                  0.0
Breast ca. MDA-N                 0.0
Breast Pool                      3.6
Trachea                          1.5
Lung                             0.9
Fetal Lung                       0.9
Lung ca. NCI-N417                0.0
Lung ca. LX-1                    1.0
Lung ca. NCI-H146                0.0
Lung ca. SHP-77                  0.0
Lung ca. A549                    6.2
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 0.3
Lung ca. NCI-H460                5.8
Lung ca. HOP-62                  0.3
Lung ca. NCI-H522                0.3
Liver                            1.3
Fetal Liver                      8.7
Liver ca. HepG2                  0.0
Kidney Pool                      6.8
Fetal Kidney                     0.6
Renal ca. 786-0                  29.9
Renal ca. A498                   51.8
Renal ca. ACHN                   0.3
Renal ca. UO-31                  0.2
Renal ca. TK-10                  2.6
Bladder                          0.7
Gastric ca. (liver met.) NCI-N87 1.8
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.3
Colon ca. SW480                  1.3
Colon ca.* (SW480 met) SW620     0.0
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.0
Colon ca. CaCo-2                 0.1
Colon cancer tissue              2.0
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.1
Colon ca. SW-48                  0.0
Colon Pool                       2.5
Small Intestine Pool             8.0
Stomach Pool                     3.0
Bone Marrow Pool                 1.7
Fetal Heart                      1.6
Heart Pool                       0.8
Lymph Node Pool                  2.2
Fetal Skeletal Muscle            1.6
Skeletal Muscle Pool             0.1
Spleen Pool                      1.5
Thymus Pool                      1.6
CNS cancer (glio/astro) U87-MG   8.5
CNS cancer (glio/astro) U-118-MG 100.0
CNS cancer (neuro; met) SK-N-AS  0.1
CNS cancer (astro) SF-539        4.6
CNS cancer (astro) SNB-75        51.1
CNS cancer (glio) SNB-19         2.9
CNS cancer (glio) SF-295         58.6
Brain (Amygdala) Pool            0.1
Brain (cerebellum)               0.1
Brain (fetal)                    0.5
Brain (Hippocampus) Pool         0.2
Cerebral Cortex Pool             0.2
Brain (Substantia nigra) Pool    0.0
Brain (Thalamus) Pool            0.1
Brain (whole)                    0.3
Spinal Cord Pool                 0.1
Adrenal Gland                    0.2
Pituitary gland Pool             0.6
Salivary Gland                   0.1
Thyroid (female)                 0.1
Pancreatic ca. CAPAN2            5.4
Pancreas Pool                    0.3

[0713]

TABLE DE
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag6776, Run
Tissue Name                      277729707
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.0
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        38.4
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.0
Secondary CD8 lymphocyte act     0.1
CD4 lymphocyte none              0.1
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   0.0
LAK cells IL-2                   0.0
LAK cells IL-2 + IL-12           0.0
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.1
LAK cells PMA/ionomycin          0.1
NK Cells IL-2 rest               0.2
Two Way MLR 3 day                0.0
Two Way MLR 5 day                0.0
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.0
PBMC PHA-L                       0.0
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.1
EOL-1 dbcAMP                     0.0
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             0.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.0
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.0
Macrophages LPS                  0.0
HUVEC none                       0.2
HUVEC starved                    0.1
HUVEC IL-1beta                   0.2
HUVEC IFN gamma                  0.2
HUVEC TNF alpha + IFN gamma      0.1
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.1
Lung Microvascular EC none       0.1
Lung Microvascular EC TNFalpha + 0.0
IL-1beta
Microvascular Dermal EC none     0.2
Microsvasular Dermal EC TNFalpha + 0.1
IL-1beta
Bronchial epithelium TNFalpha +  0.5
IL1beta
Small airway epithelium none     0.3
Small airway epithelium TNFalpha + 2.2
IL-1beta
Coronery artery SMC rest         37.4
Coronery artery SMC TNFalpha +   31.4
IL-1beta
Astrocytes rest                  13.5
Astrocytes TNFalpha + IL-1beta   7.8
KU-812 (Basophil) rest           0.0
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     0.3
CCD1106 (Keratinocytes) TNFalpha + 0.1
IL-1beta
Liver cirrhosis                  3.6
NCI-H292 none                    14.5
NCI-H292 IL-4                    4.8
NCI-H292 IL-9                    17.7
NCI-H292 IL-13                   5.6
NCI-H292 IFN gamma               5.3
HPAEC none                       0.3
HPAEC TNF alpha + IL-1 beta      1.0
Lung fibroblast none             0.3
Lung fibroblast TNF alpha + IL-1 1.4
beta
Lung fibroblast IL-4             0.2
Lung fibroblast IL-9             0.5
Lung fibroblast IL-13            0.2
Lung fibroblast IFN gamma        0.3
Dermal fibroblast CCD1070 rest   93.3
Dermal fibroblast CCD1070 TNF alpha 100.0
Dermal fibroblast CCD1070 IL-1 beta 56.6
Dermal fibroblast IFN gamma      22.8
Dermal fibroblast IL-4           69.3
Dermal Fibroblasts rest          14.6
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 0.0
Colon                            0.5
Lung                             1.4
Thymus                           0.2
Kidney                           3.0

[0714] AI_comprehensive panel_v1.0 Summary: Ag6776 Highest expression of this gene is seen in normal tissue adjacent to psoriasis (CT=19.7). Overall, this gene is highly expressed in many samples on this panel, including clusters of samples derived from psoriasis derived tissue. Please see Panel 4.1 D for discussion of utility of this gene in autoimmune disease.

[0715] CNS_neurodegeneration_v1.0 Summary: Ag6776 This panel does not show differential expression of this gene in Alzheimer's disease. However, this expression profile confirms the presence of this gene at moderate levels in the brain. The insulin and insulin-like growth factors belong to a family of polypeptides essential for proper regulation of physiologic processes such as energy metabolism, cell proliferation, development, and differentiation. The insulin-like growth factors bind to IGF with high affinity and compete with the IGF receptor for IGF binding. Transgenic mice overexpressing insulin-like growth factor binding proteins (IGFBPs) tend to show brain developmental abnormalities, suggesting a role for these proteins in neurodevelopment. Furthermore, treatment with glycosaminoglycans (which increases muscle re-innervation after motor neuron death) upregulates serum levels of both IGF and IGFBP. Thus, on the basis of its homology to other established IGFBPs, the novel IGFBP encoded by this gene may be useful in the treatment of diseases such as ALS, multiple sclerosis, and peripheral nerve injury on the basis of its homology to other established IGFBPs. [Dave Stone]

[0716] General_screening_panel_v1.6 Summary: Ag6776 Highest expression of this gene is seen in a brain cancer cell line (CT=20.5). In addition, high levels of expression are seen in a cluster of brain cancer cell lines, melanoma cell lines, renal cancer cell lines, and ovarian cancer cell lines. This gene encodes a putative insulin like growth factor binding protein 3 (IGFBP3). IGFBP-3 enhances the p53-dependent apoptotic response of colorectal cells to DNA damage and is inversely associated with risk for colorectal cancer. Expression of IGFBP-3 induces growth inhibition and differentiation of the human colon carcinoma cell line, Caco-2. Thus, therapeutic targeting modulation of this gene product may be useful in the treatment of cancer, especially in those cancer types, like brain and renal tumors where the gene is overexpressed in the tumor cell line compared to the normal tissue sample.

[0717] This gene is also expressed at moderate levels in all regions of the CNS examined. Please see Panel CNS_neurodegeneration_v1.0 for discussion of utility of this gene in the CNS.

[0718] Among tissues with metabolic function, this gene is expressed at high to moderate levels in pituitary, adipose, adrenal gland, pancreas, thyroid, and adult and fetal skeletal muscle, heart, and liver. Cortizo et. al has suggested that alterations in IGFBP3 levels may result in diabetic complications (Acta Diabetol 1998 July;35(2):85-90). This 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.

[0719] Panel 4.1D Summary: Ag6776 Highest expression of this gene is seen in TNF-alpha stimulated dermal fibroblasts (CT=25.3). In addition, high levels of expression are seen in a cluster of treated and untreated samples derived from dermal fibroblasts. Miura has suggested that dermal fibroblasts promote IGFBP mediated keratinocyte proliferation and may contribute to the epidermal hyperplasia manifest in psoriasis (Arch Dermatol Res 2000 December;292(12):590-7). Thus, based on the homology of this gene to IGFBP3 and the expression in dermal fibroblasts and psoriasis related tissue on AI_comprehensive panel_v1.0, modulation of the expression or function of this gene may be useful in the clinical management of this disease.

[0720] E. NOV5a (CG124445-02): Transmembrane Kuzbanian

[0721] Expression of gene CG124445-02 was assessed using the primer-probe set Ag7026, described in Table EA.

TABLE EA
Probe Name Ag/7026
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gattatcttacaatgtggattcattacac-3′	29	330	235
Probe	TET-5′-accagcgtgccaaaagagcagtctct-3′-	26	366	236
	TAMRA
Reverse	5′-aacttcgtgagcaaaagtaatgtg-3′	24	392	237

[0722] CNS_neurodegeneration_v1.0 Summary: Ag7026 Expression of the CG124445-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0723] General_screening_panel_v1.6 Summary: Ag7026 Expression of the CG124445-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0724] Panel 4.1D Summary: Ag7026 Expression of the CG124445-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0725] F. NOV6a (CG124590-02): Integrin Beta-4 Precursor

[0726] Expression of gene CG124590-02 was assessed using the primer-probe set Ag6832, described in Table FA. Results of the RTQ-PCR runs are shown in Tables FB and EC. Please note that CG124590-02 represents a full-length physical clone.

TABLE FA
Probe Name Ag6832
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-atgatctggacaacctcaagaa-3′	22	493	238
Probe	TET-5′-ctcaggacccgagccaggttctgc-3′-	24	521	239
	TAMRA
Reverse	5′-gtggcgctggtgagct-3′	16	547	240

[0727]

TABLE FB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%) Ag6832,
Tissue Name                    Run 278022742
AD 1 Hippo                     14.4
AD 2 Hippo                     45.1
AD 3 Hippo                     8.4
AD 4 Hippo                     22.4
AD 5 Hippo                     19.5
AD 6 Hippo                     100.0
Control 2 Hippo                18.9
Control 4 Hippo                50.0
Control (Path) 3 Hippo         8.4
AD 1 Temporal Ctx              16.8
AD 2 Temporal Ctx              26.1
AD 3 Temporal Ctx              5.0
AD 4 Temporal Ctx              20.2
AD 5 Inf Temporal Ctx          44.4
AD 5 Sup Temporal Ctx          45.7
AD 6 Inf Temporal Ctx          67.4
AD 6 Sup Temporal Ctx          74.2
Control 1 Temporal Ctx         7.2
Control 2 Temporal Ctx         12.9
Control 3 Temporal Ctx         9.1
Control 3 Temporal Ctx         17.2
Control (Path) 1 Temporal Ctx  11.5
Control (Path) 2 Temporal Ctx  7.4
Control (Path) 3 Temporal Ctx  10.4
Control (Path) 4 Temporal Ctx  12.9
AD 1 Occipital Ctx             6.3
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             4.8
AD 4 Occipital Ctx             16.2
AD 5 Occipital Ctx             12.4
AD 6 Occipital Ctx             13.7
Control 1 Occipital Ctx        4.6
Control 2 Occipital Ctx        11.0
Control 3 Occipital Ctx        9.0
Control 4 Occipital Ctx        14.7
Control (Path) 1 Occipital Ctx 23.3
Control (Path) 2 Occipital Ctx 4.0
Control (Path) 3 Occipital Ctx 4.1
Control (Path) 4 Occipital Ctx 4.3
Control 1 Parietal Ctx         10.8
Control 2 Parietal Ctx         33.9
Control 3 Parietal Ctx         9.4
Control (Path) 1 Parietal Ctx  15.5
Control (Path) 2 Parietal Ctx  9.2
Control (Path) 3 Parietal Ctx  7.4
Control (Path) 4 Parietal Ctx  12.7

[0728]

TABLE FC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag6832, Run
Tissue Name                      278022641
Secondary Th1 act                0.0
Secondary Th2 act                0.1
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.0
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        0.0
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.0
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              0.0
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   0.0
LAK cells IL-2                   0.0
LAK cells IL-2 + IL-12           0.0
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.0
LAK cells PMA/ionomycin          0.0
NK Cells IL-2 rest               0.0
Two Way MLR 3 day                0.0
Two Way MLR 5 day                0.0
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.0
PBMC PHA-L                       0.1
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.1
EOL-1 dbcAMP                     0.0
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             0.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.0
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.0
Macrophages LPS                  0.0
HUVEC none                       0.3
HUVEC starved                    0.2
HUVEC IL-1beta                   0.1
HUVEC IFN gamma                  0.4
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.7
Lung Microvascular EC none       4.9
Lung Microvascular EC TNFalpha + 0.3
IL-1beta
Microvascular Dermal EC none     1.5
Microsvasular Dermal EC TNFalpha + 0.4
IL-1beta
Bronchial epithelium TNFalpha +  50.0
IL1beta
Small airway epithelium none     50.3
Small airway epithelium TNFalpha + 75.3
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha +   0.0
IL-1beta
Astrocytes rest                  0.0
Astrocytes TNFalpha + IL-1beta   0.3
KU-812 (Basophil) rest           0.0
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     100.0
CCD1106 (Keratinocytes) TNFalpha + 33.4
IL-1beta
Liver cirrhosis                  1.2
NCI-H292 none                    20.7
NCI-H292 IL-4                    34.6
NCI-H292 IL-9                    25.2
NCI-H292 IL-13                   40.9
NCI-H292 IFN gamma               17.2
HPAEC none                       3.0
HPAEC TNF alpha + IL-1 beta      1.5
Lung fibroblast none             0.0
Lung fibroblast TNF alpha + IL-1 0.0
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.0
Lung fibroblast IL-13            0.0
Lung fibroblast IFN gamma        0.0
Dermal fibroblast CCD1070 rest   0.0
Dermal fibroblast CCD1070 TNF alpha 0.0
Dermal fibroblast CCD1070 IL-1 beta 0.0
Dermal fibroblast IFN gamma      0.0
Dermal fibroblast IL-4           0.0
Dermal Fibroblasts rest          0.0
Neutrophils TNFa + LPS           0.1
Neutrophils rest                 0.2
Colon                            1.7
Lung                             0.3
Thymus                           0.4
Kidney                           0.9

[0729] CNS_neurodegeneration_v1.0 Summary: Ag6832 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. Expression of this gene in the brain suggests that the protein encoded by this gene may play a role in central nervous system disorders such as Parkinson's disease, epilepsy, multiple sclerosis, schizophrenia and depression.

[0730] General_screening_panel_v1.6 Summary: Ag6832 Results from one experiment with the CG124590-02 gene are not included. The amp plot indicates that there were experimental difficulties with this run.

[0731] Panel 4.1D Summary: Ag6832 Highest expression of the CG124590-02 gene is detected in keratinocytes (CT=25). High levels of expression of this gene is also detected in small airway epithelium, cytokine treated bronchial epithelium, and NCI-H292 cells. Therefore, expression of this gene may be used to distinguish these samples from other samples in this panel. In addition, moderate levels of expression of this gene is also seen in HPAEC, HUVEC, lung microvascular EC, microvascular dermal EC and neutrophils. Therefore, therapeutic modulation of this gene may be useful in the treatment of autoimmune and inflammatory diseases that involve endothelial cells, such as lupus erythematosus, asthma, emphysema, Crohn's disease, ulcerative colitis, rheumatoid arthritis, osteoarthritis, and psoriasis.

[0732] Low to moderate levels of expression of this gene is also seen in normal tissues represented by colon, lung, thymus and kidney. Therefore, therapeutic modulation of the protein encoded this gene may be useful in the treatment of autoimmune and inflammatory diseases that affect these tissues.

[0733] G. NOV7a (CG124916-01): Selenoprotein P

[0734] Expression of gene CG124916-01 was assessed using the primer-probe set Ag7029, described in Table GA.

TABLE GA
Probe Name Ag7029
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-cagtgactgtggttgctcttct-3′	22	158	241
Probe	TET-5′-tcaagcctcattttatgtatttcttccca-3′-	29	180	242
	TAMRA
Reverse	5′-ttactcgcaggtcttctaatctaaaatat-3′	29	210	243

[0735] CNS_neurodegeneration_v1.0 Summary: Ag7029 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0736] General_screening_panel_v1.6 Summary: Ag7029 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0737] Panel 4.1D Summary: Ag7029 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0738] H. NOV8a (CG126224-01): Novel Type II Membrane Protein with 3 C2 Domains

[0739] Expression of gene CG126224-01 was assessed using the primer-probe set Ag4713, described in Table HA. Results of the RTQ-PCR runs are shown in Tables HB, HC and HD.

TABLE HA
Probe Name Ag4713
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-agttaaacaggcccacagatgt-3′	22	551	244
Probe	TET-5′-tctgaaagatcctcattatcctgacca-3′-	27	582	245
	TAMRA
Reverse	5′-gagcaaaatgattccaagatca-3′	22	609	246

[0740]

TABLE HB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%) Ag4713,
Tissue Name                    Run 224705458
AD 1 Hippo                     7.2
AD 2 Hippo                     22.5
AD 3 Hippo                     9.9
AD 4 Hippo                     3.4
AD 5 Hippo                     91.4
AD 6 Hippo                     51.4
Control 2 Hippo                42.0
Control 4 Hippo                4.6
Control (Path) 3 Hippo         4.8
AD 1 Temporal Ctx              8.9
AD 2 Temporal Ctx              29.3
AD 3 Temporal Ctx              4.8
AD 4 Temporal Ctx              11.5
AD 5 Inf Temporal Ctx          97.9
AD 5 Sup Temporal Ctx          3.4
AD 6 Inf Temporal Ctx          56.3
AD 6 Sup Temporal Ctx          50.7
Control 1 Temporal Ctx         5.4
Control 2 Temporal Ctx         69.3
Control 3 Temporal Ctx         13.3
Control 4 Temporal Ctx         7.3
Control (Path) 1 Temporal Ctx  82.4
Control (Path) 2 Temporal Ctx  28.1
Control (Path) 3 Temporal Ctx  4.0
Control (Path) 4 Temporal Ctx  35.1
AD 1 Occipital Ctx             8.4
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             4.2
AD 4 Occipital Ctx             8.2
AD 5 Occipital Ctx             20.7
AD 6 Occipital Ctx             61.6
Control 1 Occipital Ctx        20.7
Control 2 Occipital Ctx        52.5
Control 3 Occipital Ctx        8.7
Control 4 Occipital Ctx        2.4
Control (Path) 1 Occipital Ctx 100.0
Control (Path) 2 Occipital Ctx 6.0
Control (Path) 3 Occipital Ctx 2.6
Control (Path) 4 Occipital Ctx 11.4
Control 1 Parietal Ctx         4.7
Control 2 Parietal Ctx         42.3
Control 3 Parietal Ctx         15.2
Control (Path) 1 Parietal Ctx  98.6
Control (Path) 2 Parietal Ctx  18.3
Control (Path) 3 Parietal Ctx  4.0
Control (Path) 4 Parietal Ctx  41.2

[0741]

TABLE HC
General_screening_panel_v1.4
                                 Rel. Exp. (%) Ag4713,
Tissue Name                      Run 222825921
Adipose                          18.8
Melanoma* Hs688(A).T             0.0
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    39.8
Melanoma* LOXIMVI                42.6
Melanoma* SK-MEL-5               65.5
Squamous cell carcinoma SCC-4    10.5
Testis Pool                      4.3
Prostate ca.* (bone met) PC-3    72.7
Prostate Pool                    2.8
Placenta                         1.3
Uterus Pool                      5.8
Ovarian ca. OVCAR-3              17.0
Ovarian ca. SK-OV-3              79.0
Ovarian ca. OVCAR-4              0.1
Ovarian ca. OVCAR-5              42.9
Ovarian ca. IGROV-1              1.1
Ovarian ca. OVCAR-8              5.1
Ovary                            2.1
Breast ca. MCF-7                 0.0
Breast ca. MDA-MB-231            11.1
Breast ca. BT 549                16.8
Breast ca. T47D                  66.9
Breast ca. MDA-N                 57.4
Breast Pool                      9.6
Trachea                          8.7
Lung                             1.3
Fetal Lung                       10.4
Lung ca. NCI-N417                0.0
Lung ca. LX-1                    59.5
Lung ca. NCI-H146                10.5
Lung ca. SHP-77                  7.2
Lung ca. A549                    6.7
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 2.5
Lung ca. NCI-H460                29.9
Lung ca. HOP-62                  21.2
Lung ca. NCI-H522                7.4
Liver                            0.3
Fetal Liver                      4.3
Liver ca. HepG2                  0.1
Kidney Pool                      18.0
Fetal Kidney                     2.5
Renal ca. 786-0                  17.0
Renal ca. A498                   9.9
Renal ca. ACHN                   39.2
Renal ca. UO-31                  41.5
Renal ca. TK-10                  30.4
Bladder                          15.0
Gastric ca. (liver met.) NCI-N87 34.2
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  9.3
Colon ca.* (SW480 met) SW620     16.6
Colon ca. HT29                   9.0
Colon ca. HCT-116                0.3
Colon ca. CaCo-2                 0.9
Colon cancer tissue              20.6
Colon ca. SW1116                 0.0
Colon ca. Colo-205               3.8
Colon ca. SW-48                  0.0
Colon Pool                       9.9
Small Intestine Pool             5.7
Stomach Pool                     6.9
Bone Marrow Pool                 4.0
Fetal Heart                      1.0
Heart Pool                       4.2
Lymph Node Pool                  8.8
Fetal Skeletal Muscle            4.5
Skeletal Muscle Pool             4.8
Spleen Pool                      10.3
Thymus Pool                      9.4
CNS cancer (glio/astro) U87-MG   100.0
CNS cancer (glio/astro) U-118-MG 9.2
CNS cancer (neuro; met) SK-N-AS  1.9
CNS cancer (astro) SF-539        2.5
CNS cancer (astro) SNB-75        0.2
CNS cancer (glio) SNB-19         1.3
CNS cancer (glio) SF-295         0.9
Brain (Amygdala) Pool            20.4
Brain (cerebellum)               33.9
Brain (fetal)                    30.1
Brain (Hippocampus) Pool         20.6
Cerebral Cortex Pool             34.6
Brain (Substantia nigra) Pool    26.8
Brain (Thalamus) Pool            40.3
Brain (whole)                    28.5
Spinal Cord Pool                 5.4
Adrenal Gland                    2.4
Pituitary gland Pool             2.7
Salivary Gland                   0.6
Thyroid (female)                 1.3
Pancreatic ca. CAPAN2            11.0
Pancreas Pool                    7.7

[0742]

TABLE HD
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4713, Run
Tissue Name                      202012796
Secondary Th1 act                0.2
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.2
Secondary Th2 rest               0.1
Secondary Tr1 rest               0.2
Primary Th1 act                  0.9
Primary Th2 act                  0.5
Primary Tr1 act                  1.4
Primary Th1 rest                 1.7
Primary Th2 rest                 0.7
Primary Tr1 rest                 1.0
CD45RA CD4 lymphocyte act        0.4
CD45RO CD4 lymphocyte act        0.2
CD8 lymphocyte act               0.1
Secondary CD8 lymphocyte rest    0.9
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              1.2
2ry Th1/Th2/Tr1_anti-CD95 CH11   1.5
LAK cells rest                   20.0
LAK cells IL-2                   0.7
LAK cells IL-2 + IL-12           2.5
LAK cells IL-2 + IFN gamma       1.3
LAK cells IL-2 + IL-18           0.7
LAK cells PMA/ionomycin          33.9
NK Cells IL-2 rest               0.4
Two Way MLR 3 day                27.2
Two Way MLR 5 day                12.0
Two Way MLR 7 day                1.8
PBMC rest                        5.3
PBMC PWM                         3.7
PBMC PHA-L                       6.4
Ramos (B cell) none              0.2
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                2.6
B lymphocytes CD40L and IL-4     2.8
EOL-1 dbcAMP                     35.4
EOL-1 dbcAMP PMA/ionomycin       41.8
Dendritic cells none             8.1
Dendritic cells LPS              12.7
Dendritic cells anti-CD40        6.8
Monocytes rest                   41.8
Monocytes LPS                    88.3
Macrophages rest                 20.4
Macrophages LPS                  22.4
HUVEC none                       25.7
HUVEC starved                    82.4
HUVEC IL-1beta                   55.1
HUVEC IFN gamma                  100.0
HUVEC TNF alpha + IFN gamma      63.3
HUVEC TNF alpha + IL4            91.4
HUVEC IL-11                      33.7
Lung Microvascular EC none       50.3
Lung Microvascular EC TNFalpha + 58.2
IL-1beta
Microvascular Dermal EC none     11.8
Microsvasular Dermal EC TNFalpha + 20.7
IL-1beta
Bronchial epithelium TNFalpha +  6.3
IL1beta
Small airway epithelium none     1.2
Small airway epithelium TNFalpha + 1.8
IL-1beta
Coronery artery SMC rest         0.2
Coronery artery SMC TNFalpha +   1.2
IL-1beta
Astrocytes rest                  1.2
Astrocytes TNFalpha + IL-1beta   0.7
KU-812 (Basophil) rest           2.8
KU-812 (Basophil) PMA/ionomycin  11.7
CCD1106 (Keratinocytes) none     0.2
CCD1106 (Keratinocytes) TNFalpha + 0.3
IL-1beta
Liver cirrhosis                  3.5
NCI-H292 none                    7.9
NCI-H292 IL-4                    7.7
NCI-H292 IL-9                    12.9
NCI-H292 IL-13                   5.0
NCI-H292 IFN gamma               5.2
HPAEC none                       7.1
HPAEC TNF alpha + IL-1 beta      15.1
Lung fibroblast none             0.7
Lung fibroblast TNF alpha + IL-1 1.5
beta
Lung fibroblast IL-4             1.2
Lung fibroblast IL-9             2.5
Lung fibroblast IL-13            1.5
Lung fibroblast IFN gamma        1.2
Dermal fibroblast CCD1070 rest   0.1
Dermal fibroblast CCD1070 TNF alpha 0.4
Dermal fibroblast CCD1070 IL-1 beta 0.6
Dermal fibroblast IFN gamma      0.4
Dermal fibroblast IL-4           0.4
Dermal Fibroblasts rest          0.2
Neutrophils TNFa + LPS           71.2
Neutrophils rest                 18.0
Colon                            1.3
Lung                             5.9
Thymus                           10.3
Kidney                           1.3

[0743] CNS_neurodegeneration_v1.0 Summary: Ag4713 This panel confirms the expression of the CG126224-01 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.

[0744] General_screening_panel_v1.4 Summary: Ag4713 Highest expression of the CG126224-01 gene is detected in CNS cancer U87-MG cell line (CT=28.8). 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.

[0745] Among tissues with metabolic or endocrine function, this gene is expressed at moderate to low 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.

[0746] Interestingly, this gene is expressed at much higher levels in fetal (CT=32-33) when compared to adult lung and liver (CT=35-37). This observation suggests that expression of this gene can be used to distinguish fetal from adult lung and liver, respectively. In addition, the relative overexpression of this gene in fetal tissue 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.

[0747] 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.

[0748] Panel 4.1D Summary: Ag4713 Highest expression of the CG126224-01 gene is detected in IFN gamma treated HUVEC cells (CT=28). High to moderate levels of expression in LAK cells, two way MLR, PBMC, B lymphocytes, eosinophils, dendritic cells, monocytes, macrophages, endothelial cells, small airway epithelium, basophils, NCI-H292, lung fibroblast and activated neutrophils. In addition, moderate to low levels of expression of this gene is also seen in liver cirrhosis and normal tissues represented by colon, lung, thymus and kidney. Therefore, therapeutic modulation of this gene may be useful in the treatment of inflammatory and autoimmune diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, osteoarthritis and liver cirrhosis.

[0749] I. NOV9a (CG126233-01): ctl2

[0750] Expression of gene CG 126233-01 was assessed using the primer-probe set Ag4722, described in Table IA. Results of the RTQ-PCR runs are shown in Tables IB, IC and ID.

TABLE IA
Probe Name Ag4722
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-gcatgtactttgaactgcaaca-3′	22	947	247
Probe	TET-5′-catggttcacatttatgataatactctgca-	30	971	248
	3′-TAMRA
Reverse	5′-agcatgaggatgacaatcactt-3′	22	1007	249

[0751]

TABLE IB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%) Ag4722,
Tissue Name                    Run 224706358
AD 1 Hippo                     4.2
AD 2 Hippo                     11.7
AD 3 Hippo                     2.5
AD 4 Hippo                     4.1
AD 5 hippo                     93.3
AD 6 Hippo                     27.9
Control 2 Hippo                18.3
Control 4 Hippo                8.0
Control (Path) 3 Hippo         3.0
AD 1 Temporal Ctx              4.6
AD 2 Temporal Ctx              21.0
AD 3 Temporal Ctx              2.2
AD 4 Temporal Ctx              14.9
AD 5 Inf Temporal Ctx          35.8
AD 5 Sup Temporal Ctx          20.4
AD 6 Inf Temporal Ctx          35.4
AD 6 Sup Temporal Ctx          26.8
Control 1 Temporal Ctx         1.7
Control 2 Temporal Ctx         26.4
Control 3 Temporal Ctx         11.7
Control 4 Temporal Ctx         5.5
Control (Path) 1 Temporal Ctx  56.6
Control (Path) 2 Temporal Ctx  23.5
Control (Path) 3 Temporal Ctx  2.0
Control (Path) 4 Temporal Ctx  34.4
AD 1 Occipital Ctx             5.3
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             3.1
AD 4 Occipital Ctx             12.3
AD 5 Occipital Ctx             14.8
AD 6 Occipital Ctx             29.1
Control 1 Occipital Ctx        2.9
Control 2 Occipital Ctx        69.7
Control 3 Occipital Ctx        13.6
Control 4 Occipital Ctx        4.8
Control (Path) 1 Occipital Ctx 100.0
Control (Path) 2 Occipital Ctx 15.9
Control (Path) 3 Occipital Ctx 0.7
Control (Path) 4 Occipital Ctx 25.5
Control 1 Parietal Ctx         3.1
Control 2 Parietal Ctx         24.3
Control 3 Parietal Ctx         2.2
Control (Path) 1 Parietal Ctx  65.5
Control (Path) 2 Parietal Ctx  15.9
Control (Path) 3 Parietal Ctx  1.7
Control (Path) 4 Parietal Ctx  37.4

[0752]

TABLE IC
General_screening_panel_v1.4
                                 Rel. Exp. (%) Ag4722,
Tissue Name                      Run 222842372
Adipose                          0.3
Melanoma* Hs688(A).T             0.0
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.4
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    9.0
Testis Pool                      7.4
Prostate ca.* (bone met) PC-3    0.1
Prostate Pool                    0.3
Placenta                         4.7
Uterus Pool                      0.2
Ovarian ca. OVCAR-3              6.4
Ovarian ca. SK-OV-3              1.7
Ovarian ca. OVCAR-4              0.2
Ovarian ca. OVCAR-5              8.8
Ovarian ca. IGROV-1              8.8
Ovarian ca. OVCAR-8              3.5
Ovary                            1.9
Breast ca. MCF-7                 0.0
Breast ca. MDA-MB-231            0.2
Breast ca. BT 549                0.3
Breast ca. T47D                  11.3
Breast ca. MDA-N                 0.2
Breast Pool                      0.5
Trachea.                         4.0
Lung                             0.8
Fetal Lung                       1.8
Lung ca. NCI-N417                3.6
Lung ca. LX-1                    40.9
Lung ca. NCI-H146                17.3
Lung ca. SHP-77                  42.9
Lung ca. A549                    1.4
Lung ca. NCI-H526                10.7
Lung ca. NCI-H23                 52.1
Lung ca. NCI-H460                6.1
Lung ca. HOP-62                  5.2
Lung ca. NCI-H522                0.2
Liver                            0.0
Fetal Liver                      2.1
Liver ca. HepG2                  12.4
Kidney Pool                      1.2
Fetal Kidney                     6.9
Renal ca. 786-0                  0.1
Renal ca. A498                   0.7
Renal ca. ACHN                   0.3
Renal ca. UO-31                  5.8
Renal ca. TK-10                  5.0
Bladder                          1.8
Gastric ca. (liver met.) NCI-N87 100.0
Gastric ca. KATO III             10.6
Colon ca. SW-948                 3.2
Colon ca. SW480                  4.8
Colon ca.* (SW480 met) SW620     13.2
Colon ca. HT29                   8.0
Colon ca. HCT-116                4.9
Colon ca. CaCo-2                 24.0
Colon cancer tissue              0.2
Colon ca. SW1116                 2.9
Colon ca. Colo-205               0.4
Colon ca. SW-48                  2.6
Colon Pool                       0.4
Small Intestine Pool             0.5
Stomach Pool                     0.6
Bone Marrow Pool                 0.1
Fetal Heart                      2.4
Heart Pool                       0.1
Lymph Node Pool                  0.4
Fetal Skeletal Muscle            0.2
Skeletal Muscle Pool             5.7
Spleen Pool                      0.7
Thymus Pool                      0.8
CNS cancer (glio/astro) U87-MG   0.4
CNS cancer (glio/astro) U-118-MG 0.6
CNS cancer (neuro; met) SK-N-AS  5.2
CNS cancer (astro) SF-539        2.2
CNS cancer (astro) SNB-75        0.9
CNS cancer (glio) SNB-19         10.2
CNS cancer (glio) SF-295         1.5
Brain (Amygdala) Pool            3.3
Brain (cerebellum)               0.4
Brain (fetal)                    94.0
Brain (Hippocampus) Pool         2.8
Cerebral Cortex Pool             5.2
Brain (Substantia nigra) Pool    4.2
Brain (Thalamus) Pool            4.6
Brain (whole)                    6.4
Spinal Cord Pool                 2.1
Adrenal Gland                    1.0
Pituitary gland Pool             1.9
Salivary Gland                   0.2
Thyroid (female)                 0.3
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    2.2

[0753]

TABLE ID
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4722, Run
Tissue Name                      204172542
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.7
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.9
Primary Th2 rest                 0.8
Primary Tr1 rest                 3.3
CD45RA CD4 lymphocyte act        0.0
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.6
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              1.5
2ry Th1/Th2/Tr1_anti-CD95 CH11   3.6
LAK cells rest                   0.0
LAK cells IL-2                   0.0
LAK cells IL-2 + IL-12           0.0
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.0
LAK cells PMA/ionomycin          0.0
NK Cells IL-2 rest               1.0
Two Way MLR 3 day                0.0
Two Way MLR 5 day                0.0
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.6
PBMC PHA-L                       0.0
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.6
EOL-1 dbcAMP                     0.0
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             0.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.0
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.8
Macrophages LPS                  0.0
HUVEC none                       3.8
HUVEC starved                    7.7
HUVEC IL-1beta                   2.0
HUVEC IFN gamma                  9.3
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            4.2
HUVEC IL-11                      6.3
Lung Microvascular EC none       16.2
Lung Microvascular EC TNFalpha + 6.3
IL-1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  0.0
IL1beta
Small airway epithelium none     6.8
Small airway epithelium TNFalpha + 5.7
IL-1beta
Coronery artery SMC rest         0.8
Coronery artery SMC TNFalpha + IL- 2.5
1beta
Astrocytes rest                  5.7
Astrocytes TNFalpha + IL-1beta   4.6
KU-812 (Basophil) rest           0.0
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     0.0
CCD1106 (Keratinocytes) TNFalpha + 0.0
IL-1beta
Liver cirrhosis                  0.0
NCI-H292 none                    50.0
NCI-H292 IL-4                    53.6
NCI-H292 IL-9                    100.0
NCI-H292 IL-13                   71.2
NCI-H292 IFN gamma               39.8
HPAEC none                       7.4
HPAEC TNF alpha + IL-1 beta      9.5
Lung fibroblast none             0.0
Lung fibroblast TNF alpha + IL-1 0.0
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.6
Lung fibroblast IL-13            0.0
Lung fibroblast IFN gamma        0.0
Dermal Fibroblast CCD1070 rest   0.0
Dermal fibroblast CCD1070 TNF alpha 0.9
Dermal fibroblast CCD1070 IL-1 beta 0.6
Dermal fibroblast IFN gamma      0.0
Dermal fibroblast IL-4           0.0
Dermal Fibroblasts rest          0.0
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 0.0
Colon                            0.0
Lung                             0.0
Thymus                           4.0
Kidney                           0.7

[0754] CNS_neurodegeneration_v1.0 Summary: Ag4722 This panel does not show differential expression of this gene in Alzheimer's disease. However, this expression profile confirms the presence of this gene in the brain. Please see Panel 1.4 for discussion of utility of this gene in the central nervous system.

[0755] General_screening_panel_v1.4 Summary: Ag4722 This gene is expressed at moderate levels throughout many of the samples in this panel. Highest expression is detected in an gastric cancer cell line (CT=29). In addition, this gene is also expressed in a cluster of samples derived from lung cancer cell lines and at low but significant levels in cell lines derived from ovarian, colon and brain cancers. Therefore, therapeutic modulation of this gene or its protein product, through the use of antibodies, might be useful in the treatment of these cancers.

[0756] Among tissues involved in metabolic function, this gene is expressed in the pancreas, pituitary, fetal liver, fetal heart and skeletal muscle. Therefore, this gene or its protein product may be important in the pathogenesis and/or treatment of disease of obesity and diabetes.

[0757] There is widespread moderate expression of this gene across many of the samples derived from the CNS, including the amygdala, hippocampus, thalamus, cerebral cortex, and spinal cord. 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.

[0758] Panel 4.1D Summary: Ag4722 This transcript is most highly expressed in NCI-H292 cells stimulated by IL-9 (CT=32.5). The gene is also expressed in a cluster of treated and untreated samples derived from the 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. The transcript is also expressed at lower but still significant levels in small airway epithelium treated with IL-1 beta and TNF-alpha. The expression of the transcript in this mucoepidermoid cell line that is often used as a model for airway epithelium (NCI-H292 cells) suggests that this transcript may be important in the proliferation or activation of airway epithelium. Therefore, therapeutics designed with the protein encoded by the transcript may reduce or eliminate symptoms caused by inflammation in lung epithelia in chronic obstructive pulmonary disease, asthma, allergy, and emphysema.

[0759] J. NOV10a (CG126600-01): Fibronectin Type III Domain-Membrane Protein

[0760] Expression of gene CG126600-01 was assessed using the primer-probe set Ag7030, described in Table JA. Results of the RTQ-PCR runs are shown in Tables JB, JC and JD.

