During the process of neurulation the neural groove forms and the neural folds fuse to form the neural tube. Once the neural tube is fused, the fluid within the lumen is considered cerebrospinal fluid, whereas before fusion is complete the neuroepithelium lining the inside of the neural tube is still in contact with amniotic fluid. During the early stages of neural tube growth and development, groups of specialized neuroepithelial cells lining the neural tube are believed to secrete fluid into the neural tube space in order to support growth and development of the embryo. As the neural tube continues to elongate and develop, specific highly vascularized epithelial cell types begin to invaginate at specific locations within the neural tube to form the specialized choroid plexus.
The choroid plexus is a highly vascularized epithelial cell structure that during development may be involved in the specific intracellular transfer of proteins into the CSF from the blood (Saunders et al., Cell Mol Neurobiol, 2000. 20:29-40). The choroid plexus develops in the lateral ventricles and in the third and fourth ventricles of the brain. In rats, the choroid plexus can be first identified as early as embryonic day 13 (E13) as a midline structure and by E15 it represents paired structures protruding into the lateral ventricles. In the human embryo the choroid plexus begins to develop in the lateral and fourth ventricle at Carnegie Stage (CS) 18, approximately 44 days post-ovulation. The first appearance of cerebral cortical neurons in the human embryo occurs at CS 21, shortly following the appearance of the choroid plexus and the production of CSF, and a similar temporal sequence is seen in mice and rats.
In adults, CSF has many functions, including an intermediary between blood and brain for the transport of nutrients and growth factors and as a fluid buffer for the brain to protect both the brain and the large vessels that supply blood to the brain (Chodobski et al., Microsc Res Tech, 2001. 52:65-82; Emerich et al., Bioessays, 2005. 27:262-74). It may also be involved in elimination of toxins and other metabolic byproducts (Emerich et al., Bioessays, 2005. 27:262-74; Miyan et al., Can J Physiol Pharmacol, 2003. 81:317-28). A mathematical analysis taking into account the pulsatile nature of CSF flow suggested that the CSF pulsations buffer the capillary bed from the effects of arterial pulsations that might otherwise prevent linear blood flow due to the mechanics of the brain being enclosed in the skull (Miyan et al., Can J Physiol Pharmacol, 2003. 81:317-28). CSF contains nerve growth factor (NGF), transforming growth factor alpha (TGF-alpha); levels of these proteins are altered in neurological and developmental disorders (Miyan et al., Can J Physiol Pharmacol, 2003. 81:317-28; Kasaian et al., Biofactors, 1989. 2:99-104; Massaro et al., Ital J Neurol Sci, 1994. 15:105-8; Patterson et al., Brain Res, 1993. 605:43-9; Van Setten et al., Int J Dev Neurosci, 1999. 17:131-4), but potential functions of these factors has not been demonstrated. Recently it was shown that the ciliary action of CSF in the lateral ventricle of adult rats creates a gradient of SLIT2 protein, a chemorepulsive factor for neuronal olfactory bulb migration, within the CSF (Sawamoto et al., Science, 2006. 311:629-32), suggesting that CSF factors might have instructive roles for developing neurons or neural progenitors.
Although the role of the CSF during embryogenesis is just starting to be studied, an important role has been suggested in brain development (Miyan et al., Can J Physiol Pharmacol, 2003. 81:317-28; Gato et al., Anat Rec A Discov Mol Cell Evol Biol, 2005. 284:475-84; Martin et al., Dev Biol, 2006. 297:402-16; Mashayekhi et al., Brain, 2002. 125:1859-74; Miyan et al., Cerebrospinal Fluid Res, 2006. 3:2; Owen-Lynch et al., Brain, 2003. 126:623-31). Miyan et al. have shown that rat cortical cells are viable and proliferate in e-CSF (Miyan et al., Cerebrospinal Fluid Res, 2006. 3:2). Other studies have tested discrete signaling factors that may regulate neurogenesis. Gato et al. and Martin et al. have studied the role of chick e-CSF in regulating survival, proliferation, and neurogenesis of neuroepithelial cells, and have identified FGF-2 in the chick CSF as a vital trophic factor (Gato et al., Anat Rec A Discov Mol Cell Evol Biol, 2005. 284:475-84; Martin et al., Dev Biol, 2006. 297:402-16). Intriguingly, in mutant animals, CSF factors that may inhibit proliferation have been suggested. In studies of the hydrocephalic Texas (H-Tx) rat, cell proliferation in the ventricular zone decreases, and although cell migration still occurs, there is a decrease in the number of migrating cells (Mashayekhi et al., Brain, 2002. 125:1859-74; Miyan et al., Cerebrospinal Fluid Res, 2006. 3:2). In addition, CSF from the lateral ventricles of affected H-Tx fetuses can completely inhibit in vitro proliferation of neuronal progenitors isolated from a normal fetus at 10% CSF addition to the media, suggesting that factors intrinsic to the CSF of the H-Tx fetuses are present that inhibit proliferation.