TABLE IA
Probe Name Ag7030
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-acatccaccactactqgatacaa-3′	23	89	250
Probe	TET-5′-ttctcttttgtctgcccctattgtaagtgc-	30	134	251
	3′-TAMRA
Reverse	5′-cagaataacctgttgtgttccat-3′	23	166	252

[0761]

TABLE JB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%)
                               Ag7030, Run
Tissue Name                    282263009
AD 1 Hippo                     12.9
AD 2 Hippo                     33.2
AD 3 Hippo                     9.3
AD 4 Hippo                     8.2
AD 5 hippo                     59.0
AD 6 Hippo                     100.0
Control 2 Hippo                32.1
Control 4 Hippo                11.3
Control (Path) 3 Hippo         5.9
AD 1 Temporal Ctx              19.8
AD 2 Temporal Ctx              26.4
AD 3 Temporal Ctx              4.9
AD 4 Temporal Ctx              29.3
AD 5 Inf Temporal Ctx          62.4
AD 5 Sup Temporal Ctx          40.9
AD 6 Inf Temporal Ctx          57.8
AD 6 Sup Temporal Ctx          67.4
Control 1 Temporal Ctx         4.6
Control 2 Temporal Ctx         32.5
Control 3 Temporal Ctx         13.1
Control 4 Temporal Ctx         8.0
Control (Path) 1 Temporal Ctx  47.0
Control (Path) 2 Temporal Ctx  38.4
Control (Path) 3 Temporal Ctx  4.4
Control (Path) 4 Temporal Ctx  25.3
AD 1 Occipital Ctx             12.5
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             5.1
AD 4 Occipital Ctx             11.5
AD 5 Occipital Ctx             31.9
AD 6 Occipital Ctx             33.0
Control 1 Occipital Ctx        7.5
Control 2 Occipital Ctx        38.2
Control 3 Occipital Ctx        7.6
Control 4 Occipital Ctx        5.8
Control (Path) 1 Occipital Ctx 64.2
Control (Path) 2 Occipital Ctx 10.6
Control (Path) 3 Occipital Ctx 2.5
Control (Path) 4 Occipital Ctx 11.4
Control 1 Parietal Ctx         4.8
Control 2 Parietal Ctx         32.3
Control 3 Parietal Ctx         18.0
Control (Path) 1 Parietal Ctx  45.4
Control (Path) 2 Parietal Ctx  18.4
Control (Path) 3 Parietal Ctx  2.8
Control (Path) 4 Parietal Ctx  34.4

[0762]

TABLE JC
General_screening_panel_v1.6
                                 Rel. Exp. (%)
                                 Ag7030, Run
Tissue Name                      281813484
Adipose                          10.0
Melanoma* Hs688(A).T             8.7
Melanoma* Hs688(B).T             9.5
Melanoma* M14                    14.3
Melanoma* LOXIMVI                13.1
Melanoma* SK-MEL-5               100.0
Squamous cell carcinoma SCC-4    6.9
Testis Pool                      21.8
Prostate ca.* (bone met) PC-3    13.5
Prostate Pool                    14.4
Placenta                         75.3
Uterus Pool                      6.4
Ovarian ca. OVCAR-3              4.5
Ovarian ca. SK-OV-3              57.8
Ovarian ca. OVCAR-4              4.4
Ovarian ca. OVCAR-5              34.9
Ovarian ca. IGROV-1              25.7
Ovarian ca. OVCAR-8              20.6
Ovary                            16.2
Breast ca. MCF-7                 18.8
Breast ca. MDA-MB-231            24.8
Breast ca. BT 549                55.9
Breast ca. T47D                  2.1
Breast ca. MDA-N                 4.9
Breast Pool                      24.1
Trachea                          29.1
Lung                             5.8
Fetal Lung                       38.4
Lung ca. NCI-N417                4.8
Lung ca. LX-I                    58.6
Lung ca. NCI-H146                8.9
Lung ca. SHP-77                  19.1
Lung ca. A549                    13.6
Lung ca. NCI-H526                4.8
Lung ca. NCI-H23                 52.9
Lung ca. NCI-H460                45.4
Lung ca. HOP-62                  6.8
Lung ca. NCI-H522                8.3
Liver                            2.6
Fetal Liver                      17.7
Liver ca. HepG2                  9.8
Kidney Pool                      39.0
Fetal Kidney                     19.2
Renal ca. 786-0                  22.1
Renal ca. A498                   3.7
Renal ca. ACHN                   14.0
Renal ca. UO-31                  27.0
Renal ca. TK-10                  27.7
Bladder                          42.9
Gastric ca. (liver met.) NCI-N87 53.6
Gastric ca. KATO III             22.8
Colon ca. SW-948                 4.6
Colon ca. SW480                  26.8
Colon ca.* (SW480 met) SW620     18.7
Colon ca. HT29                   5.1
Colon ca. HCT-116                17.9
Colon ca. CaCo-2                 18.8
Colon cancer tissue              13.9
Colon ca. SW1116                 3.7
Colon ca. Colo-205               4.5
Colon ca. SW-48                  5.3
Colon Pool                       19.2
Small Intestine Pool             24.3
Stomach Pool                     19.6
Bone Marrow Pool                 9.9
Fetal Heart                      8.2
Heart Pool                       11.7
Lymph Node Pool                  38.7
Fetal Skeletal Muscle            4.2
Skeletal Muscle Pool             1.5
Spleen Pool                      13.5
Thymus Pool                      21.9
CMS cancer (glio/astro) U87-MG   14.3
CNS cancer (glio/astro) U-118-MG 73.2
CNS cancer (neuro; met) SK-N-AS  34.6
CNS cancer (astro) SF-539        5.8
CNS cancer (astro) SNB-75        17.0
CNS cancer (glio) SNB-19         27.5
CNS cancer (glio) SF-295         55.9
Brain (Amygdala) Pool            5.8
Brain (cerebellum)               13.1
Brain (fetal)                    14.5
Brain (Hippocampus) Pool         9.9
Cerebral Cortex Pool             11.8
Brain (Substantia nigra) Pool    6.0
Brain (Thalamus) Pool            14.7
Brain (whole)                    6.0
Spinal Cord Pool                 8.0
Adrenal Gland                    19.1
Pituitary gland Pool             9.7
Salivary Gland                   7.2
Thyroid (female)                 9.3
Pancreatic ca. CAPAN2            18.3
Pancreas Pool                    33.7

[0763]

TABLE JD
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag7030, Run
Tissue Name                      281810532
Secondary Th1 act                9.1
Secondary Th2 act                13.5
Secondary Tr1 act                6.6
Secondary Th1 rest               0.9
Secondary Th2 rest               1.9
Secondary Tr1 rest               1.6
Primary Th1 act                  2.8
Primary Th2 act                  8.0
Primary Tr1 act                  7.7
Primary Th1 rest                 1.1
Primary Th2 rest                 0.9
Primary Tr1 rest                 1.6
CD45RA CD4 lymphocyte act        100.0
CD45RO CD4 lymphocyte act        11.0
CD8 lymphocyte act               3.1
Secondary CD8 lymphocyte rest    5.8
Secondary CD8 lymphocyte act     1.0
CD4 lymphocyte none              1.4
2ry Th1/Th2/Tr1_anti-CD95 CH11   2.1
LAK cells rest                   9.8
LAK cells IL-2                   3.2
LAK cells IL-2 + IL-12           1.9
Lak cells IL-2 + IFN gamma       2.2
LAK cells IL-2 + IL-18           2.5
Lak cells PMA/ionomycin          42.3
NK Cells IL-2 rest               8.5
Two Way MLR 3 day                3.4
Two Way MLR 5 day                1.1
Two Way MLR 7 day                2.2
PBMC rest                        1.1
PBMC PWM                         2.2
PBMC PHA-L                       1.9
Ramos (B cell) none              8.5
Ramos (B cell) ionomycin         16.8
B lymphocytes PWM                3.6
B lymphocytes CD40L and IL-4     4.4
EOL-1 dbcAMP 1                   5.7
EOL-1 dbcAMP PMA/ionomycin       7.7
Dendritic cells none             12.1
Dendritic cells LPS              10.2
Dendritic cells anti-CD40        7.0
Monocytes rest                   2.5
Monocytes LPS                    21.2
Macrophages rest                 3.3
Macrophages LPS                  8.1
HUVEC none                       2.9
HUVEC starved                    3.7
HUVEC IL-1beta                   7.0
HUVEC IFN gamma                  6.8
HUVEC TNF alpha + IFN gamma      3.0
HUVEC TNF alpha + IL4            1.7
HUVEC IL-11                      2.7
Lung Microvascular EC none       12.0
Lung Microvascular EC TNFalpha + IL- 4.1
1beta
Microvascular Dermal EC none     1.7
Microsvasular Dermal EC TNFalpha + IL- 1.3
1beta
Bronchial epithelium TNFalpha + IL1beta 2.0
Small airway epithelium none     1.4
Small airway epithelium TNFalpha + IL- 2.1
1beta
Coronery artery SMC rest         3.7
Coronery artery SMC TNFalpha + IL-1beta 6.2
Astrocytes rest                  3.6
Astrocytes TNFalpha + IL-1beta   0.7
KU-812 (Basophil) rest           1.8
KU-812 (Basophil) PMA/ionomycin  11.1
CCD1106 (Keratinocytes) none     2.5
CCD1106 (Keratinocytes) TNFalpha + IL- 3.7
1beta
Liver cirrhosis                  1.4
NCI-H292 none                    6.8
NCI-H292 IL-4                    17.1
NCI-H292 IL-9                    10.8
NCI-H292 IL-13                   22.8
NCI-H292 IFN gamma               7.5
HPAEC none                       2.2
HPAEC TNF alpha + IL-1 beta      8.4
Lung fibroblast none             8.2
Lung fibroblast TNF alpha + IL-1 beta 16.8
Lung fibroblast IL-4             2.4
Lung fibroblast IL-9             8.6
Lung fibroblast IL-13            4.0
Lung fibroblast IFN gamma        12.7
Dermal fibroblast CCD1070 rest   12.8
Dermal fibroblast CCD1070 TNF alpha 17.9
Dermal fibroblast CCD1070 IL-1 beta 16.2
Dermal fibroblast IFN gamma      8.3
Dermal fibroblast IL-4           20.4
Dermal Fibroblasts rest          6.8
Neutrophils TNFa + LPS           8.5
Neutrophils rest                 7.6
Colon                            2.2
Lung                             1.5
Thymus                           3.9
Kidney                           10.0

[0764] CNS_neurodegeneration v1.0 Summary: Ag7030 This panel confirms the expression of the CG1 26600-01 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 1.6 for a discussion of the potential utility of this gene in treatment of central nervous system disorders.

[0765] General_screening_panel_v1.6 Summary: Ag7030 1lighest expression of the CG126600-01 gene is detected in melanoma SK-MEL-5 cell line (CT=25.7). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, 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, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0766] Among tissues with metabolic or endocrine function, this gene is expressed at 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.

[0767] 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.

[0768] Panel 4.1D Summary: Ag7030 Highest expression of the CG126600-01 gene is detected in activated CD45RA CD4 lymphocyte (CT=26.6). 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_v1.6 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.

[0769] K. NOV11a (CG127888-01): Novel Secretory Protein

[0770] Expression of gene CG127888-01 was assessed using the primer-probe set Ag4756, described in Table KA. Results of the RTQ-PCR runs are shown in Table KB.

TABLE KA
Probe Name Ag4756
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-ctttcagaataatggcaaatgg-3′	22	989	253
Probe	TET-5′-ccagtaacatcttccaaagaaattcgga-3′-	28	1018	254
	TAMRA
Reverse	tctcccagattcatgttgactt-3′	22	1050	255

[0771]

TABLE KB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%)
                               Ag4756, Run
Tissue Name                    224721730
AD 1 Hippo                     0.0
AD 2 Hippo                     0.0
AD 3 Hippo                     0.0
AD 4 Hippo                     0.0
AD 5 hippo                     0.0
AD 6 Hippo                     0.0
Control 2 Hippo                0.0
Control 4 Hippo                0.0
Control (Path) 3 Hippo         0.0
AD 1 Temporal Ctx              0.0
AD 2 Temporal Ctx              0.0
AD 3 Temporal Ctx              0.0
AD 4 Temporal Ctx              0.0
AD 5 Inf Temporal Ctx          0.0
AD 5 Sup Temporal Ctx          0.0
AD 6 Inf Temporal Ctx          0.0
AD 6 Sup Temporal Ctx          0.0
Control 1 Temporal Ctx         100.0
Control 2 Temporal Ctx         0.0
Control 3 Temporal Ctx         0.0
Control 4 Temporal Ctx         0.0
Control (Path) 1 Temporal Ctx  0.0
Control (Path) 2 Temporal Ctx  0.0
Control (Path) 3 Temporal Ctx  0.0
Control (Path) 4 Temporal Ctx  0.0
AD 1 Occipital Ctx             0.0
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             0.0
AD 4 Occipital Ctx             0.0
AD 5 Occipital Ctx             0.0
AD 6 Occipital Ctx             0.0
Control 1 Occipital Ctx        0.0
Control 2 Occipital Ctx        0.0
Control 3 Occipital Ctx        0.0
Control 4 Occipital Ctx        0.0
Control (Path) 1 Occipital Ctx 0.0
Control (Path) 2 Occipital Ctx 0.0
Control (Path) 3 Occipital Ctx 0.0
Control (Path) 4 Occipital Ctx 0.0
Control 1 Parietal Ctx         0.0
Control 2 Parietal Ctx         0.0
Control 3 Parietal Ctx         0.0
Control (Path) 1 Parietal Ctx  0.0
Control (Path) 2 Parietal Ctx  0.0
Control (Path) 3 Parietal Ctx  0.0
Control (Path) 4 Parietal Ctx  0.0

[0772] CNS_neurodegeneration_v1.0 Summary: Ag4756 Low expression of this gene is seen in control temporal cortex (CT=34.6). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. In addition, therapeutic modulation of this gene may be useful for the treatment of neurological disorders.

[0773] General_screening_panel_v1.4 Summary: Ag4756 Expression of the CG127888-01 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0774] Panel 4.1D Summary: Ag4756 Expression of the CG 127888-01 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0775] L. NOV12a (CG128249-02): Ephrin-A4 Precursor

[0776] Expression of gene CG128249-02 was assessed using the primer-probe set Ag6833, described in Table LA. Results of the RTQ-PCR runs are shown in Table LB. Please note that CG128249-02 represents a full-length physical clone.

TABLE LA
Probe Name Ag6833
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gccatgttcaattctcagagaa-3′	22	338	256
Probe	TET-5′-cttcacacccttctccctcggctt3′-	24	369	257
	TAMRA
Reverse	5′-gccactctctccaggtaagaa-3′	21	397	258

[0777]

TABLE LB
General_screening_panel_v1.6
                                 Rel. Exp. (%)
                                 Ag6833, Run
Tissue Name                      278019620
Adipose                          0.9
Melanoma* Hs688(A).T             4.5
Melanoma* Hs688(B).T             4.5
Melanoma* M14                    3.8
Melanoma* LOXIMVI                8.0
Melanoma* SK-MEL-5               16.5
Squamous cell carcinoma SCC-4    6.7
Testis Pool                      3.6
Prostate ca.* (bone met) PC-3    22.1
Prostate Pool                    7.2
Placenta                         10.2
Uterus Pool                      0.0
Ovarian ca. OVCAR-3              75.3
Ovarian ca. SK-OV-3              34.2
Ovarian ca. OVCAR-4              13.9
Ovarian ca. OVCAR-5              100.0
Ovarian ca. IGROV-1              32.3
Ovarian ca. OVCAR-8              3.1
Ovary                            10.7
Breast ca. MCF-7                 48.6
Breast ca. MDA-MB-231            17.4
Breast ca. BT 549                40.6
Breast ca. T47D                  26.4
Breast ca. MDA-N                 18.9
Breast Pool                      7.2
Trachea                          13.8
Lung                             2.1
Fetal Lung                       17.0
Lung ca. NCI-N417                1.3
Lung ca. LX-1                    10.7
Lung ca. NCI-H146                0.0
Lung ca. SHP-77                  2.0
Lung ca. A549                    9.5
Lung ca. NCI-H526                3.7
Lung ca. NCI-H23                 15.4
Lung ca. NCI-H460                31.9
Lung ca. HOP-62                  10.0
Lung ca. NCI-H522                25.0
Liver                            0.8
Fetal Liver                      0.0
Liver ca. HepG2                  10.1
Kidney Pool                      7.0
Fetal Kidney                     6.6
Renal ca. 786-0                  37.9
Renal ca. A498                   9.8
Renal ca. ACHN                   18.8
Renal ca. UO-31                  16.6
Renal ca. TK-10                  46.0
Bladder                          12.9
Gastric ca. (liver met.) NCI-N87 32.1
Gastric ca. KATO III             79.0
Colon ca. SW-948                 10.5
Colon ca. SW480                  65.1
Colon ca.* (SW480 met) SW620     0.0
Colon ca. HT29                   31.0
Colonca. HCT-116                 30.6
Colon ca. CaCo-2                 21.8
Colon cancer tissue              26.2
Colon ca. SW1116                 14.7
Colon ca. Colo-205               10.4
Colon ca. SW-48                  43.5
Colon Pool                       4.7
Small Intestine Pool             5.9
Stomach Pool                     5.1
Bone Marrow Pool                 2.7
Fetal Heart                      7.7
Heart Pool                       2.5
Lymph Node Pool                  7.4
Fetal Skeletal Muscle            1.5
Skeletal Muscle Pool             0.0
Spleen Pool                      3.8
Thymus Pool                      9.8
CNS cancer (glio/astro) U87-MG   4.1
CNS cancer (glio/astro) U-118-MG 13.7
CNS cancer (neuro; met) SK-N-AS  33.2
CNS cancer (astro) SF-539        13.3
CNS cancer (astro) SNB-75        37.6
CNS cancer (glio) SNB-19         36.3
CNS cancer (glio) SF-295         40.1
Brain (Amygdala) Pool            1.0
Brain (cerebellum)               2.0
Brain (fetal)                    1.9
Brain (Hippocampus) Pool         0.0
Cerebral Cortex Pool             0.0
Brain (Substantia nigra) Pool    0.0
Brain (Thalamus) Pool            0.0
Brain (whole)                    4.6
Spinal Cord Pool                 2.6
Adrenal Gland                    8.7
Pituitary gland Pool             0.0
Salivary Gland                   12.7
Thyroid (female)                 4.0
Pancreatic ca. CAPAN2            34.4
Pancreas Pool                    10.4

[0778] CNS_neurodegeneration_v1.0 Summary: Ag6833 Expression of the CG128249-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0779] General_screening_panel_v1.6 Summary: Ag6833 Highest expression of the CG128249-02 gene is detected in ovarian OVCAR-5 cell line (CT=32.8). Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Interestingly, this gene is expressed at low/undectactable levels in normal tissues (CTs>35). Thus, expression of this gene could be used to distinguish cancer cell lines from the normal tissue samples in this panel and also 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, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0780] Panel 4.1 D Summary: Ag6833 Expression of the CG128249-02 (gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0781] M. NOV13a (CGt28785-01): alt Spliced SPUF

[0782] Expression of gene CG128785-01 was assessed using the primer-probe set Ag5883, described in Table MA.

TABLE MA
Probe Name Ag5883
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gcttttcaccgaggaggag-3′	19	135	259
Probe	TET-5′-agcttctcccctgctttctaggaaga-3′-	26	176	260
	TAMRA
Reverse	5′-ttcactgccaagtagatggg-3′	20	206	261

[0783] General_screening_panel_v1.5 Summary: Ag5883 Expression of the CG128785-01 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0784] Panel 4.1D Summary: Ag5883 Expression of the CG128785-01 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0785] N. NOV14a (CG129005-01): 54TM Splice Variant.

[0786] Expression of gene CG129005-01 was assessed using the primer-probe set Ag4799, described in Table NA. Results of the RTQ-PCR runs are shown in Tables NB and NC.

TABLE NA
Probe Name Ag4799
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-tgcagtacagtcgtgatgct-3′	20	373	262
Probe	TET-5′-aagacctcaacqcccctgacctctat-3′-	26	409	263
	TAMRA
Reverse	5′-ccaggagcacgtaagtaatgaa-3′	22	450	264

[0787]

TABLE NB
General_screening_panel_v1.4
                                 Rel. Exp. (%)
                                 Ag4799, Run
Tissue Name                      223203328
Adipose                          0.6
Melanoma* Hs688(A).T             21.0
Melanoma* Hs688(B).T             21.8
Melanoma* M14                    18.6
Melanoma* LOXIMVI                18.8
Melanoma* SK-MEL-5               15.8
Squamous cell carcinoma SCC-4    12.2
Testis Pool                      1.6
Prostate ca.* (bone met) PC-3    39.8
Prostate Pool                    1.5
Placenta                         4.8
Uterus Pool                      1.2
Ovarian ca. OVCAR-3              11.4
Ovarian ca. SK-OV-3              19.8
Ovarian ca. OVCAR-4              18.2
Ovarian ca. OVCAR-5              41.5
Ovarian ca. IGROV-1              21.8
Ovarian ca. OVCAR-8              14.2
Ovary                            2.3
Breast ca. MCF-7                 17.7
Breast ca. MDA-MB-231            21.3
Breast ca. BT 549                20.4
Breast ca. T47D                  100.0
Breast ca. MDA-N                 9.9
Breast Pool                      2.7
Trachea                          3.1
Lung                             0.7
Fetal Lung                       3.1
Lung ca. NCI-N417                16.4
Lung ca. LX-1                    8.7
Lung ca. NCI-H146                3.5
Lung ca. SHP-77                  14.3
Lung ca. A549                    15.9
Lung ca. NCI-H526                9.6
Lung ca. NCI-H23                 8.8
Lung ca. NCI-H460                8.2
Lung ca. HOP-62                  9.5
Lung ca. NCI-H522                11.4
Liver                            3.0
Fetal Liver                      8.4
Liver ca. HepG2                  10.9
Kidney Pool                      3.4
Fetal Kidney                     1.3
Renal ca. 786-0                  14.6
Renal ca. A498                   4.9
Renal ca. ACHN                   8.2
Renal ca. UO-31                  15.5
Renal ca TK-10                   11.8
Bladder                          4.6
Gastric ca. (liver met.) NCI-N87 22.7
Gastric ca. KATO III             38.2
Colon ca. SW-948                 12.6
Colon ca. SW480                  28.1
Colon ca.* (SW480 met) SW620     12.9
Colon ca. HT29                   14.7
Colon ca. HCT-116                9.9
Colon ca. CaCo-2                 21.5
Colon cancer tissue              7.6
Colon ca. SW1116                 4.0
Colon ca. Colo-205               7.4
Colon ca. SW-48                  9.7
Colon Pool                       3.4
Small Intestine Pool             1.5
Stomach Pool                     1.2
Bone Marrow Pool                 1.3
Fetal Heart                      1.4
Heart Pool                       1.4
Lymph Node Pool                  3.5
Fetal Skeletal Muscle            1.0
Skeletal Muscle Pool             4.4
Spleen Pool                      1.3
Thymus Pool                      1.9
CNS cancer (glio/astro) U87-MG   36.3
CNS cancer (glio/astro) U-118-MG 31.9
CNS cancer (neuro; met) SK-N-AS  7.6
CNS cancer (astro) SF-539        15.9
CNS cancer (astro) SNB-75        41.5
CNS cancer (glio) SNB-19         18.0
CNS cancer (glio) SF-295         22.4
Brain (Amygdala) Pool            2.5
Brain (cerebellum)               4.7
Brain (fetal)                    1.4
Brain (Hippocampus) Pool         1.9
Cerebral Cortex Pool             1.4
Brain (Substantia nigra) Pool    3.0
Brain (Thalamus) Pool            1.9
Brain (whole)                    2.6
Spinal Cord Pool                 2.7
Adrenal Gland                    4.0
Pituitary gland Pool             1.5
Salivary Gland                   2.6
Thyroid (female)                 4.4
Pancreatic ca. CAPAN2            15.4
Pancreas Pool                    4.2

[0788]

TABLE NC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4799, Run
Tissue Name                      223235948
Secondary Th1 act                23.0
Secondary Th2 act                25.7
Secondary Tr1 act                24.0
Secondary Th1 rest               4.3
Secondary Th2 rest               6.0
Secondary Tr1 rest               3.2
Primary Th1 act                  15.2
Primary Th2 act                  23.2
Primary Tr1 act                  24.5
Primary Th1 rest                 4.0
Primary Th2 rest                 1.7
Primary Tr1 rest                 6.9
CD45RA CD4 lymphocyte act        37.4
CD45RO CD4 lymphocyte act        26.4
CD8 lymphocyte act               22.5
Secondary CD8 lymphocyte rest    14.1
Secondary CD8 lymphocyte act     12.9
CD4 lymphocyte none              1.5
2ry Th1/Th2/Tr1_anti-CD95 CH11   5.2
LAK cells rest                   10.7
LAK cells IL-2                   11.4
LAK cells IL-2 + IL-12           8.2
LAK cells IL-2 + IFN gamma       7.9
LAK cells IL-2 + IL-18           16.5
LAK cells PMA/ionomycin          10.1
NK Cells IL-2 rest               13.5
Two Way MLR 3 day                8.7
Two Way MLR 5 day                12.1
Two Way MLR 7 day                7.3
PBMC rest                        2.5
PBMC PWM                         20.7
PBMC PHA-L                       16.7
Ramos (B cell) none              35.1
Ramos (B cell) ionomycin         55.9
B lymphocytes PWM                12.7
B lymphocytes CD40L and IL-4     9.9
EOL-1 dbcAMP                     17.1
EOL-1 dbcAMP PMA/ionomycin       6.9
Dendritic cells none             14.8
Dendritic cells LPS              7.1
Dendritic cells anti-CD40        14.6
Monocytes rest                   5.7
Monocytes LPS                    12.4
Macrophages rest                 17.3
Macrophagcs LPS                  5.6
HUVEC none                       23.7
HUVEC starved                    39.8
HUVEC IL-1beta                   42.0
HUVEC IFN gamma                  25.7
HUVEC TNF alpha + IFN gamma      44.8
HUVEC TNF alpha + IL4            46.3
HUVEC IL-11                      12.8
Lung Microvascular EC none       100.0
Lung Microvascular EC TNFalpha + IL- 69.3
1beta
Microvascular Dermal EC none     24.0
Microsvasular Dermal EC TNFalpha + IL- 34.9
1beta
Bronchial epithelium TNFalpha + IL1beta 26.1
Small airway epithelium none     17.0
Small airway epithelium TNFalpha + IL- 31.6
1beta
Coronery artery SMC rest         39.0
Coronery artery SMC TNFalpha + IL-1beta 48.0
Astrocytes rest                  15.4
Astrocytes TNFalpha + IL-1beta   16.7
KU-812 (Basophil) rest           25.2
KU-812 (Basophil) PMA/ionomycin  45.7
CCD1106 (Keratinocytes) none     44.4
CCD1106 (Keratinocytes) TNFalpha + IL- 24.0
1beta
Liver cirrhosis                  2.3
NCI-H292 none                    20.4
NCI-H292 IL-4                    38.2
NCI-H292 IL-9                    40.6
NCI-H292 IL-13                   39.0
NCI-H292 IFN gamma               44.8
HPAEC none                       13.4
HPAEC TNF alpha + IL-1 beta      54.7
Lung fibroblast none             30.6
Lung fibroblast TNF alpha + IL-1 beta 33.0
Lung fibroblast IL-4             33.4
Lung fibroblast IL-9             45.4
Lung fibroblast IL-13            37.1
Lung fibroblast IFN gamma        41.8
Dermal fibroblast CCD1070 rest   55.9
Dermal fibroblast CCD1070 TNF alpha 40.9
Dermal fibroblast CCD1070 IL-1 beta 35.8
Dermal fibroblast IFN gamma      20.9
Dermal fibroblast IL-4           26.6
Dermal Fibroblasts rest          38.7
Neutrophils TNFa + LPS           0.3
Neutrophils rest                 0.9
Colon                            7.6
Lung                             12.2
Thymus                           3.0
Kidney                           17.3

[0789] General_screening_panel_v1.4 Summary: Ag4799 Highest expression of the CG129005-01 gene is detected in breast cancer T47D cell line (CT=23.9). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, 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 gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0790] 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, 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.

[0791] 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.

[0792] Panel 4.1D Summary: Ag4799 Highest expression of the CG129005-01 gene is detected in lung microvascular EC cells (CT=27.3). 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.

[0793] O. NOV15a (CG132086-01): Novel Membrane Protein

[0794] Expression of gene CG132086-01 was assessed using the primer-probe set Ag4809, described in Table OA. Results of the RTQ-PCR runs are shown in Table OB.

TABLE GA
Probe Name Ag4809
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gatgccacagaggagttcatt-3′	21	6986	265
Probe	TET-5′-tccctqgactctactacagatgaagaaga-3′-	29	7010	266
Reverse	5′-ccatcacaccagccatttta-3′	20	7057	267

[0795]

TABLE OB
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4809, Run
Tissue Name                      223273407
Secondary Th1 act                49.7
Secondary Th2 act                55.5
Secondary Tr1 act                36.3
Secondary Th1 rest               12.0
Secondary Th2 rest               24.7
Secondary Tr1 rest               14.1
Primary Th1 act                  20.6
Primary Th2 act                  32.1
Primary Tr1 act                  34.2
Primary Th1 rest                 9.8
Primary Th2 rest                 8.0
Primary Tr1 rest                 18.2
CD45RA CD4 lymphocyte act        50.7
CD45RO CD4 lymphocyte act        48.3
CD8 lymphocyte act               38.4
Secondary CD8 lymphocyte rest    35.4
Secondary CD8 lymphocyte act     16.0
CD4 lymphocyte none              9.9
2ry Th1/Th2/Tr1_anti-CD95 CH11   27.2
LAK cells rest                   24.8
LAK cells IL-2                   25.9
LAK cells IL-2 + IL-12           14.7
LAK cells IL-2 + IFN gamma       16.6
LAK cells IL-2 + IL-18           23.2
LAK cells PMA/ionomycin          33.9
NK Cells IL-2 rest               30.1
Two Way MLR 3 day                29.3
Two Way MLR 5 day                32.1
Two Way MLR 7 day                18.7
PBMC rest                        8.5
PBMC PWM                         31.6
PBMC PHA-L                       33.0
Ramos (B cell) none              29.1
Ramos (B cell) ionomycin         36.9
B lymphocytes PWM                41.8
B lymphocytes CD40L and IL-4     37.6
EOL-1 dbcAMP                     21.0
EOL-1 dbcAMP PMA/ionomycin       27.7
Dendritic cells none             29.3
Dendritic cells LPS              24.5
Dendritic cells anti-CD40        21.2
Monocytes rest                   15.4
Monocytes LPS                    100.0
Macrophages rest                 22.7
Macrophages LPS                  21.9
HUVEC none                       17.3
HUVEC starved                    30.8
HUVEC IL-1beta                   27.2
HUVEC IFN gamma                  34.6
HUVEC TNF alpha + IFN gamma      24.8
HUVEC TNF alpha + IL4            26.4
HUVEC IL-11                      19.9
Lung Microvascular EC none       36.6
Lung Microvascular EC TNFalpha + IL- 29.9
1beta
Microvascular Dermal EC none     26.6
Microsvasular Dermal EC TNFalpha + IL- 24.8
1beta
Bronchial epithelium TNFalpha +  31.2
IL1beta
Small airway epithelium none     16.8
Small airway epithelium TNFalpha + IL- 27.0
1beta
Coronery artery SMC rest         17.7
Coronery artery SMC TNFalpha + IL- 26.2
1beta
Astrocytes rest                  13.4
Astrocytes TNFalpha + IL-1beta   13.3
KU-812 (Basophil) rest           59.0
KU-812 (Basophil) PMA/ionomycin  97.9
CCD1106 (Keratinocytes) none     25.3
CCD1106 (Keratinocytes) TNFalpha + IL- 29.3
1beta
Live cirrhosis                   6.7
NCI-H292 none                    12.5
NCI-H292 IL-4                    20.6
NCI-H292 IL-9                    22.1
NCI-H292 IL-13                   22.1
NCI-H292 IFN gamma               12.7
HPAEC none                       15.5
HPAEC TNF alpha + IL-1 beta      51.4
Lung fibroblast none             37.9
Lung fibroblast TNF alpha + IL-1 beta 36.9
Lung fibroblast IL-4             14.7
Lung fibroblast IL-9             15.8
Lung fibroblast IL-13            18.6
Lung fibroblast IFN gamma        25.3
Dermal fibroblast CCD1070 rest   51.4
Dermal fibroblast CCD1070 TNF alpha 84.1
Dermal fibroblast CCD1070 IL-1 beta 52.1
Dermal fibroblast IFN gamma      15.0
Dermal fibroblast IL-4           33.2
Dermal Fibroblasts rest          17.7
Neutrophils TNFa + LPS           11.7
Neutrophils rest                 12.5
Colon                            6.8
Lung                             11.6
Thymus                           32.8
Kidney                           9.8

[0796] General_screening_panel_v1.4 Summary: Ag4809 Results from one experiment with the CG132086-01 gene are not included. The amp plot indicates that there were experimental difficulties with this run.

[0797] Panel 4.1D Summary: Ag4809 Highest expression of the CG132086-01 gene is detected in LPS treated monocytes and PMA/ionomycin treated basophils (CTs=29.5). 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 expression pattern 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.

[0798] P. NOV16a and NOV16b (CG132297-01 and CG132297-02): Elastin

[0799] Expression of gene CG132297-01 and CG132297-02 was assessed using the primer-probe set Ag7016, described in Table PA. Results of the RTQ-PCR runs are shown in Tables PB, PC and PD. Please note that CG132297-01 represents a full-length physical clone.

TABLE PA
Probe Name Ag7016
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gctgccactccgtatttagct-3′	21	101	268
Probe	TET-5′-agctggaggtatacctccaaggcccc-3′-	26	136	269
	TAMRA
Reverse	5′-ggagggcttggagttcc-3′	17	170	270

[0800]

TABLE PB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%)
                               Ag7016, Run
Tissue Name                    282263005
AD 1 Hippo                     29.3
AD 2 Hippo                     50.3
AD 3 Hippo                     13.8
AD 4 Hippo                     39.8
AD 5 Hippo                     43.2
AD 6 Hippo                     77.9
Control 2 Hippo                42.9
Control 4 Hippo                55.9
Control (Path) 3 Hippo         19.8
AD 1 Temporal Ctx              30.1
AD 2 Temporal Ctx              55.1
AD 3 Temporal Ctx              7.2
AD 4 Temporal Ctx              55.1
AD 5 Inf Temporal Ctx          57.8
AD 5 Sup Temporal Ctx          68.8
AD 6 Inf Temporal Ctx          68.3
AD 6 Sup Temporal Ctx          100.0
Control 1 Temporal Ctx         14.7
Control 2 Temporal Ctx         34.2
Control 3 Temporal Ctx         11.6
Control 3 Temporal Ctx         45.7
Control (Path) 1 Temporal Ctx  71.2
Control (Path) 2 Temporal Ctx  31.2
Control (Path) 3 Temporal Ctx  24.5
Control (Path) 4 Temporal Ctx  24.1
AD 1 Occipital Ctx             31.4
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             9.2
AD 4 Occipital Ctx             59.5
AD 5 Occipital Ctx             77.9
AD 6 Occipital Ctx             81.2
Control 1 Occipital Ctx        14.7
Control 2 Occipital Ctx        26.8
Control 3 Occipital Ctx        21.3
Control 4 Occipital Ctx        66.4
Control (Path) 1 Occipital Ctx 36.3
Control (Path) 2 Occipital Ctx 22.7
Control (Path) 3 Occipital Ctx 18.6
Control (Path) 4 Occipital Ctx 29.3
Control 1 Parietal Ctx         30.1
Control 2 Parietal Ctx         67.4
Control 3 Parietal Ctx         20.3
Control (Path) 1 Parietal Ctx  35.6
Control (Path) 2 Parietal Ctx  47.6
Control (Path) 3 Parietal Ctx  27.2
Control (Path) 4 Parietal Ctx  58.6

[0801]

TABLE PC
General_screening_panel_v1.6
                                 Rel. Exp. (%)
                                 Ag7016, Run
Tissue Name                      282263474
Adipose                          9.9
Melanoma* Hs688(A).T             42.0
Melanoma* Hs688(B).T             21.8
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    0.0
Testis Pool                      5.3
Prostate ca.* (bone met) PC-3    0.0
Prostate Pool                    4.4
Placenta                         6.9
Uterus Pool                      2.7
Ovarian ca. OVCAR-3              0.0
Ovarian ca. SK-OV-3              0.0
Ovarian ca. OVCAR-4              0.0
Ovarian ca. OVCAR-5              0.1
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.1
Ovary                            3.8
Breast ca. MCF-7                 0.0
Breast ca. MDA-MB-231            0.0
Breast ca. BT 549                0.0
Breast ca. T47D                  0.0
Breast ca. MDA-N                 0.0
Breast Pool                      4.6
Trachea                          7.0
Lung                             1.3
Fetal Lung                       100.0
Lung ca. NCI-N417                27.9
Lung ca. LX-1                    0.1
Lung ca. NCI-H146                0.2
Lung ca. SHP-77                  1.3
Lung ca. A549                    0.1
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 0.0
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  0.0
Lung ca. NCI-H522                0.0
Liver                            0.2
Fetal Liver                      2.9
Liver ca. HepG2                  0.1
Kidney Pool                      10.2
Fetal Kidney                     5.3
Renal ca. 786-0                  0.0
Renal ca. A498                   0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.0
Renal ca. TK-10                  0.1
Bladder                          6.0
Gastric ca. (liver met.) NCI-N87 0.1
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  0.0
Colon ca.* (SW480 met) SW620     0.0
Colon ca. HT29                   0.1
Colon ca. HCT-116                0.0
Colon ca. CaCo-2                 0.0
Colon cancer tissue              7.6
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.2
Colon ca. SW-48                  0.2
Colon Pool                       7.6
Small Intestine Pool             6.7
Stomach Pool                     3.7
Bone Marrow Pool                 6.2
Fetal heart                      21.0
Heart Pool                       3.3
Lymph Node Pool                  8.5
Fetal Skeletal Muscle            10.6
Skeletal Muscle Pool             1.1
Spleen Pool                      3.2
Thymus Pool                      3.0
CNS cancer (glio/astro) U87-MG   0.0
CNS cancer (glio/astro) U-118-MG 6.9
CNS cancer (neuro; met) SK-N-AS  0.8
CNS cancer (astro) SF-539        0.0
CNS cancer (astro) SNB-75        0.1
CNS cancer (glio) SNB-19         0.0
CNS cancer (glio) SF-295         0.0
Brain (Amygdala) Pool            0.4
Brain (cerebellum)               5.1
Brain (fetal)                    2.6
Brain (Hippocampus) Pool         1.3
Cerebral Cortex Pool             0.7
Brain (Substantia nigra) Pool    0.6
Brain (Thalamus) Pool            0.6
Brain (whole)                    1.2
Spinal Cord Pool                 2.5
Adrenal Gland                    1.9
Pituitary gland Pool             0.7
Salivary Gland                   1.4
Thyroid (female)                 0.6
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    1.7

[0802]

TABLE PD
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag7016, Run
Tissue Name                      282263182
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.0
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        15.6
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.0
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              0.0
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   0.0
LAK cells IL-2                   0.0
LAK cells IL-2 + IL-12           0.0
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.0
LAK cells PMA/ionomycin          0.0
NK Cells IL-2 rest               0.0
Two Way MLR 3 day                0.0
Two Way MLR 5 day                0.0
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.0
PBMC PHA-L                       0.0
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.2
EOL-1 dbcAMP                     0.0
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             0.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.0
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.0
Macrophages LPS                  0.0
HUVEC none                       0.0
HUVEC starved                    0.1
HUVEC IL-1beta                   0.0
HUVEC IFN gamma                  0.0
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.0
Lung Microvascular EC none       0.5
Lung Microvascular EC TNFalpha + IL- 0.0
1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  0.0
IL1beta
Small airway epithelium none     0.2
Small airway epithelium TNFalpha + 0.0
IL-1beta
Coronery artery SMC rest         0.4
Coronery artery SMC TNFalpha + IL- 0.1
1beta
Astrocytes rest                  7.9
Astrocytes TNFalpha + IL-1beta   27.4
KU-812 (Basophil) rest           0.0
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     0.0
CCD1106 (Keratinocytes) TNFalpha + 0.0
IL-1beta
Liver cirrhosis                  2.4
NCI-H292 none                    0.0
NCI-H292 IL-4                    0.0
NCI-H292 IL-9                    0.0
NCI-H292 IL-13                   0.0
NCI-H292 IFN gamma               0.0
HPAEC none                       0.1
HPAEC TNF alpha + IL-1beta       0.1
Lung fibroblast none             4.5
Lung fibroblast TNF alpha + IL-1 beta 22.2
Lung fibroblast IL-4             6.0
Lung fibroblast IL-9             6.8
Lung fibroblast IL-13            7.9
Lung fibroblast IFN gamma        7.9
Dermal fibroblast CCD1070 rest   47.0
Dermal fibroblast CCD1070 TNF alpha 46.0
Dermal fibroblast CCD1070 IL-1 beta 100.0
Dermal fibroblast IFN gamma      0.6
Dermal fibroblast IL-4           1.6
Dermal Fibroblasts rest          1.1
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 0.0
Colon                            0.7
Lung                             6.4
Thymus                           0.2
Kidney                           0.5

[0803] CNS_neurodegeneration_v1.0 Summary: Ag7016 This panel confirms the expression of the CG 132297-01 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 1.6 for a discussion of the potential utility of this gene in treatment of central nervous system disorders.

[0804] General_screening_panel_v1.6 Summary: Ag7016 Highest expression of the CG132297-01 gene of this gene is detected in fetal lung (CT=26.3). Interestingly, this gene is expressed at much higher levels in fetal (CTs=26-31) when compared to adult lung and liver (CT=32-35). This observation suggests that expression of this gene can be used to distinguish fetal from adult lung and liver, respectively. In addition, the relative overexpression of this gene in fetal tissues suggests that the elastin encoded by this gene may enhance growth or development of lung and liver in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the elastin encoded by this gene could be useful in treatment of lung and liver related diseases.

[0805] Among tissues with metabolic or endocrine function, this gene is expressed at moderate 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.

[0806] 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.

[0807] Moderate levels of expression of this gene is also seen in colon cancer and in number of cancer cell lines derived from melanoma, brain, and lung cancer cell lines. Therefore, therapeutic modulation of the elastin encoded by this gene may be useful in the treatment of melanoma, colon, brain and lung cancer.

[0808] Panel 4.1D Summary: Ag7016 Highest expression of the CG132297-01 gene of this gene is detected in IL-1 beta treated dermal fibroblasts CCD1070 (CT=28.1). In addition, moderate to low levels of expression of this gene is also seen in dermal and lung fibroblasts, activated CD45RA CD4 lymphocyte and lung. CD45RA CD4 lymphocytes represent activated naive T cells. In activated memory cells (CD45RO CD4 lymphocyte) or CD4 Th1 or Th2 cells, resting CD4 cells (CTs=40), the expression of this gene is strongly down regulated suggesting a role for this putative protein in differentiation or activation of naive T cells. Therefore, modulation of the expression and/or activity of this putative protein encoded by this gene might be beneficial for the control of autoimmune diseases and T cell mediated diseases such as COPD, emphysema, atopic asthma, asthma, arthritis, psoriasis, IBD and allergy.

[0809] Q. NOV17a (CG132343-01): Novel Transmembrane Protein.

[0810] Expression of gene CGI132343-01 was assessed using the primer-probe set Ag4819, described in Table QA. Results of the RTQ-PCR runs are shown in Tables QB and QC.