Prior to the present invention, the identification of such CSF factors with a developmental role has been impeded, as the components of the CSF were previously not known. While a first glimpse of the protein composition of e-CSF has been provided, a (Parada et al., Proteomics, 2006. 6:312-20; Parada et al., J Proteome Res, 2005. 4:2420-8), a complete analysis of the contents of e-CSF would be allow for identification of proteins important for neural developmental and differentiation.
We have developed methods for isolating embryonic cerebrospinal fluid (e-CSF) and have identified the proteins found in rat and human e-CSF. On this basis, the invention features a method of isolating embryonic cerebrospinal fluid (e-CSF). As e-CSF is capable of supporting the culture of developing neural cells, the invention also features methods of culturing cells in the presence of various components of the e-CSF, as well as compositions including cells and e-CSF component(s).
In a first aspect, the invention features a composition including at least one (e.g., at least 2, 3, 4, 5, 6, 8, 10, 15, 25, 50, 75, or 100) component(s) of e-CSF (e.g., rat, mouse, or human). The composition may include the component or components at an enhanced level relative to the level in e-CSF and the composition is capable of supporting proliferation, maintenance, or differentiation of a cultured cell (e.g., a stem cell or progenitor cell such as neural cell). The component may be a polypeptide, or a functional fragment thereof (e.g., a soluble fragment). The polypeptide may be isolated, purified, or produced recombinantly. The component may be present at a level sufficient to enhance cell proliferation, maintenance, or differentiation, as compared to in the absence of the component. The component may be one that is not found in adult CSF.
The invention also features a cell culture composition including a cell (e.g., any described herein) and a composition of the first aspect.
The invention also features a kit including (a) a composition including at least one component of e-CSF, wherein the component is present at an enhanced level relative to naturally occurring e-CSF (e.g., the compositions described above); and (b) instructions for using (a) for cell culture.
In another aspect, the invention features a method of culturing a cell (e.g., a stem cell or a progenitor cell, such as a neural cell), including incubating the cell in culture media containing at least one isolated component of rat or human e-CSF (e.g., any of the compositions of the first aspect of the invention). The component may be a polypeptide, or a functional fragment thereof (e.g., a soluble fragment). The polypeptide may be isolated, purified, or produced recombinantly. In certain embodiments, the component is one which is not found in adult CSF.
In any of the above aspects, the e-CSF component may be one described in Tables 1-4.
In another aspect, the invention features a method of isolating embryonic cerebrospinal fluid (e-CSF) including (a) providing an embryo; (b) inserting a capillary needle into a ventricle of the central nervous system of the embryo such that the tip of the needle contacts CSF; and (c) extracting CSF from the embryo through the needle (e.g., a microcapillary pipette or syringe), thereby isolating e-CSF. The method may further include (d) removing intact contaminating cells (e.g., by filtration or centrifugation). Step (c) may be performed such that the needle tip does not contact the neuroepithelium during the extraction. The e-CSF may be removed from a lateral ventricle or from the third or fourth ventricle of the embryo, or a combination thereof. The method may further include storing the e-CSF at less than about 0-20° C. to about −80, −90, −100, −150° C.
By “isolated” is meant, with respect to a naturally occurring compound (e.g., a polypeptide), that the compound is at least partially free from the components (e.g., other polypeptides, nucleic acids, cell membranes) with which it naturally is found.
By “purified” is meant, with respect to a compound (e.g., a polypeptide), that the compound makes up at least 20% (e.g., at least 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, or 99%) of the composition with which is it found.
By “enhanced level” of a component is meant that the component is present either a higher concentration (e.g., at least 10%, 25%, 50%, 100%, 250%, 500%, or 1000% greater) or at higher purity level (e.g., with 5%, 10%, 25%, 50%, or 75% less by mass other components, not including solvents or buffers) relative to the concentration or purity of the component in a control composition (e.g., a naturally occurring composition).
By “stem cell” is meant a self-renewing cell that is capable of differentiation into multiple mature cell types (e.g., a neuron, glial cell, or astrocyte).
By “progenitor cell” (e.g., neural progenitor cells) is meant a cell that is capable of forming at least one cell type has at least some capacity for self-renewal.