TABLE PA
Probe Name Ag4819
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gagttacccatacaccggctat-3′	22	88	271
Probe	TET-5′-atttcacggccaggagagtcctcttt-3′-	26	110	272
	TAMRA
Reverse	5′-taaqgatgatgcccatacaaag-3′	22	163	273

[0811]

TABLE QB
General_screening_panel_v1.5
                                 Rel. Exp. (%)
                                 Ag4819, Run
Tissue Name                      228783855
Adipose                          0.2
Melanoma* Hs688(A).T             0.8
Melanoma* Hs688(B).T             1.0
Melanoma* M14                    1.3
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.1
Squamous cell carcinoma SCC-4    0.1
Testis Pool                      12.8
Prostate ca.* (bone met) PC-3    0.3
Prostate Pool                    0.0
Placenta                         0.0
Uterus Pool                      0.2
Ovarian ca. OVCAR-3              1.0
Ovarian ca. SK-OV-3              2.3
Ovarian ca. OVCAR-4              0.4
Ovarian ca. OVCAR-5              0.7
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.0
Ovary                            0.6
Breast ca. MCF-7                 0.6
Breast ca. MDA-MB-231            2.0
Breast ca. BT 549                1.0
Breast ca. T47D                  100.0
Breast ca. MDA-N                 1.1
Breast Pool                      0.0
Trachea                          0.0
Lung                             0.7
Fetal Lung                       0.7
Lung ca. NCI-N417                0.3
Lung ca. LX-I                    2.4
Lung ca. NCI-H146                0.3
Lung ca. SHP-77                  1.0
Lung ca. A549                    0.9
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 2.1
Lung ca. NCI-H460                2.9
Lung ca. HOP-62                  0.6
Lung ca. NCI-H522                1.2
Liver                            0.2
Fetal Liver                      0.7
Liver ca. HepG2                  1.2
Kidney Pool                      2.1
Fetal Kidney                     0.6
Renal ca. 786-0                  0.4
Renal ca. A498                   0.9
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.5
Renal ca. TK-10                  2.5
Bladder                          0.5
Gastric ca. (liver met.) NCI-N87 2.9
Gastric ca. KATO III             0.6
Colon ca. SW-948                 0.0
Colon ca. SW480                  1.1
Colon ca.* (SW480 met) SW620     2.1
Colon ca. HT29                   0.2
Colon ca. HCT-116                2.3
Colon ca. CaCo-2                 4.4
Colon cancer tissue              0.9
Colon ca. SW1116                 1.5
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.0
Colon Pool                       0.9
Small Intestine Pool             0.2
Stomach Pool                     0.5
Bone Marrow Pool                 0.0
Fetal Heart                      0.5
Heart Pool                       0.5
Lymph Node Pool                  0.6
Fetal Skeletal Muscle            0.5
Skeletal Muscle Pool             0.1
Spleen Pool                      0.5
Thymus Pool                      0.7
CNS cancer (glio/astro) U87-MG   1.1
CNS cancer (glio/astro) U-118-MG 3.9
CNS cancer (neuro; met) SK-N-AS  2.5
CNS cancer (astro) SF-539        1.0
CNS cancer (astro) SNB-75        5.0
CNS cancer (glio) SNB-19         0.3
CNS cancer (glio) SF-295         4.7
Brain (Amygdala) Pool            0.0
Brain (cerebellum)               2.4
Brain (fetal)                    0.5
Brain (Hippocampus) Pool         0.0
Cerebral Cortex Pool             0.2
Brain (Substantia nigra) Pool    0.0
Brain (Thalamus) Pool            1.6
Brain (whole)                    0.2
Spinal Cord Pool                 0.3
Adrenal Gland                    0.3
Pituitary gland Pool             0.3
Salivary Gland                   0.0
Thyroid (female)                 0.0
Pancreatic ca. CAPAN2            0.6
Pancreas Pool                    0.8

[0812]

TABLE QC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4819, Run
Tissue Name                      223302997
Secondary Th1 act                57.4
Secondary Th2 act                25.7
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  26.1
Primary Th1 rest                 7.6
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        28.7
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               70.7
Secondary CD8 lymphocyte rest    64.6
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              19.5
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   14.5
LAK cells IL-2                   45.1
LAK cells IL-2 + IL-12           22.1
LAK cells IL-2 + IFN gamma       40.1
LAK cells IL-2 + IL-18           0.0
LAK cells PMA/ionomycin          20.3
NK Cells IL-2 rest               50.7
Two Way MLR 3 day                0.0
Two Way MLR 5 day                32.1
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         44.1
PBMC PHA-L                       0.0
Ramos (B cell) none              15.5
Ramos (B cell) ionomycin         50.7
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     8.8
EOL-1 dbcAMP                     46.7
EOL-1 dbcAMP PMA/ionomycin       27.2
Dendritic cells none             38.7
Dendritic cells LPS              34.2
Dendritic cells anti-CD40        15.2
Monocytes rest                   18.9
Monocytes LPS                    8.8
Macrophages rest                 29.5
Macrophages LPS                  0.0
HUVEC none                       0.0
HUVEC starved                    0.0
HUVEC IL-1beta                   33.7
HUVEC IFN gamma                  55.9
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            13.4
HUVEC IL-11                      0.0
Lung Microvascular EC none       51.4
Lung Microvascular EC TNFalpha + IL- 0.0
1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  15.4
IL1beta
Small airway epithelium none     15.2
Small airway epithelium TNFalpha + 61.6
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha + IL- 0.0
1beta
Astrocytes rest                  51.1
Astrocytes TNFalpha + IL-1beta   14.4
KU-812 (Basophil) rest           25.3
KU-812 (Basophil) PMA/ionomycin  51.1
CCD1106 (Keratinocytes) none     18.2
CCD1106 (Keratinocytes) TNFalpha + 55.1
IL-1beta
Liver cirrhosis                  0.0
NCI-H292 none                    17.7
NCI-H292 IL-4                    16.6
NCI-H292 IL-9                    14.6
NCI-H292 IL-13                   31.0
NCI-H292 IFN gamma               30.4
HPAEC none                       0.0
HPAEC TNF alpha + IL-1 beta      12.1
Lung fibroblast none             23.2
Lung fibroblast TNF alpha + IL-1 beta 0.0
Lung fibroblast IL-4             42.0
Lung fibroblast IL-9             47.3
Lung fibroblast IL-13            30.8
Lung fibroblast IFN gamma        36.3
Dermal fibroblast CCD1070 rest   27.7
Dermal fibroblast CCD1070 TNF alpha 28.1
Dermal fibroblast CCD1070 IL-1 beta 10.2
Dermal fibroblast IFN gamma      15.7
Dermal fibroblast IL-4           34.2
Dermal Fibroblasts rest          22.5
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 0.0
Colon                            0.0
Lung                             0.0
Thymus                           0.0
Kidney                           100.0

[0813] General_screening_panel_v1.5 Summary: Ag4819 Expression of this gene is restricted to a few samples in this panel, with highest expression in a breast cancer cell line (CT=29). Low, but significant levels of expression are seen in cell lines derived from brain, renal and gastric cancers, as well as in normal testis. Thus, the expression of this gene could be used to distinguish the breast cancer cell line sample from other samples on this panel, and as a marker of breast cancer. In addition, therapeutic modulation of this gene or its protein product may be useful in the treatment of breast, gastric, renal and brain cancers.

[0814] Panel 4.1D Summary: Ag4819 This gene is only expressed at detectable levels in the kidney (CT=34.5). Thus, 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.

[0815] R. NOV18a (CG132423-01): Pregnancy-specific Beta-1-glycoprotein 2 Precursor.

[0816] Expression of gene CG132423-01 was assessed using the primer-probe set Ag7021, described in Table RA.

TABLE RA
Probe Name Ag7021
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-aggtccctgatttggacaag-3′	20	848	274
Probe	TET-5′-aagaacatccttcccctcggacactt-3′-	26	871	275
	TAMRA
Reverse	5′-ctgcccaagtcatgattgaa-3′	20	910	276

[0817] CNS_neurodegeneration_v1.0 Summary: Ag7021 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0818] General_screening_panel_v1.6 Summary: Ag7021 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0819] Panel 4.1D Summary: Ag7021 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0820] S. Nov19a and NOV19b (CG132541-01 and CG132541-02): Protocadherin 16 Precursor.

[0821] Expression of gene CG132541 -01 and CG132541-02 was assessed using the primer-probe sets Ag1076, Ag1311, Ag482, and Ag6709 described in Tables SA, SB, SC, and SD. Results of the RTQ-PCR runs are shown in Tables SE, SF, SG, SH, SI, SJ, SK and SL. Please note that probe and primer set Ag6709 is specific for CG132541-01 and probe Ag482 is specific for CG132541-02.

TABLE SA
Probe Name Ag1076
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-tgacagacactgtggtgcttag-3′	22	6228	277
Probe	TET-5′-accatccactgcactcacagaaaagg-3′-	26	6187	278
	TAMRA
Reverse	5′-agagaacagtgtcccagctaca-3′	22	6165	279

[0822]

TABLE SB
Probe Name Ag1311
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-tccagtacctgagctggtagtt-3′	22	1016	280
Probe	TET-5′-tggaccgagagaaccgctcacactat-3′-	26	1048	281
	TAMRA
Reverse	5′-atcataggcctccagctgtag-3′	21	1077	282

[0823]

TABLE SC
Probe Name Ag482
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-acagtgcttgtggaggatgtca-3′	22	7497	283
Probe	TET-5′-aatgcacctgccttctcacagagcctc-3′-	27	7524	284
	TAMRA
Reverse	5′-gctcaagcagcattacctggt-3′	21	7552	285

[0824]

TABLE SD
Probe Name Ag6709
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-tcatcgacaccaatgacaatc-3′	21	6800	286
Probe	TET-5′-ctgacactcggagctcccagggtt-3′-	24	6836	287
	TAMRA
Reverse	5′-acacatggcttgccatctt-3′	19	6860	288

[0825]

TABLE SE
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%)
                               Ag1311, Run
Tissue Name                    273207795
AD 1 Hippo                     27.0
AD 2 Hippo                     44.4
AD 3 Hippo                     15.7
AD 4 Hippo                     21.3
AD 5 Hippo                     75.8
AD 6 Hippo                     100.0
Control 2 Hippo                41.2
Control 4 Hippo                33.9
Control (Path) 3 Hippo         20.7
AD 1 Temporal Ctx              31.2
AD 2 Temporal Ctx              48.3
AD 3 Temporal Ctx              16.3
AD 4 Temporal Ctx              35.4
AD 5 Inf Temporal Ctx          91.4
AD 5 Sup Temporal Ctx          50.3
AD 6 Inf Temporal Ctx          82.4
AD 6 Sup Temporal Ctx          88.9
Control 1 Temporal Ctx         36.3
Control 2 Temporal Ctx         64.6
Control 3 Temporal Ctx         33.2
Control 3 Temporal Ctx         28.9
Control (Path) 1 Temporal Ctx  72.2
Control (Path) 2 Temporal Ctx  45.7
Control (Path) 3 Temporal Ctx  24.7
Control (Path) 4 Temporal Ctx  47.3
AD 1 Occipital Ctx             27.2
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             24.1
AD 4 Occipital Ctx             22.5
AD 5 Occipital Ctx             52.1
AD 6 Occipital Ctx             21.5
Control 1 Occipital Ctx        30.1
Control 2 Occipital Ctx        61.1
Control 3 Occipital Ctx        39.0
Control 4 Occipital Ctx        25.3
Control (Path) 1 Occipital Ctx 90.1
Control (Path) 2 Occipital Ctx 16.7
Control (Path) 3 Occipital Ctx 18.6
Control (Path) 4 Occipital Ctx 20.7
Control 1 Parietal Ctx         31.6
Control 2 Parietal Ctx         59.0
Control 3 Parietal Ctx         31.0
Control (Path) 1 Parietal Ctx  77.4
Control (Path) 2 Parietal Ctx  38.7
Control (Path) 3 Parietal Ctx  24.5
Control (Path) 4 Parietal Ctx  55.9

[0826]

TABLE SF
General_screening_panel_v1.4
                                 Rel. Exp. (%)
                                 Ag1311, Run
Tissue Name                      213323270
Adipose                          7.6
Melanoma* Hs688(A).T             16.4
Melanoma* Hs688(B).T             1.0
Melanoma* M14                    2.2
Melanoma* LOXIMVI                0.1
Melanoma* SK-MEL-5               0.3
Squamous cell carcinoma SCC-4    0.1
Testis Pool                      0.8
Prostate ca.* (bone met) PC-3    0.1
Prostate Pool                    6.0
Placenta                         17.8
Uterus Pool                      6.3
Ovarian ca. OVCAR-3              1.1
Ovarian ca. SK-OV-3              12.2
Ovarian ca. OVCAR-4              0.0
Ovarian ca. OVCAR-5              0.2
Ovarian ca. IGROV-1              2.9
Ovarian ca. OVCAR-8              0.2
Ovary                            21.5
Breast ca. MCF-7                 0.1
Breast ca. MDA-MB-231            0.3
Breast ca. BT 549                1.1
Breast ca. T47D                  0.1
Breast ca. MDA-N                 0.3
Breast Pool                      45.7
Trachea                          7.0
Lung                             2.6
Fetal Lung                       43.8
Lung ca. NCI-N417                0.1
Lung ca. LX-1                    0.9
Lung ca. NCI-H146                10.2
Lung ca. SHP-77                  0.0
Lung ca. A549                    0.0
Lung ca. NCI-H526                4.4
Lung ca. NCI-H23                 2.5
Lung ca. NCI-H460                0.6
Lung ca. HOP-62                  0.4
Lung ca. NCI-H522                1.9
Liver                            1.1
Fetal Liver                      0.0
Liver ca. HepG2                  0.0
Kidney Pool                      67.8
Fetal Kidney                     14.5
Renal ca. 786-0                  0.2
Renal ca. A498                   0.1
Renal ca. ACHN                   0.6
Renal ca. UO-31                  0.2
Renal ca. TK-10                  0.0
Bladder                          5.1
Gastric ca. (liver met.) NCI-N87 0.0
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.1
Colon ca. SW480                  0.4
Colon ca.* (SW480 met) SW620     0.4
Colon ca. HT29                   0.1
Colon ca. HCT-116                0.2
Colon ca. CaCo-2                 0.9
Colon cancer tissue              10.1
Colon ca. SW1116                 0.2
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.1
Colon Pool                       59.0
Small Intestine Pool             29.5
Stomach Pool                     21.0
Bone Marrow Pool                 17.2
Fetal Heart                      23.0
Heart Pool                       16.6
Lymph Node Pool                  52.1
Fetal Skeletal Muscle            13.6
Skeletal Muscle Pool             2.8
Spleen Pool                      8.4
Thymus Pool                      19.3
CNS cancer (glio/astro) U87-MG   0.4
CNS cancer (glio/astro) U-118-MG 5.8
CNS cancer (neuro; met) SK-N-AS  46.0
CNS cancer (astro) SF-539        4.1
CNS cancer (astro) SNB-75        2.5
CNS cancer (glio) SNB-19         3.1
CNS cancer (glio) SF-295         33.2
Brain (Amygdala) Pool            3.3
Brain (cerebellum)               17.1
Brain (fetal)                    100.0
Brain (Hippocampus) Pool         5.2
Cerebral Cortex Pool             5.6
Brain (Substantia nigra) Pool    5.9
Brain (Thalamus) Pool            4.5
Brain (whole)                    14.1
Spinal Cord Pool                 2.1
Adrenal Gland                    4.4
Pituitary gland Pool             0.4
Salivary Gland                   0.8
Thyroid (female)                 2.5
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    27.4

[0827]

TABLE SG
HASS Panel v1.0
                              Rel. Exp. (%)
Tissue                        Ag1311, Run
Name                          268362648
MCF-7 C1                      0.1
MCF-7 C2                      0.0
MCF-7 C3                      0.0
MCF-7 C4                      0.1
MCF-7 C5                      0.0
MCF-7 C6                      0.1
MCF-7 C7                      0.0
MCF-7 C9                      0.0
MCF-7 C10                     0.0
MCF-7 C11                     0.0
MCF-7 C12                     0.0
MCF-7 C13                     0.0
MCF-7 C15                     0.0
MCF-7 C16                     0.0
MCF-7 C17                     0.1
T24 D1                        3.2
T24 D2                        3.0
T24 D3                        3.6
T24 D4                        4.5
T24 D5                        1.9
T24 D6                        3.1
T24 D7                        1.4
T24 D9                        1.7
T24 D10                       1.7
T24 D11                       1.3
T24 D12                       1.8
T24 D13                       1.1
T24 D15                       3.4
T24 D16                       1.6
T24 D17                       2.0
CAPaN B1                      0.0
CAPaN B2                      0.0
CAPaN B3                      0.0
CAPaN B4                      0.0
CAPaN B5                      0.1
CAPaN B6                      0.1
CAPaN B7                      0.0
CAPaN B8                      0.0
CAPaN B9                      0.0
CAPaN B10                     0.2
CAPaN B11                     0.0
CAPaN B12                     0.0
CAPaN B13                     0.0
CAPaN B14                     0.0
CAPaN B15                     0.0
CAPaN B16                     0.0
CAPaN B17                     0.1
U87-MG F1 (B)                 0.2
U87-MG F2                     0.9
U87-MG F3                     1.5
U87-MG F4                     0.5
U87-MG F5                     2.4
U87-MG F6                     1.1
U87-MG F7                     0.9
U87-MG F8                     1.4
U87-MG F9                     1.0
U87-MG F10                    0.8
U87-MG F11                    0.6
U87-MG F12                    0.3
U87-MG F13                    1.4
U87-MG F14                    1.5
U87-MG F15                    0.9
U87-MG F16                    1.4
U87-MG F17                    1.9
LnCAP A1                      0.3
LnCAP A2                      0.6
LnCAP A3                      0.2
LnCAP A4                      0.5
LnCAP A5                      0.7
LnCAP A6                      0.1
LnCAP A7                      0.9
LnCAP A8                      1.3
LnCAP A9                      0.3
LnCAP A10                     0.1
LnCAP A11                     2.4
LnCAP A12                     0.1
LnCAP A13                     0.1
LnCAP A14                     0.7
LnCAP A15                     0.4
LnCAP A16                     0.4
LnCAP A17                     1.3
Primary Astrocytes            29.1
Primary Renal Proximal Tubule 0.1
Epithelial cell A2
Primary melanocytes A5        2.8
126443-341 medullo            2.3
126444-487 medullo            77.4
126445-425 medullo            3.4
126446-690 medullo            90.8
126447-54 adult glioma        0.2
126448-245 adult glioma       6.0
126449-317 adult glioma       38.4
126450-212 glioma             100.0
126451-456 glioma             27.4

[0828]

TABLE SH
Oncology_cell_line_screening_panel_v3.2
                                 Rel. Exp. (%)
                                 Ag1311, Run
Tissue Name                      264977450
94905_Daoy_Medulloblastoma/      1.0
Cerebellum_sscDNA
94906_TE671_Medulloblastoma/     15.4
Cerebellum_sscDNA
94907_D283 Med_Medulloblastoma/  4.7
Cerebellum_sscDNA
94908_PFSK-1_Primitive Neuroectodermal/ 1.1
Cerebellum_sscDNA
94909_XF-498_CNS_sscDNA          2.0
94910_SNB-78_CNS/glioma_sscDNA   0.0
94911_SF-268_CNS/glioblastoma_sscDNA 0.9
94912_T98G_Glioblastoma_sscDNA   0.6
96776_SK-N-SH_Neuroblastoma      16.2
(metastasis)_sscDNA
94913_SF-295_CNS/glioblastoma_sscDNA 10.2
132565_NT2 pool_sscDNA           4.2
94914_Cerebellum_sscDNA          5.7
96777_Cerebellum_sscDNA          8.9
94916_NCI-H292_Mucoepidermoid lung 0.5
carcinoma_sscDNA
94917_DMS-114_Small cell lung    7.7
cancer_sscDNA
94918_DMS-79_Small cell lung     100.0
cancer/neuroendocrine_sscDNA
94919_NCI-H146_Small cell lung   24.3
cancer/neuroendocrine_sscDNA
94920_NCI-H526_Small cell lung   11.4
cancer/neuroendocrine_sscDNA
94921_NCI-N417_Small cell lung   0.0
cancer/neuroendocrine_sscDNA
94923_NCI-H82_Small cell lung    28.5
cancer/neuroendocrine_sscDNA
94924_NCI-H157_Squamous cell     0.4
lung cancer (metastasis)_sscDNA
94925_NCI-H1155_Large cell lung  25.3
cancer/neuroendocrine_sscDNA
94926_NCI-H1299_Large cell lung  0.3
cancer/neuroendocrine_sscDNA
94927_NCI-H727_Lung carcinoid—   0.2
sscDNA
94928_NCI-UMC-11_Lung carcinoid— 0.8
sscDNA
94929_LX-1_Small cell lung       0.2
cancer_sscDNA
94930_Colo-205_Colon cancer_sscDNA 0.0
94931_KM12_Colon cancer_sscDNA   0.1
94932_KM20L2_Colon cancer_sscDNA 0.1
94933_NCI-H716_Colon cancer_sscDNA 0.5
94935_SW-48_Colon adenocarcinoma— 0.0
sscDNA
94936_SW1116_Colon               0.6
adenocarcinoma_sscDNA
94937_LS 174T_Colon              0.1
adenocarcinoma_sscDNA
94938_SW-948_Colon               0.0
adenocarcinoma_sscDNA
94939_SW-480_Colon               0.0
adenocarcinoma_sscDNA
94940_NCI-SNU-5_Gastric          0.1
carcinoma_sscDNA
112197_KATO III_Stomach_sscDNA   0.0
94943_NCI-SNU-16_Gastric         0.0
carcinoma_sscDNA
94944_NCI-SNU-1_Gastric          0.1
carcinoma_sscDNA
94946_RF-1_Gastric               0.3
adenocarcinoma_sscDNA
94947_RF-48_Gastric              0.4
adenocarcinoma_sscDNA
96778_MKN-45_Gastric             0.0
carcinoma_sscDNA
94949_NCI-N87_Gastric            0.0
carcinoma_sscDNA
94951_OVCAR-5_Ovarian            0.0
carcinoma_sscDNA
94952_RL95-2_Uterine             0.0
carcinoma_sscDNA
94953_HelaS3_Cervical            0.0
adenocarcinoma_sscDNA
94954_Ca Ski_Cervical            0.0
epidermoid carcinoma
(metastasis)_sscDNA
94955_ES-2_Ovarian clear         2.2
cell carcinoma_sscDNA
94957_Ramos/6 h stim_Stimulated  0.0
with PMA/ionomycin 6 h_sscDNA
94958_Ramos/14 h stim_Stimulated 0.2
with PMA/ionomycin 14 h_sscDNA
94962_MEG-01_Chronic myelogenous 0.3
leukemia (megokaryoblast)_sscDNA
94963_Raji_Burkitt's lymphoma—   0.0
sscDNA
94964_Daudi_Burkitt's lymphoma—  0.0
sscDNA
94965_U266_B-cell plasmacytoma/  0.1
myeloma_sscDNA
94968_CA46_Burkitt's lymphoma_sscDNA 0.0
94970_RL_non-Hodgkin's B-cell    0.0
lymphoma_sscDNA
94972_JM1_pre-B-cell lymphoma/   0.4
leukemia_sscDNA
94973_Jurkat_T cell leukemia_sscDNA 0.3
94974_TF-1_Erythroleukemia_sscDNA 0.0
94975_HUT 78_T-cell lymphoma_sscDNA 0.0
94977_U937_Histiocytic lymphoma— 0.2
sscDNA
94980_KU-812_Myelogenous         0.1
leukemia_sscDNA
94981_769-P_Clear cell renal     0.2
carcinoma_sscDNA
94983_Caki-2_Clear cell renal    0.1
carcinoma_sscDNA
94984_SW 839_Clear cell renal    0.0
carcinoma_sscDNA
94986_G401_Wilms' tumor_sscDNA   0.2
126768_293 cells_sscDNA          1.6
94987_Hs766T_Pancreatic carcinoma 0.3
(LN metastasis)_sscDNA
94988_CAPAN-1_Pancreatic         0.0
adenocarcinoma (liver
metastasis)_sscDNA
94989_SU86.86_Pancreatic         1.0
carcinoma (liver
metastasis)_sscDNA
94990_BxPC-3_Pancreatic          0.4
adenocarcinoma_sscDNA
94991_HPAC_Pancreatic            0.0
adenocarcinoma_sscDNA
94992_MIA PaCa-2_Pancreatic      0.2
carcinoma_sscDNA
94993_CFPAC-1_Pancreatic ductal  0.1
adenocarcinoma_sscDNA
94994_PANC-1_Pancreatic          1.3
epithelioid ductal
carcinoma_sscDNA
94996_T24_Bladder carcinma       0.2
(transitional cell)_sscDNA
94997_5637_Bladder carcinoma—    0.0
sscDNA
94998_HT-1197_Bladder carcinoma— 0.1
sscDNA
94999_UM-UC-3_Bladder carcinma   0.0
(transitional cell)_sscDNA
95000_A204_Rhabdomyosarcoma_sscDNA 0.3
95001_HT-1080_Fibrosarcoma—      0.6
sscDNA
95002_MG-63_Osteosarcoma (bone)— 5.0
sscDNA
95003_SK-LMS-1_Leiomyosarcoma    3.5
(vulva)_sscDNA
95004_SJRH30_Rhabdomyosarcoma (met 6.4
to bone marrow)_sscDNA
95005_A431_Epidermoid carcinoma— 0.1
sscDNA
95007_WM266-4_Melanoma_sscDNA    0.1
112195_DU 145_Prostate_sscDNA    0.0
95012_MDA-MB-468_Breast          0.1
adenocarcinoma_sscDNA
112196_SSC-4_Tongue_sscDNA       0.0
112194_SSC-9_Tongue_sscDNA       0.1
112191_SSC-15_Tongue_sscDNA      0.1
95017_CAL 27_Squamous cell       0.0
carcinoma of tongue_sscDNA

[0829]

TABLE SI
Panel 1
                                 Rel. Exp. (%)
                                 Ag482, Run
Tissue Name                      121039178
Endothelial cells                21.3
Endothelial cells (treated)      17.6
Pancreas                         10.4
Pancreatic ca. CAPAN2            0.0
Adrenal gland                    12.2
Thyroid                          5.5
Salivary gland                   6.6
Pituitary gland                  35.4
Brain (fetal)                    49.0
Brain (whole)                    10.7
Brain (amygdala)                 18.0
Brain (cerebellum)               11.2
Brain (hippocampus)              14.8
Brain (substantia nigra)         11.0
Brain (thalamus)                 13.6
Brain (hypothalamus)             14.9
Spinal cord                      8.1
glio/astro U87-MG                0.0
glio/astro U-118-MG              2.7
astrocytoma SW1783               3.8
neuro*; met SK-N-AS              61.6
astrocytoma SF-539               1.3
astrocytoma SNB-75               0.1
glioma SNB-19                    17.2
glioma U251                      0.6
glioma SF-295                    23.7
Heart                            38.2
Skeletal muscle                  8.0
Bone marrow                      3.6
Thymus                           20.6
Spleen                           18.2
Lymph node                       9.9
Colon (ascending)                19.9
Stomach                          11.3
Small intestine                  20.4
Colon ca. SW480                  2.1
Colon ca.* SW620 (SW480 met)     0.0
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.0
Colon ca. CaCo-2                 4.5
Colon ca. HCT-15                 0.0
Colon ca. HCC-2998               5.1
Gastric ca.* (liver met) NCI-N87 0.0
Bladder                          15.3
Trachea                          7.6
Kidney                           21.6
Kidney (fetal)                   33.4
Renal ca. 786-0                  0.1
Renal ca. A498                   0.0
Renal ca. RXF 393                0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.0
Renal ca. TK-10                  0.0
Liver                            13.2
Liver (fetal)                    14.2
Liver ca. (hepatoblast) HepG2    0.0
Lung                             17.1
Lung (fetal)                     10.2
Lung ca. (small cell) LX-1       2.6
Lung ca. (small cell) NCI-H69    1.6
Lung ca. (s. cell var.) SHP-77   0.0
Lung ca. (large cell)NCI-H460    3.0
Lung ca. (non-sm. cell) A549     0.0
Lung ca. (non-s. cell) NCI-H23   2.4
Lung ca. (non-s. cell) HOP-62    1.9
Lung ca. (non-s. cl) NCI-H522    5.4
Lung ca. (squam.) SW 900         0.0
Lung ca. (squam.) NCI-H596       1.5
Mammary gland                    57.4
Breast ca.* (pl. ef) MCF-7       0.1
Breast ca.* (pl. ef) MDA-MB-231  0.1
Breast ca.* (pl. ef) T47D        0.0
Breast ca. BT-549                0.0
Breast ca. MDA-N                 0.1
Ovary                            100.0
Ovarian ca. OVCAR-3              4.4
Ovarian ca. OVCAR-4              0.0
ovarian ca. OVCAR-5              0.0
Ovarian ca. OVCAR-8              19.9
Ovarian ca. IGROV-1              3.3
Ovarian ca. (ascites) SK-OV-3    13.1
Uterus                           17.6
Placenta                         30.4
Prostate                         17.2
Prostate ca.* (bone met) PC-3    0.0
Testis                           22.7
Melanoma Hs688(A).T              11.7
Melanoma* (met) Hs688(B).T       3.8
Melanoma UACC-62                 1.6
Melanoma M14                     0.4
Melanoma LOX IMVI                0.0
Melanoma* (met) SK-MEL-5         0.0
Melanoma SK-MEL-28               0.0

[0830]

TABLE SJ
Panel 1.2
                                 Rel. Exp. (%)
                                 Ag1311, Run
Tissue Name                      129674732
Endothelial cells                30.1
Heart (Fetal)                    100.0
Pancreas                         3.3
Pancreatic ca. CAPAN 2           0.0
Adrenal Gland                    8.4
Thyroid                          2.7
Salivary gland                   4.8
Pituitary gland                  4.8
Brain (fetal)                    10.9
Brain (whole)                    4.7
Brain (amygdala)                 3.8
Brain (cerebellum)               4.5
Brain (hippocampus)              7.2
Brain (thalamus)                 2.9
Cerebral Cortex                  25.7
Spinal cord                      4.2
glio/astro U87-MG                0.3
glio/astro U-118-MG              2.2
astrocytoma SW1783               1.0
neuro*; met SK-N-AS              22.5
astrocytoma SF-539               2.1
astrocytoma SNB-75               0.7
glioma SNB-19                    4.6
glioma U251                      0.2
glioma SF-295                    0.2
Heart                            36.9
Skeletal Muscle                  5.8
Bone marrow                      0.3
Thymus                           2.2
Spleen                           2.7
Lymph node                       5.0
Colorectal Tissue                3.1
Stomach                          9.4
Small intestine                  9.3
Colon ca. SW480                  0.0
Colon ca.* SW620 (SW480 met)     0.1
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.1
Colon ca. CaCo-2                 0.4
Colon ca. Tissue (ODO3866)       4.1
Colon ca. HCC-2998               0.1
Gastric ca.* (liver met) NCI-N87 0.0
Bladder                          9.3
Trachea                          2.5
Kidney                           7.6
Kidney (fetal)                   26.8
Renal ca. 786-0                  0.1
Renal ca. A498                   0.1
Renal ca. RXF 393                0.0
Renal ca. ACHN                   0.1
Renal ca. UO-31                  0.1
Renal ca. TK-10                  0.0
Liver                            5.8
Liver (fetal)                    3.3
Liver ca. (hepatoblast) HepG2    0.2
Lung                             4.9
Lung (fetal)                     7.0
Lung ca. (small cell) LX-1       0.2
Lung ca. (small cell) NCI-H69    0.9
Lung ca. (s. cell var.) SHP-77   0.0
Lung ca. (large cell) NCI-H460   1.1
Lung ca. (non-sm. cell) A549     0.1
Lung ca. (non-s. cell)NCI-H23    0.2
Lung ca. (non-s. cell) HOP-62    4.4
Lung ca. (non-s. cl) NCI-H522    1.3
Lung ca. (squam.) SW 900         0.2
Lung ca. (squam.) NCI-H596       0.6
Mammary gland                    12.6
Breast ca.* (pl. ef) MCF-7       0.0
Breast ca.* (pl. ef) MDA-MB-231  0.1
Breast ca.* (pl. ef) T47D        0.0
Breast ca. BT-549                0.1
Breast ca. MDA-N                 0.2
Ovary                            41.5
Ovarian ca. OVCAR-3              0.3
Ovarian ca. OVCAR-4              0.1
Ovarian ca. OVCAR-5              0.1
Ovarian ca. OVCAR-8              1.0
Ovarian ca. IGROV-1              0.0
Ovarian ca. (ascites) SK-OV-3    4.0
Uterus                           12.4
Placenta                         19.6
Prostate                         7.0
Prostate ca.* (bone met) PC-3    0.1
Testis                           3.2
Melanoma Hs688(A).T              4.6
Melanoma* (met) Hs688(B).T       13.0
Melanoma UACC-62                 0.3
Melanoma M14                     0.1
Melanoma LOX IMVI                0.0
Melanoma* (met) SK-MEL-5         0.1

[0831]

TABLE SK
Panel 4D
                                 Rel. Exp. (%)
                                 Ag1311, Run
Tissue Name                      138960982
Secondary Th1 act                0.4
Secondary Th2 act                2.0
Secondary Tr1 act                1.6
Secondary Th1 rest               0.2
Secondary Th2 rest               0.1
Secondary Tr1 rest               0.3
Primary Th1 act                  0.7
Primary Th2 act                  1.2
Primary Tr1 act                  0.6
Primary Th1 rest                 2.8
Primary Th2 rest                 2.4
Primary Tr1 rest                 0.7
CD45RA CD4 lymphocyte act        11.8
CD45RO CD4 lymphocyte act        2.2
CD8 lymphocyte act               1.4
Secondary CD8 lymphocyte rest    1.2
Secondary CD8 lymphocyte act     0.3
CD4 lymphocyte none              8.5
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.5
LAK cells rest                   5.9
LAK cells IL-2                   0.6
LAK cells IL-2 + IL-12           2.2
LAK cells IL-2 + IFN gamma       2.5
LAK cells IL-2 + IL-18           1.3
LAK cells PMA/ionomycin          8.5
NK Cells IL-2 rest               3.7
Two Way MLR 3 day                1.7
Two Way MLR 5 day                2.4
Two Way MLR 7 day                2.4
PBMC rest                        1.4
PBMC PWM                         1.2
PBMC PHA-L                       1.7
Ramos (B cell) none              0.3
Ramos (B cell) ionomycin         1.4
B lymphocytes PWM                1.6
B lymphocytes CD40L and IL-4     1.0
EOL-1 dbcAMP                     0.1
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             2.8
Dendritic cells LPS              0.6
Dendritic cells anti-CD40        0.9
Monocytes rest                   1.0
Monocytes LPS                    1.1
Macrophages rest                 1.7
Macrophages LPS                  1.4
HUVEC none                       45.7
HUVEC starved                    75.8
HUVEC IL-1beta                   22.4
HUVEC IFN gamma                  100.0
HUVEC TNF alpha + IFN gamma      11.7
HUVEC TNF alpha + IL4            24.5
HUVEC IL-11                      38.2
Lung Microvascular EC none       54.3
Lung Microvascular EC TNFalpha + IL- 24.3
1beta
Microvascular Dermal EC none     79.0
Microsvasular Dermal EC TNFalpha + 51.4
IL-1beta
Bronchial epithelium TNFalpha +  0.0
IL1beta
Small airway epithelium none     0.0
Small airway epithelium TNFalpha + 1.2
IL-1beta
Coronery artery SMC rest         2.1
Coronery artery SMC TNFalpha + IL- 3.5
1beta
Astrocytes rest                  19.3
Astrocytes TNFalpha + IL-1beta   8.2
KU-812 (Basophil) rest           0.3
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     0.7
CCD1106 (Keratinocytes) TNFalpha + 0.6
IL-1beta
Liver cirrhosis                  3.3
Lupus kidney                     1.4
NCI-H292 none                    1.6
NCI-H292 IL-4                    1.4
NCI-H292 IL-9                    0.7
NCI-H292 IL-13                   1.7
NCI-H292 IFN gamma               2.1
HPAEC none                       56.6
HPAEC TNF alpha + IL-1 beta      41.8
Lung fibroblast none             22.4
Lung fibroblast TNF alpha + IL-1 beta 14.8
Lung fibroblast IL-4             33.4
Lung fibroblast IL-9             23.2
Lung Fibroblast IL-13            50.7
Lung fibroblast IFN gamma        52.1
Dermal fibroblast CCD1070 rest   23.5
Dermal fibroblast CCD1070 TNF alpha 19.3
Dermal fibroblast CCD1070 IL-1 beta 19.9
Dermal fibroblast IFN gamma      29.7
Dermal fibroblast IL-4           62.0
IBD Colitis 2                    2.1
IBD Crohn's                      2.6
Colon                            20.0
Lung                             75.3
Thymus                           29.7
Kidney                           32.5

[0832]

TABLE SL
general oncology screening panel_v_2.4
                               Rel. Exp. (%)
                               Ag1311, Run
Tissue Name                    259733190
Colon cancer 1                 10.6
Colon cancer NAT 1             7.6
Colon cancer 2                 6.6
Colon cancer NAT 2             3.1
Colon cancer 3                 9.4
Colon cancer NAT 3             12.9
Colon malignant cancer 4       8.2
Colon normal adjacent tissue 4 2.0
Lung cancer 1                  4.3
Lung NAT 1                     2.1
Lung cancer 2                  50.3
Lung NAT 2                     2.9
Squamous cell carcinoma 3      9.9
Lung NAT 3                     0.6
metastatic melanoma 1          24.5
Melanoma 2                     2.7
Melanoma 3                     0.7
metastatic melanoma 4          100.0
metastatic melanoma 5          87.7
Bladder cancer 1               1.5
Bladder cancer NAT 1           0.0
Bladder cancer 2               2.8
Bladder cancer NAT 2           0.5
Bladder cancer NAT 3           0.4
Bladder cancer NAT 4           6.5
Prostate adenocarcinoma 1      43.2
Prostate adenocarcinoma 2      3.5
Prostate adenocarcinoma 3      2.7
Prostate adenocarcinoma 4      7.6
Prostate cancer NAT 5          2.9
Prostate adenocarcinoma 6      2.1
Prostate adenocarcinoma 7      5.6
Prostate adenocarcinoma 8      1.8
Prostate adenocarcinoma 9      28.7
Prostate cancer NAT 10         1.4
Kidney cancer 1                17.6
Kidney NAT 1                   2.6
Kidney cancer 2                20.2
Kidney NAT 2                   5.2
Kidney cancer 3                8.7
Kidney NAT 3                   3.0
Kidney cancer 4                11.2
Kidney NAT 4                   2.4

[0833] CNS_neurodegeneration_v1.0 Summary: Ag1311 This panel confirms the expression of this gene at moderate levels in the brain in an independent group of individuals. This gene appears 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. Ag6709 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0834] General_screening_panel_v1.4 Summary: Ag1311 Highest expression of this gene is seen in the fetal brain (CT=25). Thus, expression of this gene could be used to differentiate between fetal and adult brain tissue. Moderate levels of expression are seen in all regions of the CNS examined. This gene has homology to cadherin, transmembrane glycoproteins that are involved in many biological processes such as cell adhesion, cytoskeletal organization and morphogenesis. Cadherins can act as axon guidance and cell adhesion proteins, specifically during development and in the response to injury (Ranscht B. Int. J. Dev. Neurosci. 18: 643-651). Therefore, manipulation of levels of this protein may be of use in inducing a compensatory synaptogenic response to neuronal death in Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar ataxia, progressive supranuclear palsy, ALS, head trauma, stroke, or any other disease/condition associated with neuronal loss.

[0835] As in Panel 1.2, this gene is expressed at high to moderate levels in metabolic tissues, including pancreas, pituitary, adipose, adrenal gland, pancreas, thyroid, liver and adult and fetal skeletal muscle, and heart. Please see Panel 1.2 for discussion of utility of this gene in metabolic disease.

[0836] Moderate levels of expression are also seen in cancer cell lines derived from melanoma, ovarian, lung, colon and brain cancers.

[0837] General_screening_panel_v1.6 Summary: Ag6709 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0838] HASS Panel v1.0 Summary: Ag1311 Highest expression of this gene is detected in glioma cells (CT=27.3). This gene is expressed at a low to moderate level in samples of brain cancer as well as primary astrocytes in culture. Expression is also slightly increased in LnCAP and U87 cells that are subjected to cell stresses such as reduced oxygen, low serum or an acidotic environment which are some of the conditions seen in tumors.

[0839] Oncology_cell_line_screening_panel_v3.2 Summary: Ag1311 Highest expression of this gene is seen in a lung cancer cell line (CT=27.5). Moderate levels of expression of this gene are also seen in a cluster of samples derived from lung cancer cell lines, bone cancer cell lines and brain cancer cell lines. Please see Panels 1.2 and 2.4 for discussion of utility of this gene in cancer.

[0840] Panel 1 Summary: Ag482 Highest expression is seen in ovary (CT=24.3), with high levels of expression in many samples on this panel including melanoma, ovarian, and brain cancer cell lines and normal lung, liver, heart, muscle, brain, pancreas, adrenal, and endothelial cells. This expression is in agreement with results of panels run with Ag1311. Please see those experiments for discussion of utility of this gene in metabolic and autoimmune disorders and cancer.

[0841] Panel 1.2 Summary: Ag1311 The protein encoded by this gene is homologous to cadherin, a cell-adhesion protein and is highly expressed in a number of samples on panel 1.2. Specifically, the highest expression is detected in fetal heart (CT value=22.6), although it is also highly expressed in adult heart. This may suggest a potential role for this gene in cardiovascular diseases such as 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), and valve diseases. Overall, gene expression in this panel is associated with normal tissues rather than cancel cell lines. Loss of function of the related E-cadherin protein has been described in many tumors, along with an increased invasiveness and a decreased prognosis of many carcinomas, including tumors of endocrine glands and their target systems (ref 1). Thus, this gene product might similarly be useful as a protein therapeutic to treat a variety of tumors, since it is found in normal cells but missing from cancer cells.

[0842] In addition, this gene is highly expressed in pituitary gland, adrenal gland, thyroid, pancreas, skeletal muscle, and liver, reflecting the widespread role of cadherins in cell-cell adhesion. This observation may suggest that the gene plays a role in normal metabolic and neuroendocrine function and that disregulated expression of this gene may contribute to metabolic diseases (such as obesity and diabetes) or neuroendocrine disorders.

[0843] Expression of this gene is also high in many regions of the brain, including the amygdala, thalamus, cerebellum, and cerebral cortex, with highest expression in the hippocampus. Expression is also detected in the spinal cord. Cadherins can act as axon guidance and cell adhesion proteins, specifically during development and in the response to injury (ref 2). Manipulation of levels of this protein may be of use in inducing a compensatory synaptogenic response to neuronal death in Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar ataxia, progressive supranuclear palsy, ALS, head trauma, stroke, or any other disease/condition associated with neuronal loss.

[0844] Reference:

[0845] 1. Potter E., Bergwitz C., Brabant G. (1999) The cadherin-catenin system: implications for growth and differentiation of endocrine tissues. Endocr. Rev. 20: 207-239.

[0846] 2. Ranscht B. (2000) Cadherins: molecular codes for axon guidance and synapse formation. Int. J. Dev. Neurosci. 18: 643-651.

[0847] Panel 4D Summary: Ag1311 Expression of this gene is primarily in endothelial cells and in fibroblasts. However, this gene is also expressed in the kidney, thymus, lung and colon. The expression of this gene is high in normal tissue and untreated cells and is not affected by most treatments with the exception of IL-1 alpha and TNFbeta, which reduce expression of this gene by half in treated HUVECs and reduce expression 10-fold in gamma interferon treated HUVECs. Therefore, the protein encoded for by this gene may be important in normal function of endothelium and fibroblasts. Protein therapeutics designed with the protein encoded for by this transcript could reduce or block inflammation in diseases such as asthma, emphysema, allergy, arthritis, IBD and psoriasis.