Other features and advantages of the invention will be apparent from the following Detailed Description, the drawings, and the claims.
Here we undertake a systematic, detailed, and unbiased proteomic analysis of human e-CSF from Carnegie Stage 19-20 (approximately 48-51 days post ovulation). We also report an extensive proteome analysis of rat e-CSF from three different time points E12.5, E14.5, and E17.5 during cortical development and list all the proteins that are common among the three time points as well as those proteins that are different.
We report a list of the common proteins found between the human and rat e-CSF. Furthermore, using various gene ontology programs we categorize the proteins in the e-CSF and compare the subcellular localization, molecular function, and biological process of embryonic human and rat CSF. We find 130 proteins shared between the human and rat e-CSF and that there are many similarities in the categories of proteins found within the CSF based on molecular function and biological process. This systematic analysis of proteins common to many ages lays the groundwork for analysis of changing CSF components that may have more specific developmental roles.
As described herein, rat embryonic CSF proteome is a complex and dynamic milieu of extracellular matrix proteins, intracellular proteins, and signaling factors (see also, Zappaterra et al., J Proteome Res 6, 3537-48 (2007)). However, prior to the present invention, the direct influence of embryonic CSF on cortical progenitor cells had been challenging to assess due to the difficulty of obtaining substantial amounts of CSF. In addition, we developed a cortical explant culture system in which embryonic cortex dissected from a consistent location of the lateral wall is placed on polycarbonate membranes and floated on embryonic CSF (
On the basis of this work, the present invention features methods for isolation of e-CSF, and methods of culturing cells (e.g., stem cells or progenitor cells such as neural stem cells) using one or more (e.g., 2, 3, 4, 5, 6, 8, or 10) components (e.g., a purified or recombinantly produced polypeptide) of e-CSF and compositions including cells with one or more such components.
Isolation of CSF from Human Embryos
In general, CSF can be isolated from any mammalian embryo using the methods described herein. Typically the embryos at the appropriate stage are collected, and the extra embryonic membranes and tissues are dissected away in a buffer solution (e.g., phosphate-buffer saline (PBS) or Hanks' Balanced Salt Solution (HBSS)). A capillary needle (e.g., a syringe or microcapillary pipette) is placed into a CNS ventricle (e.g., lateral, third, or fourth ventricle) and the CSF is withdrawn. To avoid contaminating cells, it is desirable that contact with either blood vessels or with the neuroepithelium be avoid. To ensure that the e-CSF sample is cell-free, the sample can treated to remove cells (e.g., by centrifugation or by filtration).
In one example, human embryos were collected through the joint MRC-Wellcome Trust Human Developmental Biology Resource at the University of Newcastle, Institute of Human Genetics. The embryos at CS 19-20 were placed in ice-cold sterile Phosphate Buffered Saline (PBS) solution and all extra-embryonic membranes and tissues were removed. The embryos were washed in sterile PBS and carefully placed on the dissection platform under the microscope. A Hamilton syringe was placed carefully into the fourth ventricle and the CSF was collected paying close attention not to make contact with the neuroepithelium lining of the fourth ventricle. The samples used for analysis had no microscopically visible contaminating neuroepithelial cells or red blood cells. Nonetheless, the CSF samples were centrifuged at 10,000 g at 4° C. for 10 minutes to remove any intact contaminating cells and then were frozen at −80° C. until further analysis.
In another example, rat embryos (Sprague Dawley) at stage E12.5, E14.5 and E17.5 were removed from extra-embryonic membranes and tissues and placed in sterile Hanks Balanced Salt Solution (HBSS). Each embryo was handled individually and washed in HBSS, gently patted dry and placed on a microdissection tray. The CSF was carefully aspirated from each rat embryo under the microscope with a pulled tip glass microcapillary pipette (Drummond Scientific Company 20 μl). The needle was steadily held within the inside of the ventricle so as to prevent major contact with the neuroepithelial wall and the CSF was slowly aspirated. For E17.5, the embryo was placed on its back and the glass needle was inserted into the left lateral ventricle and then into the right lateral ventricle to collect the maximum amount of CSF from the lateral ventricles. For E12.5, the embryo was placed on its side and the glass needle was inserted directly into the lateral ventricle. Due to the patency of the neural tube at this stage, the CSF was collected from the developing lateral, third, and fourth ventricle. For E14.5, the embryo was also placed on its side and the glass needle was either inserted into the lateral ventricle or into the fourth ventricle and the CSF was collected from each location separately.