[0848] Panel 4.1D Summary: Ag6709 Expression of this gene is low/undetectable in all samples on this panel (CTs>35).

[0849] general oncology screening panel_v—2.4 Summary: Ag1311 Highest expression of this gene is seen in a sample from metastatic melanoma (CT=27). Moderate to high levels of expression are also seen samples from colon, kidney, bladder, and prostate cancers. In addition, higher levels of expression are seen in prostate, lung, and kidney cancers when compared to expression in normal adjacent tissue. This gene encodes a putative cadherin, similar to VE cadherin that shows specific expression in mesenchymal cells, fibroblasts and endothelial cells. On Panel 4 this gene shows expression in fibroblasts and endothelial cells and is induced by starvation in Huvec. Activated fibroblasts have shown to be involved in supporting tumor cells (Okada, Lab Invest 2000 November;80(11): 1617-28). Corada et al (Blood Mar 15, 2001;97(6):1679-84) has shown that there are epitopes in VE Cadherin that are only exposed upon activation of the endothelial cells, probably due to changes in cell-cell adhesions. mAbs against those epitopes have antitumor activities without inducing bleeding. Therefore, based on the expression of this gene in fibroblasts and tumors, and the homology of the protein product to cadherin, targeting of this gene product with a human monoclonal antibody that results in an inhibition of the activity of this protein, preferably as it relates to endothelial and fibroblast activation by tumor cells, may have therapeutic effect on all solid tumors that depend on angiogenesis, and specifically on colon, lung, kidney, melanoma, prostate and bladder. Results from a second experiment with the same probe and primer set, run 263102793, are not included because the amp plot indicates there were experimental difficulties with this run.

[0850] T. NOV20a (CG132888-02): M130 Antigen.

[0851] Expression of gene CG132888-02 was assessed using the primer-probe set Ag4955, described in Table TA. Results of the RTQ-PCR runs are shown in Tables TB, TC and TD.

TABLE TA
Probe Name Ag4955
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gaggagacctggatcacatgt-3′	21	2841	289
Probe	TET-5′-aagacttcaggaaggacccacttcct-3′-	26	2873	290
	TAMRA
Reverse	5′-agatctccacacgtccagaac-3′	21	2899	291

[0852]

TABLE TB
General_screening_panel_v1.5
                                 Rel. Exp. (%)
                                 Ag4955, Run
Tissue Name                      228886961
Adipose                          27.7
Melanoma* Hs688(A).T             0.2
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.1
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    0.2
Testis Pool                      6.5
Prostate ca.* (bone met) PC-3    0.0
Prostate Pool                    2.4
Placenta                         8.2
Uterus Pool                      6.8
Ovarian ca. OVCAR-3              0.0
Ovarian ca. SK-OV-3              0.0
Ovarian ca. OVCAR-4              0.0
Ovarian ca. OVCAR-5              0.0
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.0
Ovary                            11.2
Breast ca. MCF-7                 0.0
Breast ca. MDA-MB-231            0.0
Breast ca. BT 549                0.4
Breast ca. T47D                  0.0
Breast ca. MDA-N                 0.0
Breast Pool                      5.6
Trachea                          5.1
Lung                             1.0
Fetal Lung                       5.0
Lung ca. NCI-N417                0.0
Lung ca. LX-1                    0.0
Lung ca. NCI-H146                0.0
Lung ca. SHP-77                  0.0
Lung ca. A549                    0.0
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 0.0
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  0.0
Lung ca. NCI-H522                0.0
Liver                            9.0
Fetal Liver                      29.5
Liver ca. HepG2                  0.0
Kidney Pool                      15.8
Fetal Kidney                     2.1
Renal ca. 786-0                  0.0
Renal ca. A498                   0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.0
Renal ca. TK-10                  0.0
Bladder                          100.0
Gastric ca. (liver met.) NCI-N87 1.8
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  0.0
Colon ca.* (SW480 met) SW620     0.0
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.0
Colon ca. CaCo-2                 0.1
Colon cancer tissue              38.4
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.0
Colon Pool                       10.0
Small Intestine Pool             5.3
Stomach Pool                     18.3
Bone Marrow Pool                 4.1
Fetal Heart                      0.9
Heart Pool                       3.3
Lymph Node Pool                  5.1
Fetal Skeletal Muscle            2.3
Skeletal Muscle Pool             11.7
Spleen Pool                      28.1
Thymus Pool                      14.2
CNS cancer (glio/astro) U87-MG   0.1
CNS cancer (glio/astro) U-118-MG 0.1
CNS cancer (neuro; met) SK-N-AS  0.0
CNS cancer (astro) SF-539        0.0
CNS cancer (astro) SNB-75        0.0
CNS cancer (glio) SNB-19         0.0
CNS cancer (glio) SF-295         0.1
Brain (Amygdala) Pool            0.5
Brain (cerebellum)               1.2
Brain (fetal)                    2.4
Brain (Hippocampus) Pool         1.3
Cerebral Cortex Pool             1.2
Brain (Substantia nigra) Pool    0.3
Brain (Thalamus) Pool            0.6
Brain (whole)                    4.6
Spinal Cord Pool                 4.4
Adrenal Gland                    41.2
Pituitary gland Pool             0.7
Salivary Gland                   1.0
Thyroid (female)                 3.0
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    10.4

[0853]

TABLE TC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4955, Run
Tissue Name                      223629644
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.1
Primary Th1 rest                 0.0
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        0.0
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.3
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              0.2
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   12.2
LAK cells IL-2                   0.1
LAK cells IL-2 + IL-12           0.2
LAK cells 1L-2 + IFN gamma       0.1
LAK cells IL-2 + IL-18           0.3
LAK cells PMA/ionomycin          14.6
NK Cells IL-2 rest               0.0
Two Way MLR 3 day                10.6
Two Way MLR 5 day                4.6
Two Way MLR 7 day                0.6
PBMC rest                        10.0
PBMC PWM                         0.8
PBMC-PHA-L                       7.8
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.0
EOL-1 dbcAMP                     0.2
EOL-1 dbcAMP PMA/ionomycin       1.5
Dendritic cells none             36.3
Dendritic cells LPS              1.9
Dendritic cells anti-CD40        20.3
Monocytes rest                   60.7
Monocytes LPS                    100.0
Macrophages rest                 59.5
Macrophages LPS                  10.2
HUVEC none                       0.0
HUVEC starved                    0.0
HUVEC IL-1beta                   0.0
HUVEC IFN gamma                  0.0
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.2
Lung Microvascular EC none       0.0
Lung Microvascular EC TNFalpha + 0.0
IL-1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  0.0
IL1beta
Small airway epithelium none     0.0
Small airway epithelium TNFalpha + 0.0
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha + IL- 0.0
1beta
Astrocytes rest                  0.0
Astrocytes TNFalpha + IL-1beta   0.0
KU-812 (Basophil) rest           0.1
KU-812 (Basophil) PMA/ionomycin  0.1
CCD1106 (Keratinocytes) none     0.1
CCD1106 (Keratinocytes) TNFalpha + 0.0
IL-1beta
Liver cirrhosis                  12.5
NCI-H292 none                    0.0
NCI-H292 IL-4                    0.0
NCI-H292 IL-9                    0.0
NCI-H292 IL-13                   0.0
NCI-H292 IFN gamma               0.0
HPAEC none                       0.0
HPAEC TNF alpha + IL-1 beta      0.0
Lung fibroblast none             0.0
Lung fibroblast TNF alpha + IL-1 0.2
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.0
Lung fibroblast IL-13            0.5
Lung fibroblast IFN gamma        0.1
Dermal fibroblast CCD1070 rest   0.0
Dermal fibroblast CCD1070 TNF alpha 0.0
Dermal fibroblast CCD1070 IL-1 beta 0.1
Dermal fibroblast IFN gamma      0.2
Dermal fibroblast IL-4           0.2
Dermal Fibroblasts rest          0.5
Neutrophils TNFa + LPS           0.4
Neutrophils rest                 0.2
Colon                            3.7
Lung                             55.1
Thymus                           11.3
Kidney                           2.6

[0854]

TABLE TD
Panel 5 Islet
                                 Rel. Exp. (%)
                                 Ag4955, Run
Tissue Name                      263594804
97457_Patient-02go_adipose       1.1
97476_Patient-07sk_skeletal muscle 4.8
97477_Patient-07ut_uterus        9.3
97478_Patient-07pl_placenta      42.6
99167_Bayer Patient 1            0.0
97482_Patient-08ut_uterus        63.7
97483_Patient-08pl_placenta      2.3
97486_Patient-09sk_skeletal muscle 0.7
97487_Patient-09ut_uterus        7.1
97488_Patient-09pl_placenta      33.7
97492_Patient-10ut_uterus        29.3
97493_Patient-10pl_placenta      100.0
97495_Patient-11go_adipose       0.1
97496_Patient-11sk_skeletal muscle 1.1
97497_Patient-11ut_uterus        12.2
97498_Patient-11pl_placenta      12.1
97500_Patient-12go_adipose       84.1
97501_Patient-12sk_skeletal muscle 24.1
97502_Patient-12ut_uterus        1.0
97503_Patient-12pl_placenta      1.8
94721_Donor 2 U - A_Mesenchymal Stem 0.0
Cells
94722_Donor 2 U - B Mesenchymal Stem 0.0
Cells
94723_Donor 2 U - C_Mesenchymal Stem 0.1
Cells
94709_Donor 2 AM - A_adipose     0.9
94710_Donor 2 AM - B_adipose     0.0
94711_Donor 2 AM - C_adipose     0.0
94712_Donor 2 AD - A_adipose     0.0
94713_Donor 2 AD - B_adipose     0.0
94714_Donor 2 AD - C_adipose     0.3
94742_Donor 3 U - A_Mesenchymal  0.0
Stem Cells
94743_Donor 3 U - B_Mesenchymal  0.0
Stem Cells
94730_Donor 3 AM - A_adipose     0.0
94731_Donor 3 AM - B_adipose     0.0
94732_Donor 3 AM - C_adipose     0.0
94733_Donor 3 AD - A_adipose     0.0
94734_Donor 3 AD - B_adipose     0.0
94735_Donor 3 AD - C_adipose     1.0
77138_Liver_HepG2untreated       0.0
73556_Heart Cardiac stromal cells 0.0
(primary)
81735_Small Intestine            24.5
72409_Kidney_Proximal Convoluted 0.0
Tubule
82685_Small intestine_Duodenum   51.1
90650_Adrenal_Adrenocortical     3.8
adenoma
72410_Kidney_HRCE                0.0
72411_Kidney_HRE                 0.0
73139_Uterus_Uterine smooth      0.0
muscle cells

[0855] General_screening_panel_v1.5 Summary: Ag4955 Highest expression of this gene is detected in bladder (CT=26.8). Therefore, expression of this gene may be useful in distinguishing bladder from other samples used in this panel. In addition, therapeutic modulation of this gene may be useful in the treatment of bladder related diseases. 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, 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.

[0856] In addition, this gene is expressed at moderate to low 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.

[0857] Panel 4.1D Summary: Ag4955 Highest expression of this gene is detected in LPS treated monocytes (CT=28.3). In addition, moderate to low levels of expression of this gene is also seen in LAK cells, two way MLRs, PBMC, dendritic cells, activated eosinophils and normal tissues represented by colon, lung, thymus and kidney. This gene encodes splice variant of M130 antigen (CD163) precursor. CD163 is a macrophage-associated antigen belonging to the scavenger receptor cysteine rich (SRCR) domain family and it scavenges haemoglobin by mediating endocytosis of haptoglobin-haemoglobin complexes (Kristiansen, 2001, Nature 409(6817):198-201, PMID: 11196644). CD163 is expressed exclusively on human monocytes and macrophages and it is significantly upregulated by glucocorticoids and IL-10. The highly purified CD163 protein is shown to inhibit phorbol ester-induced human T-lymphocyte activation, thus attenuating the immune response to the inflammatory mediator (Hogger P, Sorg C., 2001, Biochem Biophys Res Commun Nov. 9, 2001;288(4):841-3, PMID: 11688984). Furthermore, macrophages expressing the scavenger receptor CD163 are shown to be increased in synovium and in colonic mucosa in patients with spondyloarthropathy (SpA). Therefore, therapeutic modulation of the CD163 encoded by this gene may be useful in the treatment of asthma, emphysema, inflammatory bowel disease, arthritis, psoriasis and SpA.

[0858] Moderate levels of expression of this gene is also seen in liver cirrhosis sample. Therefore, therapeutic modulation of this gene may be beneficial in the treatment of liver cirrhosis.

[0859] Panel 5 Islet Summary: Ag4955 Highest expression of this gene is detected in placenta (CT=30.2). In addition, moderate to low levels of expression of this gene is also seen in uterus, skeletal muscle, adipose and small intestine. Please see panel 1.5 for the discussion on utility of this gene.

[0860] U. NOV22a (CGI33508-01): Synaptotagmin VI.

[0861] Expression of gene CG133508-01 was assessed using the primer-probe set Ag4837, described in Table UA. Results of the RTQ-PCR runs are shown in Tables UB, UC and UD.

TABLE UA
Probe Name Ag4837
				SEQ ID
Primers	Sequences	Length	Start Position	No
Forward	5′-ggagagatcatgttctcccttt-3′	22	1147	292
Probe	TET-5′-caggcaggctcaccctcacagtg-3′-	23	1184	293
	TAMRA
Reverse	5′-ccttgaggttccgacacttaat-3′	22	1207	294

[0862]

TABLE UB
CNS_neurodegeneration_v1.0
                               Rel. Exp. (%)
                               Ag4837, Run
Tissue Name                    249271251
AD 1 Hippo                     4.4
AD 2 Hippo                     10.1
AD 3 Hippo                     1.8
AD 4 Hippo                     4.7
AD 5 Hippo                     100.0
AD 6 Hippo                     17.8
Control 2 Hippo                9.2
Control 4 Hippo                3.8
Control (Path) 3 Hippo         1.4
AD 1 Temporal Ctx              7.0
AD 2 Temporal Ctx              5.8
AD 3 Temporal Ctx              2.7
AD 4 Temporal Ctx              3.6
AD 5 Inf Temporal Ctx          17.3
AD 5 Sup Temporal Ctx          17.7
AD 6 Inf Temporal Ctx          7.0
AD 6 Sup Temporal Ctx          9.3
Control 1 Temporal Ctx         0.6
Control 2 Temporal Ctx         7.4
Control 3 Temporal Ctx         3.1
Control 3 Temporal Ctx         1.1
Control (Path) 1 Temporal Ctx  8.4
Control (Path) 2 Temporal Ctx  4.5
Control (Path) 3 Temporal Ctx  0.8
Control (Path) 4 Temporal Ctx  2.6
AD 1 Occipital Ctx             16.6
AD 2 Occipital Ctx (Missing)   0.0
AD 3 Occipital Ctx             0.7
AD 4 Occipital Ctx             2.6
AD 5 Occipital Ctx             26.1
AD 6 Occipital Ctx             26.6
Control 1 Occipital Ctx        1.3
Control 2 Occipital Ctx        82.4
Control 3 Occipital Ctx        19.1
Control 4 Occipital Ctx        0.9
Control (Path) 1 Occipital Ctx 34.9
Control (Path) 2 Occipital Ctx 6.0
Control (Path) 3 Occipital Ctx 0.5
Control (Path) 4 Occipital Ctx 28.9
Control 1 Parietal Ctx         1.0
Control 2 Parietal Ctx         6.2
Control 3 Parietal Ctx         5.1
Control (Path) 1 Parietal Ctx  11.9
Control (Path) 2 Parietal Ctx  4.5
Control (Path) 3 Parietal Ctx  0.8
Control (Path) 4 Parietal Ctx  10.9

[0863]

TABLE UC
General_screening_panel_v1.5
                                 Rel. Exp. (%)
                                 Ag4837, Run
Tissue Name                      228787809
Adipose                          0.2
Melanoma* Hs688(A).T             0.0
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    0.8
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.1
Squamous cell carcinoma SCC-4    0.0
Testis Pool                      2.9
Prostate ca.* (bone met) PC-3    0.0
Prostate Pool                    1.5
Placenta                         0.6
Uterus Pool                      0.0
Ovarian ca. OVCAR-3              0.0
Ovarian ca. SK-OV-3              0.0
Ovarian ca. OVCAR-4              0.0
Ovarian ca. OVCAR-5              0.0
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.4
Ovary                            9.0
Breast ca. MCF-7                 0.0
Breast ca. MDA-MB-231            0.0
Breast ca. BT 549                0.0
Breast ca. T47D                  0.0
Breast ca. MDA-N                 0.0
Breast Pool                      0.5
Trachea                          0.8
Lung                             2.9
Fetal Lung                       5.5
Lung ca. NCI-N417                2.4
Lung ca. LX-1                    0.0
Lung ca. NCI-H146                0.0
Lung ca. SHP-77                  0.0
Lung ca. A549                    1.4
Lung ca. NCI-H526                51.1
Lung ca. NCI-H23                 0.3
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  0.0
Lung ca. NCI-H522                0.0
Liver                            0.0
Fetal Liver                      0.6
Liver ca. HepG2                  0.0
Kidney Pool                      0.4
Fetal Kidney                     5.6
Renal ca. 786-0                  0.0
Renal ca. A498                   0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.0
Renal ca. TK-10                  0.0
Bladder                          5.1
Gastric ca. (liver met.) NCI-N87 0.0
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  0.4
Colon ca.* (SW480 met) SW620     0.0
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.0
Colon ca. CaCo-2                 1.0
Colon cancer tissue              0.1
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.0
Colon Pool                       0.4
Small Intestine Pool             0.3
Stomach Pool                     0.7
Bone Marrow Pool                 0.3
Fetal Heart                      0.1
Heart Pool                       0.0
Lymph Node Pool                  0.2
Fetal Skeletal Muscle            3.3
Skeletal Muscle Pool             3.6
Spleen Pool                      0.4
Thymus Pool                      0.5
CNS cancer (glio/astro) U87-MG   0.4
CNS cancer (glio/astro) U-118-MG 0.0
CNS cancer (neuro; met) SK-N-AS  0.0
CNS cancer (astro) SF-539        0.0
CNS cancer (astro) SNB-75        0.0
CNS cancer (glio) SNB-19         0.0
CNS cancer (glio) SF-295         0.0
Brain (Amygdala) Pool            10.2
Brain (cerebellum)               6.2
Brain (fetal)                    100.0
Brain (Hippocampus) Pool         12.6
Cerebral Cortex Pool             12.1
Brain (Substantia nigra) Pool    14.2
Brain (Thalamus) Pool            15.0
Brain (whole)                    22.5
Spinal Cord Pool                 13.0
Adrenal Gland                    0.8
Pituitary gland Pool             0.4
Salivary Gland                   0.4
Thyroid (female)                 0.0
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    1.2

[0864]

TABLE UD
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4837, Run
Tissue Name                      223335536
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.6
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.0
Primary Th2 rest                 0.0
Primary Tr1 rest                 1.1
CD45RA CD4 lymphocyte act        0.0
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.5
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              0.0
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.4
LAK cells rest                   0.0
LAK cells IL-2                   0.0
LAK cells IL-2 + IL-12           0.5
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.0
LAK cells PMA/ionomycin          8.2
NK Cells IL-2 rest               0.0
Two Way MLR 3 day                0.0
Two Way MLR 5 day                0.8
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.0
PBMC PHA-L                       0.0
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.0
B lymphocytes CD40L and IL-4     0.0
EOL-1 dbcAMP                     0.0
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             3.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.7
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.4
Macrophages LPS                  0.0
HUVEC none                       0.0
HUVEC starved                    0.0
HUVEC IL-1beta                   0.0
HUVEC IFN gamma                  0.0
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.0
Lung Microvascular EC none       0.0
Lung Microvascular EC TNFalpha + 0.0
IL-1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  0.0
IL1beta
Small airway epithelium none     0.0
Small airway epithelium TNFalpha + 0.0
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha + IL- 0.0
1beta
Astrocytes rest                  1.6
Astrocytes TNFalpha + IL-1beta   0.0
KU-812 (Basophil) rest           0.0
KU-812 (Basophil) PMA/ionomycin  0.0
CCD1106 (Keratinocytes) none     1.6
CCD1106 (Keratinocytes) TNFalpha + 0.0
IL-1beta
Liver cirrhosis                  0.0
NCI-H292 none                    0.0
NCI-H292 IL-4                    0.0
NCI-H292 IL-9                    0.0
NCI-H292 IL-13                   0.0
NCI-H292 IFN gamma               0.0
HPAEC none                       0.0
HPAEC TNF alpha + IL-1 beta      0.0
Lung fibroblast none             0.0
Lung fibroblast TNF alpha + IL-1 0.0
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.0
Lung fibroblast IL-13            0.5
Lung fibroblast IFN gamma        0.0
Dermal fibroblast CCD1070 rest   0.0
Dermal fibroblast CCD1070 TNF alpha 0.0
Dermal fibroblast CCD1070 IL-1 beta 0.0
Dermal fibroblast IFN gamma      0.4
Dermal fibroblast IL-4           0.0
Dermal Fibroblasts rest          1.9
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 1.1
Colon                            6.0
Lung                             4.3
Thymus                           14.1
Kidney                           100.0

[0865] CNS_neurodegeneration_v1.0 Summary: Ag4837 Expression of this gene is ubiquitous throughout the samples in this panel, with highest expression in the hippocampus of a patient with Alzheimer's disease (CT=28). While no association between the expression of this gene and the presence of Alzheimer's disease is detected in this panel, these results confirm the expression of this gene in areas that degenerate in Alzheimer's disease, including the cortex, hippocampus, amygdala and thalamus. Synaptotagmin expression is altered in the brain of Alzheimer's patients, possibly explaining impaired synaptogenesis and/or synaptosomal loss secondary to neuronal loss observed in the neurodegenerative disorder. It may also represent, reflect or account for the impaired neuronal transmission in Alzheimer's disease (AD), caused by deterioration of the exocytic machinery. Since this gene is a homolog of synaptotagmin, agents that potentiate the expression or function of the protein encoded by this gene may be useful in the treatment of Alzheimer's disease.

[0866] References:

[0867] Sze C I, Bi H, Kleinschmidt-DeMasters B K, Filley C M, Martin L J. (2000) J Neurol Sci. 175:81-90.

[0868] Masliah F, Mallory M, Alford M, DeTeresa R, Hansen L A, McKeel D W Jr, Morris J C. (2001)Neurology 56:127-9.

[0869] Yoo B C, Cairns N, Fountoulakis M, Lubec G. (2001) Dement Geriatr Cogn Disord. 12:219-25.

[0870] General_screening_panel_v1.5 Summary: Ag4837 This gene encodes a homolog of synaptotagmin which appears to be almost exclusively expressed in the brain. This experiment shows moderate to high expression across all brain regions with highest expression in the fetal brain (CT=28.3). Synaptotagmin is a presynaptic protein involved in synaptic vesicle release, making this an ideal drug target for diseases such as epilepsy, in which reduction of neurotransmission is beneficial. Selective inhibition of this gene or its protein product may therefore be useful in the treatment of seizure disorders. Furthermore, selective inhibition of neural transmission through antagonism of the protein encoded by this gene may show therapeutic benefit in psychiatric diseases where it is believed that inappropriate neural connections have been established, such as schizophrenia and bipolar disorder. In addition, antibodies against synaptotagmin may cause Lambert-Eaton myasthenic syndrome. Therefore, peptide fragments of the protein encoded by this gene may serve to block the action of these antibodies and treat Lambert-Eaton myasthenic syndrome.

[0871] References:

[0872] Takamori M, Komai K, Iwasa K. (2000) Am J Med Sci. 319:204-8.

[0873] Sokolov B P, Tcherepanov A A, Haroutunian V, Davis K L. (2000) Biol Psychiatry. 48:184-96.

[0874] Panel 4.1D Summary: Ag4837 This gene is expressed at detectable levels in the kidney (CT=29.8). Thus, 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.

[0875] V. NOV23a and NOV23b (CG133548-01 and CG133548-02): 1300003P13RIK Protein Homolog (TmMP)

[0876] Expression of gene CG133548-01 and CG133548-02 was assessed using the primer-probe set Ag4839, described in Table VA. Results of the RTQ-PCR runs are shown in Tables VB and VC.

TABLE VA
Probe Name Ag4839
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-ttccaatgttctttggttttgt-3′	22	1216	295
Probe	TET-5′-tctgctgctcttatggccaggtttct-3′-	26	1250	296
	TAMRA
Reverse	5′-gaaactcgaagtcctcaaatcc-3′	22	1293	297

[0877]

TABLE VB
General_screening_panel_v1.5
                                 Rel. Exp. (%)
                                 Ag4839, Run
Tissue Name                      228787839
Adipose                          3.3
Melanoma* Hs688(A).T             21.8
Melanoma* Hs688(B).T             26.2
Melanoma* M14                    13.9
Melanoma* LOXIMVI                9.0
Melanoma* SK-MEL-5               44.4
Squamous cell carcinoma SCC-4    6.8
Testis Pool                      5.6
Prostate ca.* (bone met) PC-3    8.1
Prostate Pool                    8.8
Placenta                         3.0
Uterus Pool                      4.5
Ovarian ca. OVCAR-3              100.0
Ovarian ca. SK-OV-3              34.2
Ovarian ca. OVCAR-4              14.3
Ovarian ca. OVCAR-5              46.7
Ovarian ca. IGROV-1              14.6
Ovarian ca. OVCAR-8              9.2
Ovary                            8.6
Breast ca. MCF-7                 21.5
Breast ca. MDA-MB-231            25.2
Breast ca. BT 549                10.5
Breast ca. T47D                  4.7
Breast ca. MDA-N                 16.3
Breast Pool                      7.6
Trachea                          10.5
Lung                             4.4
Fetal Lung                       18.7
Lung ca. NCI-N417                1.9
Lung ca. LX-1                    20.3
Lung ca. NCI-H146                4.5
Lung ca. SHP-77                  14.8
Lung ca. A549                    27.4
Lung ca. NCI-H526                2.6
Lung ca. NCI-H23                 33.2
Lung ca. NCI-H460                19.2
Lung ca. HOP-62                  12.0
Lung ca. NCI-H522                18.3
Liver                            0.8
Fetal Liver                      16.3
Liver ca. HepG2                  29.1
Kidney Pool                      0.0
Fetal Kidney                     12.6
Renal ca. 786-0                  27.0
Renal ca. A498                   5.6
Renal ca. ACHN                   49.7
Renal ca. UO-31                  33.9
Renal ca. TK-10                  32.3
Bladder                          20.6
Gastric ca. (liver met.) NCI-N87 33.7
Gastric ca. KATO III             17.6
Colon ca. SW-948                 5.1
Colon ca. SW480                  39.2
Colon ca.* (SW480 met) SW620     14.9
Colon ca. HT29                   6.5
Colon ca. HCT-116                5.5
Colon ca. CaCo-2                 39.2
Colon cancer tissue              20.0
Colon ca. SW1116                 1.4
Colon ca. Colo-205               2.5
Colon ca. SW-48                  4.9
Colon Pool                       5.5
Small Intestine Pool             8.3
Stomach Pool                     7.5
Bone Marrow Pool                 3.5
Fetal Heart                      4.7
Heart Pool                       3.8
Lymph Node Pool                  10.0
Fetal Skeletal Muscle            3.6
Skeletal Muscle Pool             16.4
Spleen Pool                      7.2
Thymus Pool                      5.6
CNS cancer (glio/astro) U87-MG   21.6
CNS cancer (glio/astro) U-118-MG 25.2
CNS cancer (neuro; met) SK-N-AS  12.2
CNS cancer (astro) SF-539        8.5
CNS cancer (astro) SNB-75        17.6
CNS cancer (glio) SNB-19         15.4
CNS cancer (glio) SF-295         37.4
Brain (Amygdala) Pool            3.4
Brain (cerebellum)               13.5
Brain (fetal)                    7.9
Brain (Hippocampus) Pool         3.7
Cerebral Cortex Pool             3.4
Brain (Substantia nigra) Pool    2.6
Brain (Thalamus) Pool            5.1
Brain (whole)                    2.7
Spinal Cord Pool                 3.4
Adrenal Gland                    21.8
Pituitary gland Pool             2.1
Salivary Gland                   5.7
Thyroid (female)                 5.9
Pancreatic ca. CAPAN2            17.7
Pancreas Pool                    12.2

[0878]

TABLE VC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4839, Run
Tissue Name                      223335453
Secondary Th1 act                54.0
Secondary Th2 act                56.6
Secondary Tr1 act                23.0
Secondary Th1 rest               11.7
Secondary Th2 rest               12.9
Secondary Tr1 rest               18.4
Primary Th1 act                  32.3
Primary Th2 act                  37.1
Primary Tr1 act                  40.9
Primary Th1 rest                 13.3
Primary Th2 rest                 13.5
Primary Tr1 rest                 24.8
CD45RA CD4 lymphocyte act        54.7
CD45RO CD4 lymphocyte act        34.9
CD8 lymphocyte act               34.2
Secondary CD8 lymphocyte rest    26.8
Secondary CD8 lymphocyte act     20.4
CD4 lymphocyte none              8.1
2ry Th1/Th2/Tr1_anti-CD95 CH11   26.1
LAK cells rest                   48.3
LAK cells IL-2                   27.2
LAK cells IL-2 + IL-12           30.8
LAK cells IL-2 + IFN gamma       27.4
LAK cells IL-2 + IL-18           42.6
LAK cells PMA/ionomycin          43.8
NK Cells IL-2 rest               36.6
Two Way MLR 3 day                36.6
Two Way MLR 5 day                29.7
Two Way MLR 7 day                31.0
PBMC rest                        7.3
PBMC PWM                         27.4
PBMC PHA-L                       29.1
Ramos (B cell) none              50.3
Ramos (B cell) ionomycin         53.2
B lymphocytes PWM                27.5
B lymphocytes CD40L and IL-4     33.0
EOL-1 dbcAMP                     33.7
EOL-1 dbcAMP PMA/ionomycin       50.3
Dendritic cells none             64.6
Dendritic cells LPS              55.1
Dendritic cells anti-CD40        49.0
Monocytes rest                   29.7
Monocytes LPS                    76.8
Macrophages rest                 60.3
Macrophages LPS                  44.8
HUVEC none                       30.1
HUVEC starved                    47.6
HUVEC IL-1beta                   55.1
HUVEC IFN gamma                  45.7
HUVEC TNF alpha + IFN gamma      33.4
HUVEC TNF alpha + IL4            44.4
HUVEC IL-11                      22.1
Lung Microvascular EC none       100.0
Lung Microvascular EC TNFalpha + 85.9
IL-1beta
Microvascular Dermal EC none     53.6
Microsvasular Dermal EC          41.2
TNFalpha + IL-1beta
Bronchial epithelium TNFalpha +  59.0
IL1beta
Small airway epithelium none     32.8
Small airway epithelium          60.7
TNFalpha + IL-1beta
Coronery artery SMC rest         37.1
Coronery artery SMC TNFalpha +   25.5
IL-1beta
Astrocytes rest                  51.4
Astrocytes TNFalpha + IL-1beta   61.1
KU-8l2 (Basophil) rest           12.2
KU-812 (Basophil) PMA/ionomycin  33.2
CCD1106 (Keratinocytes) none     53.2
CCD1106 (Keratinocytes)          37.4
TNFalpha + IL-1beta
Liver cirrhosis                  14.6
NCI-H292 none                    40.6
NCI-H292 IL-4                    69.3
NCI-H292 IL-9                    75.8
NCI-H292 IL-13                   56.3
NCI-H292 IFN gamma               55.1
HPAEC none                       28.3
HPAEC TNF alpha + IL-1 beta      61.1
Lung fibroblast none             62.0
Lung fibroblast TNF alpha +      56.6
IL-1 beta
Lung fibroblast IL-4             82.4
Lung fibroblast IL-9             95.9
Lung fibroblast IL-13            62.9
Lung fibroblast IFN gamma        0.0
Dermal fibroblast CCD1070 rest   80.7
Dermal fibroblast CCD1070 TNF    81.8
alpha
Dermal fibroblast CCD 1070 IL-1  42.6
beta
Dermal fibroblast IFN gamma      51.8
Dermal fibroblast IL-4           96.6
Dermal Fibroblasts rest          58.2
Neutrophils TNFa + LPS           8.1
Neutrophils rest                 16.8
Colon                            32.1
Lung                             22.5
Thymus                           55.1
Kidney                           64.6

[0879] General_screening_panel_v1.5 Summary: Ag4839 Highest expression of the CG133548-01 gene is detected in ovarian cancer OVCAR-3 cell line (CT=24.8). High to moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, 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 gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0880] 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, 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.

[0881] In addition, this gene is expressed at high to 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.

[0882] Interestingly, this gene is expressed at much higher levels in fetal (CT=27.8) when compared to adult kidney (CT=40). This observation suggests that expression of this gene can be used to distinguish fetal from adult kidney. In addition, the relative overexpression of this gene in fetal kidney suggests that the protein product may enhance kidney 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 kidney related diseases.

[0883] Panel 4.1D Summary: Ag4839 Highest expression of the CG133548-01 gene is detected in lung microvascular EC (CT=27.4). 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_v1.5 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.

[0884] W. NOV24a and NOV24b (CG133569-01 and CG133569-02): Type I Membrane Protein with SH3 Domain

[0885] Expression of gene CG133569-01 and CG133569-02 was assessed using the primer-probe set Ag4843, described in Table WA. Results of the RTQ-PCR runs are shown in Tables WB and WC.

TABLE WA
Probe Name Ag4843
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-gagcaatggaagagatgcaa-3′	20	3170	298
Probe	TET-5′-ccactgcatgaagataatttctcacga-3′-	27	3190	299
	TAMRA
Reverse	5′-cttcaggaacctgcacattaag-3′	22	3232	300

[0886]

TABLE WB
General_screening_panel_v1.5
                                 Rel. Exp. (%)
                                 Ag4843, Run
Tissue Name                      228796268
Adipose                          18.7
Melanoma* Hs688(A).T             36.9
Melanoma* Hs688(B).T             42.0
Melanoma* M14                    17.2
Melanoma* LOXIMVI                10.5
Melanoma* SK-MEL-5               25.0
Squamous cell carcinoma SCC-4    16.4
Testis Pool                      22.7
Prostate ca.* (bone met) PC-3    80.7
Prostate Pool                    44.1
Placenta                         2.8
Uterus Pool                      29.5
Ovarian ca. OVCAR-3              18.4
Ovarian ca. SK-OV-3              16.5
Ovarian ca. OVCAR-4              2.1
Ovarian ca. OVCAR-5              27.9
Ovarian ca. IGROV-1              17.0
Ovarian ca. OVCAR-8              10.4
Ovary                            12.3
Breast ca. MCF-7                 25.0
Breast ca. MDA-MB-231            35.1
Breast ca. BT 549                63.3
Breast ca. T47D                  14.8
Breast ca. MDA-N                 6.0
Breast Pool                      27.7
Trachea                          18.8
Lung                             7.6
Fetal Lung                       32.1
Lung ca. NCI-N417                4.5
Lung ca. LX-1                    21.3
Lung ca. NCI-H146                8.8
Lung ca. SHP-77                  46.0
Lung ca. A549                    21.3
Lung ca. NCI-H526                1.9
Lung ca. NCI-H23                 25.3
Lung ca. NCI-H460                31.9
Lung ca. HOP-62                  15.8
Lung ca. NCI-H522                31.6
Liver                            2.9
Fetal Liver                      25.9
Liver ca. HepG2                  13.7
Kidney Pool                      41.2
Fetal Kidney                     17.4
Renal ca. 786-0                  23.8
Renal ca. A498                   11.7
Renal ca. ACHN                   11.7
Renal ca. UO-31                  12.5
Renal ca. TK-10                  34.2
Bladder                          32.8
Gastric ca. (liver met.) NCI-N87 28.5
Gastric ca. KATO III             45.7
Colon ca. SW-948                 5.9
Colon ca. SW480                  14.8
Colon ca.* (SW480 met) SW620     18.0
Colon ca. HT29                   18.8
Colon ca. HCT-116                21.6
Colon ca. CaCo-2                 23.3
Colon cancer tissue              11.2
Colon ca. SW1116                 3.1
Colon ca. Colo-205               2.9
Colon ca. SW-48                  2.5
Colon Pool                       26.8
Small Intestine Pool             19.9
Stomach Pool                     15.3
Bone Marrow Pool                 11.8
Fetal Heart                      15.6
Heart Pool                       9.5
Lymph Node Pool                  29.5
Fetal Skeletal Muscle            5.6
Skeletal Muscle Pool             24.3
Spleen Pool                      11.3
Thymus Pool                      18.8
CNS cancer (glio/astro) U87-MG   37.1
CNS cancer (glio/astro) U-118-MG 47.6
CNS cancer (neuro; met) SK-N-AS  47.3
CNS cancer (astro) SF-539        19.1
CNS cancer (astro) SNB-75        100.0
CNS cancer (glio) SNB-19         15.3
CNS cancer (glio) SF-295         92.7
Brain (Amygdala) Pool            l3.4
Brain (cerebellum)               30.8
Brain (fetal)                    19.1
Brain (Hippocampus) Pool         16.5
Cerebral Cortex Pool             21.6
Brain (Substantia nigra) Pool    10.8
Brain (Thalamus) Pool            22.2
Brain (whole)                    9.2
Spinal Cord Pool                 7.7
Adrenal Gland                    8.5
Pituitary gland Pool             8.3
Salivary Gland                   5.6
Thyroid (female)                 5.1
Pancreatic ca. CAPAN2            6.9
Pancreas Pool                    26.1

[0887]

TABLE WC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4843, Run
Tissue Name                      223335454
Secondary Th1 act                31.6
Secondary Th2 act                30.8
Secondary Tr1 act                27.5
Secondary Th1 rest               15.8
Secondary Th2 rest               22.2
Secondary Tr1 rest               23.3
Primary Th1 act                  23.2
Primary Th2 act                  35.4
Primary Tr1 act                  28.9
Primary Th1 rest                 14.4
Primary Th2 rest                 19.6
Primary Tr1 rest                 38.4
CD45RA CD4 lymphocyte act        47.0
CD45RO CD4 lymphocyte act        41.8
CD8 lymphocyte act               49.0
Secondary CD8 lymphocyte rest    27.7
Secondary CD8 lymphocyte act     19.5
CD4 lymphocyte none              32.3
2ry Th1/Th2/Tr1_anti-CD95 CH11   24.8
LAK cells rest                   36.1
LAK cells IL-2                   35.6
LAK cells IL-2 + IL-12           23.0
LAK cells IL-2 + IFN gamma       40.6
LAK cells IL-2 + IL-18           44.8
LAK cells PMA/ionomycin          20.3
NK Cells IL-2 rest               42.3
Two Way MLR 3 day                54.0
Two Way MLR 5 day                25.5
Two Way MLR 7 day                24.5
PBMC rest                        25.7
PBMC PWM                         23.8
PBMC PHA-L                       26.8
Ramos (B cell) none              59.0
Ramos (B cell) ionomycin         52.9
B lymphocytes PWM                37.1
B lymphocytes CD40L and IL-4     32.8
EOL-1 dbcAMP                     34.6
EOL-1 dbcAMP PMA/ionomycin       17.4
Dendritic cells none             28.3
Dendritic cells LPS              20.6
Dendritic cells anti-CD40        37.4
Monocytes rest                   48.3
Monocytes LPS                    44.8
Macrophages rest                 24.5
Macrophages LPS                  10.7
HUVEC none                       35.1
HUVEC starved                    38.2
HUVEC IL-1beta                   50.3
HUVEC IFN gamma                  49.3
HUVEC TNF alpha + IFN gamma      31.0
HUVEC TNF alpha + IL4            46.7
HUVEC IL-11                      36.9
Lung Microvascular EC none       66.0
Lung Microvascular EC TNFalpha + 56.6
IL-1beta
Microvascular Dermal EC none     54.7
Microsvasular Dermal EC TNFalpha + 37.4
IL-1beta
Bronchial epithelium TNFalpha +  48.6
IL1beta
Small airway epithelium none     11.6
Small airway epithelium TNFalpha + 20.0
IL-1beta
Coronery artery SMC rest         42.9
Coronery artery SMC TNFalpha + IL- 46.0
1beta
Astrocytes rest                  28.5
Astrocytes TNFalpha + IL-1beta   13.5
KU-812 (Basophil) rest           49.7
KU-812 (Basophil) PMA/ionomycin  100.0
CCD1106 (Keratinocytes) none     20.7
CCD1106 (Keratinocytes) TNFalpha + 22.2
IL-1beta
Liver cirrhosis                  28.9
NCI-H292 none                    25.7
NCI-H292 IL-4                    39.0
NCI-H292 IL-9                    44.8
NCI-H292 IL-13                   41.5
NCI-H292 IFN gamma               38.4
HPAEC none                       40.6
HPAEC TNF alpha + IL-1 beta      72.2
Lung fibroblast none             88.3
Lung fibroblast TNF alpha + IL-1 88.3
beta
Lung fibroblast IL-4             50.7
Lung fibroblast IL-9             84.1
Lung fibroblast IL-13            47.0
Lung fibroblast IFN gamma        37.9
Dermal fibroblast CCD1070 rest   51.8
Dermal fibroblast CCD1070 TNF alpha 69.7
Dermal fibroblast CCD1070 IL-1 beta 59.9
Dermal fibroblast IFN gamma      42.9
Dermal fibroblast IL-4           75.8
Dermal Fibroblasts rest          66.9
Neutrophils TNFa + LPS           8.1
Neutrophils rest                 23.8
Colon                            22.7
Lung                             38.2
Thymus                           41.8
Kidney                           35.8

[0888] General_screening_panel_v1.5 Summary: Ag4843 Highest expression of the CG133569-01 gene is detected in CNS cancer SNB-75 cell line (CT=26). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, 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, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0889] 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.

[0890] 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.

[0891] Panel 4.1D Summary: Ag4843 Highest expression of the CG133569-01 gene is detected in PMA/ionomycin treated basophils (CT=29). 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 v1.5 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.

[0892] X. NOV26a and NOV26b (CG134100-01 and CG134100-02): Amidase—2 Domain Protein

[0893] Expression of gene CG134100-01 and CG134100-02 was assessed using the primer-probe sets Ag44387, Ag4893 and Ag4894, described in Tables XA, XB and XC. Results of the RTQ-PCR runs are shown in Tables XD, XE, XF and XG.

TABLE XA
Probe Name Ag4387
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-tgtatccacagactgccagact-3′	22	753	301
Probe	TET-5′-tcgtccgaaacatacagtcctttcaca-3′-	27	776	302
	TAMRA
Reverse	5′-atgtcacaaaagttccgtgtgt-3′	22	806	303

[0894]

TABLE XB
Probe Name Ag4893
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-aacatcatcaaacgatctgctt-3′	22	646	304
Probe	TET-5′-cacactgccctaaaatgaacctccca-3′-	26	683	305
	TAMRA
Reverse	5′-tggatgatgatgacatatttgg-3′	22	710	306

[0895]

TABLE XC
Probe Name Ag4894
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-aacatcatcaaacgatctgctt-3′	22	646	307
Probe	TET-5′-cacactgccctaaaatgaacctccca-3′-	26	683	308
	TAMRA
Reverse	5′-tggatgatgatgacatatttgg-3′	22	710	309

[0896]

TABLE XD
General_screening_panel_v1.4
                                 Rel. Exp. (%)
                                 Ag4387, Run
Tissue Name                      222567011
Adipose                          0.5
Melanoma* Hs688(A).T             0.0
Melanoma* Hs688(B).T             0.0
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    4.4
Testis Pool                      1.8
Prostate ca.* (bone met) PC-3    0.0
Prostate Pool                    0.0
Placenta                         0.0
Uterus Pool                      15.9
Ovarian ca. OVCAR-3              2.8
Ovarian ca. SK-OV-3              0.0
Ovarian ca. OVCAR-4              0.0
Ovarian ca. OVCAR-5              0.4
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.0
Ovary                            0.0
Breast ca. MCF-7                 1.1
Breast ca. MDA-MB-231            0.0
Breast ca. BT 549                0.0
Breast ca. T47D                  0.7
Breast ca. MDA-N                 0.0
Breast Pool                      0.0
Trachea                          10.1
Lung                             0.0
Fetal Lung                       0.4
Lung ca. NCI-N417                0.0
Lung ca. LX-1                    0.0
Lung ca. NCI-H146                0.0
Lung ca. SHP-77                  0.0
Lung ca. A549                    1.7
Lung ca. NCI-H526                0.0
Lung ca. NCI-H23                 1.5
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  0.0
Lung ca. NCI-H522                0.0
Liver                            0.0
Fetal Liver                      0.0
Liver ca. HepG2                  0.0
Kidney Pool                      0.7
Fetal Kidney                     0.0
Renal ca. 786-0                  0.5
Renal ca. A498                   0.0
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.0
Renal ca. TK-10                  0.0
Bladder                          7.8
Gastric ca. (liver met.) NCI-N87 4.6
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  0.0
Colon ca* (SW480 met) SW620      0.0
Colon ca. HT29                   0.0
Colon ca. HCT-116                1.2
Colon ca. CaCo-2                 0.0
Colon cancer tissue              0.0
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.0
Colon Pool                       0.0
Small Intestine Pool             0.0
Stomach Pool                     0.0
Bone Marrow Pool                 100.0
Fetal Heart                      0.0
Heart Pool                       0.0
Lymph Node Pool                  0.0
Fetal Skeletal Muscle            0.0
Skeletal Muscle Pool             0.0
Spleen Pool                      0.0
Thymus Pool                      1.3
CNS cancer (glio/astro) U87-MG   0.0
CNS cancer (glio/astro) U-118-MG 0.6
CNS cancer (neuro; met) SK-N-AS  0.0
CNS cancer (astro) SF-539        0.0
CNS cancer (astro) SNB-75        0.0
CNS cancer (glio) SNB-19         0.0
CNS cancer (glio) SF-295         0.0
Brain (Amygdala) Pool            0.5
Brain (cerebellum)               0.0
Brain (fetal)                    0.0
Brain (Hippocampus) Pool         0.0
Cerebral Cortex Pool             0.0
Brain (Substantia nigra) Pool    0.0
Brain (Thalamus) Pool            0.0
Brain (whole)                    0.0
Spinal Cord Pool                 0.0
Adrenal Gland                    0.0
Pituitary gland Pool             0.0
Salivary Gland                   2.4
Thyroid (female)                 0.0
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    0.0

[0897]

TABLE XE
General_screening_panel_v1.5
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag4893, Run	Ag4894, Run
Tissue Name	228829406	228829491
Adipose	0.0	1.0
Melanoma* Hs688(A).T	0.0	0.0
Melanoma* Hs688(B).T	0.0	0.0
Melanoma* M14	0.0	0.0
Melanoma* LOXIMVI	0.0	0.0
Melanoma* SK-MEL-5	0.0	0.0
Squamous cell carcinoma SCC-4	7.6	11.4
Testis Pool	0.0	2.5
Prostate ca.* (bone met) PC-3	0.0	0.0
Prostate Pool	0.0	0.0
Placenta	0.0	1.9
Uterus Pool	43.2	48.6
Ovarian ca. OVCAR-3	3.7	2.8
Ovarian ca. SK-OV-3	0.0	0.0
Ovarian ca. OVCAR-4	0.0	0.0
Ovarian ca. OVCAR-5	0.0	0.8
Ovarian ca. IGROV-1	0.0	0.0
Ovarian ca. OVCAR-8	0.0	0.0
Ovary	0.0	0.5
Breast ca. MCF-7	0.0	0.0
Breast ca. MDA-MB-231	0.0	0.0
Breast ca. BT 549	0.0	0.0
Breast ca. T47D	0.0	0.0
Breast ca. MDA-N	0.0	0.0
Breast Pool	0.0	0.5
Trachea	15.4	14.6
Lung	0.0	0.0
Fetal Lung	3.6	1.1
Lung ca. NCI-N417	0.0	0.0
Lung ca. LX-1	0.0	0.0
Lung ca. NCI-H146	0.0	0.0
Lung ca. SHP-77	0.0	0.0
Lung ca. A549	0.0	0.0
Lung ca. NCI-H526	0.0	0.0
Lung ca. NCI-H23	0.0	0.0
Lung ca. NCI-H460	0.0	0.0
Lung ca. HOP-62	0.0	0.0
Lung ca. NCI-H522	0.0	0.0
Liver	0.0	0.0
Fetal Liver	0.0	0.0
Liver ca. HepG2	0.0	0.0
Kidney Pool	0.0	0.8
Fetal Kidney	0.0	0.0
Renal ca. 786-0	0.0	0.0
Renal ca. A498	0.0	0.0
Renal ca. ACHN	0.0	0.0
Renal ca. UO-31	0.0	0.0
Renal ca. TK-10	0.0	0.0
Bladder	9.2	5.7
Gastric ca. (liver-met.) NCI-N87	7.9	8.0
Gastric ca. KATO III	0.0	0.0
Colon ca. SW-948	0.0	1.7
Colon ca. SW480	0.0	0.0
Colon ca.* (SW480 met) SW620	0.0	0.0
Colon ca. HT29	0.0	0.0
Colon ca. HCT-116	0.0	0.0
Colon ca. CaCo-2	0.0	0.0
Colon cancer tissue	0.0	0.0
Colon ca. SW1116	0.0	0.0
Colon ca. Colo-205	0.0	0.0
Colon ca. SW-48	0.0	0.7
Colon Pool	0.0	0.0
Small Intestine Pool	0.0	0.0
Stomach Pool	0.0	0.0
Bone Marrow Pool	100.0	100.0
Fetal Heart	0.0	0.0
Heart Pool	0.0	0.9
Lymph Node Pool	0.0	0.0
Fetal Skeletal Muscle	0.0	0.0
Skeletal Muscle Pool	0.0	0.0
Spleen Pool	0.0	0.0
Thymus Pool	2.0	1.7
CNS cancer (glio/astro) U87-MG	0.0	0.0
CNS cancer (glio/astro) U-118-MG	0.0	0.0
CNS cancer (neuro; met) SK-N-AS	0.0	0.0
CNS cancer (astro) SF-539	0.0	0.0
CNS cancer (astro) SNB-75	0.0	0.0
CNS cancer (glio) SNB-19	0.0	0.0
CNS cancer (glio) SF-295	0.0	0.0
Brain (Amygdala) Pool	0.0	0.0
Brain (cerebellum)	0.0	0.7
Brain (fetal)	0.0	1.7
Brain (Hippocampus) Pool	0.0	0.0
Cerebral Cortex Pool	0.0	0.0
Brain (Substantia nigra) Pool	0.0	0.0
Brain (Thalamus) Pool	0.0	0.0
Brain (whole)	0.0	0.0
Spinal Cord Pool	0.0	0.6
Adrenal Gland	0.0	0.0
Pituitary gland Pool	0.0	0.0
Salivary Gland	3.0	1.7
Thyroid (female)	0.0	0.0
Pancreatic ca. CAPAN2	0.0	0.0
Pancreas Pool	0.0	0.0

[0898]

TABLE XF
Oncology_cell_line_screening_panel_v3.1
                                 Rel. Exp. (%)
                                 Ag4893, Run
Tissue Name                      225052585
Daoy Medulloblastoma/Cerebellum  0.0
TE671 Medulloblastom/Cerebellum  0.0
D283 Med Medulloblastoma/Cerebellum 0.0
PFSK-1 Primitive Neuroectodermal/Cerebellum 0.0
XF-498_CNS                       0.0
SNB-78_CNS/glioma                0.6
SF-268_CNS/glioblastoma          0.0
T98G_Glioblastoma                0.0
SK-N-SH_Neuroblastoma (metastasis) 0.0
SF-295_CNS/glioblastoma          0.0
Cerebellum                       0.0
Cerebellum                       0.0
NCI-H292_Mucoepidermoid lung ca. 0.5
DMS-114_Small cell lung cancer   0.0
DMS-79_Small cell lung cancer/neuroendocrine 0.0
NCI-H146_Small cell lung cancer/ 0.0
neuroendocrine
NCI-H526_Small cell lung cancer/ 0.0
neuroendocrine
NCI-N417_Small cell lung cancer/ 0.0
neuroendocrine
NCI-H82_Small cell lung cancer/  0.0
neuroendocrine
NCI-H157_Squamous cell lung cancer 0.0
(metastasis)
NCI-H1155_Large cell lung cancer/ 0.0
neuroendocrine
NCI-H1299_Large cell lung cancer/ 0.0
neuroendocrine
NCI-H727_Lung carcinoid          0.0
NCI-UMC-11_Lung carcinoid        0.0
LX-1_Small cell lung cancer      0.0
Colo-205_Colon cancer            0.0
KM12_Colon cancer                0.0
KM20L2_Colon cancer              0.0
NCI-H716 Colon cancer            0.0
SW-48_Colon adenocarcinoma       0.0
SW1116_Colon adenocarcinoma      0.0
LS 174T_Colon adenocarcinoma     0.0
SW-948_Colon adenocarcinoma      0.0
SW-480_Colon adenocarcinoma      0.0
NCI-SNU-5_Gastric ca             0.0
KATO III_Stomach                 0.0
NCI-SNU-16_Gastric ca.           0.0
NCI-SNU-1_Gastric ca.            0.0
RF-1_Gastric adenocarcinoma      0.0
RF-48_Gastric adenocarcinoma     1.1
MKN-45_Gastric ca                2.0
NCI-N87_Gastric ca.              20.3
OVCAR-5_Ovarian ca.              0.0
RL95-2_Uterine carcinoma         6.3
HelaS3_Cervical adenocarcinoma   0.0
Ca Ski_Cervical epidermoid carcinoma 0.0
(metastasis)
ES-2_Ovarian clear cell carcinoma 0.0
Ramos/6 h stim_Stimulated with PMA/ 0.0
ionomycin 6 h
Ramos/14 h stim_Stimulated with PMA/ 0.0
ionomycin 14 h
MEG-01_Chronic myelogenous leukemia 0.0
(megokaryoblast)
Raji_Burkitt's lymphoma          0.0
Daudi_Burkitt's lymphoma         0.0
U266_B-cell plasmacytoma/myeloma 0.0
CA46_Burkitt's lymphoma          0.0
RL_non-Hodgkin's B-cell lymphoma 0.0
JM1_pre-B-cell lymphoma/leukemia 0.0
Jurkat_T cell leukemia           0.0
TF-1_Erythroleukemia             0.0
HUT 78_T-cell lymphoma           100.0
U937_Histiocytic lymphoma        0.0
KU-812 Myelogenous leukemia      19.6
769-P_Clear cell renal ca.       0.0
Caki-2_Clear cell renal ca.      0.0
SW 839_Clear cell renal ca.      0.0
G401_Wilms' tumor                0.0
Hs766T_Pancreatic ca. (LN metastasis) 0.0
CAPAN-1_Pancreatic adenocarcinoma (liver 0.0
metastasis)
SU86.86_Pancreatic carcinoma (liver 2.1
metastasis)
BxPC-3_Pancreatic adenocarcinoma 1.2
HPAC_Pancreatic adenocarcinoma   0.0
MIA PaCa-2_Pancreatic ca.        0.0
CFPAC-1_Pancreatic ductal adenocarcinoma 10.4
PANC-1_Pancreatic epithelioid ductal ca. 0.0
T24_Bladder ca. (transitional cell) 0.0
5637_Bladder ca.                 0.6
HT-1197_Bladder ca.              3.7
UM-UC-3_Bladder ca. (transitional cell) 0.0
A204_Rhabdomyosarcoma            0.0
HT-1080_Fibrosarcoma             0.0
MG-63_Osteosarcoma (bone)        0.0
SK-LMS-1_Leiomyosarcoma (vulva)  0.0
SJRH30_Rhabdomyosarcoma (met to bone 0.0
marrow)
A431_Epidermoid ca.              69.7
WM266-4_Melanoma                 0.0
DU 145_Prostate                  0.0
MDA-MB-468_Breast adenocarcinoma 1.5
SSC-4_Tongue                     1.7
SSC-9_Tongue                     2.7
SSC-15_Tongue                    24.0
CAL 27_Squamous cell ca. of tongue 14.5

[0899]

TABLE XG
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4387, Run
Tissue Name                      186501500
Secondary Th1 act                0.0
Secondary Th2 act                0.0
Secondary Tr1 act                0.0
Secondary Th1 rest               0.0
Secondary Th2 rest               0.0
Secondary Tr1 rest               0.0
Primary Th1 act                  0.0
Primary Th2 act                  0.0
Primary Tr1 act                  0.0
Primary Th1 rest                 0.3
Primary Th2 rest                 0.0
Primary Tr1 rest                 0.0
CD45RA CD4 lymphocyte act        0.0
CD45RO CD4 lymphocyte act        0.0
CD8 lymphocyte act               0.0
Secondary CD8 lymphocyte rest    0.0
Secondary CD8 lymphocyte act     0.0
CD4 lymphocyte none              0.0
2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0
LAK cells rest                   0.6
LAK cells IL-2                   1.0
LAK cells IL-2 + IL-12           0.9
LAK cells IL-2 + IFN gamma       0.0
LAK cells IL-2 + IL-18           0.9
LAK cells PMA/ionomycin          0.6
NK Cells IL-2 rest               0.0
Two Way MLR 3 day                0.0
Two Way MLR 5 day                0.0
Two Way MLR 7 day                0.0
PBMC rest                        0.0
PBMC PWM                         0.9
PBMC PHA-L                       0.0
Ramos (B cell) none              0.0
Ramos (B cell) ionomycin         0.0
B lymphocytes PWM                0.5
B lymphocytes CD40L and IL-4     0.0
EOL-1 dbcAMP                     0.0
EOL-1 dbcAMP PMA/ionomycin       0.0
Dendritic cells none             0.0
Dendritic cells LPS              0.0
Dendritic cells anti-CD40        0.0
Monocytes rest                   0.0
Monocytes LPS                    0.0
Macrophages rest                 0.0
Macrophages LPS                  0.0
HUVEC none                       0.0
HUVEC starved                    0.0
HUVEC IL-1beta                   0.0
HUVEC IFN gamma                  0.0
HUVEC TNF alpha + IFN gamma      0.0
HUVEC TNF alpha + IL4            0.0
HUVEC IL-11                      0.9
Lung Microvascular EC none       0.0
Lung Microvascular EC TNFalpha + 0.0
IL-1beta
Microvascular Dermal EC none     0.0
Microsvasular Dermal EC TNFalpha + 0.0
IL-1beta
Bronchial epithelium TNFalpha +  4.6
IL1beta
Small airway epithelium none     20.0
Small airway epithelium TNFalpha + 22.4
IL-1beta
Coronery artery SMC rest         0.0
Coronery artery SMC TNFalpha + IL- 0.0
1beta
Astrocytes rest                  0.0
Astrocytes TNFalpha + IL-1beta   0.0
KU-812 (Basophil) rest           6.7
KU-812 (Basophil) PMA/ionomycin  16.3
CCD1106 (Keratinocytes) none     0.4
CCD1106 (Keratinocytes) TNFalpha + 2.5
IL-1beta
Liver cirrhosis                  0.0
NCI-H292 none                    0.4
NCI-H292 IL-4                    0.9
NCI-H292 IL-9                    0.0
NCI-H292 IL-13                   0.0
NCI-H292 IFN gamma               0.0
HPAEC none                       0.0
HPAEC TNF alpha + IL-1 beta      0.0
Lung fibroblast none             1.0
Lung fibroblast TNF alpha + IL-1 0.4
beta
Lung fibroblast IL-4             0.0
Lung fibroblast IL-9             0.0
Lung fibroblast IL-13            0.8
Lung fibroblast IFN gamma        0.0
Dermal fibroblast CCD1070 rest   0.0
Dermal fibroblast CCD1070 TNF    0.0
alpha
Dermal fibroblast CCD1070 IL-1   0.0
beta
Dermal fibroblast IFN gamma      0.0
Dermal fibroblast IL-4           0.0
Dermal Fibroblasts rest          0.0
Neutrophils TNFa + LPS           0.0
Neutrophils rest                 1.8
Colon                            2.0
Lung                             2.1
Thymus                           18.4
Kidney                           100.0

[0900] CNS_neurodegeneration_v1.0 Summary: Ag4387 Expression of the CG134100-01 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0901] General_screening_panel v1.4 Summary: Ag4387 Highest expression of the CG134100-01 gene is detected in bone marrow (CT=30.6). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. In addition, therapeutic modulation of this gene product may be useful in the bone marrow related diseases such as leukemia.

[0902] Low levels of expression of this gene is also seen in uterus, trachea and bladder. Therefore, therapeutic modulation of this gene may be useful in the treatment of diseases that affect these tissues.

[0903] General_screening_panel_v1.5 Summary: Ag4893/Ag4894 Two experiments with same probe and primer sets are in excellent agreement. Highest expression of the CG134100-01 gene is detected in bone marrow (CT=30-34). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. In addition, therapeutic modulation of this gene product may be useful in the bone marrow related diseases such as leukemia.

[0904] Oncology_cell_line_screening_panel_v3.1 Summary: Ag4893 Highest expression of the CG134100-01 gene is detected in T cell lymphoma (CT=29.6). In addition, high to moderate levels of expression of this gene is also seen number of cancer samples derived from tongue squamous cell carcinoma, epidermoid carcinoma, bladder carcinoma, pancreatic ductal adenocarcinoma, myelogenous leukemia, uterine and gastric carcinoma. Therefore, expression of this gene may be useful as marker to detect the presence of these cancers.

[0905] Ag4894 Results from one experiment with this gene are not included. The amp plot indicates that there were experimental difficulties with this run.

[0906] Panel 4.1D Summary: Ag4387 Highest expression of the CG134100-01 gene is detected in kidney (CT=30.9). Therefore, expression of this gene may be used to distinguish kidney from other samples used in this panel. In addition, therapeutic modulation of this gene may be beneficial in the treatment of autoimmune of inflammatory disease that affect kidney including lupus and glomerulonephritis.

[0907] Moderate to low levels of expression of this gene is also seen in thymus, basophils, and small airway epithelium. Therefore, therapeutic modulation of this gene product may be beneficial in the treatment of asthma, allergies, COPD, and emphysema, inflammatory bowel disease, and autoimmune diseases.

[0908] Y. NOV27a (CG134403-01): 2510042P03RIK Homolog (TmSP)

[0909] Expression of gene CG134403-01 was assessed using the primer-probe set Ag4871, described in Table YA. Results of the RTQ-PCR runs are shown in Tables YB and YC. Table YA. Probe Name Ag4871

TABLE YA
Probe Name Ag4871
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-cctaacagatttcttgcgacaa-3′	22	7	310
Probe	TET-5′-agtcttccgcttccggttgctctgtt-3′-	26	39	311
	TAMRA
Reverse	5′-tgttatgggtgcggttactatg-3′	22	67	312

[0910]

TABLE YB
General_screening_panel_v1.5
                                 Rel. Exp. (%)
                                 Ag4871, Run
Tissue Name                      228903633
Adipose                          2.2
Melanoma* Hs688(A).T             8.3
Melanoma* Hs688(B).T             5.7
Melanoma* M14                    25.5
Melanoma* LOXIMVI                9.6
Melanoma* SK-MEL-5               10.3
Squamous cell carcinoma SCC-4    6.0
Testis Pool                      26.8
Prostate ca.* (bone met) PC-3    13.0
Prostate Pool                    3.2
Placenta                         1.4
Uterus Pool                      2.7
Ovarian ca. OVCAR-3              28.5
Ovarian ca. SK-OV-3              29.7
Ovarian ca. OVCAR-4              3.0
Ovarian ca. OVCAR-5              15.3
Ovarian ca. IGROV-1              7.7
Ovarian ca OVCAR-8               6.2
Ovary                            4.3
Breast ca. MCF-7                 9.5
Breast ca. MDA-MB-231            15.5
Breast ca. BT 549                8.1
Breast ca. T47D                  6.0
Breast ca. MDA-N                 14.1
Breast Pool                      13.4
Trachea                          3.9
Lung                             0.5
Fetal Lung                       4.6
Lung ca. NCI-N417                6.5
Lung ca. LX-1                    13.4
Lung ca. NCI-H146                18.3
Lung ca. SHP-77                  11.0
Lung ca. A549                    14.7
Lung ca. NCI-H526                5.8
Lung ca. NCI-H23                 10.1
Lung ca. NCI-H460                6.0
Lung ca. HOP-62                  4.3
Lung ca. NCI-H522                11.3
Liver                            0.7
Fetal Liver                      7.5
Liver ca. HepG2                  9.2
Kidney Pool                      8.5
Fetal Kidney                     19.2
Renal ca. 786-0                  17.2
Renal ca. A498                   5.4
Renal ca. ACHN                   8.4
Renal ca. UO-31                  8.1
Renal ca. TK-10                  12.4
Bladder                          3.0
Gastric ca. (liver met.) NCI-N87 31.9
Gastric ca. KATO III             8.0
Colon ca. SW-948                 1.8
Colon ca. SW480                  30.1
Colon ca.* (SW480 met) SW620     9.5
Colon ca. HT29                   9.3
Colon ca. HCT-116                9.7
Colon ca. CaCo-2                 15.9
Colon cancer tissue              2.6
Colon ca. SW1116                 5.0
Colon ca. Colo-205               4.1
Colon ca. SW-48                  2.1
Colon Pool                       9.7
Small Intestine Pool             3.0
Stomach Pool                     2.1
Bone Marrow Pool                 1.3
Fetal Heart                      5.6
Heart Pool                       1.5
Lymph Node Pool                  8.3
Fetal Skeletal Muscle            4.7
Skeletal Muscle Pool             4.8
Spleen Pool                      2.7
Thymus Pool                      4.3
CNS cancer (glio/astro) U87-MG   20.3
CNS cancer (glio/astro) U-118-MG 27.0
CNS cancer (neuro; met) SK-N-AS  100.0
CNS cancer (astro) SF-539        8.9
CNS cancer (astro) SNB-75        13.2
CNS cancer (glio) SNB-19         12.8
CNS cancer (glio) SF-295         22.4
Brain (Amygdala) Pool            4.5
Brain (cerebellum)               5.4
Brain (fetal)                    8.3
Brain (Hippocampus) Pool         3.7
Cerebral Cortex Pool             5.9
Brain (Substantia nigra) Pool    4.3
Brain (Thalamus) Pool            6.3
Brain (whole)                    6.4
Spinal Cord Pool                 9.6
Adrenal Gland                    4.1
Pituitary gland Pool             3.0
Salivary Gland                   2.9
Thyroid (female)                 3.4
Pancreatic ca. CAPAN2            8.8
Pancreas Pool                    8.0

[0911]

TABLE YC
Panel 4.1D
                                 Rel. Exp. (%)
                                 Ag4871, Run
Tissue Name                      223458798
Secondary Th1 act                21.9
Secondary Th2 act                25.0
Secondary Tr1 act                23.8
Secondary Th1 rest               11.5
Secondary Th2 rest               4.2
Secondary Tr1 rest               0.0
Primary Th1 act                  1.5
Primary Th2 act                  34.6
Primary Tr1 act                  40.1
Primary Th1 rest                 0.0
Primary Th2 rest                 8.4
Primary Tr1 rest                 17.6
CD45RA CD4 lymphocyte act        29.7
CD45RO CD4 lymphocyte act        34.9
CD8 lymphocyte act               27.4
Secondary CD8 lymphocyte rest    5.3
Secondary CD8 lymphocyte act     24.7
CD4 lymphocyte none              26.2
2ry Th1/Th2/Tr1_anti-CD95 CH11   24.8
LAK cells rest                   9.8
LAK cells IL-2                   26.4
LAK cells IL-2 + IL-12           20.4
LAK cells IL-2 + IFN gamma       35.8
LAK cells IL-2 + IL-18           21.3
LAK cells PMA/ionomycin          21.9
NK Cells IL-2 rest               14.7
Two Way MLR 3 day                7.2
Two Way MLR 5 day                12.7
Two Way MLR 7 day                12.4
PBMC rest                        18.6
PBMC PWM                         39.8
PBMC PHA-L                       10.4
Ramos (B cell) none              4.3
Ramos (B cell) ionomycin         25.9
B lymphocytes PWM                2.4
B lymphocytes CD40L and IL-4     31.6
EOL-1 dbcAMP                     9.7
EOL-1 dbcAMP PMA/ionomycin       5.0
Dendritic cells none             17.2
Dendritic cells LPS              9.4
Dendritic cells anti-CD40        1.0
Monocytes rest                   11.5
Monocytcs LPS                    20.3
Macrophages rest                 21.2
Macrophages LPS                  15.2
HUVEC none                       18.7
HUVEC starved                    50.7
HUVEC IL-1beta                   60.7
HUVEC IFN gamma                  100.0
HUVEC TNF alpha + IFN gamma      70.2
HUVEC TNF alpha + IL4            28.3
HUVEC IL-11                      28.7
Lung Microvascular EC none       90.1
Lung Microvascular EC TNFalpha + 39.8
IL-1beta
Microvascular Dermal EC none     49.0
Microsvasular Dermal EC TNFalpha + 10.9
IL-1beta
Bronchial epithelium TNFalpha +  27.2
IL1beta
Small airway epithelium none     11.0
Small airway epithelium TNFalpha + 21.5
IL-1beta
Coronery artery SMC rest         22.7
Coronery artery SMC TNFalpha + IL- 71.7
1beta
Astrocytes rest                  8.7
Astrocytes TNFalpha + IL-1beta   9.3
KU-812 (Basophil) rest           30.4
KU-812 (Basophil) PMA/ionomycin  25.7
CCD1106 (Keratinocytes) none     37.9
CCD1106 (Keratinocytes) TNFalpha + 47.6
IL-1beta
Liver cirrhosis                  9.7
NCI-H292 none                    39.8
NCI-H292 IL-4                    47.6
NCI-H292 IL-9                    79.6
NCI-H292 IL-13                   59.0
NCI-H292 IFN gamma               45.1
HPAEC none                       43.2
HPAEC TNF alpha + IL-1 beta      40.3
Lung fibroblast none             46.0
Lung fibroblast TNF alpha + IL-1 46.7
beta
Lung fibroblast IL-4             18.9
Lung fibroblast IL-9             42.6
Lung fibroblast IL-13            17.2
Lung fibroblast IFN gamma        26.8
Dermal fibroblast CCD1070 rest   25.3
Dermal fibroblast CCD1070 TNF alpha 57.8
Dermal fibroblast CCD1070 IL-1 beta 20.6
Dermal fibroblast IFN gamma      38.4
Dermal fibroblast IL-4           25.2
Dermal Fibroblasts rest          12.7
Neutrophils TNFa + LPS           0.7
Neutrophils rest                 13.8
Colon                            3.4
Lung                             23.5
Thymus                           36.3
Kidney                           32.3

[0912] General_screening_panel_v1.5 Summary: Ag4871 Highest expression of this gene is detected in CNS cancer SK-N-AS cell line (CT=28.5). Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from gastric, colon, lung, 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 gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.

[0913] Among tissues with metabolic or endocrine function, this gene is expressed at moderate to low 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.

[0914] Interestingly, this gene is expressed at much higher levels in fetal (CTs=32.2-32.9) when compared to adult liver and lung, respectively (CTs=36). This observation suggests that expression of this gene can be used to distinguish fetal from adult liver and lung, respectively. In addition, the relative overexpression of this gene in fetal tissues suggests that the protein product may enhance growth or development of liver and lung 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.

[0915] 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.

[0916] Panel 4.1D Summary: Ag4871 Highest expression of this gene is detected in IFN gamma treated HUVEC cells (CT=31.9). This gene is expressed at low 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_v1.5 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.

[0917] Z. NOV32a (CG56711-01): Kallistatin Precursor.

[0918] Expression of gene CG56711-01 was assessed using the primer-probe set Ag1689, described in Table ZA. Results of the RTQ-PCR runs are shown in Tables ZB, ZC and ZD. Please note that CG56711-01 represents a full-length physical clone

TABLE ZA
Probe Name Ag1689
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-aatgaggtggaacaacttgttg-3′	22	894	313
Probe	TET-5′-caagaagctagagttgcatcttccca-3′-	26	933	314
	TAMRA
Reverse	5′-ataggagccagaaatggagaac-3′	22	960	315

[0919]

TABLE ZB
Panel 1.3D
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag1689, Run	Ag1689, Run
Tissue Name	159350722	165534829
Liver adenocarcinoma	0.0	0.0
Pancreas	12.7	18.4
Pancreatic ca. CAPAN 2	0.0	0.0
Adrenal gland	0.0	0.0
Thyroid	0.0	0.0
Salivary gland	0.0	0.0
Pituitary gland	0.0	0.0
Brain (fetal)	0.0	0.0
Brain (whole)	0.0	0.0
Brain (amygdala)	0.0	0.0
Brain (cerebellum)	0.0	0.0
Brain (hippocampus)	0.0	0.0
Brain (substantia nigra)	0.0	0.0
Brain (thalamus)	0.0	0.0
Cerebral Cortex	0.0	0.0
Spinal cord	0.0	0.1
glio/astro U87-MG	0.0	0.0
glio/astro U-118-MG	0.0	0.0
astrocytoma SW1783	0.0	0.0
neuro*; met SK-N-AS	0.0	0.0
astrocytoma SF-539	0.0	0.0
astrocytoma SNB-75	0.0	0.0
glioma SNB-19	0.0	0.0
glioma U251	0.0	0.0
glioma SF-295	0.0	0.0
Heart (fetal)	0.0	0.0
Heart	0.0	0.0
Skeletal muscle (fetal)	0.0	0.0
Skeletal muscle	0.0	0.0
Bone marrow	0.0	0.0
Thymus	0.0	0.0
Spleen	0.0	0.8
Lymph node	0.0	0.0
Colorectal	0.0	0.0
Stomach	8.7	10.5
Small intestine	0.0	0.0
Colon ca. SW480	0.0	0.0
Colon ca.* SW620 (SW480 met)	0.0	0.0
Colon ca. HT29	0.5	0.3
Colon ca. HCT-116	0.0	0.0
Colon ca. CaCo-2	2.5	3.0
Colon ca. tissue (ODO3866)	1.9	0.4
Colon ca. HCC-2998	0.0	0.0
Gastric ca.* (liver met) NCI-N87	0.0	0.0
Bladder	7.2	12.4
Trachea	0.0	0.0
Kidney	2.0	0.1
Kidney (fetal)	10.9	8.4
Renal ca. 786-0	0.0	0.0
Renal ca. A498	0.0	0.0
Renal ca. RXF 393	0.0	0.0
Renal ca. ACHN	0.0	0.0
Renal ca. UO-31	0.0	0.0
Renal ca. TK-10	0.0	0.0
Liver	91.4	100.0
Liver (fetal)	100.0	93.3
Liver ca. (hepatoblast) HepG2	14.0	25.9
Lung	0.0	0.0
Lung (fetal)	0.0	0.0
Lung ca. (small cell) LX-1	0.0	0.1
Lung ca. (small cell) NCI-H69	0.0	0.0
Lung ca. (s. cell var.) SHP-77	0.0	0.0
Lung ca. (large cell) NCI-H460	0.0	0.0
Lung ca. (non-sm. cell) A549	0.0	0.1
Lung ca. (non-s. cell) NCI-H23	0.0	0.0
Lung ca. (non-s. cell) HOP-62	0.0	0.0
Lung ca. (non-s. cl) NCI-H522	0.0	0.0
Lung ca. (squam.) SW 900	0.0	0.0
Lung ca. (squam.) NCI-H596	0.0	0.0
Mammary gland	0.1	0.2
Breast ca.* (pl. ef) MCF-7	0.0	0.1
Breast ca.* (pl. ef) MDA-MB-231	0.0	0.0
Breast ca.* (pl. ef) T47D	0.0	0.1
Breast ca. BT-549	0.0	0.0
Breast ca. MDA-N	0.0	0.0
Ovary	0.0	0.0
Ovarian ca. OVCAR-3	0.0	0.0
Ovarian ca. OVCAR-4	0.0	0.1
Ovarian ca. OVCAR-5	0.0	0.0
Ovarian ca. OVCAR-8	0.0	0.0
Ovarian ca. IGROV-1	0.0	0.0
Ovarian ca.* (ascites) SK-OV-3	0.0	0.0
Uterus	0.0	0.0
Placenta	0.0	0.0
Prostate	0.1	0.4
Prostate ca.* (bone met) PC-3	0.0	0.0
Testis	0.3	0.2
Melanoma Hs688(A).T	0.0	0.0
Melanoma* (met) Hs688(B).T	0.0	0.0
Melanoma UACC-62	0.0	0.0
Melanoma M14	0.0	0.0
Melanoma LOX IMVI	0.0	0.0
Melanoma* (met) SK-MEL-5	0.0	0.0
Adipose	0.0	0.0

[0920]

TABLE ZC
Panel 2D
                                 Rel. Exp. (%)
                                 Ag1689, Run
Tissue Name                      159352635
Normal Colon                     0.8
CC Well to Mod Diff (ODO3866)    0.9
CC Margin (ODO3866)              0.0
CC Gr.2 rectosigmoid (ODO3868)   0.1
CC Margin (ODO3868)              0.0
CC Mod Diff (ODO3920)            0.3
CC Margin (ODO3920)              0.0
CC Gr.2 ascend colon (ODO3921)   0.1
CC Margin (ODO3921)              0.0
CC From Partial Hepatectomy (ODO4309) 9.9
Mets
Liver Margin (ODO4309)           100.0
Colon mets to lung (OD04451-01)  0.1
Lung Margin (OD04451-02)         0.0
Normal Prostate 6546-1           0.1
Prostate Cancer (OD04410)        0.0
Prostate Margin (OD04410)        0.1
Prostate Cancer (OD04720-01)     0.0
Prostate Margin (OD04720-02)     0.0
Normal Lung 061010               0.5
Lung Met to Muscle (ODO4286)     0.0
Muscle Margin (ODO4286)          0.0
Lung Malignant Cancer (OD03126)  0.1
Lung Margin (OD03126)            0.0
Lung Cancer (OD04404)            0.0
Lung Margin (OD04404)            0.0
Lung Cancer (OD04565)            0.0
Lung Margin (OD04565)            0.0
Lung Cancer (OD04237-01)         0.0
Lung Margin (OD04237-02)         0.0
Ocular Mel Met to Liver (ODO4310) 0.0
Liver Margin (ODO4310)           69.7
Melanoma Mets to Lung (OD04321)  0.0
Lung Margin (OD04321)            3.6
Normal Kidney                    3.9
Kidney Ca, Nuclear grade 2 (OD04338) 0.3
Kidney Margin (OD04338)          3.1
Kidney Ca Nuclear grade 1/2 (OD04339) 0.2
Kidney Margin (OD04339)          4.8
Kidney Ca, Clear cell type (OD04340) 0.0
Kidney Margin (OD04340)          1.1
Kidney Ca, Nuclear grade 3 (OD04348) 0.0
Kidney Margin (OD04348)          1.2
Kidney Cancer (OD04622-01)       0.0
Kidney Margin (OD04622-03)       0.5
Kidney Cancer (OD04450-01)       0.0
Kidney Margin (OD04450-03)       1.3
Kidney Cancer 8120607            0.0
Kidney Margin 8120608            1.3
Kidney Cancer 8120613            0.0
Kidney Margin 8120614            2.7
Kidney Cancer 9010320            0.1
Kidney Margin 9010321            1.4
Normal Uterus                    0.0
Uterus Cancer 064011             2.7
Normal Thyroid                   0.0
Thyroid Cancer 064010            0.6
Thyroid Cancer A302152           0.0
Thyroid Margin A302153           0.0
Normal Breast                    0.0
Breast Cancer (OD04566)          0.0
Breast Cancer (OD04590-01)       0.0
Breast Cancer Mets (OD04590-03)  0.0
Breast Cancer Metastasis (OD04655-05) 0.0
Breast Cancer 064006             1.0
Breast Cancer 1024               0.0
Breast Cancer 9100266            0.1
Breast Margin 9100265            0.0
Breast Cancer A209073            0.0
Breast Margin A209073            0.0
Normal Liver                     72.7
Liver Cancer 064003              21.0
Liver Cancer 1025                73.7
Liver Cancer 1026                63.3
Liver Cancer 6004-T              84.7
Liver Tissue 6004-N              5.5
Liver Cancer 6005-T              40.1
Liver Tissue 6005-N              48.3
Normal Bladder                   33.7
Bladder Cancer 1023              0.1
Bladder Cancer A302173           0.2
Bladder Cancer (OD04718-01)      0.8
Bladder Normal Adjacent (OD04718-03) 0.0
Normal Ovary                     0.0
Ovarian Cancer 064008            0.0
Ovarian Cancer (OD04768-07)      0.8
Ovary Margin (OD04768-08)        0.0
Normal Stomach                   3.7
Gastric Cancer 9060358           0.7
Stomach Margin 9060359           9.9
Gastric Cancer 9060395           0.1
Stomach Margin 9060394           4.9
Gastric Cancer 9060397           8.6
Stomach Margin 9060396           2.2
Gastric Cancer 064005            0.2

[0921]

TABLE ZD
Panel 4D
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag1689, Run	Ag1689, Run
Tissue Name	159350723	165725926
Secondary Th1 act	0.0	0.0
Secondary Th2 act	0.0	0.0
Secondary Tr1 act	0.0	0.0
Secondary Th1 rest	0.0	0.0
Secondary Th2 rest	0.0	0.0
Secondary Tr1 rest	0.0	0.0
Primary Th1 act	0.0	0.0
Primary Th2 act	0.0	0.0
Primary Tr1 act	0.0	0.0
Primary Th1 rest	0.0	0.0
Primary Th2 rest	0.0	0.0
Primary Tr1 rest	0.0	0.0
CD45RA CD4 lymphocyte act	0.0	0.0
CD45RO CD4 lymphocyte act	0.0	0.0
CD8 lymphocyte act	0.0	0.0
Secondary CD8 lymphocyte rest	0.0	0.0
Secondary CD8 lymphocyte act	0.0	0.0
CD4 lymphocyte none	0.0	0.0
2ry Th1/Th2/Tr1_anti-CD95 CH11	0.0	0.0
LAK cells rest	0.0	0.0
LAK cells IL-2	0.0	0.0
LAK cells IL-2 + IL-12	0.0	0.0
LAK cells IL-2 + IFN gamma	0.0	0.0
LAK cells IL-2 + IL-18	0.0	0.0
LAK cells PMA/ionomycin	0.0	0.0
NK Cells IL-2 rest	0.0	0.0
Two Way MLR 3 day	0.0	0.0
Two Way MLR 5 day	0.0	0.0
Two Way MLR 7 day	0.0	0.0
PBMC rest	0.0	0.0
PBMC PWM	0.0	0.0
PBMC PHA-L	0.0	0.0
Ramos (B cell) none	0.0	0.0
Ramos (B cell) ionomycin	0.0	0.0
B lymphocytes PWM	0.0	0.0
B lymphocytes CD40L and IL-4	0.0	0.0
EOL-1 dbcAMP	0.0	0.0
EOL-1 dbcAMP PMA/ionomycin	0.0	0.0
Dendritic cells none	0.0	0.0
Dendritic cells LPS	0.0	0.0
Dendritic cells anti-CD40	0.0	0.0
Monocytes rest	0.0	0.0
Monocytes LPS	0.0	0.0
Macrophages rest	0.0	0.0
Macrophages LPS	0.0	0.0
HUVEC none	0.0	0.0
HUVEC starved	0.0	0.0
HUVEC IL-1beta	0.0	0.0
HUVEC IFN gamma	0.0	0.0
HUVEC TNF alpha + IFN gamma	0.0	0.0
HUVEC TNF alpha + IL4	0.0	0.0
HUVEC IL-11	0.0	0.0
Lung Microvascular EC none	0.3	0.0
Lung Microvascular EC TNF alpha +	0.0	0.0
IL-1beta
Microvascular Dermal EC none	0.0	0.0
Microsvasular Dermal EC TNF	0.0	0.0
alpha + IL-1beta
Bronchial epithelium TNF alpha +	0.0	0.0
IL1beta
Small airway epithelium none	0.0	0.0
Small airway epithelium	0.0	0.0
TNFalpha + IL-1beta
Coronery artery SMC rest	0.0	0.0
Coronery artery SMC TNFalpha +	0.0	0.0
IL-1beta
Astrocytes rest	0.0	0.0
Astrocytes TNF alpha + IL-1beta	0.0	0.0
KU-812 (Basophil) rest	0.0	0.0
KU-812 (Basophil) PMA/ionomycin	0.0	0.0
CCD1106 (Keratinocytes) none	0.0	0.0
CCD1106 (Keratinocytes) TNF	0.0	0.0
alpha + IL-1beta
Liver cirrhosis	100.0	100.0
Lupus kidney	5.7	4.6
NCI-H292 none	0.0	0.0
NCI-H292 IL-4	0.0	0.0
NCI-H292 IL-9	0.0	0.0
NCI-H292 IL-13	0.0	0.0
NCI-H292 IFN gamma	0.0	0.0
HPAEC none	0.0	0.0
HPAEC TNF alpha + IL-1 beta	0.0	0.0
Lung fibroblast none	0.0	0.0
Lung fibroblast TNF alpha + IL-1	0.0	0.0
beta
Lung fibroblast IL-4	0.0	0.0
Lung fibroblast IL-9	0.0	0.0
Lung fibroblast IL-13	0.0	0.0
Lung fibroblast IFN gamma	0.0	0.0
Dermal fibroblast CCD1070 rest	0.0	0.0
Dermal fibroblast CCD1070 TNF	0.0	0.0
alpha
Dermal fibroblast CCD1070 IL-1 beta	0.0	0.0
Dermal fibroblast IFN gamma	0.0	0.0
Dermal fibroblast IL-4	0.0	0.0
IBD Colitis 2	0.0	0.0
IBD Crohn's	0.0	0.2
Colon	0.7	0.4
Lung	0.5	0.1
Thymus	45.1	17.9
Kidney	0.0	0.1

[0922] CNS_neurodegeneration_v1.0 Summary: Ag1689 Expression of this gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0923] Panel 1.3D Summary: Ag1689 Two experiment with same probe and primer sets arc in excellent agreement with highest expression of the CG56711-01 gene in adult and fetal liver (CTs=27-29). Therefore, expression of this gene may be used to distinguish these samples from other samples in this panel. Moderate to low expression of this gene is also seen in liver cancer and colon cancer cell line. Therefore, therapeutic modulation of this gene may be useful in the treatment of liver related diseases, liver and colon cancers.