Cell Culture Using e-CSF Components
As we have shown that e-CSF stimulates proliferation and maintenance of neural stem cells in vitro and have, for the first time, identified many of the polypeptides found in e-CSF, it now becomes possible to uses these identified proteins in a cell culture system as proliferation, differentiation and maintenance, particularly with regard to stem cells and progenitors, especially those of neural origin. On this basis, the invention features methods of cell culture using e-CSF or one or more e-CSF components (e.g., polypeptides, either alone or as a supplement to standard cell culture media, and cell culture compositions including one or more components of e-CSF.
Any of the polypeptides identified in e-CSF may be used as a supplement in a cell culture (e.g., those described in Tables 1-4), or a combination of components from e-CSF (e.g., polypeptides) may be used for cell culture (e.g., for proliferating cells such as stem cells). Functional fragments (e.g., soluble fragments) of any of the proteins described herein) may be used in the invention. Soluble fragments are particularly useful for membrane bound proteins.
The compositions and methods of the invention may employ any type of cultured cell known in the art. In particular embodiments, a proliferating cell, such as a stem cell or progenitor cell is used. Neural cells (e.g., neural stem cells and neural progenitor cells) can be used in the invention as well. Human and non-human mammal cells (e.g., rat or mouse) cells are used in certain embodiments. Stem cell lines are, for example, commercially available or can be obtained directly from laboratory animals such as mice or rats.
In one embodiment, the cell media composition of the invention includes any medium known in the art supplemented with at least one (e.g., at least 2, 3, 4, 5, 6, 8, 10, 15, 25, 50) components identified in e-CSF (e.g., those described herein). Exemplary media types used for culturing neural stem cells include Neuralbasal Media (Invitrogen Corp.), Neural Stem Cell Commitment Media or Neural Stem Cell Growth Meida (AlphaGenix, Inc.), and NeuroCult NS-A Proliferation, Human; Kit or NeuroCult NS-A Differentiation Humam Kit (Stem Cell Technologies, Inc.). In another embodiment, the cell culture media is derived entirely from e-CSF components.
Determining Whether a Component of e-CSF Enhances Proliferation, Maintenance, or Differentiation of a Cell
Any component of e-CSF (e.g., those described herein) may be analyzed to determine its effect on a cell (e.g., a neuronal progenitor or stem cell described herein) in culture. Desirable components are those which result in maintenance of the cells or those that result in more rapid proliferation or differentiation of the cell. Assays to measure proliferation (e.g., using cell dyes or incorporation of a modified nucleotide such as BrdU) and differention (e.g., using differentiation markers known in the art) are well known by those of skill in the art.
The Role of e-CSF in Brain Development
Embryonic CSF plays a fundamental, dynamic role in defining an endogenous niche for the survival and proliferation of cortical neural progenitors. CSF alone supports the growth and proliferation of cortical explants in the absence of exogenous media or factors. CSF from different ages in development harbors distinct proliferative capacities for neural progenitor cells the characterization of the CSF proteome has identified several classes of proteins in the CSF established as essential regulators of proliferation and maintenance of neuronal progenitor cells; and we identified and characterized a novel role for IGF2 signaling in the embryonic CSF as a regulator of cortical progenitor cell proliferation.
The CSF has been traditionally considered as a fluid cushion that bathes the central nervous system, acting as a passive sink for biomarkers of central nervous system function and pathology. Collectively, our study represents a paradigm shift in developmental neuroscience, suggesting that the embryonic CSF proteome as a dynamic milieu of growth-promoting signals for neural stem cells (
The CSF-choroid-plexus system is ideally suited to act as a rapid, spatially synchronized medium for triggering local and global changes in molecular signaling. Dynamism of factors such as IGF2 levels in the CSF is consistent with a role of the CSF as a vehicle for orchestrating cortical neurogenesis: IGF2 expression increases during development, is maximal during the peak of cortical neurogenesis in the rat brain (E17-E19), and declines as cortical neurogenesis nears completion around birth. Therefore, the appearance of signaling factors such as IGF2 stimulate the proliferation of cortical progenitors to maintain them in an uncommitted state through development. Igf2 and other molecules (Martin et al., Dev Biol 297, 402-16 (2006)) appear to be released in the CSF by choroid plexus, which appears in the lateral ventricles between E13 and E15. These signaling molecules, via the CSF must act widely on cortical precursors that, in the case of the embryonic human brain, may be centimeters away from the source of the factor. It is unclear whether there is a gradient of Igf2 in the embryonic CSF influences regional differences in proliferation across the cortical mantle (Bayer et al., Prog Neurobiol 29, 57-106 (1987)), as has been shown for Slit in the adult CSF (Sawamoto et al., Science 311, 629-32 (2006)), or whether ciliary movement or diffusion through a far smaller volume equilibrates Igf2 concentration in the embryonic ventricles. A fundamental aspect of neural differentiation may be the simple isolation of developing cells from this growth-promoting environment, by the withdrawal of the ventricular process (Cappello et al., Nat Neurosci 9, 1099-107 (2006)).