[0924] Moderate levels of expression of this gene is also seen in pancreas and stomach. This gene codes for a kallistatin precursor, a serine proteinase inhibitor (serpin) with Phe-Phe residues at the P2 and P1 positions. Kallistatin inhibits the proliferation, migration and adhesion of endothelial cells in vitro and angiogenesis in the rat model of hindlimb ischemia. It induces vasorelaxation of isolated aortic rings and reduces renal perfusion pressure in isolated rat kidneys. It also inhibits the proliferation, migration and adhesion of endothelial cells in vitro and angiogenesis in the rat model of hindlimb ischemia (Chao et al., 2001, Biol Chem 382(1):15-21, PMID: 11258665). Furthermore, kallistatin expression is lower in the eye of patients suffering from diabetes and thus may be involved in diabetic retinopathy (Ma et al., 1996, Curr Eye Res 1996 November;15(11):1117-23, PMID: 8950506). Thus, therapeutic modulation of the activity of the kallistatin precursor encoded by this gene, through the use of protein therapeutics or antibodies, may be useful in the treatment of diabetes, diabetic retinopathy, blood pressure regulation and vascular remodeling.

[0925] Panel 2D Summary: Ag1689 Highest expression of the CG56711-01 gene is detected in liver (ODO4309)(CT=25.8). Interestingly, expression of this gene is much lower in the samples derived hepatectomy (ODO4309) metastasis and occular cancer metastasis to liver (ODO4310) (CT=29-40) as compared to corresponding adjacent control samples (CTs=25-26). High levels of expression of this gene is also seen in normal and liver cancer samples. Therefore, therapeutic modulation of expression of this gene or use of the protein encoded by this gene in the form of protein therapeutics may be useful in the treatment of these cancers and their metastasis.

[0926] Moderate to low levels of expression of this gene is also seen in gastric and kidney normal tissue samples compared with the adjacent tumor sample. It is also expressed in a sample of uterine and breast cancer. It may thus be used as a marker for these cancers and modulation of the activity of this gene or its protein product, through the use of protein therapeutics or antibodies, might be beneficial in the treatment of these cancers.

[0927] Panel 4D Summary: Ag1689 Two experiment with same probe and primer sets are in excellent agreement with highest expression of the CG56711-01 gene in liver cirrhosis (CTs=27-3 1). Therefore, expression of this gene may be useful distinguishing this sample from other samples in this panel and also as a marker for the diagnosis of liver cirrhosis. Furthermore, therapeutic modulation of this gene or its product may be beneficial in the treatment of liver cirrhosis.

[0928] In addition, moderate levels of expression of this gene is also seen in thymus. Thus, drugs that inhibit the function of this protein may regulate T cell development in the thymus and reduce or eliminate the symptoms of T cell mediated autoimmune or inflammatory diseases, including asthma, allergies, inflammatory bowel disease, lupus erythematosus, or rheumatoid arthritis. Additionally, small molecule or antibody therapeutics designed against this putative protein may disrupt T cell development in the thymus and function as an immunosuppresant for tissue transplant.

[0929] AA. NOV40a and NOV21a (CG95205-02 and CG133159-01): TEM-1 Splice Variant.

[0930] Expression of gene CG95205-02 and CG133159-01 was assessed using the primer-probe sets Ag389, Ag4808 and Ag4834, described in Tables AAA, AAB and AAC. Results of the RTQ-PCR runs are shown in Tables AAD, AAE, AAF, AAG, AAH, AAI and AAJ. Please note that the probes and primer sets Ag4808 and Ag4834 are specific for CG95205-02.

TABLE AAA
Probe Name Ag389
			Start	SEQ ID
Primers	Sequences	Length	Position	No
Forward	5′-catgtccctcgctacaataacact-3′	24	1006	316
Probe	TET-5′-agccaccaacgtagttgacacacatctgc-3′-	29	974	317
	TAMRA
Reverse	5′-gccagattgccggtgtg-3′	17	952	318

[0931]

TABLE AAB
Probe Name Ag4808
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-gggtcctctctcaaccactaga-3′	22	1346	319
Probe	TET-5′-cttggctctcaggaactctgcttcct-3′-	26	1368	320
	TAMRA
Reverse	5′-aggtcttaagggctttggtgta-3′	22	1417	321

[0932]

TABLE AAC
Probe Name Ag4834
Primers	Sequences	Length	Start Position	SEQ ID No
Forward	5′-ggagcccacctggcca-3′	16	1280	322
Probe	TET-5′-gctgcccagctggacagat-3′-TAMRA	19	1301	323
Reverse	5′-cctggggagcaggaagc-3′	17	1321	324

[0933]

TABLE AAD
General_screening_panel_v1.4
                                 Rel. Exp. (%)
                                 Ag4808, Run
Tissue Name                      223204451
Adipose                          17.8
Melanoma* Hs688(A).T             71.7
Melanoma* Hs688(B).T             100.0
Melanoma* M14                    0.0
Melanoma* LOXIMVI                0.0
Melanoma* SK-MEL-5               0.0
Squamous cell carcinoma SCC-4    0.5
Testis Pool                      4.5
Prostate ca.* (bone met) PC-3    0.1
Prostate Pool                    3.1
Placenta                         20.0
Uterus Pool                      3.1
Ovarian ca. OVCAR-3              0.2
Ovarian ca. SK-OV-3              0.1
Ovarian ca. OVCAR-4              0.3
Ovarian ca. OVCAR-5              0.1
Ovarian ca. IGROV-1              0.0
Ovarian ca. OVCAR-8              0.0
Ovary                            6.3
Breast ca. MCF-7                 0.0
Breast ca. MDA-MB-231            0.1
Breast ca. BT 549                1.1
Breast ca. T47D                  0.3
Breast ca. MDA-N                 0.0
Breast Pool                      8.1
Trachea                          6.6
Lung                             5.2
Fetal Lung                       24.1
Lung ca. NCI-N417                5.0
Lung ca. LX-1                    0.0
Lung ca. NCI-H146                0.0
Lung ca. SHP-77                  3.2
Lung ca. A549                    0.1
Lung ca. NCI-H526                0.1
Lung ca. NCI-H23                 0.5
Lung ca. NCI-H460                0.0
Lung ca. HOP-62                  0.1
Lung ca. NCI-H522                0.8
Liver                            0.0
Fetal Liver                      4.2
Liver ca. HepG2                  0.8
Kidney Pool                      16.2
Fetal Kidney                     6.8
Renal ca. 786-0                  0.0
Renal ca. A498                   0.1
Renal ca. ACHN                   0.0
Renal ca. UO-31                  0.1
Renal ca. TK-10                  0.1
Bladder                          12.9
Gastric ca. (liver met.) NCI-N87 0.2
Gastric ca. KATO III             0.0
Colon ca. SW-948                 0.0
Colon ca. SW480                  0.1
Colon ca.* (SW480 met) SW620     0.2
Colon ca. HT29                   0.0
Colon ca. HCT-116                0.3
Colon ca. CaCo-2                 0.6
Colon cancer tissue              29.1
Colon ca. SW1116                 0.0
Colon ca. Colo-205               0.0
Colon ca. SW-48                  0.0
Colon Pool                       7.2
Small Intestine Pool             9.4
Stomach Pool                     8.5
Bone Marrow Pool                 2.9
Fetal Heart                      2.7
Heart Pool                       4.0
Lymph Node Pool                  7.7
Fetal Skeletal Muscle            4.4
Skeletal Muscle Pool             8.3
Spleen Pool                      2.7
Thymus Pool                      13.6
CNS cancer (glio/astro) U87-MG   0.5
CNS cancer (glio/astro) U-118-MG 0.9
CNS cancer (neuro; met) SK-N-AS  58.2
CNS cancer (astro) SF-539        0.3
CNS cancer (astro) SNB-75        1.4
CNS cancer (glio) SNB-19         0.0
CNS cancer (glio) SF-295         0.0
Brain (Amygdala) Pool            0.6
Brain (cerebellum)               1.4
Brain (fetal)                    2.3
Brain (Hippocampus) Pool         1.1
Cerebral Cortex Pool             0.9
Brain (Substantia nigra) Pool    1.4
Brain (Thalamus) Pool            0.4
Brain (whole)                    0.6
Spinal Cord Pool                 0.6
Adrenal Gland                    3.9
Pituitary gland Pool             0.3
Salivary Gland                   0.9
Thyroid (female)                 2.9
Pancreatic ca. CAPAN2            0.0
Pancreas Pool                    17.0

[0934]

TABLE AAE
HASS Panel v1.0
                              Rel. Exp. (%)
                              Ag389, Run
Tissue Name                   268362650
MCF-7 C1                      0.3
MCF-7 C2                      0.5
MCF-7 C3                      1.1
MCF-7 C4                      0.1
MCF-7 C5                      0.2
MCF-7 C6                      0.6
MCF-7 C7                      0.1
MCF-7 C9                      0.8
MCF-7 C10                     0.2
MCF-7 C11                     0.2
MCF-7 C12                     0.3
MCF-7 C13                     0.4
MCF-7 C15                     0.3
MCF-7 C16                     0.5
MCF-7 C17                     0.8
T24 D1                        0.1
T24 D2                        0.1
T24 D3                        0.5
T24 D4                        0.2
T24 D5                        0.2
T24 D6                        0.0
T24 D7                        0.2
T24 D9                        0.0
T24 D10                       0.0
T24 D11                       0.3
T24 D12                       0.1
T24 D13                       0.3
T24 D15                       0.1
T24 D16                       0.1
T24 D17                       0.0
CAPaN B1                      0.0
CAPaN B2                      0.0
CAPaN B3                      0.1
CAPaN B4                      0.0
CAPaN B5                      0.0
CAPaN B6                      0.2
CAPaN B7                      0.0
CAPaN B8                      0.0
CAPaN B9                      0.0
CAPaN B10                     0.0
CAPaN B11                     0.0
CAPaN B12                     0.0
CAPaN B13                     0.0
CAPaN B14                     0.0
CAPaN B15                     0.0
CAPaN B16                     0.0
CAPaN B17                     0.0
U87-MG F1 (B)                 0.2
U87-MG F2                     0.1
U87-MG F3                     1.2
U87-MG F4                     0.0
U87-MG F5                     0.5
U87-MG F6                     0.9
U87-MG F7                     0.4
U87-MG F8                     0.1
U87-MG F9                     0.1
U87-MG F10                    0.9
U87-MG F11                    2.0
U87-MG F12                    0.2
U87-MG F13                    0.3
U87-MG F14                    0.5
U87-MG F15                    0.4
U87-MG F16                    0.3
U87-MG F17                    0.4
LnCAP A1                      0.0
LnCAP A2                      0.0
LnCAP A3                      0.0
LnCAP A4                      0.6
LnCAP A5                      0.2
LnCAP A6                      0.7
LnCAP A7                      0.2
LnCAP A8                      0.3
LnCAP A9                      0.2
LnCAP A10                     0.0
LnCAP A11                     1.3
LnCAP A12                     0.0
LnCAP A13                     0.0
LnCAP A14                     0.0
LnCAP A15                     0.1
LnCAP A16                     0.0
LnCAP A17                     0.2
Primary Astrocytes            52.5
Primary Renal Proximal Tubule 0.0
Epithelial cell A2
Primary melanocytes A5        100.0
126443 - 341 medullo          0.7
126444 - 487 medullo          61.1
126445 - 425 medullo          0.0
126446 - 690 medullo          0.7
126447 - 54 adult glioma      0.5
126448 - 245 adult glioma     0.1
126449 - 317 adult glioma     3.0
126450 - 212 glioma           0.9
126451 - 456 glioma           1.1

[0935]

TABLE AAF
Panel 1.1
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag389, Run	Ag389, Run
Tissue Name	109668399	129785554
Adrenal gland	8.7	8.0
Bladder	15.8	13.8
Brain (amygdala)	0.4	0.5
Brain (cerebellum)	2.9	2.4
Brain (hippocampus)	1.4	2.2
Brain (substantia nigra)	6.6	3.8
Brain (thalamus)	1.7	1.3
Cerebral Cortex	3.1	1.9
Brain (fetal)	3.0	3.0
Brain (whole)	2.1	1.5
glio/astro U-118-MG	0.1	0.2
astrocytoma SF-539	0.0	0.1
astrocytoma SNB-75	0.0	0.0
astrocytoma SW1783	1.7	1.2
glioma U251	0.0	0.0
glioma SF-295	0.0	0.0
glioma SNB-19	0.0	0.0
glio/astro U87-MG	0.0	0.1
neuro*; met SK-N-AS	95.3	100.0
Mammary gland	85.3	80.7
Breast ca. BT-549	5.6	5.1
Breast ca. MDA-N	0.0	0.0
Breast ca.* (pl. ef) T47D	0.1	0.1
Breast ca.* (pl. ef) MCF-7	0.0	0.0
Breast ca.* (pl. ef) MDA-MB-231	0.0	0.0
Small intestine	51.4	37.6
Colorectal	0.8	0.8
Colon ca. HT29	0.1	0.1
Colon ca. CaCo-2	0.5	0.3
Colon ca HCT-15	0.1	0.1
Colon ca. HCT-116	0.0	0.0
Colon ca. HCC-2998	0.3	0.2
Colon ca. SW480	0.0	0.0
Colon ca.* SW620 (SW480 met)	0.1	0.1
Stomach	8.8	20.4
Gastric ca. (liver met) NCI-N87	0.0	0.1
Heart	45.7	41.2
Skeletal muscle (Fetal)	24.0	27.4
Skeletal muscle	44.1	31.6
Endothelial cells	0.0	0.0
Heart (Fetal)	20.3	18.6
Kidney	13.5	11.0
Kidney (fetal)	27.2	16.2
Renal ca. 786-0	0.0	0.0
Renal ca. A498	0.0	0.1
Renal ca. ACHN	0.0	0.0
Renal ca TK-10	0.0	0.0
Renal ca. UO-31	0.1	0.0
Renal ca. RXF 393	0.0	0.0
Liver	5.3	3.5
Liver (fetal)	4.8	3.2
Liver ca. (hepatoblast) HepG2	0.0	0.0
Lung	4.8	4.9
Lung (fetal)	17.8	17.4
Lung ca. (non-s. cell) HOP-62	0.8	0.4
Lung ca. (large cell) NCI-H460	0.1	0.0
Lung ca. (non-s. cell) NCI-H23	0.2	0.2
Lung ca. (non-s. cl) NCI-H522	1.7	0.7
Lung ca. (non-sm. cell) A549	0.0	0.1
Lung ca. (s. cell var.) SHP-77	1.9	1.4
Lung ca. (small cell) LX-1	0.1	0.2
Lung ca. (small cell) NCI-H69	1.0	0.7
Lung ca. (squam.) SW 900	0.1	0.0
Lung ca. (squam.) NCI-H596	2.8	2.7
Lymph node	9.3	10.6
Spleen	3.2	3.3
Thymus	7.1	3.5
Ovary	23.0	22.1
Ovarian ca. IGROV-1	0.0	0.0
Ovarian ca. OVCAR-3	0.0	0.0
Ovarian ca. OVCAR-4	0.3	0.2
Ovarian ca. OVCAR-5	0.7	0.2
Ovarian ca. OVCAR-8	0.1	0.1
Ovarian ca.* (ascites) SK-OV-3	0.1	0.0
Pancreas	12.7	9.5
Pancreatic ca. CAPAN 2	0.0	0.0
Pituitary gland	4.5	1.8
Placenta	87.1	89.5
Prostate	11.1	5.1
Prostate ca.* (bone met) PC-3	0.2	0.2
Salivary gland	10.9	13.5
Trachea	17.1	8.9
Spinal cord	5.5	3.7
Testis	3.7	2.9
Thyroid	24.1	15.8
Uterus	19.6	9.4
Melanoma M14	0.0	0.0
Melanoma LOX IMVI	0.0	0.0
Melanoma UACC-62	0.0	0.0
Melanoma SK-MEL-28	0.0	0.0
Melanoma* (met) SK-MEL-5	0.0	0.0
Melanoma Hs688(A).T	69.7	66.0
Melanoma* (met) Hs688(B).T	100.0	95.9

[0936]

TABLE AAG
Panel 1.2
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag389, Run	Ag389, Run
Tissue Name	139735024	142359249
Endothelial cells	0.0	0.0
Heart (Fetal)	77.9	74.2
Pancreas	0.3	2.4
Pancreatic ca. CAPAN 2	0.0	0.0
Adrenal Gland	25.0	22.1
Thyroid	1.2	1.8
Salivary gland	12.2	20.0
Pituitary gland	1.1	2.5
Brain (fetal)	0.3	0.4
Brain (whole)	0.1	0.8
Brain (amygdala)	1.2	0.8
Brain (cerebellum)	0.2	0.9
Brain (hippocampus)	2.8	2.0
Brain (thalamus)	2.2	1.6
Cerebral Cortex	7.1	6.5
Spinal cord	0.8	1.0
glio/astro U87-MG	0.0	0.1
glio/astro U-118-MG	0.1	0.2
astrocytoma SW1783	1.6	1.6
neuro*; met SK-N-AS	63.3	62.4
astrocytoma SF-539	0.0	0.0
astrocytoma SNB-75	0.0	0.0
glioma SNB-19	0.0	0.0
glioma U251	0.0	0.0
glioma SF-295	0.0	0.0
Heart	85.3	82.9
Skeletal Muscle	33.0	40.6
Bone marrow	0.9	1.2
Thymus	1.5	1.1
Spleen	3.0	3.0
Lymph node	1.1	1.3
Colorectal Tissue	3.6	1.8
Stomach	3.1	5.7
Small intestine	45.1	44.1
Colon ca. SW480	0.0	0.0
Colon ca.* SW620 (SW480 met)	0.0	0.0
Colon ca. HT29	0.0	0.0
Colon ca. HCT-116	0.0	0.0
Colon ca. CaCo-2	0.1	0.2
Colon ca. Tissue (ODO3866)	6.8	5.2
Colon ca. HCC-2998	0.1	0.3
Gastric ca.* (liver met) NCI-N87	0.8	0.0
Bladder	37.4	29.5
Trachea	0.9	1.6
Kidney	19.8	20.2
Kidney (fetal)	13.3	22.1
Renal ca. 786-0	0.0	0.0
Renal ca. A498	0.0	0.0
Renal ca. RXF 393	0.0	0.0
Renal ca. ACHN	0.0	0.0
Renal ca. UO-31	0.0	0.1
Renal ca. TK-10	0.0	0.0
Liver	5.9	5.2
Liver (fetal)	5.4	4.2
Liver ca. (hepatoblast) HepG2	1.1	1.6
Lung	0.8	0.9
Lung (fetal)	3.3	2.7
Lung ca. (small cell) LX-1	0.1	0.1
Lung ca. (small cell) NCI-H69	0.8	0.8
Lung ca. (s. cell var.) SHP-77	1.3	1.1
Lung ca. (large cell) NCI-H460	0.0	0.0
Lung ca. (non-sm. cell) A549	0.0	0.0
Lung ca. (non-s. cell) NCI-H23	0.1	0.3
Lung ca. (non-s. cell) HOP-62	0.1	0.2
Lung ca. (non-s. cl) NCI-H522	1.2	1.7
Lung ca. (squam.) SW 900	0.0	0.0
Lung ca. (squam.) NCI-H596	3.0	2.8
Mammary gland	20.0	44.8
Breast ca.* (pl. ef) MCF-7	0.0	0.0
Breast ca.* (pl. ef) MDA-MB-231	0.0	0.0
Breast ca.* (pl. ef) T47D	0.0	0.1
Breast ca. BT-549	4.6	4.1
Breast ca. MDA-N	0.0	0.1
Ovary	48.3	42.3
Ovarian ca. OVCAR-3	0.0	0.0
Ovarian ca. OVCAR-4	0.4	0.4
Ovarian ca. OVCAR-5	0.3	0.7
Ovarian ca. OVCAR-8	0.0	0.1
Ovarian ca. IGROV-1	0.0	0.1
Ovarian ca. (ascites) SK-OV-3	0.0	0.0
Uterus	9.9	10.0
Placenta	8.0	24.7
Prostate	7.7	9.8
Prostate ca.* (bone met) PC-3	0.1	0.1
Testis	0.5	0.5
Melanoma Hs688(A).T	87.1	83.5
Melanoma* (met) Hs688(B).T	100.0	100.0
Melanoma UACC-62	0.0	0.0
Melanoma M14	0.0	0.0
Melanoma LOX IMVI	0.0	0.0
Melanoma* (met) SK-MEL-5	0.0	0.0

[0937]

TABLE AAH
Panel 2D
                                 Rel. Exp. (%)
                                 Ag389, Run
Tissue Name                      145188404
Normal Colon                     26.2
CC Well to Mod Diff (ODO3866)    21.6
CC Margin (ODO3866)              15.6
CC Gr.2 rectosigmoid (ODO3868)   10.4
CC Margin (ODO3868)              3.3
CC Mod Diff (ODO3920)            2.8
CC Margin (ODO3920)              4.5
CC Gr.2 ascend colon (ODO3921)   13.0
CC Margin (ODO3921)              10.2
CC from Partial Hepatectomy (ODO4309) Mets 5.9
Liver Margin (ODO4309)           1.5
Colon mets to lung (OD04451-01)  8.5
Lung Margin (OD04451-02)         5.8
Normal Prostate 6546-1           9.5
Prostate Cancer (OD04410)        8.0
Prostate Margin (OD04410)        11.7
Prostate Cancer (OD04720-01)     5.5
Prostate Margin (OD04720-02)     12.6
Normal Lung 061010               12.7
Lung Met to Muscle (ODO4286)     2.6
Muscle Margin (ODO4286)          54.0
Lung Malignant Cancer (OD03126)  31.6
Lung Margin (OD03126)            7.3
Lung Cancer (OD04404)            10.4
Lung Margin (OD04404)            47.6
Lung Cancer (OD04565)            9.0
Lung Margin (OD04565)            5.0
Lung Cancer (OD04237-01)         7.3
Lung Margin (OD04237-02)         17.4
Ocular Mel Met to Liver (ODO4310) 0.6
Liver Margin (ODO4310)           0.7
Melanoma Mets to Lung (OD04321)  1.3
Lung Margin (OD04321)            12.5
Normal Kidney                    14.4
Kidney Ca, Nuclear grade 2 (OD04338) 2.7
Kidney Margin (OD04338)          6.9
Kidney Ca Nuclear grade 1/2 (OD04339) 1.1
Kidney Margin (OD04339)          11.0
Kidney Ca, Clear cell type (OD04340) 19.9
Kidney Margin (OD04340)          11.8
Kidney Ca, Nuclear grade 3 (OD04348) 23.5
Kidney Margin (OD04348)          13.7
Kidney Cancer (OD04622-01)       24.0
Kidney Margin (OD04622-03)       2.6
Kidney Cancer (OD04450-01)       0.4
Kidney Margin (OD04450-03)       10.2
Kidney Cancer 8120607            7.1
Kidney Margin 8120608            13.6
Kidney Cancer 8120613            1.8
Kidney Margin 8120614            9.2
Kidney Cancer 9010320            64.2
Kidney Margin 9010321            16.6
Normal Uterus                    16.2
Uterus Cancer 064011             17.9
Normal Thyroid                   22.7
Thyroid Cancer 064010            6.6
Thyroid Cancer A302152           5.3
Thyroid Margin A302153           5.4
Normal Breast                    32.1
Breast Cancer (OD04566)          6.0
Breast Cancer (OD04590-01)       26.6
Breast Cancer Mets (OD04590-03)  37.4
Breast Cancer Metastasis (OD04655-05) 8.4
Breast Cancer 064006             15.1
Breast Cancer 1024               26.6
Breast Cancer 9100266            16.8
Breast Margin 9100265            16.4
Breast Cancer A209073            32.1
Breast Margin A209073            27.7
Normal Liver                     1.0
Liver Cancer 064003              0.5
Liver Cancer 1025                1.5
Liver Cancer 1026                13.0
Liver Cancer 6004-T              2.3
Liver Tissue 6004-N              3.5
Liver Cancer 6005-T              12.8
Liver Tissue 6005-N              1.5
Normal Bladder                   14.2
Bladder Cancer 1023              6.9
Bladder Cancer A302173           4.8
Bladder Cancer (OD04718-01)      11.7
Bladder Normal Adjacent (OD04718-03) 100.0
Normal Ovary                     19.6
Ovarian Cancer 064008            15.5
Ovarian Cancer (OD04768-07)      5.0
Ovary Margin (OD04768-08)        40.6
Normal Stomach                   18.3
Gastric Cancer 9060358           9.9
Stomach Margin 9060359           7.9
Gastric Cancer 9060395           13.1
Stomach Margin 9060394           9.2
Gastric Cancer 9060397           13.3
Stomach Margin 9060396           3.6
Gastric Cancer 064005            9.7

[0938]

TABLE AAI
Panel 4D
	Rel. Exp. (%)	Rel. Exp. (%)
	Ag389, Run	Ag389, Run
Tissue Name	139853806	140196439
Secondary Th1 act	0.0	0.0
Secondary Th2 act	0.0	0.0
Secondary Tr1 act	0.0	0.0
Secondary Th1 rest	0.0	0.0
Secondary Th2 rest	0.0	0.1
Secondary Tr1 rest	0.0	0.0
Primary Th1 act	0.0	0.0
Primary Th2 act	0.0	0.0
Primary Tr1 act	0.1	0.0
Primary Th1 rest	0.2	0.5
Primary Th2 rest	0.1	0.2
Primary Tr1 rest	0.6	0.5
CD45RA CD4 lymphocyte act	11.0	11.2
CD45RO CD4 lymphocyte act	0.1	0.1
CD8 lymphocyte act	0.8	0.7
Secondary CD8 lymphocyte rest	0.0	0.0
Secondary CD8 lymphocyte act	0.0	0.1
CD4 lymphocyte none	0.1	0.1
2ry Th1/Th2/Tr1_anti-CD95 CH11	0.0	0.1
LAK cells rest	0.1	0.1
LAK cells IL-2	0.1	0.2
LAK cells IL-2 + IL-12	0.1	0.3
LAK cells IL-2 + IFN gamma	0.2	0.2
LAK cells IL-2 + IL-18	0.1	0.4
LAK cells PMA/ionomycin	0.0	0.0
NK Cells IL-2 rest	0.1	0.1
Two Way MLR 3 day	0.2	0.3
Two Way MLR 5 day	0.1	0.2
Two Way MLR 7 day	0.1	0.1
PBMC rest	0.1	0.2
PBMC PWM	0.1	0.3
PBMC PHA-L	0.7	1.2
Ramos (B cell) none	0.0	0.0
Ramos (B cell) ionomycin	0.0	0.0
B lymphocytes PWM	0.1	0.2
B lymphocytes CD40L and IL-4	0.2	0.1
EOL-1 dbcAMP	0.1	0.0
EOL-1 dbcAMP PMA/ionomycin	0.1	0.0
Dendritic cells none	0.0	0.1
Dendritic cells LPS	0.0	0.0
Dendritic cells anti-CD40	0.0	0.0
Monocytes rest	0.0	0.0
Monocytes LPS	0.0	0.0
Macrophages rest	0.0	0.0
Macrophages LPS	0.0	0.0
HUVEC none	0.0	0.0
HUVEC starved	0.0	0.0
HUVEC IL-1beta	0.0	0.0
HUVEC IFN gamma	0.0	0.0
HUVEC TNF alpha + IFN gamma	0.0	0.0
HUVEC TNF alpha + IL4	0.0	0.0
HUVEC IL-11	0.0	0.0
Lung Microvascular EC none	0.0	0.0
Lung Microvascular EC TNFalpha +	0.0	0.0
IL-1beta
Microvascular Dermal EC none	0.0	0.0
Microsvasular Dermal EC TNF	0.0	0.0
alpha + IL-1beta
Bronchial epithelium TNFalpha +	0.0	0.0
IL1beta
Small airway epithelium none	0.2	0.5
Small airway epithelium TNF	0.0	0.0
alpha + IL-1beta
Coronery artery SMC rest	6.2	6.7
Coronery artery SMC TNF alpha +	6.0	4.4
IL-1beta
Astrocytes rest	0.3	0.4
Astrocytes TNFalpha + IL-1beta	1.1	1.5
KU-812 (Basophil) rest	0.0	0.0
KU-812 (Basophil) PMA/ionomycin	0.0	0.0
CCD1106 (Keratinocytes) none	0.0	0.0
CCD1106 (Keratinocytes)	0.0	0.0
TNFalpha + IL-1beta
Liver cirrhosis	0.8	0.7
Lupus kidney	0.7	1.0
NCI-H292 none	0.0	0.0
NCI-H292 IL-4	0.0	0.0
NCI-H292 IL-9	0.0	0.0
NCI-H292 IL-13	0.0	0.0
NCI-H292 IFN gamma	0.0	0.0
HPAEC none	0.0	0.0
HPAEC TNF alpha + IL-1 beta	0.0	0.0
Lung fibroblast none	24.3	25.7
Lung fibroblast TNF alpha + IL-1	3.8	5.4
beta
Lung fibroblast IL-4	22.5	31.2
Lung fibroblast IL-19	20.6	24.7
Lung fibroblast IL-13	41.2	59.0
Lung fibroblast IFN gamma	24.1	29.9
Dermal fibroblast CCD1070 rest	61.6	69.3
Dermal fibroblast CCD1070 TNF alpha	25.9	28.9
Dermal fibroblast CCD1070 IL-1 beta	55.1	42.6
Dermal fibroblast IFN gamma	51.1	42.3
Dermal fibroblast IL-4	100.0	100.0
IBD Colitis 2	0.0	0.1
IBD Crohn's	0.6	0.6
Colon	1.6	2.1
Lung	9.8	13.2
Thymus	1.0	1.4
Kidney	1.5	1.4

[0939]

TABLE AAJ
Panel 5 Islet
                                 Rel. Exp. (%)
                                 Ag4808, Run
Tissue Name                      259154757
97457_Patient-02go_adipose       80.7
97476_Patient-07sk_skeletal muscle 22.4
97477_Patient-07ut_uterus        35.8
97478_Patient-07pl_placenta      12.9
99167_Bayer Patient 1            1.8
97482_Patient-08ut_uterus        32.8
97483_Patient-08pl_placenta      6.1
97486_Patient-09sk_skeletal muscle 3.3
97487_Patient-09ut_uterus        11.9
97488_Patient-09pl_placenta      8.3
97492_Patient-10ut_uterus        23.2
97493_Patient-10pl_placenta      15.0
97495_Patient-11go_adipose       6.9
97496_Patient-11sk_skeletal muscle 5.0
97497_Patient-11ut_uterus        27.4
97498_Patient-11pl_placenta      12.8
97500_Patient-12go_adipose       72.7
97501_Patient-12sk_skeletal muscle 22.2
97502_Patient-12ut_uterus        54.7
97503_Patient-12pl_placenta      3.5
94721_Donor 2 U - A_Mesenchymal Stem Cells 49.0
94722_Donor 2 U - B_Mesenchymal Stem Cells 46.7
94723_Donor 2 U - C_Mesenchymal Stem Cells 57.0
94709_Donor 2 AM - A adipose     46.0
94710_Donor 2 AM - B_adipose     46.0
94711_Donor 2 AM - C_adipose     41.5
94712_Donor 2 AD - A_adipose     30.6
94713_Donor 2 AD - B_adipose     53.6
94714_Donor 2 AD - C_adipose     49.0
94742_Donor 3 U - A_Mesenchymal Stem Cells 69.3
94743_Donor 3 U - B_Mesenchymal Stem Cells 82.4
94730_Donor 3 AM - A_adipose     100.0
94731_Donor 3 AM - B_adipose     67.8
94732_Donor 3 AM - C_adipose     80.1
94733_Donor 3 AD - A_adipose     85.9
94734_Donor 3 AD - B_adipose     69.7
94735_Donor 3 AD - C_adipose     62.4
77138_Liver_HepG2untreated       4.8
73556_Heart_Cardiac stromal cells (primary) 0.0
81735_Small Intestine            9.4
72409_Kidney_Proximal Convoluted Tubule 0.0
82685_Small intestine_Duodenum   0.9
90650_Adrenal_Adrenocortical adenoma 3.9
72410_Kidney_HRCE                0.0
72411_Kidney_HRE                 0.1
73139_Uterus_Uterine smooth muscle cells 28.1

[0940] AI_comprehensive panel_v1.0 Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0941] General_screening_panel_v1.4 Summary: Ag4808 Highest expression of this gene is detected in melanoma Hs688(B).T cell line (CT=26.7). In addition, high to moderate expression of this is also seen in colon cancer, melanoma melanoma Hs688(A).T cell line, and cell lines derived from brain, liver, lung and breast cancers. This gene codes for endosialin (TEM1) protein, a cell surface glycoprotein identified with monoclonal antibody FB5. It is a highly expressed by tumor blood vessel endothelium in a broad range of human cancers but not detected in blood vessels or other cell types in many normal tissues (Carson-Walter et al., 2001, Cancer Res 61(18):6649-55, PMID: 11559528; Christian et al., 2001, J Biol Chem 276(10):7408-14, PMID: 11084048). Therefore, therapeutic modulation of the protein encoded by this gene through the use of antibody or small molecule drug, may be beneficial in the treatment of these cancers.

[0942] Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adipose, adrenal gland, thyroid, 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.

[0943] Interestingly, this gene is expressed at much higher levels in fetal (CT=31.2) when compared to adult liver (CT=37.9). 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 skeletal muscle 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 TEM1 encoded by this gene could be useful in treatment of liver related diseases.

[0944] In addition, this gene is expressed at moderate to low 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.

[0945] General_screening_panel_v1.5 Summary: Ag4834 Expression of the CG95205-02 gene (Runs 228726951 and 228783170) is low/undetectable (CTs>35) across all of the samples on this panel.

[0946] HASS Panel v1.0 Summary: Ag389 Highest expression of this gene is detected in primary melanocytes A5 (CT=29.5). Moderate levels of expression of this gene is detected in a sample of brain cancer, as well as, in cultured primary melanocytes and astrocytes.

[0947] Oncology_cell_line_screening_panel_v3.1 Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0948] Panel 1.1 Summary: Ag4808 Two experiment with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in melanoma Hs688(B).T and neuronial metastatic SK-N-AS cell lines (CTs=22-24). In addition, high to moderate expression of this is also seen in colon cancer, melanoma melanoma Hs688(A).T cell line, and cell lines derived from brain, liver, lung and breast cancers. Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. In addition, this gene is expressed at moderate to low levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Please see panel 1.4 for discussion on utility of this gene.

[0949] Panel 1.2 Summary: Ag389 Two experiment with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in melanoma Hs688(B).T (CTs=25). In addition, high to moderate expression of this is also seen in colon cancer, melanoma melanoma Hs688(A).T cell line, and cell lines derived from brain, liver, lung and breast cancers Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. In addition, this gene is expressed at moderate to low levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Please see panel 1.4 for discussion on utility of this gene.

[0950] Results from two experiments (Runs 138522289 and 138564094) with this gene are not included. The amp plot indicates that there were experimental difficulties with this run.

[0951] Panel 2D Summary: Ag389 Highest expression of this gene is detected in normal bladder (CT=30). Moderate to low expression of this gene is seen in both normal and cancer samples derived from colon, stomach, ovary, bladder, liver, thyroid, uterus, kidney, lung, and prostate. Therefore, therapeutic modulation of the protein encoded by this gene through the use of antibody or small molecule drug, may be beneficial in the treatment of these cancers. Please see panel 1.4 for more discussion.

[0952] Panel 4.1D Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

[0953] Panel 4D Summary: Ag389 Two experiment with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in IL-4 treated dermal fibroblast (CTs=27.4). In addition, high to moderate expression of this gene is seen in lung and dermal fibroblasts, coronary artery SMC, PHA-L activated PBMC cells, and normal tissues represented by colon, lung, thymus and kidney. Moderate expression of this gene is also detected in CD45RA CD4 lymphocytes, which represents activated naive T cells. Interestingly, the expression of this gene is strongly down regulated in activated memory T cells (CD45RO CD4 lymphocyte) or CD4 Th1 or Th2 cells, resting CD4 cells (CTs>35), suggesting a role for this putative protein in differentiation or activation of naive T cells. Therefore, modulation of the expression and/or activity of this putative protein encoded by this gene might be beneficial for the control of autoimmune diseases and T cell mediated diseases such as arthritis, IBD, asthma, COPD and skin disorders such as psoriasis and emphysema.

[0954] Panel 5 Islet Summary: Ag4808 Highest expression of this gene is detected in midway differentiated adipose (CT=28.3). Moderate to low expression of this gene is also seen in differentiated adipocytes and undifferentiated mesenchymal cells, skeletal muscle, islet cells, small intestine, placenta and uterus. Please see panel 1.4 for further discussion on the utility of this gene.

[0955] General oncology screening panel_v—2.4 Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs>35) across all of the samples on this panel.

Example D

[0956] Identification of Single Nucleotide Polymorphisms in NOVX Nucleic Acid Sequences

[0957] 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.

[0958] 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, HMMER, FASTA, Hybrid and other relevant programs.

[0959] 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.

[0960] 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).

[0961] 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. Ps NOV1a SNP Data:

[0962] Four ploymorphic variants of NOV1a have been identified and are shown in Table D1.

	TABLE D1
	Nucleotides	Amino Acids
	Base			Base
	Position	Wild-		Position	Wild-
Variant	of SNP	type	Variant	of SNP	type	Variant
13379739	743	C	G	215	Arg	Gly
13379740	910	C	T	270	Ala	Ala
13379741	975	G	A	292	Gly	Asp
13379738	1500	T	C	467	Val	Ala

[0963] NOV4a SNP Data:

[0964] Two polymorphic variants of NOV4a have been identified and are shown in Table D2.

	TABLE D2
	Nucleotides	Amino Acids
	Base			Base
	Position	Wild-		Position	Wild-
Variant	of SNP	type	Variant	of SNP	type	Variant
13379812	153	G	C	32	Gly	Ala
13379809	954	C	T	0

[0965] NOV5a SNP Data:

[0966] Two polymorphic variants of NOV5a have been identified and are shown in Table D3.

	TABLE D3
	Nucleotides	Amino Acids
	Base			Base
	Position	Wild-		Position	Wild-
Variant	of SNP	type	Variant	of SNP	type	Variant
13379756	409	C	T	60	His	His
13379755	966	G	T	246	Gly	Val

[0967] NOV6a SNP Data:

[0968] One polymorphic variant of NOV6a has been identified and is shown in Table D4.

	TABLE D4
	Nucleotides	Amino Acids
	Base			Base
	Position	Wild-		Position	Wild-
Variant	of SNP	type	Variant	of SNP	type	Variant
13378086	216	G	A	52	Ala	Thr

[0969] NOV7a SNP Data:

[0970] Two polymorphic variants of NOV7a were identified and are shown in Table D5.

	TABLE D5
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379781	534	A	G	173	Gly	Gly
13379782	715	G	A	234	Ala	Thr

[0971] NOV9a SNP Data:

[0972] One polymorphic variant of NOV9a has been identified and is shown in Table D6.

	TABLE D6
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379810	84	G	A	28	Lys	Lys

[0973] NOV10a SNP Data:

[0974] Four polymorphic variants of NOv10a have been identified and are shown in Table D7.

	TABLE D7
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379776	3528	C	T	1150	Pro	Ser
13379775	3619	T	C	1180	Leu	Pro
13379785	4588	T	G	0
13379813	5742	A	G	0

[0975] NOV11a SNP Data:

[0976] One polymorphic variant of NOV11a has been identified and is shown in Table D8.

	TABLE D8
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379811	62	C	T	21	Pro	Leu

[0977] NOV12a SNP Data:

[0978] Two polymorphic variants of NOV12a have been identified and are shown in Table D9.

	TABLE D9
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13377332	461	T	C	145	Leu	Pro
13377331	473	T	C	149	Leu	Pro

[0979] NOV13a SNP Data:

[0980] One polymorphic variant of NOV13a has been identified and is shown in Table D10.

	TABLE D10
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379842	236	T	C	79	Val	Ala

[0981] NOV14a SNP Data:

[0982] Four polymorphic variants of NOV14a have been identified and are shown in Table D11.

	TABLE D11
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379829	14	T	C	0
13379827	124	C	T	37	Pro	Leu
13379825	576	C	T	188	Leu	Phe
13379824	675	C	T	221	Leu	Leu

[0983] NOV15a SNP data:

[0984] Ten polymorphic variants of NOV15a have been identified and are shown in Table D12.

	TABLE D12
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379865	1039	A	G	290	Gly	Gly
13379864	1884	T	C	572	Val	Ala
13379863	3619	G	C	1150	Leu	Leu
13379860	7248	T	C	2360	Leu	Pro
13379859	7505	C	A	2446	Leu	Ile
13379858	8017	G	A	2616	Lys	Lys
13379857	8237	A	T	2690	Met	Leu
13379856	8515	T	C	2782	His	His
13379867	8611	G	A	2814	Pro	Pro
13379868	8689	T	C	2840	Phe	Phe

[0985] NOV16a SNP data:

[0986] One polymorphic variant of NOV16a has been identified and is shown in Table D13.

	TABLE D13
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379817	1300	A	G	427	Ser	Gly

[0987] NOV22a SNP data:

[0988] One polymorphic variant of NOV22a has been identified and is shown in Table D14.

	TABLE D14
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379940	1864	A	G	0

[0989] NOV25a SNP data:

[0990] One polymorphic variant of NOV25a has been identified and is shown in Table D15.

	TABLE D15
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379938	994	T	C	332	Cys	Arg

[0991] NOV27a SNP data:

[0992] Five polymorphic variants of NOV27a have been identified and are shown in Table D16.

	TABLE D16
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379875	1309	T	C	403	Asn	Asn
13379874	1709	G	A	537	Asp	Asn
13379873	1713	A	G	538	Lys	Arg
13379872	1777	T	C	559	Asn	Asn
13379871	1843	C	T	581	Asp	Asp

[0993] NOV28a SNP data:

[0994] Four polymorphic variants of NOV28a have been identified and are shown in Table D17.

	TABLE D17
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379839	248	C	T	78	Leu	Leu
13379838	880	C	T	288	Asn	Asn
13379837	883	C	G	289	Thr	Thr
13379836	1078	G	T	354	Val	Val

[0995] NOV32a SNP data:

[0996] Eleven polymorphic variants of NOV32a have been identified and are shown in D18.

	TABLE D18
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13378189	33	G	T	11	Leu	Leu
13378332	68	A	G	23	His	Arg
13375660	197	T	C	66	Ile	Thr
13376793	266	T	C	89	Leu	Pro
13379841	699	T	C	233	Phe	Phe
13375659	833	T	C	278	Phe	Ser
c110.5826	1145	G	C	382	Ser	Thr
c110.6324	1146	C	G	382	Ser	Arg
13377867	1193	G	A	398	Arg	Gln
13376792	1247	T	C	416	Leu	Pro
13374618	1264	G	A	422	Val	Ile

[0997] NOV40a SNP data:

[0998] Two polymorphic variants of NOV40a have been identified and are shown in Table D19.

	TABLE D19
	Nucleotides	Amino Acids
	Base			Base
	Position			Position
	of	Wild-		of	Wild-
Variant	SNP	type	Variant	SNP	type	Variant
13379845	722	C	T	239	Asn	Asn
13379846	1298	C	T	431	Pro	Pro

Example E

[0999] Each of the clones listed below is related to a clone or family of clones listed in Example A. The relationship is identifiable as the clone listed below will have the same NOVX number as the clones to which it is related. For example, NOV30g below is related to the NOV30 family of Example A.

[1000] The NOV30g and NOV30h clones were analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E1.

                 TABLE E1
                 SEQ ID NO: 111 728 bp
NOV30g,          AGTCTTGCCTTCTTTTGAGCCTAAGTCATGAGTTGGATGTTCCTCAGAGATCTCCTGAGT
CG56315-01
DNA Sequence     GGAGTAAATAAATACTCCACTGGGACTGGATGGATTTGGCTGGCTGTCGTGTTTGTCTTC
                 CGTTTGCTGGTCTACATGGTGGCAGCAGAGCACGTGTGGAAAGATGAGCAGAAAGAGTTT
                 GAGTGCAACAGTAGACAGCCCGGTTGCAAAAATGTGTGTTTTGATGACTTCTTCCCCATT
                 TCCCAAGTCAGACTTTGGGCCTTACAACTGATAATGGTCTCCACACCTTCACTTCTGGTG
                 GTTTTACATGTAGCCTATCATGAGGGTAGAGAGAAAAGGCACAGAAAGAAACTCTATGTC
                 AGCCCAGGTACAATGGATGGGGGCCTATGGTACGCTTATCTTATCAGCCTCATTGTTAAA
                 ACTGGTTTTGAAATTGGCTTCCTTGTTTTATTTTATAAGCTATATGATGGCTTTAGTGTT
                 CCCTACCTTATAAAGTGTGATTTGAAGCCTTGTCCCAACACTGTGGACTGCTTCATCTCC
                 AAACCCACTGAGAAGACGATCTTCATCCTCTTCTTGGTCATCACCTCATGCTTGTGTATT
                 GTGTTGAATTTCATTGAACTGAGTTTTTTGGTTCTCAAGTGCTTTATTAAGTGCTGTCTC
                 CAAAAATATTTAAAAAAACCTCAAGTCCTCAGTGTGTGAGTGCCACAGCCTCAGATATGT
                 TGAATGTG
                 SEQ ID NO: 112 223 aa
NOV30g,          MSWMFLRDLLSGVNKYSTGTGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGC
CG56315-01
Protein Sequence KNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGL
                 WYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFI
                 LFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV
                 SEQ ID NO: 113 727 bp
NOV30h,          AGTCTTGCTTCTTTTGAGCCTAAGTCATGAGTTGGATGTTCCTCAGAGATCTCCTGAGTG
CG56315-02
DNA Sequence     GAGTAAATAAATACTCCACTGGGATTGGATGGATTTGGCTGGCTGTCGTGTTTGTCTTCC
                 GTTTGCTGGTCTACATGGTGGCAGCAGAGCACGTGTGGAAAGATGAGCAGAAAGAGTTTG
                 AGTGCAACAGTAGACAGCCCGGTTGCAAAAATGTGTGTTTTGATGACTTCTTCCCCATTT
                 CCCAAGTCAGACTTTGGGCCTTACAACTGATAATGGTCTCCACACCTTCACTTCTGGTGG
                 TTTTACATGTAGCCTATCATGAGGGTAGAGAGAAAAGGCACAGAAAGAAACTCTATGTCA
                 GCCCAGGTACAATGGATGGGGGCCTATGGTACGCTTATCTTATCAGCCTCATTGTTAAAA
                 CTGGTTTTGAAATTGGCTTCCTTGTTTTATTTTATAAGCTATATGATGGCTTTAGTGTTC
                 CCTACCTTATAAAGTGTGATTTGAAGCCTTGTCCCAACACTGTGGACTGCTTCATCTCCA
                 AACCCACTGAGAAGACGATCTTCATCCTCTTCTTGGTCATCACCTCATGCTTGTGTATTG
                 TGTTGAATTTCATTGAACTGAGTTTTTTGGTTCTCAAGTGCTTTATTAAGTGCTGTCTCC
                 AAAAATATTTAAAAAAACCTCAAGTCCTCAGTGTGTGAGTGCCACAGCCTCAGATATGTT
                 GAATGTG
                 SEQ ID NO: 114 223 aa
NOV30h,          MSWMFLRDLLSGVNKYSTGIGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGC
CG56315-02
Protein Sequence KNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGL
                 WYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFI
                 LFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV

[1001] The NOV33g clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E2.

                 TABLE E2
                 SEQ ID NO: 147 1120 bp
NOV33g           GAGGCCATGCCCGCTTCCTCTCTTCCAGGAAAGCTCTGGTTCGTCCTCACGATGCTGCTG
CG57658-01
DNA Sequence     CGGATGCTGGTGATTGTCTTGGCGGGGCGACCCGTCTACCAGGACGAGCAGGAGAGGTTT
                 GTCTGCAACACGCTGCAGCCGGGATGCGCCAATGTTTGCTACGACGTCTTCTCCCCCGTG
                 TCTCACCTGCGGTTCTGGCTGATCCAGGGCGTGTGCGTCCTCCTCCCCTCCGCCGTCTTC
                 AGCGTCTATGTCCTGCACCGAGGAGCCACGCTCGCCGCGCTGGGCCCCCGCCGCTGCCCC
                 GACCCCCGGGAGCCGGCCTCCGGGCAGAGACGCTGCCCGCGGCCATTCGGGGAGCGCGGC
                 GGCCTCCAGGTGCCCGACTTTTCGGCCGGCTACATCATCCACCTCCTCCTCCGGACCCTG
                 CTGGAGGCAGCCTTCGGGGCCTTGCACTACTTTCTCTTTGGATTCCTGGCCCCGAAGAAG
                 TTCCCTTGCACGCGCCCTCCGTGCACGGGCGTGGTGGACTGCTACGTGTCGCGGCCCACA
                 GAGAAGTCCCTGCTGATGCTGTTCCTCTGGGCGGTCAGCGCGCTGTCTTTTCTGCTGGGC
                 CTCGCCGACCTGGTCTGCAGCCTGCGGCGGCGGATGCGCAGGAGGCCGGGACCCCCCACA
                 AGCCCCTCCATCCGGAAGCAGAGCGGAGCCTCAGGCCACGCGGAGGGACGCCGGACTGAC
                 GAGGAGGGTGGGCGGGAGGAAGAGGGGGCACCGGCGCCCCCGGGTGCACGCGCCGGAGGG
                 GAGGGGGCTGGCAGCCCCAGGCGTACATCCAGGGTGTCAGGGCACACGAAGATTCCGGAT
                 GAGGATGAGAGTGAGGTGACATCCTCCGCCAGCGAAAAGCTGGGCAGACAGCCCCGGGGC
                 AGGCCCCACCGAGAGGCCGCCCAGGACCCCAGGGGCTCAGGATCCGAGGAGCAGCCCTCA
                 GCAGCCCCCAGCCGCCTGGCCGCGCCCCCTTCCTGCAGCAGCCTGCAGCCCCCTGACCCG
                 CCTGCCAGCTCCAGTGGTGCTCCCCACCTGAGAGCCAGGAAGTCTGAGTGGGTGTGAAAA
                 AAACAGCACCTGGCGGTGCCCCGGGGCTCACGCCTGTAAT
                 SEQ ID NO: 148 356 aa
NOV33g,          MPASSLPGKLWFVLTMLLRMLVIVLAGRPVYQDEQERFVCNTLQPGCANVCYDVFSPVSH
CG57658-01
Protein Sequence LRFWLIQGVCVLLPSAVFSVYVLHRGATLAALGPRRCPDPREPASGQRRCPRPFGERGGL
                 QVPDFSAGYIIHLLLRTLLEAAFGALHYFLFGFLAPKKFPCTRPPCTGVVDCYVSRPTEK
                 SLLMLFLWAVSALSFLLGLADLVCSLRRRMRRRPGPPTSPSIRKQSGASGHAEGRRTDEE
                 GGREEEGAPAPPGARAGGEGAGSPRRTSRVSGHTKIPDEDESEVTSSASEKLGRQPRGRP
                 HREAAQDPRGSGSEEQPSAAPSRLAAPPSCSSLQPPDPPASSSGAPHLRARKSEWV

[1002] The NOV34b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E3.

                 TABLE E3
                 SEQ ID NO: 151 1400 bp
NOV34b,          ATTCTCCCCAAACGCCAGGGATGGGGGTCATGGCTCCCCGAACCCTCCTCCTGCTGCTCT
CG57664-01
DNA Sequence     TGGGGGCCCTGGCCCTGACCGAGACCTGGGCCGGTGAGTGCGGGGTCGGGAGGGAAAGGG
                 CCTCTGCGGGGAGAAGCGAGTGGCCCGCCCGGCCCGGGGAGCCGCGCCTCAGCCTCTCCT
                 CGCCTCCAGGCTCCCACTCCTTGAGGTATTTCAGCACCGCAGTGTCCCAGCCCGGCCGCG
                 GGGAGCCCCGGTTCATCGCCGTGGGCTACGTGGACGACACAGAGTTCGTGCGGTTCGACA
                 GCGACTCCGTGAGTCCGAGGATGGAGCGGCGGGCGCCGTGGGTGGAGCAGGAGGGGCTGG
                 AGTATTGGGACCAGGAGACACGGAACGCCAAGGGCCACGCGCAGATTTACCGAGTGAACC
                 TGCGGACCCTGCTCCGCTATTACAACCAGAGCGAGGCCGGTGGTTCTCACACCATCCAGA
                 GGAAGCATGACTGCGACGTGGGCCCGACAGGCGGGCCCGACAGGCGCCTCCTCCGCAGGT
                 ATGAACAGTTCGCCTACGATGGCAAGGATTACATCGCCCTGAACGAGGACCTGCCCTCCT
                 GGACCGCCGCGAACACAGCGGCTCAGATCTCCCAGCACAAGTGGGAAGCGGACAAATACT
                 CAGAGCAGGTCAGGGCCTACCTGAGGGCAAGTGCATGGAGTGGCGAGGGCAAGTGCATGG
                 AGTGGCTCCGCAGACACCTGGAGAACGGGAAGGAGACGCTGCAGCGCGCGTCAGATCCCC
                 CAAAGGCACATGTGACCCAGCACCCCGTCTCTGACCATGAGGCCACCCTTGAGGTGCTGG
                 GCCCTGGGCCTCTACCCTTGAGGTGCTGGGCCCTGGGCCTCTACCCTGCGGAGATCACAC
                 TGACCTGGCAGCAGGATGGGGAGGACCAGACCCAGGACACGGAGCTTGTGGAGACCAGGC
                 CTGCAGGGGACGGAACCTTCCAGAAGTGGGTGGCTGTAGTGGTGCCTTCCGGAGAGGAGC
                 AGAGATACATGTGCCATGTGCAGCATGAGGGGCTGCCAGAGCCCCTCACCCTGAGATGGC
                 CCTCACCTCCCTCTCCTTTCCCAGAGCCGTCTTCTCAGCCCACCATCCCCATCGTGGGCA
                 TCGTTGCTGGCCTGTTTCTCCTTGGAGCTGTGGTCACTGGAGCTGTGGTTGCTGCTGTGA
                 TGAAGAGGAAGAAAAGCTCAGGTAGGGAAGGGGTGAGAGGTGGGATCTGGGTTTTCTTGT
                 TCCACTGTGGGTTTCAAGCCACAGGTAGAATTGTGACTTGCTTCATCACTGGGAAGCACC
                 GTCCACACACAGGCCGACCTAGCCTGGGGCCCTGTGTGCCAACACTTGCTCTTTTGTGAA
                 GCACATGTGAAAACGAAGGA
                 SEQ ID NO: 152 452 aa
NOV34b,          MGVMAPRTLLLLLLGALALTETWAGECGVGRERASAGRSEWPARPGEPRLSLSSPPGSHS
CG57664-01
Protein Sequence LRYFSTAVSQPGRGEPRFIAVGYVDDTEFVRFDSDSVSPRMERPAPWVEQEGLEYWDQET
                 RNAKGHAQIYRVNLRTLLRYYNQSEAGGSHTIQRKHDCDVGPTGGPDRRLLRRYEQFAYD
                 GKDYIALNEDLPSWTAANTAAQISQHKWEADKYSEQVRAYLRASAWSGEGKCMEWLRRHL
                 ENGKETLQRASDPPKAHVTQHPVSDHEATLEVLGPGPLPLRCWALGLYPAEITLTWQQDG
                 EDQTQDTELVETRPAGDGTFQKWVAVVVPSGEEQRYMCHVQHEGLPEPLTLRWPSPPSPF
                 PEPSSQPTIPIVGIVAGLFLLGAVVTGAVVAAVMKRKKSSGREGVRGGIWVFLFHCGFQA
                 TGRIVTCFITGKHRPHTGRPSLGPCVPTLALL

[1003] The NOV35b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E4.

                 TABLE E4
                 SEQ ID NO: 155 1159 bp
NOV35b,          TCTCCCCAGACGCCGAGGATGGTGCTCATGGCGCCCCGAACCCTCCTCCTGCTGCTCTCA
CG57668-01
DNA Sequence     GGGGCCCTGACCCAGACCTGGGCGCGTTCCCACTCCATGAGGTATTTCTACACCACCATG
                 TCCCGGCCCGGCCGCGGGGAGCCCCGCTTCATCTCCGTCGGCTACGTGGACTATACGCAG
                 TTCGTGCGGTTCGACAGCGACGACGCGAGTCCGAGAGAGGAGCCGCGGGCGCCGTGGATG
                 GAGCGGGAGGGGCCGGAGTATTGGGACCGGAACACACAGATCTGCAAGGCCCAAGCACGG
                 ACTGAACGAGAGAACCTGCGGATCGCGCTCCGCTACTACAACCAGAGCGAGGGCGGTGGT
                 TCCCACACCATGCAGGTGATGTATGGCTGCGACGTGGGGCCCGACGGGCGCTTCCTCCGC
                 GGGTATGAACAGCACGCCTACGACGGCAAGGATTACATCGCTCTGAACGAGGACCTGCGC
                 TCCTGGACCGCGGCGGACATGGCAGCTCAGATCACCAAGCGCAAGTGGGAGGCGGCCCGT
                 GTGGCGGAGCAGCTGAGAGCCTACCTGGAGGGCGAGTTCGTGGAGTGGCTCCGCAGATAC
                 CTGGAGAACGGGAAGGAGACGCTGCAGCGCGCGTCAGACCCCCCCAAGACACATATGACC
                 CACTACCCCATCTCTGACCATGAGGCCACCCTGAGGTGCTGGGCCCTGGGCTTCTACCCT
                 GCGGAGATCACACTGACCTGGCAGCGGGATGGGGAGGACCAGACCACGGAGCTCGTGGAG
                 ACCAGGCCTGCAGGGGATGGAACCTTCCAGAAGTGGGCGGCTGTGGTGGTGCCTTCTGGA
                 GAGGAGCAGAGATACACCTGCCATGTGCAGCATGAGGGTCTGCCCGAGCCCCTCACCCTG
                 AGATGGCAGGGTCAGGGTCCCTCACCTTCCCCCCTTTTCCCAGAGCCATCTTCCCAGCCC
                 ACCATCCCCATCGTGGGCATCATTGCTGGCCTGGTTCTACTTGTAGCTGTGGTCACTGGA
                 GCTGTGGTCACTGCTGTAATGTGGAGGAAGAAGAGCTCAGGTAAGGAAGGGGATGGGTAT
                 TCTACTCCAGGCGGCAACAGTGCCCAGGGCTCTGATGTGTCTCTCACGGCGTGAAAGGTG
                 AGACCTTGGGGGGCCTGAT
                 SEQ ID NO: 156 371 aa
NOV35b,          MVLMAPRTLLLLLSGALTQTWARSHSMRYFYTTMSRPGRGEPRFISVGYVDYTQFVRFDS
CG57668-01
Protein Sequence DDASPREEPRAPWMEREGPEYWDRNTQICKAQARTERENLRIALRYYNQSEGGGSHTMQV
                 MYGCDVGPDGRFLRGYEQHAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAARVAEQLR
                 AYLEGEFVEWLRRYLENGKETLQRASDPPKTHMTHYPISDHEATLRCWALGFYPAEITLT
                 WQRDGEDQTTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWQGQG
                 PSPSPLFPEPSSQPTIPIVGIIAGLVLLVAVVTGAVVTAVMWRKKSSGKEGDGYSTPGGN
                 SAQGSDVSLTA

[1004] The NOV36b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E5.

                 TABLE E5
                 SEQ ID NO: 159 1210 bp
NOV36b,          TCGCTCACCCACCCGGACTCATTCTCCCCAGACGCCAAGGATGGTGGTCATGGCACCCCG
CG59256-01
DNA Seuence      AACCCTCTTCCTGCTACTCTCGGGGGCCCTGACCCTGACCGAGACCTGGGCGGGCTCCCA
                 CTCCATGAGGTATTTCAGCGCCGCCGTGTCCCGGCCCGCCCGCCGGGAGCCCCGCTTCAT
                 CGCCATGGGCTACGTGGACGACACGCAGTTCGTGCGGTTCGACAGCGACTCGGCGTGTCC
                 GAGGATGGAGCCGCGGGCGCCGTGGGTGGAGCAGGAGGGGCCAGAGTATTGGGAAGAGGA
                 GACACGGAACACCAAGGCCCACGCACAGACTGACAGAATGAACCTGCAGACCCTGCGCGG
                 CTACTACAACCAGAGCGAGGGGGTGGGGCCAGGTTCTCATACCCTCCAGTGGATGATTGG
                 CTGCGACCTGGGGTCCGACGGACGCCTCCTCCGCGGGTATGAACAGTATGCCTACGATGG
                 CAAGGATTACCTCGCCCTGAACGAGGACCTGCGCTCCTGGACCGCACCGGACACTGCGGC
                 TCAGATCTCCAAGCGCAAGTGTGAGGCGGCCAATGTGGCTGAACAAAGGAGAGCCTACCT
                 GCACGGCACGTGCGTGGAGTGGCTCCACAGATACCTGGAGAACGGGAAGGAGATGCTGCA
                 GCGCGCGGACCCCCCCAAGACACACGTGACCCACCACCCTGTCTTTGACTATCAGGCCAC
                 CCTGAGGTGCTGGGCCCTGGGCTTCTACCCTGCGGAGATCATACTGACCTGGCACCGGGA
                 TCGGGAGGACCAGACCCAGGACGTGGAGCTCGTGGAGACCAGGCCTGCAGGGGATGGAAC
                 CTTCCAGAAGTGGCCAGCTGTGGTGGTGCCTTCTGGAGAGGAGCAGAGATACACGTGCCA
                 TGTGCAGCATGAGGGGCTGCCGGAGCCCCTCATGCTGAGATGGGAGCAGTCTTCCCTGCC
                 CACCATCCCCATCATGGGTATCGTTGCTGGTCTGGTTGTCCTTGCAGCTGTAGTCACTGG
                 AGCTGCGGTCGCTGCTGTGCTGTGGAGGAAGAAGAGCTCAGGTAAGAAAGGAGGGAGCTA
                 CTCTCAQGCTGCAAGTAGTGACAGTGCCCAGGGCTCTAATGTGTCTCTCACGGCTTGTAA
                 ATGTGACACCCCGGGGGGCCTGATGTGTGTGGGTTGTTGAGGGAAACAGTGGACATAGCT
                 GTGCTATGAC
                 SEQ ID NO: 160 379 aa
NOV36b,          MVVMAPRTLFLLLSGALTLTETWAGSHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRF
CG59256-01
Protein Sequence DSDSACPRMEPRAPWVEQEGPEYWEEEThNTKAHAQTDRMNLQTLRGYYNQSEGVGPGSH
                 TLQWMIGCDLGSDGRLLRGYEQYAYDGKDYLALNEDLRSWTAADTAAQISKRKCEAANVA
                 EQRRAYLEGTCVEWLHRYLENCKEMLQRADPPKTHVTHHPVFDYEATLRCWALGFYPAEI
                 ILTWQRDGEDQTQDVELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLR
                 WEQSSLPTIPIMGIVAGLVVLAAVVTGAAVAAVLWRKKSSGKKGGSYSQAASSDSAQGSN
                 VSLTACKCDTPGGLMCVGC

[1005] The NOV39b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E6.

                 TABLE E6
                 SEQ ID NO: 173 1266 bp
                 NOV39b, ATGGCGCCCCGAACCCTCCTCCTGCTGCTCTCGGGGACCCTGGCCCTGGCCGAGACCTGG
                 CG94630-01,
                 DNA Sequence   GCGGGCTCCCACTCCATGAGGTATTTCAGCACCGCCGTTTCCTGGCCGGGCCGCGGGGAG
                                CCCAGCTTCATTGCCGTGGGCTACGTGGACGACACGCAGTTCGTGCGGGTCGACAGTGAC
                                GCCGTGAGTCTGACCATGAAGACGCGGGCGCGGTGGGTGGAGCAGGAGGGGCCGGAGTAT
                                TGGGACCTACAGACACTGGGCGCCAAGGCCCAGGCACAGACTGACCGAGTGAACCTGCGG
                                ACCCTGCTCCGCTACTACAACCAGAGCGAGGCGGGGTATCACATCCTCCAGGGAATGTTT
                                GGCTGCGACCTGGGGCCCGACGGGCGTCTCCTCCGCGGGTATGAGCAGTATGCCTACGAC
                                GGCAAGGATTACATCGCCCTGAACGAGGACCTCCCCTCCTGGACCGCCGCGGATACCGCG
                                GCTCAGATTACCCAGCGCAAGTATGAGGCGGCCAATGTGGCTGAGCAAAGGAGAGCCTAC
                                CTGGAGGGCACCTGCATGQAQTGGCTCCGCAGACACCTGGAGAACGGGAAGGAGACCCTG
                                CAGCGCGCGGGCATAACGAGGTCCTGGGTTCTGGGCTTCTACCCTGCGGAGATCACATTG
                                ACCTGGCAGCGGGATGGGGAGGACCAGACCCAGGACATGGAGCTCGTGGAGACCAGGCCC
                                ACAGGGGATGGAACCTTCCAGAAGTGGGCGGTTGTGGTAGTGCCTTCTGGAGAGGAACAG
                                AGATACACATGCCATGTGCAGCACAAGGGGCTGCCCAAGCCCCTCATCCTGAGATGGGAG
                                CCCTCTCCCCAGCCCACCATCCCCATTGTGGGTATCATTGCTGGCCTGGTTCTCCTTGGA
                                GCTGTGGTCACTGGAGCTGTGGTCACTGCTGTGATGTGGAGGAAGAAGAGCTCAGATAGA
                                AAAGGAGGGAGCTACTCTCAGGCTGCAAAAAACATCATTAAAGTAAAAACAGAAAAATTT
                                CTGGCCTTGTGGTGTATACGTTCTAGATGCAAGCTTGTCCAACCTGCAGCTCTCGGGCTG
                                CGTGTGGCCCGGGACAGCTTTGAATTTCCCTCCCTTGACTCCATCAACATCGGCACCTGC
                                CAGACGCCCACCACCCACCATCGAAGTGCTGAGAAGAAGTGCAAGGTACTCAACCTGCTC
                                TGGGGATACAGCAGGAAAGCAGAGTGTTTACGGATTTCACATTCCATCAAAGAAAATCCA
                                TTTTGA
                 SEQ ID NO: 174 421 aa
NOV39b,          MAPRTLLLLLSGTLALAETWAGSHSMRYFSTAVSWPGRGEPSFIAVGYVDDTQFVRVDSD
CG94630-01
Protein Sequence AVSLRMKTRARWVEQEGPEYWDLQTLGAKAQAQTDRVNLRTLLRYYNQSEAGYHILQGMF
                 GCDLGPDGRLLRGYEQYAYDGKDYIALNEDLRSWTAADTAAQITQRKYEAANVAEQRRAY
                 LEGTCMEWLRRHLENGKETLQRAGITRSNXTLGFYPAEITLTWQRDGEDQTQDMELVETRP
                 TGDGTFQKWAVVVVPSGEEQRYTCHVQHKGLPKPLILRWEPSPQPTIPIVGIIAGLVLLG
                 AVVTGAVVTAVMWRKKSSDRKGGSYSQAAKNIIKVKTEKFLALWCIRSRCKLVQPAALCL
                 RVARDSFEFPSLDSINIGTCQTPTTHHRSAEKKCKVLNLLWGYSRKAECLRISHSIKENP
                 F

Example F

[1006] Polynucleotide and Polypeptide Sequences, and Homology Data

Example 1

[1007] The NOV41 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table F1A.

TABLE F1A
NOV41 Sequence Analysis
	SEQ ID NO: 177	1050 bp
NOV41a,	TCGCCATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAGGTGAT
CG55676-01
DNA Sequence	GCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATCGGGTCGCCCTG
	TGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTTCAATT
	TGGCCGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTATTACCT
	CAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCACGTTG
	GCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGACAGGTATT
	TCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCGGCTGG
	CATCCTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGCTGGAG
	AACCATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGAGTCGG
	CCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATOCCCCTCGGCATCAT
	CTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGGCCAGA
	CAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTTCATCA
	CATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCCTCGAG
	TGCCTGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCTACATG
	AACAGCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAAATTCT
	ACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCAAAAACACA
	AAGGCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTGTGGCA
	AATAGTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTGGCACT
	GAACAA
	ORE Start: ATG at 6	ORE Stop: TGA at 1044
	SEQ ID NO: 178	346 aa	MW at 39294.8kD
NOV41a,	MYNGSCCRIEGDTISQVNPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA
CG55676-01
Protein Sequence	VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFK
	VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAN
	GWHDIMPQLEFPMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC
	YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN
	KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH
	SEQ ID NO: 179	1104 bp
NOV41b,	GTGCCATTGTGGGGACTCCCTGGGCTGCTCTGCACCCGGACACTTGCTCTGTCCCCGC
CG55676-02
DNA Sequence	CATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAGGTGATGCCG
	CCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCGCCCTGTGTG
	GTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTTCAATTTGGC
	CGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTATTACCTCAOA
	CGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCACGTTGGCCA
	TGAACAGGGCCGGCAGCATCGTGTTCCTTACGGTGGTGGCTGCGGGCAGGTATTTCAA
	AGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCGGCTGGCATC
	GTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGCTGGAGAACC
	ATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGAGTCGGCCAA
	TGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGCATCATCTTA
	TTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGGCCAGACAGG
	CTCGGATGAAGAAGGCGACCCGCTTCATCATGGTGGTGGCAATTGTGTTCATCACATG
	CTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCCTCGAGTGCC
	TGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCTACATGAACA
	GCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAAATTCTACAA
	CAAGCTCAAAATCTGCACTCTGAAACCCAAGCAGCCAGGACACTCAAAAACACAAAGG
	CCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTGTGGCAAATA
	GTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTGGCACTGAAC
	AA
	ORF Start: ATG at 60	ORF Stop: TGA at 1098
	SEQ ID NO: 180	346 aa	MW at 39236.8kD
NOV41b,	MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA
CG55676-02
Protein Sequence	VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAAGRYFK
	VVHPHHAVNTTSTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESEIMESAN
	GWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC
	YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN
	KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH
	SEQ ID NO: 181	1104 bp
NOV41c,	GTGCCATTGTGGGGACTCCCTGGGCTGCTCTGCACCCGGACACTTGCTCTGTCCCCGC
CG55676-03
DNA Sequence	CATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAGGTGATGCCG
	CCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGACAATGGGGTCCCCCTGTGTG
	GTTTCTGCTTCCACATGAAGACCTGGPAGCCCAGCACTGTTTACCTTTTCAATTTGGC
	CGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTATTACCTCAGA
	CGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTCGGGCTCTTCACGTTGGCCA
	TGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGCCAGGTATTTCAA
	AGTGGTCCACCCCCACCACCCGGTGAACACTATCTCCACCCGGGTGGCGGCTGGCATC
	GTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGCTGGAGAACC
	ATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGAGTCGGCCAA
	TGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGCATCATCTTA
	TTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGGCCAGACAGG
	CTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTTCATCACATG
	CTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCCTCGAGTGCC
	TGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCTACATGAACA
	GCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAAATTCTACAA
	CAAGCTCAAAATCTGCAGTCTGAAACCCPAGCAGCCAGGACACTCAAAAACACAAAGG
	CCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTGTGGCAAATA
	GTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTGGCACTGAAC
	AA
	ORF Start: ATG at 60	ORF Stop: TGA at 1098
	SEQ ID NO: 182	346 aa	MW at 39294.8kD
NOV41c,	MYNGSCCRIEGDTISQVMPPLLIVAFVLGALDNGVALCGFCFHMKTWKPSTVYLFNLA
CG55676-03
Protein Sequence	VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAAGRYFK
	VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAN
	GWHDIMFQLEFPMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC
	YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN
	KLKICSLKRKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH
	SEQ ID NO: 183	1057 bp
NOV41d,	CACCAGATCTATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAG
CG55676-04
DNA Sequence	GTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCG
	CCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTT
	CAATTTGGCCGTGGCTGATTTCCTCCTTATCATCTGCCTGCCTTTTCGGACAGACTAT
	TACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCA
	CGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTCGTCGCTGCGGACAG
	GTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCG
	GCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGC
	TGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGA
	GTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGC
	ATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCACCAGCTGG
	CCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTT
	CATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCC
	TCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCT
	ACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAA
	ATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCAAAA
	ACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTCCATCAGTG
	TGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGCGATCCCCACATTGTTGAGTG
	GCACAAGCTTGGC
	ORF Start: ATG at 11	ORF Stop: at 1049
	SEQ ID NO: 184	346 aa	MW at 39294.8kD
NOV41d,	MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA
CG55676-04
Protein Sequence	VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFK
	VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAN
	GWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC
	YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN
	KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSPQSQSDGQWDPHIVEWH
	SEQ ID NO: 185	961 bp
NOV41e,	CACCAGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG
CG55676-05
Protein Sequence	CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC
	TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC
	CTGCCGAGTGGGGCTCTTCACGTTCGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT
	ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA
	CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT
	TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG
	AGTTCTTTATCCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCT
	GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC
	ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCT
	ATTTCCTCTGGACGGTGCCCTCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCA
	CATAACCCTCAGCTTCACCTACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTT
	TCAAGCCCCTCCTTTCCCAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCA
	AGCAGCCAGGACACTCAAAAACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGG
	TCGCAGGAGTTGCATCAGTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGG
	GATCCCCACATTGTTGAGTGGCACAAGCTTGGC
	ORE Start: at 11	ORE Stop: at 953
	SEQ ID NO: 186	314 aa	MW at 35943.9kD
NOV41e,	NGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRV
CG55676-05
Protein Sequence	GLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTV
	YLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRR
	QQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALHITL
	SFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLGRRS
	CISVANSPQSQSDGQWDPHIVEWH
	SEQ ID NO: 187	1060 bp
NOV41f,	CACCTCGCGAACCATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCC
CG55676-06
DNA Sequence	CAGGTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGG
	TCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCACCACTGTTTACCT
	TTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGCACAGAC
	TATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGCCTCT
	TCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGA
	CAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTG
	GCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGCGAACAGTCTATCTTT
	TGCTGGAGAACCATCTCTGCGTGCAACAGACCCCCGTCTCCTGTGAGAGCTTCATCAT
	GGAGTCGGCCAATGGCTGGCATGACATCATGTTCCACCTGCAGTTCTTTATCCCCCTC
	GGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGC
	TGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGT
	GTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTG
	CCCTCGAGTGCCTGCQATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCA
	CCTACATGAACAGCATGCTGGATCCCCTGGTCTATTATTTTTCAAGCCCCTCCTTTCC
	CAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCA
	AAAACACAAACCCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCA
	GTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGA
	GTGCCACGTCGACGGC
	ORF Start: at 14	ORF Stop: at 1052
	SEQ ID NO: 188	346 aa	MW at 39294.8kD
NOV41f,	MYNGSCCRIEGDTISQVNPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA
CG55676-06
Protein Sequence	VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFK
	VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAV
	GWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC
	YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN
	KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH
	SEQ ID NO: 189	961 bp
NOV41g,	CACCTCGCGAAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG
CG556676-07
DNA Sequence	CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC
	TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC
	CTGCCGAGTGGGGCTCTTCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT
	ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA
	CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT
	GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC
	TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG
	AGTTCTTTATGCCCCTCGGCATCATCTTATTTTCCTCCTTCAAGATTGTTTGGAGCCT
	GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC
	ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCT
	ATTTCCTCTGGACGGTGCCCTCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCA
	CATAACCCTCAGCTTCACCTACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTT
	TCAAGCCCCTCCTTTCCCAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCA
	AGCAGCCAGGACACTCAAAAACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGG
	TCGCAGGAGTTGCATCAGTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGG
	GATCCCCACATTGTTGAGTGGCACGTCGACGGC
	ORF Start: at 2	ORF Stop: end of sequence
	SEQ ID NO: 190	320 aa	MW at 36559.5kD
NOV41g,	TSRNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIP
CG55676-07
Protein Sequence	CRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVIL
	GTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSL
	RRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALH
	ITLSPTYMNSMLDPLVYYFSSRSFRKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLG
	RRSCISVANSFQSQSDGQWDPHIVEWHVDG
	SEQ ID NO: 191	1057 bp
NOV41h,	CACCAGATCTATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAG
248209538 DNA
Sequence	GTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCG
	CCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTT
	CAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTAT
	TACCTCAGACGTAGACACTGGGCTTTTGGGCACATTCCCTGCCGAGTGGGGCTCTTCA
	CGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCCGACAG
	GTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCG
	GCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGC
	TGCAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGA
	GTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATCCCCCTCGGC
	ATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGACGCGGAOGCAGCAGCTGG
	CCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTCGTCCCAATTGTGTT
	CATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCC
	TCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCT
	ACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAA
	ATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCAAAA
	ACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTG
	TGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTG
	GCACAAGCTTGGC
	ORE Start: at 2	ORF Stop: end of sequence
	SEQ ID NO: 192	352 aa	MW at 39937.6kD
NOV41h,	TRSMYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLF
24820938
Protein Sequence	NLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADR
	YFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIME
	SANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVF
	ITCYLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPK
	FYNKLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEW
	HKLG
	SEQ ID NO: 193	961 bp
NOV41j,	CACCAGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG
248209591 DNA
Sequence	CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC
	TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC
	CTGCCGAGTGGGGCTCTTCACCTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT
	ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA
	CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT
	GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC
	TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG
	AGTTCTTTATGCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGACCCT
	GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCCGATGAAGAAGGCGACCCGGTTCATC
	ATGGTGGTCGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCT
	ATTTCCTCTGGACGGTGCCCTCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCA
	CATAACCCTCAGCTTCACCTACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTT
	TCAAGCCCCTCCTTTCCCAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCA
	AGCAGCCAGGACACTCAAAAACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGG
	TCGCAGGAGTTGCATCAGTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGG
	GATCCCCACATTGTTGAGTGGCACAAGCTTGGC
	ORE Start: at 2	ORF Stop: end of sequence
	SEQ ID NO: 194	320 aa	MW at 36586.6kD
NOV41i,	TRSNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIP
248209591
Protein Sequence	CRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVIL
	GTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSL
	RRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVP2SACDPSVHGALH
	ITLSFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRREEMPISNLG
	RRSCISVANSFQSQSDGQWDPHIVEWHKLG
	SEQ ID NO: 195	742 bp
NOV41j,	CACCAGATCTATGTACAACGGCTCGTCCTCCCCCATCCACCGCGACACCATCTCCCAG
248209663 DNA
Sequence	GTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCG
	CCCTGTGTGGTTTCTGCTTCCACATCAAGACCTGGAAGCCCAGCACTGTTTACCTTTT
	CAATTTGGCCGTCGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCCGACAGACTAT
	TACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCA
	CGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGACAG
	GTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCG
	GCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGC
	TGGAGAACCATCTCTGCGTGCAAGAGACCGCCGTCTCCTGTGAGAGCTTCATCATGGA
	GTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGC
	ATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGG
	CCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTT
	CATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCAAGCTTGGC
	ORE Start: at 2	ORE Stop: end of sequence
	SEQ ID NO: 196	247 aa	MW at 27932.0kD
NOV41j,	TRSMYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLF
248209663
Protein Sequence	NLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADR
	YFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIME
	SANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVF
	ITCYLPSVSARLKLG
	SEQ ID NO: 197	646 bp
NOV41k,	CACCAGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG
24809745 DNA
Sequence	CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC
	TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC
	CTGCCGAGTGGGGCTCTTCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT
	ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA
	CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT
	GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC
	TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG
	AGTTCTTTATGCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCT
	GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC
	ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCA
	AGCTTGGC
	ORE Start: at 2	ORF Stop: end of sequence
	SEQ ID NO: 198	215 aa	MW at 24581.1kD
NOV41k,	TRSNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIP
24809745
Protein Sequence	CRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVIL
	GTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSL
	RRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLKLG

[1008] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table F1B.

TABLE F1B
Comparison of NOV41a against NOV41b through NOV41k.
			Identities/
	Protein	NOV41a Residues/	Similarities for
	Sequence	Match Residues	the Matched Region
	NOV41b	1 . . . 346	333/346 (96%)
		1 . . . 346	333/346 (96%)
	NOV41c	1 . . . 346	332/346 (95%)
		1 . . . 346	332/346 (95%)
	NOV41d	1 . . . 346	334/346 (96%)
		1 . . . 346	334/346 (96%)
	NOV41e	33 . . . 346	302/314 (96%)
		1 . . . 314	302/314 (96%)
	NOV41f	1 . . . 346	334/346 (96%)
		1 . . . 346	334/346 (96%)
	NOV41g	33 . . . 346	302/314 (96%)
		4 . . . 317	302/314 (96%)
	NOV41h	1 . . . 346	334/346 (96%)
		4 . . . 349	334/346 (96%)
	NOV41i	33 . . . 346	302/314 (96%)
		4 . . . 317	302/314 (96%)
	NOV41j	1 . . . 241	229/241 (95%)
		4 . . . 244	229/241 (95%)
	NOV41k	33 . . . 241	197/209 (94%)
		4 . . . 212	197/209 (94%)

[1009] Further analysis of the NOV41a protein yielded the following properties shown in Table F1C.

TABLE F1C
Protein Sequence Properties NOV41a
PSort     0.6850 probability located in endoplasmic reticulum
analysis: (membrane); 0.6400 probability located in plasma
          membrane; 0.4600 probability located in Golgi body;
          0.1000 probability located in endoplasmic reticulum
          (lumen)
SignalP   Cleavage site between residues 33 and 34
analysis:

[1010] 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 F1D.

TABLE F1D
Geneseq Results for NOV41a
		NOV41a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
ABB08596	Human lipocyte-originated G	1 . . . 346	346/346 (100%)	0.0
	protein-coupled receptor protein	1 . . . 346	346/346 (100%)
	TGR13 - Homo sapiens, 346 aa.
	[WO200202767-A1, 10 JAN 2002]
AAO14788	Human purinergic-like G-protein	1 . . . 346	346/346 (100%)	0.0
	coupled receptor (AXOR87) -	1 . . . 346	346/346 (100%)
	Homo sapiens, 346 aa.
	[GB2365868-A, 27 FEB 2002]
AAE17077	Human G-protein coupled receptor	1 . . . 346	346/346 (100%)	0.0
	(GPCRx14) protein - Homo	1 . . . 346	346/346 (100%)
	sapiens, 346 aa.
	[WO200198330-A2, 27 DEC 2001]
AAE16172	Human G-protein coupled receptor 3	1 . . . 346	346/346 (100%)	0.0
	(GCREC-3) protein - Homo	1 . . . 346	346/346 (100%)
	sapiens, 346 aa.
	[WO200187937-A2, 22 NOV 2001]
AAU11401	HM74-like G-protein coupled receptor	1 . . . 346	346/346 (100%)	0.0
	(GPCR) - Homo sapiens, 346 aa.	1 . . . 346	346/346 (100%)
	[WO200177320-A2, 18 OCT 2001]

[1011] 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 F1E.

TABLE F1E
Public BLASTP Results for NOV41a
		NOV41a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched	Expect
Number	Protein/Organism/Length	Residues	Portion	Value
Q9BXC0	Putative chemokine receptor	1 . . . 346	346/346 (100%)	0.0
	(G protein-coupled receptor)	1 . . . 346	346/346 (100%)
	(Putative G-protein coupled
	receptor) - Homo sapiens (Human),
	346 aa.
Q8TDS4	Putative G-protein coupled receptor -	5 . . . 340	180/341 (52%)	6e−94
	Homo sapiens (Human), 363 aa.	17 . . . 355	227/341 (65%)
BAC06083	Seven transmembrane helix	5 . . . 340	178/341 (52%)	1e−93
	receptor - Homo sapiens (Human),	17 . . . 355	227/341 (66%)
	387 aa.
P49019	Probable G protein-coupled	5 . . . 340	178/341 (52%)	1e−93
	receptor HM74 - Homo sapiens	17 . . . 355	227/341 (66%)
	(Human), 387 aa.
Q9EP66	Putative seven transmembrane	5 . . . 316	176/317 (55%)	4e−92
	spanning receptor - Mus musculus	14 . . . 329	215/317 (67%)
	(Mouse), 360 aa.

[1012] PFam analysis predicts that the NOV41a protein contains the domains shown in the Table F1F.

TABLE F1F
Domain Analysis of NOV41a
			Identities/
			Similarities for
	Pfam	NOV41a	the Matched	Expect
	Domain	Match Region	Region	Value
	7tm_1	32 . . . 278	72/272 (26%)	5.3e−42
			175/272 (64%)

Example 2

[1013] The NOV42 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table F2A.

TABLE F2A
NOV42 Sequence Analysis
	SEQ ID NO: 199	1012 bp
NOV42a,	GCATTCACAAGCAGGATGTTCCTTCCCAATGACACCCAGTTTCACCCCTCCTCCTTCC
CG53677-01
DNA Sequence	TGTTGCTGGGGATCCCAGGACTAGAAACACTTCACATCTGGATCGGCTTTCCCTTCTG
	TGCTGTGTACATGATCGCACTCATAGGGAACTTCACTATTCTACTTGTGATCAAGACT
	GACAGCAGCCTACACCAGCCCATGTTCTACTTCCTGGCCATGTTGGCCACCACTGATG
	TGGGTCTCTCAACAGCTACCATCCCTAAGATGCTTGGAATCTTCTGGATCAACCTCAG
	AGGGATCATCTTTGAAGCCTGCCTCACCCAGATGTTTTTTATCCACAACTTCACACTT
	ATGGAGTCAGCAGTCCTTGTGGCAATGGCTTATGACAGCTATGTGGCCATCTGCAATC
	CACTCCAATATAGCGCCATCCTCACCAACAAGGTTGTTTCTGTGATTGGTCTTGGTGT
	GTTTGTGAGGGCTTTAATTTTCGTCATTCCCTCTATACTTCTTATATTGCGGTTGCCC
	TTCTGTGGGAATCATGTAATTCCCCACACCTACTGTGAGCACATGGGTCTTGCTCATC
	TATCTTGTGCCAGCATCAAAATCAATATTATTTATGGTTTATGTGCCATTTGTAATCT
	GQTGTTTGACATCACAGTCATTGCCCTCTCTTATGTGCATATTCTTTGTGCTGTTTTC
	CGTCTTCCTACTCATGAGCCCCGACTCAAGTCCCTCAGCACATGTGGTTCACATGTGT
	GTGTAATCCTTGCCTTCTATACACCAGCCCTCTTTTCCTTTATGACTCATTGCTTTGG
	CCGAAATGTGCCCCGCTATATCCATATACTCCTAGCCAATCTCTATGTTGTGGTGCCA
	CCAATGCTCAATCCTGTCATATATGGAGTCAGAACCAAGCAGATCTATAAATGTGTAA
	AGAAAATATTATTGCAGGAACAAGGAATGGAAAAGGAAGAGTACCTAATACATACGAG
	GTTCTGAATGCAATTTTATGAAATTT
	ORF Start: ATG at 16	ORE Stop: TGA at 991
	SEQ ID NO: 200	325 aa	MW at 36602.5kD
NOV42a,	MFLPNDTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYMIALIGNFTILLVIKTDSSLH
CG53677-01
Protein Sequence	QPMFYFLAMLATTDVGLSTATIPKMLGIFWINLRGIIFEACLTQMFFIHNFTLMESAV
	LVANAYDSYVAICNPLQYSAILTNKVVSVIGLGVFVRALIFVIPSILLILRLPFCGNH
	VIPHTYCEHMGLAHLSCASIKINIIYGLCAICNLVFDITVIALSYVHILCAVFRLPTH
	EPRLKSLSTCGSHVCVILAFYTPALFSFMTHCFGRNVPRYIHILLANLYVVVPPMLNP
	VIYGVRTKQIYKCVKKILLQEQGMEKEEYLIHTRF
	SEQ ID NO: 201	988 bp
NOV42b,	TAGGATGTTCCTTCCCAATGACACCCAGTTTCACCCCTCCTCCTTCCTGTTGCTGGGG
CG53677-02
DNA Sequence	ATCCCAGGACTAGAAACACTTCACATCTGGATCGGCTTTCCCTTCTGTGCTGTGTACA
	TGATCGCACTCATAGGGAACTTCACTATTCTACTTGTGATCAAGACTGACAGCAGCCT
	ACACCAGCCCATGTTCTACTTCCTGGCCATGTTGGCCACCACTGATGTGGGTCTCTCA
	ACAGCTACCATCCCTAAGATGCTTGGAATCTTCTGGATCAACCTCAGAGGGATCATCT
	TTGAAGCCTGCCTCACCCAGATGTTTTTTATCCACAACTTCACACTTATGCAGTCAGC
	AGTCCTTGTGGCAATGGCTTATGACAGCTATGTGGCCATCTGCAATCCACTCCAATAT
	AGCGCCATCCTCACCAACAAGGTTGTTTCTGTGATTGGTCTTGGTGTGTTTGTGAGGG
	CTTTAATTTTCGTCATTCCCTCTATACTTCTTATATTGCGGTTGCCCTTCTGTGGGAA
	TCATGTAATTCCCCACACCTACTGTGAGCACATGGGTCTTGCTCATCTATCTTGTGCC
	AGCATCAAAATCAATATTATTTATGGTTTATGTGCCATTTGTAATCTAGTGTTTGACA
	TCACAGTCATTGCCCTTTCTTATGTGCATATTCTTTGTGCTGTTTTCCGTCTTCCTAC
	TCATGAAGCCCGACTCAAGTCCCTCAGCACATGTGGTTCACATGTGTGTGTAATCCTT
	GCCTTCTATACACCAGCCCTCTTTTCCTTTATGACTCATCGCTTTGGCCGAAATGTGC
	CCCGCTATATCCATATACTCCTAGCCAATCTCTATGTTGTGGTGCCACCAATGCTCAA
	TCCTGTCATATATGGAGTCAGAACCAAGCAGATCTATAAATGTGTGAAGAAAATATTA
	TTGCAGCAACAAGGAATGGAAAAGGAAGAGTACCTAATACATACGAGGTTCTGAATGC
	AA
	ORF Start: ATG at 5	ORE Stop: TGA at 980
	SEQ ID NO: 202	325 aa	MW at 36629.6kD
NOV42b,	MFLPNDTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYMIALIGNFTILLVIKTDSSLH
CG53677-02
Protein Sequecne	QPMFYFLAMLATTDVGLSTATIPKMLGIPWINLRGIIFEACLTQMFFIHNFTLMESAV
	LVAMAYDSYVAICNPLQYSAILTNKVVSVIGLGVFVRALIFVIPSILLILRLPPCGNH
	VTPHTYCEHMGLAHLSCASIKINIIYGLCAICNLVFDITVIALSYVHILCAVFRLPTH
	EARLKSLSTCGSHVCVILAFYTPALFSFMThRFGRNVPRYIHILLANLYVVVPPMLNPI
	VIYGVRTKQIYKCVKKILLQEQGMEKEEYLILHTRF
	SEQ ID NO: 203	646 bp
NOV42c,	CACCAGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGCAAG
116781634 DNA
Sequence	CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC
	TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC
	CTGCCGAGTGGGGCTCTTCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT
	ACGGTGGTGGCTGCGGACAGGTATTTcAAAGTGGTCCACCCCCACCACGCGGTGAACA
	CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT
	GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC
	TGTGAGAGCTTCATCATGGAGTCGGCCAATCGCTGGCATGACATCATGTTCCAGCTGG
	AGTTCTTTATGCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCT
	GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC
	ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCA
	AGCTTGGC
	ORF Start: at 288	ORE Stop: TGA at 522
	SEQ ID NO: 204	78 aa	MW a 8506.6kD
NOV42c,	TLSPPGWRLASSAPCGPWSSWEQCIFCWRTISACKRRPSPVRASSWSRPMAGMTSCSS
116781634
Protein Sequence	WSSLCPSASSYFAPSRLFGA

[1014] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table F2B.

TABLE F2B
Comparison of NOV42a against NOV42b and NOV42c.
			Identities/
			Similarities for
	Protein	NOV42a Residues/	the Matched
	Sequence	Match Residues	Region
	NOV42b	1 . . . 325	323/325 (99%)
		1 . . . 325	323/325 (99%)
	NOV42c	No Significant Alignment Found.

[1015] Further analysis of the NOV42a protein yielded the following properties shown in Table F2C.

TABLE F2C
Protein Sequence Properties NOV42a
PSort     0.6850 probability located in endoplasmic reticulum
analysis: (membrane); 0.6400 probability located in plasma
          membrane; 0.4600 probability located in Golgi
          body; 0.1000 probability located in endoplasmic
          reticulum (lumen)
SignalP   Cleavage site between residues 56 and 57
analysis:

[1016] 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 F2D.

TABLEF2D
Geneseq Results for NOV42a
		NOV42a	Identities/
		Residues/	Similarities for
Geneseq	Protein/Organism/Length	Match	the Matched	Expect
Identifier	[Patent #, Date]	Residues	Region	Value
AAU95728	Human olfactory and pheromone G	1 . . 325	325/325 (100%)	0.0
	protein-coupled receptor #215 -	1 . . 325	325/325 (100%)
	Homo sapiens, 325 aa.
	[WO200224726-A2, 28 MAR.
	2002]
AAU85190	G-coupled olfactory receptor #51 -	1 . . 325	325/325 (100%)	0.0
	Homo sapiens, 325 aa.	1 . . 325	325/325 (100%)
	[WO200198526-A2, 27 DEC.
	2001]
AAU24570	Human olfactory receptor	1 . . 325	325/325 (100%)	0.0
	AOLFR60 - Homo sapiens, 325 aa.	1 . . 325	325/325 (100%)
	[WO200168805-A2, 20 SEP. 2001]
ABB44531	Human GPCR6a polypeptide SEQ	1 . . 325	325/325 (100%)	0.0
	ID NO 22 - Homo sapiens, 325 aa.	1 . . 325	325/325 (100%)
	[WO200174904-A2, 11 OCT.
	2001]
ABB44532	Human GPCR6b polypeptide SEQ	1 . . 325	323/325 (99%)	0.0
	ID NO 24 - Homo sapiens, 325 aa.	1 . . 325	323/325 (99%)
	[WO200174904-A2, 11 OCT.
	2001]

[1017] 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 F2E.

TABLE F2E
Public BLASTP Results for NOV42a
		NOV42a	Identities/
Protein		Residues/	Similarities for
Accession		Match	the Matched
Number	Protein/Organism/Length	Residues	Portion	Expect Value
BAC06019	Seven transmembrane helix	1 . . 325	324/325 (99%)	0.0
	receptor - Homo sapiens	1 . . 325	324/325 (99%)
	(Human), 325 aa.
Q8VGV8	Olfactory receptor MOR32-3 -	1 . . 317	264/317 (83%)	e−155
	Mus musculus (Mouse), 317 aa.	1 . . 317	284/317 (89%)
BAC06020	Seven transmembrane helix	5 . . 311	216/307 (70%)	e−126
	receptor - Homo sapiens	2 . . 308	252/307 (81%)
	(Human), 308 aa
Q8VG26	Olfactory receptor MOR32-5 -	1 . . 308	216/308 (70%)	e−124
	Mus musculus (Mouse), 313 aa.	1 . . 308	251/308 (81%)
BAC06036	Seven transmembrane helix	5 . . 312	211/308 (68%)	e−124
	receptor - Homo sapiens	5 . . 312	251/308 (80%)
	(Human), 312 aa.

[1018] PFam analysis predicts that the NOV42a protein contains the domains shown in the Table F2F.

TABLE F2F
Domain Analysis of NOV42a
			Identities/
		NOV42a	Similarities
	Pfam	Match	for the	Expect
	Domain	Region	Matched Region	Value
	7tm_1	43 . . 293	54/270 (20%)	6.3e−11
			166/270 (61%)

Example G

[1019] Quantitative Expression Analysis of Clones in Various Cells and Tissues

[1020] 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/5I (containing human tissues and cell lines with an emphasis on metabolic diseases), AI_comprehensive_panel (containing normal tissue and samples from autoimmune diseases), Panel CNSD.01 (containing central nervous system samples from normal and diseased brains) and CNS_neurodegeneration_panel (containing samples from normal and Alzheimer's diseased brains).

[1021] 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.

[1022] 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.

[1023] In other cases, non-normalized RNA samples were converted to single strand cDNA (sscDNA) using Superscript 11 (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.

[1024] Probes and primers were designed for each assay according to Applied Biosystems Primer Express Software package (version 1 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.

[1025] 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.

[1026] 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.

[1027] Panels 1, 1.1, 1.2, and 1.3D

[1028] 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, cancel, breast cancer, melanoma, colon cancel, 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.

[1029] In the results for Panels 1, 1.1, 1.2 and 1.3D, the following abbreviations are used:

[1030] ca.=carcinoma,

[1031] *=established from metastasis,

[1032] met=metastasis,

[1033] s cell var=small cell variant,

[1034] non-s=non-sm=non-small,

[1035] squam=squamous,

[1036] pl. eff=pl effusion=pleural effusion,

[1037] glio=glioma,

[1038] astro=astrocytoma, and

[1039] neuro=neuroblastoma.

[1040] General_screening_panel_v1.4

[1041] The plates for Panel 1.4 include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in Panel 1.4 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 Panel 1 4 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 Panel 1.4 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.

[1042] Panels 2D and 2.2

[1043] The plates for Panels 2D and 2.2 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). The tissues arc 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 or CHTN). 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.

[1044] Panel 3D

[1045] The plates of Panel 3D 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 arc 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 cancel 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 and 1.3D are of the most common cell lines used in the scientific literature.

[1046] Panels 4D, 4R, and 4.1D

[1047] 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.).

[1048] 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, IFN 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.

[1049] 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 1-2 μg/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 mitogell) 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.

[1050] 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 100 ng/ml. Dendritic cells were also stimulated with anti-CD40 monoclonal antibody (Pharmingen) at 10 μg/ml for 6 and 12-14 hours.

[1051] 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 welt 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 5.5×10−5M (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.

[1052] 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 106 cells/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.

[1053] 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 105-106 cells/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 (1 μg/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 5×10−5M (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 alter 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.

[1054] 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 5×105cells/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 mg/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.

[1055] For these cell lines and blood cells, RNA was prepared by lysing approximately 107 cells/ml using Trizol (Gibco BRL). Briefly, 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 1/10 volume of 3M sodium acetate and 2 volumes of 100% ethanol. The RNA was spun down and placed in RNAse flee water. RNA was stored at −80° C.

[1056] AI_comprehensive panel_v1.0

[1057] 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.

[1058] 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.

[1059] 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.

[1060] 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.

[1061] 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-lanti-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.

[1062] In the labels employed to identify tissues in the AI_comprehensive panel_v1.0 panel, the following abbreviations are used:

[1063] AI=Autoimmunity

[1064] Syn=Synovial

[1065] Normal=No apparent disease

[1066] Rep22 /Rep20=individual patients

[1067] RA=Rheumatoid arthritis

[1068] Backus=From Backus Hospital

[1069] OA=Osteoarthritis

[1070] (SS)(BA)(MF)=Individual patients

[1071] Ad=Adjacent tissue

[1072] Match control=adjacent tissues

[1073] -M=Male

[1074] -F=Female

[1075] COPD=Chronic obstructive pulmonary disease

[1076] Panels 5D and 5I

[1077] 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.

[1078] 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:

Patient 2   Diabetic Hispanic, overweight, not on insulin
Patient 7-9 Nondiabetic Caucasian and obese (BMI > 30)
Patient 10  Diabetic Hispanic, overweight, on insulin
Patient 11  Nondiabetic African American and overweight
Patient 12  Diabetic Hispanic on insulin

[1079] Adipocyte 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:

[1080] Donor 2 and 3 U: Mesenchymal Stem cells, Undifferentiated Adipose

[1081] Donor 2 and 3 AM: Adipose, AdiposeMidway Differentiated

[1082] Donor 2 and 3 AD: Adipose, Adipose Differentiated

[1083] 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.

[1084] 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.

[1085] In the labels employed to identify tissues in the 5D and 5I panels, the following abbreviations are used:

[1086] GO Adipose=Greater Omentum Adipose

[1087] SK=Skeletal Muscle

[1088] UT=Uterus

[1089] Plt=Placenta

[1090] AD=Adipose Differentiated

[1091] AM=Adipose Midway Differentiated

[1092] U=Undifferentiated Stem Cells

[1093] Panel CNSD.01

[1094] 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 calvazia 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 neuropathlologists to confirm diagnoses with clear associated neuropathology.

[1095] 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.

[1096] In the labels employed to identify tissues in the CNS panel, the following abbreviations are used:

[1097] PSP=Progressive supranuclear palsy

[1098] Sub Nigra=Substantia nigra

[1099] Glob Palladus=Globus palladus

[1100] Temp Pole=Temporal pole

[1101] Cing Gyr=Cingulate gyrus

[1102] BA 4=Brodman Area 4

[1103] Panel CNS_Neurodegeneration_V1.0

[1104] 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.

[1105] 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 coitex is spared in AD and therefore acts as a “control” region within AD patients. Not all brain regions are represented in all cases.

[1106] In the labels employed to identify tissues in the CNS_Neurodegeneration_V1.0 panel, the following abbreviations are used:

[1107] AD=Alzheimer's disease brain; patient was demented and showed AD-like pathology upon autopsy

[1108] Control=Control brains; patient not demented, showing no neuropathology

[1109] Control (Path)=Control brains; patient not demented but showing sever AD-like pathology

[1110] SupTemporal Ctx=Superior Temporal Cortex

[1111] Inf Temporal Ctx=Inferior Temporal Cortex

[1112] GA. NOV41b and NOV41c (CG55676-02 and CG55676-03): GPCR-like

[1113] Expression of genes CG55676-02 and CG55676-03 were assessed using the primer-probe set Ag2378, described in Table GA. Results of the RTQ-PCR runs are shown in Tables GB-GF.

TABLE GA
Probe Name Ag2378
			Start
Primers	Sequences	Length	Position	SEQ ID No
Forward	5′-GTTCAGTGCCACTCAACAATG-3′	21	3	325
Probe	FAM-5′-ATCCCATTGCCCATCAGACTGGCTTT-3′-	26	29	326
	TAMRA
Reverse	5′-GCATCAGTGTGGCAAATAGTTT-3′	22	57	327

[1114]

TABLE GB
Panel A/I
                                 Rel. Exp. (%)
                                 tm8262f—
Tissue Name                      Ag2378_A2
110967 COPD-F                    2.0
110980 COPD-F                    0.0
110968 COPD-M                    1.7
110977 COPD-M                    2.6
110989 Emphysema-F               3.1
110992 Emphysema-F               0.9
110993 Emphysema-F               2.2
110994 Emphysema-F               1.1
110995 Emphysema-F               2.9
110996 Emphysema-F               1.1
110997 Asthma-M                  1.5
111001 Asthma-F                  0.7
111002 Asthma-F                  0.7
111003 Atopic Asthma-F           3.5
111004 Atopic Asthma-F           3.8
111005 Atopic Asthma-F           2.2
111006 Atopic Asthma-F           0.9
111417 Allergy-M                 2.3
112347 Allergy-M                 0.7
112349 Normal Lung-F             0.1
112357 Normal Lung-F             5.6
112354 Normal Lung-M             2.4
112374 Crohns-F                  0.3
112389 Match Control Crohns-F    1.1
112375 Crohns-F                  0.3
112732 Match Control Crohns-F    0.0
112725 Crohns-M                  0.0
112387 Match Control Crohns-M    0.4
112378 Crohns-M                  1.1
112390 Match Control Crohns-M    3.1
112726 Crohns-M                  3.4
112731 Match Control Crohns-M    7.3
112380 Ulcer Col-F               2.5
112734 Match Control Ulcer Col-F 0.0
112384 Ulcer Col-F               1.6
112737 Match Control Ulcer Col-F 3.6
112386 Ulcer Col-F               0.0
112738 Match Control Ulcer Col-F 0.0
112381 Ulcer Col-M               1.3
112735 Match Control Ulcer Col-M 0.0
112382 Ulcer Col-M               1.1
112394 Match Control Ulcer Col-M 0.0
112383 Ulcer Col-M               3.3
112736 Match Control Ulcer Col-M 1.3
112423 Psoriasis-F               0.7
112427 Match Control Psoriasis-F 2.6
112418 Psoriasis-M               0.4
112723 Match Control Psoriasis-M 2.6
112419 Psoriasis-M               3.0
112424 Match Control Psoriasis-M 2.6
112420 Psoriasis-M               4.9
112425 Match Control Psoriasis-M 2.3
104689 (MF) OA Bone-Backus       30.4
104690 (MF) Adj “Normal” Bone-Backus 56.1
104691 (MF) OA Synovium-Backus   11.4
104692 (BA) OA Cartilage-Backus  5.0
104694 (BA) OA Bone-Backus       9.0
104695 (BA) Adj “Normal” Bone-Backus 75.1
104696 (BA) OA Synovium-Backus   10.1
104700 (SS) OA Bone-Backus       19.4
104701 (SS) Adj “Normal” Bone-Backus 23.4
104702 (SS) OA Synovium-Backus   100.0
117093 OA Cartilage Rep7         1.8
112672 OA Bone5                  3.1
112673 OA Synovium5              1.1
112674 OA Synovial Fluid cells5  0.5
117100 OA Cartilage Rep 14       0.0
112756 OA Bone9                  55.5
112757 OA Synovium9              0.9
112758 OA Synovial Fluid Cells9  0.4
117125 RA Cartilage Rep2         1.2
113492 Bone2 RA                  5.9
113493 Synovium2 RA              1.1
113494 Syn Fluid Cells RA        3.5
113499 Cartilage4 RA             1.0
113500 Bone4 RA                  2.2
113501 Synovium4 RA              0.2
113502 Syn Fluid Cells4 RA       0.3
113495 Cartilage3 RA             2.6
113496 Bone3 RA                  1.6
113497 Synovium3 RA              1.1
113498 Syn Fluid Cells3 RA       1.7
117106 Normal Cartilage Rep20    0.1
113663 Bone3 Normal              0.3
113664 Synovium3 Normal          0.1
113665 Syn Fluid Cells3 Normal   0.2
117107 Normal Cartilage Rep22    1.2
113667 Bone4 Normal              0.8
113668 Synovium4 Normal          1.3
113669 Syn Fluid Cells4 Normal   1.3

[1115]

TABLE GC
Panel 1.3D
                           Rel. Exp., %
                           1.3dx4tm4870f—
Tissue Name                ag2378_a1
Liver adenocarcinoma       0
Pancreas                   0
Pancreatic ca. CAPAN 2     4.1
Adrenal gland              0.2
Thyroid                    0.5
Salivary gland             0.5
Pituitary gland            0.2
Brain (fetal)              0
Brain (whole)              0
Brain (amygdala)           0
Brain (cerebellum)         0
Brain (hippocampus)        0.1
Brain (substantia nigra)   0
Brain (thalamus)           0
Cerebral Cortex            0.9
Spinal cord                1
glio/astro U87-MG          0
glio/astro U-118-MG        0
astro SW1783               0.2
neuro; met SK-N-AS         0
astro SF-539               0.2
astro SNB-75               2.3
glio SNB-19                0
glio U251                  0
glio SF-295                0
Heart (fetal)              0
Heart                      0
Fetal Skeletal             2.4
Skeletal muscle            0.1
Bone marrow                0
Thymus                     2.2
Spleen                     1.9
Lymph node                 0.2
Colorectal                 0.4
Stomach                    0.3
Small intestine            0
Colon SW480                0
Colon SW620(SW480 met)     0
Colon HT29                 41.3
Colon HCT-116              0
Colon CaCo-2               9.4
Colon Ca. tissue(ODO3866)  100
Colon HCC-2998             0
Gastric(liver met) NCI-N87 2.8
Bladder                    0.2
Trachea                    2.1
Kidney                     1
Kidney (fetal)             0.8
Renal 786-0                0
Renal A498                 0
Renal RXF 393              0.2
Renal ACHN                 0
Renal UO-31                4.9
Renal TK-10                0
Liver                      0
Liver (fetal)              0.2
Liver (hepatoblast) HepG2  8.7
Lung                       0.5
Lung (fetal)               0.4
Lung (small cell) LX-1     0
Lung (small cell) NCI-H69  0
Lung (s. cell var.) SHP-77 9.6
Lung (large cell)NCI-H460  0
Lung (non-sm. cell) A549   0
Lung (non-s. cell) NCI-H23 1
Lung (non-s. cell) HOP-62  1.6
Lung (non-s. cl) NCI-H522  0
Lung (squam.) SW 900       6.1
Lung (squam.) NCI-H596     0.2
Mammary gland              7.6
Breast (pl. ef) MCF-7      19.6
Breast (pl. ef) MDA-MB-231 0.3
Breast (pl. ef) T47D       4.2
Breast BT-549              0.8
Breast MDA-N               0
Ovary                      2.5
Ovarian OVCAR-3            1.3
Ovarian OVCAR-4            0
Ovarian OVCAR-5            9.6
Ovarian OVCAR-8            0.2
Ovarian IGROV-1            0
Ovarian (ascites) SK-OV-3  0
Uterus                     0
Plancenta                  0.5
Prostate                   0.9
Prostate (bone met)PC-3    2.3
Testis                     1.1
Melanoma Hs688(A).T        0
Melanoma (met) Hs688(B).T  0
Melanoma UACC-62           0
Melanoma M14               0
Melanoma LOXIMVI           0
Melanoma (met) SK-MEL-5    0
Adipose                    6.3

[1116]

TABLE GD
Panel 2D
                           Rel. Expr., %
                           2dx4tm4693f—
Tissue Name                ag2378_a2
Normal Colon               1.7
CCa 1                      1.1
CCa 1 Margin               0.2
CCa 2                      0
CCa 2 Margin               0.1
CCa 3                      2.4
CCa 3 Margin               0.3
CCa 4                      0.1
CCa 4 Margin               0.2
CCa 5 Metastasis           0
CCa 5 Margin (Liver)       0
CCa 6 Metastatsis          1.1
CCa 6 Margin (Lung)        0.6
Normal Prostate            14.6
PCa 1                      2.2
PCa 1 Margin               3.7
PCa 2                      1.2
PCa 2 Margin               1.5
Normal Lung                2.1
LCa 1 Metastasis           8
LCa 1 Margin (muscle)      0.7
LCa 2                      3.9
LCa 2 Margin               0.6
LCa 3                      0.7
LCa 3 Margin               1.9
LCa 4                      1.6
LCa 4 Margin               0.6
LCa 5                      3.2
LCa 5 Margin               0.3
Ocular Melanoma Metastasis 0.3
Liver Margin               0
Melanoma Metastasis        0.1
Lung Margin                1.2
Normal Kidney              3.2
RCC 1                      0.6
RCC 1 Margin               2.1
RCC 2                      1.1
RCC 2 Margin               2.6
RCC 3                      0.2
RCC 3 Margin               2.3
RCC 4                      0.2
RCC 4 Margin               1.4
RCC 5                      0.4
RCC 5 Margin               0.8
RCC 6                      3.1
RCC 6 Margin               5
RCC 7                      0.1
RCC 7 Margin               1.2
RCC 8                      19.2
RCC 8 Margin               2
RCC 9                      3.2
RCC 9 Margin               1.5
Normal Uterus              0
UtCa                       0.4
Normal Thyroid             3.6
ThyCa 1                    2.6
ThyCa 2                    2.1
ThyCa 2 Margin             4.8
Normal Breast              28.2
BCa 1                      30.2
BCa 2                      37.3
BCa 3 Metastasis           27.6
BCa 4 Metastasis           100
BCa 5                      4.1
BCa 6                      63.1
BCa 7                      73.3
BCa 7 Margin               37.8
BCa 8                      24
BCa 8 Margin               14
Normal Liver               0
HCC 1                      0
HCC 2                      0.2
HCC 3                      0
HCC 4                      0
HCC 4 Margin               0.5
HCC 5                      0
HCC 5 Margin               0
Normal Bladder             0.5
TCC 1                      0.3
TCC 2                      0.3
TCC 3                      25.9
TCC 3 Margin               0
Normal Ovary               1.3
OVCa 2                     0
OVCa 2 Margin              0.7
Normal Stomach             1.9
GaCa 1                     0.3
GaCa 1 Margin              1.3
GaCa 2                     0
GaCa 2 Margin              0.6
GaCa 3                     0
GaCa 3 Margin              0.8
GaCa 4                     3.3

[1117]

TABLE GE
Panel 3D
                                 Rel. Exp., %
                                 3dx4tm5123f—
Tissue Name                      ag2378_b1
Daoy- Medulloblastoma            0
TE671- Medulloblastoma           0
D283 Med- Medulloblastoma        0
PFSK-1- Primitive Neuroectodermal 0.9
XF-498- CNS                      0.5
SNB-78- Glioma                   0
SF-268- Glioblastoma             0
T98G- Glioblastoma               0
SK-N-SH- Neuroblastoma (metastasis) 0
SF-295- Glioblastoma             0
Cerebellum                       0.1
Cerebellum                       0.2
NCI-H292- Mucoepidermoid lung carcinoma 12.3
DMS-114- Small cell lung cancer  0
DMS-79- Small cell lung cancer   100
NCI-H146- Small cell lung cancer 1.6
NCI-H526- Small cell lung cancer 16.9
NCI-N417- Small cell lung cancer 0
NCI-H82- Small cell lung cancer  0
NCI-H157- Squamous cell lung cancer 0.2
(metastasis)
NCI-H1155- Large cell lung cancer 0.6
NCI-H1299- Large cell lung cancer 0
NCI-H727- Lung carcinoid         6.4
NCI-UMC-11- Lung carcinoid       0
LX-1- Small cell lung cancer     0
Colo-205- Colon cancer           0.4
KM12- Colon cancer               0
KM20L2- Colon cancer             29.9
NCI-H716- Colon cancer           0
SW-48- Colon adenocarcinoma      0
SW1116- Colon adenocarcinoma     0
LS 174T- Colon adenocarcinoma    0.3
SW-948- Colon adenocarcinoma     0
SW-480- Colon adenocarcinoma     0
NCI-SNU-5- Gastric carcinoma     0
KATO III- Gastric carcinoma      1
NCI-SNU-16- Gastric carcinoma    3.7
NCI-SNU-1- Gastric carcinoma     0.5
RF-1- Gastric adenocarcinoma     0
RF-48- Gastric adenocarcinoma    0.1
MKN-45- Gastric carcinoma        7.2
NCI-N87- Gastric carcinoma       8.7
OVCAR-5- Ovarian carcinoma       7.7
RL95-2- Uterine carcinoma        0
HelaS3- Cervical adenocarcinoma  0
Ca Ski- Cervical epidermoid carcinoma 0
(metastasis)
ES-2- Ovarian clear cell carcinoma 0.4
Ramos- Stimulated with PMA/ionomycin 6 h 0
Ramos- Stimulated with PMA/ionomycin 14 h 0
MEG-01- Chronic myelogenous leukemia 0
(megokaryoblast)
Raji- Burkitt's lymphoma         0
Daudi- Burkitt's lymphoma        0
U266- B-cell plasmacytoma        0
CA46- Burkitt's lymphoma         0
RL- non-Hodgkin's B-cell lymphoma 0
JM1- pre-B-cell lymphoma         0
Jurkat- T cell leukemia          0.2
TF-1- Erythroleukemia            0
HUT 78- T-cell lymphoma          0.1
U937- Histiocytic lymphoma       0
KU-812- Myelogenous leukemia     0
769-P- Clear cell renal carcinoma 0
Caki-2- Clear cell renal carcinoma 0
SW 839- Clear cell renal carcinoma 0
G401- Wilms' tumor               0
Hs766T- Pancreatic carcinoma (LN 11.8
metastasis)
CAPAN-1- Pancreatic adenocarcinoma 9.7
(liver metastasis)
SU86.86- Pancreatic carcinoma (liver 15.1
metastasis)
BxPC-3- Pancreatic adenocarcinoma 14.4
HPAC- Pancreatic adenocarcinoma  8.8
MIA PaCa-2- Pancreatic carcinoma 0
CFPAC-1- Pancreatic ductal adenocarcinoma 24.4
PANC-1- Pancreatic epithelioid ductal 0
carcinoma
T24- Bladder carcinma (transitional cell) 10.3
5637- Bladder carcinoma          12.6
HT-1197- Bladder carcinoma       4
UM-UC-3- Bladder carcinma (transitional 0
cell)
A204- Rhabdomyosarcoma           17.4
HT-1080- Fibrosarcoma            0
MG-63- Osteosarcoma              0.1
SK-LMS-1- Leiomyosarcoma (vulva) 0
SJRH30- Rhabdomyosarcoma (met to 0
bone marrow)
A431- Epidermoid carcinoma       0
WM266-4- Melanoma                1.6
DU 145- Prostate carcinoma (brain 0
metastasis)
MDA-MB-468- Breast adenocarcinoma 4.9
SCC-4- Squamous cell carcinoma of tongue 0.5
SCC-9- Squamous cell carcinoma of tongue 0
SCC-15- Squamous cell carcinoma of tongue 0
CAL27- Squamous cell carcinoma of tongue 0

[1118]

TABLE GF
Panel 4D
                                 Rel. Exp., %
                                 4dx4tm4604f—
Tissue Name                      ag2378_b2
Secondary Th1 act                10.3
Secondary Th2 act                20.2
Secondary Tr1 act                13.4
Secondary Th1 rest               0.4
Secondary Th2 rest               1.4
Secondary Tr1 rest               2.5
Primary Th1 act                  38.1
Primary Th2 act                  46.1
Primary Tr1 act                  65.3
Primary Th1 rest                 11
Primary Th2 rest                 9.2
Primary Tr1 rest                 4.2
CD45RA CD4 lymphocyte act        2.8
CD45RO CD4 lymphocyte act        10.4
CD8 lymphocyte act               0.4
Secondary CD8 lymphocyte rest    0.5
Secondary CD8 lymphocyte act     0.8
CD4 lymphocyte none              0
2ry Th1/Th2/Tr1_anti-CD95 CH11   9.7
LAK cells rest                   0.9
LAK cells IL-2                   0.9
LAK cells IL-2 + IL-12           2.5
LAK cells IL-2 + IFN gamma       2.9
LAK cells IL-2 + IL-18           2
LAK cells PMA/ionomycin          5.4
NK Cells IL-2 rest               0
Two Way MLR 3 day                0
Two Way MLR 5 day                0.8
Two Way MLR 7 day                1.9
PBMC rest                        0
PBMC PWM                         2.8
PBMC PHA-L                       4.2
Ramos (B cell) none              0
Ramos (B cell) ionomycin         0
B lymphocytes PWM                8.3
B lymphocytes CD40L and IL-4     0.5
EOL-1 dbcAMP                     0
EOL-1 dbcAMP PMA/ionomycin       0
Dendritic cells none             0.2
Dendritic cells LPS              0
Dendritic cells anti-CD40        0
Monocytes rest                   0
Monocytes LPS                    0
Macrophages rest                 0
Macrophages LPS                  0.4
HUVEC none                       0
HUVEC starved                    0
HUVEC IL-1beta                   0.3
HUVEC IFN gamma                  0
HUVEC TNF alpha + IFN gamma      0
HUVEC TNF alpha + IL4            0
HUVEC IL-11                      0
Lung Microvascular EC none       1.3
Lung Microvascular EC TNFalpha + 0.3
IL-1beta
Microvascular Dermal EC none     0
Microsvasular Dermal EC TNFalpha + 0
IL-1beta
Bronchial epithelium TNFalpha +  0.3
IL1beta
Small airway epithelium none     0.4
Small airway epithelium TNFalpha + 4.4
IL-1beta
Coronery artery SMC rest         0.3
Coronery artery SMC TNFalpha +   0.5
IL-1beta
Astrocytes rest                  0
Astrocytes TNFalpha + IL-1beta   0.7
KU-812 (Basophil) rest           0
KU-812 (Basophil) PMA/ionomycin  0
CCD1106 (Keratinocytes) none     1.3
CCD1106 (Keratinocytes) TNFalpha + 1.3
IL-1beta
Liver cirrhosis                  1.4
Lupus kidney                     0.3
NCI-H292 none                    100
NCI-H292 IL-4                    64.9
NCI-H292 IL-9                    90.2
NCI-H292 IL-13                   28.6
NCI-H292 IFN gamma               38.3
HPAEC none                       0
HPAEC TNF alpha + IL-1 beta      0
Lung fibroblast none             2.2
Lung fibroblast TNF alpha + IL-1 beta 1.5
Lung fibroblast IL-4             0
Lung fibroblast IL-9             0.4
Lung fibroblast IL-13            0
Lung fibroblast IFN gamma        0.4
Dermal fibroblast CCD1070 rest   0.7
Dermal fibroblast CCD1070 TNF alpha 0.5
Dermal fibroblast CCD1070 IL-1 beta 0
Dermal fibroblast IFN gamma      0
Dermal fibroblast IL-4           0
IBD Colitis 1                    0
IBD Colitis 2                    0
IBD Crohn's                      0
Colon                            1.3
Lung                             2
Thymus                           11.8
Kidney                           8.8

[1119] Expression in panel 4D: CG55676-02 is expressed highly during initial activation and polarization of T cells regardless of whether polarization is to Th1, Th2 or Tr1 pathway. It is not expressed in untreated CD4 T cells and the level of expression is much less in chronically activated T cells.

[1120] Role in inflammation: CG55676-02 is a putative GPCR and may play an important role in the regulation of or cell polarization, differentiation, and T cell trafficking.

[1121] Potential therapeutic value: Antagonistic antibodies, preferably fully human monoclonal antibodies directed against the protein encoded for by CG55676-02 could reduce or block inflammation by blocking ligand interaction with this putative GPCR and preventing T cell function in diseases such as asthma, emphysema, allergy, arthritis, diabetes, and psoriasis. Alternatively, if this putative GPCR down regulates T cell activation then agonistic antibodies (Ligand-like) could also block inflammation in these diseases (Bromley et al, J. Immunol. 165(1) 15-9).

[1122] Expression in panel of relevance to Oncology 1.3D and 2D: In Panel 1.3D, CG55676-02 is expressed in tumor derived cell lines especially from colon, lung, ovarian and breast cancers. In panel 2D it is overexpressed in breast, lung and bladder tumor tissues compared to normal adjacent tissues.

[1123] Role in inflammation: CG55676-02 is a putative GPCR and may play a role tumor cell growth

[1124] Potential therapeutic value: Antagonistic antibodies, preferably fully human monoclonal antibodies directed against the protein encoded for by CG55676-02 could reduce or block tumor growth by blocking ligand interaction with this putative GPCR resulting in therapeutic treatment for tumor like lung, breast, bladder, kidney and colon.

[1125] A/I panel: The transcript of CG55676-03 is found in bone of 4 out of 4 patients with osteoarthritis and in synovium from 1 out of 4 patients.

[1126] Role in inflammation: CG55676-03 encodes a transcript for a putative GPCR that is expressed on cells within the bone and in the synovium of patients with osteoarthritis.

[1127] Potential therapeutic value: Antagonistic antibodies, preferably fully human monoclonal antibodies or small molecule therapeutics directed against the protein encoded for by CG55676-03 could reduce or block inflammation by preventing ligand interaction with this putative GPCR and as asthma, emphysema, allergy, arthritis, diabetes, and psoriasis.

[1128] Other Embodiments

[1129] 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 in aterial, 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 102.

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 102.

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 102.

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 102.

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 pathlology 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 or 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 102 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 102.

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 102.

23. An isolated nucleic acid molecule encoding the mature forth 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 102.

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 102.

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 102, 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 102.

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 102.

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.