Our findings have several important implications. First, CSF in the embryo and the adult is a dynamic fluid that contacts a number of CNS precursors as well as differentiating neurons and glia. Second, CSF components can be dispersed over large areas and thus may be more significant and pervasive regulators of development, stem cell renewal, disease, neurodegeneration and behavior than previously thought. Third, since the CNS represents just one example of an epithelium that grows in relation to an extracellular fluid, our findings may generalize to other epithelia which are likely to develop using similar rules, with a major contributor to the “stem cell niche” being the fluid that bathes the epithelium (Bendall et al., Nature 448, 1015-21 (2007)), similar to the microenvironment that invests hematopoietic stem cells, of which Igf2 is also an essential component (Zhang et al., Blood 103, 2513-21 (2004); Orkin et al., Cell 132, 631-44 (2008)), as in the embryonic CSF. Finally, if a major component of the stem cell niche reflects secreted factors acting at large distances from their sources, a deeper understanding of the proteomic composition of extracellular fluids may provide unexpected ways to regulate stem cell behavior.
To determine the protein contents of e-CSF, frozen CSF samples were thawed on ice. Sample buffer was added and the samples were boiled for 5 minutes and subjected to SDS-PAGE using either 10% or 7.5% polyacrylamide (37.5:1 acrylamide:bis-acrylamide) gels as indicated in
Human CSF was collected from the fourth ventricle, as mentioned above, from two independent embryos at Carnegie Stage (CS) 19-20. From the first embryo (CS19) a total of 15 μl was collected, and from the second embryo (CS20) a total of 70 μl was collected. The CSF from these two independent samples was separated by I-D SDS-PAGE;
Homo
sapiens (Human) APOLIPOPROTEIN B-100 PRECURSOR. [MASS = 515563
Homo
sapiens (Human) DYNEIN HEAVY CHAIN, CYTOSOLIC. [MASS = 532408
Homo
sapiens (Human) MICROTUBULE-ASSOCIATED PROTEIN 1B. [MASS = 270620
Homo
sapiens (Human) MYOSIN-10. [MASS = 228939
Homo
sapiens (Human) FILAMIN A, ALPHA. [MASS = 280018
Homo
sapiens (Human) ISOFORM 1 OF SPECTRIN ALPHA CHAIN, BRAIN. [MASS = 284539
Homo
sapiens (Human) FATTY ACID SYNTHASE. [MASS = 273400
Homo
sapiens (Human) VIMENTIN. [MASS = 53520
Homo
sapiens (Human) ISOFORM LONG OF SPECTRIN BETA CHAIN, BRAIN 1. [MASS = 274631
Homo
sapiens (Human) NESTIN. [MASS = 176706
Homo
sapiens (Human) ALB PROTEIN. [MASS = 71705
Homo
sapiens (Human) SEROTRANSFERRIN PRECURSOR. [MASS = 77050
Homo
sapiens (Human) Heat shock 70 kDa protein 5. [MASS = 72422
Homo
sapiens (Human) ISOFORM 1 OF FIBRONECTIN PRECURSOR. [MASS = 262607
Homo
sapiens (Human) MOESIN. [MASS = 67689
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP761K0511. [MASS = 84843
Homo
sapiens (Human) ISOFORM 1 OF HEAT SHOCK COGNATE 71 KDA PROTEIN. [MASS = 70898
Homo
sapiens (Human) ELONGATION FACTOR 2. [MASS = 95207
Homo
sapiens (Human) PRE-MRNA-PROCESSING-SPLICING FACTOR 8. [MASS = 273600
Homo
sapiens (Human) APOLIPOPROTEIN A-IV PRECURSOR. [MASS = 45399
Homo
sapiens (Human) GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE. [MASS = 35922
Homo
sapiens (Human) ISOFORM 1 OF DNA-DEPENDENT PROTEIN KINASE CATALYTIC
Homo
sapiens (Human) TUBULIN BETA-2C CHAIN. [MASS = 49831
Homo
sapiens (Human) CLATHRIN HEAVY CHAIN 1. [MASS = 191615
Homo
sapiens (Human) MYOSIN-9. [MASS = 226401
Homo
sapiens (Human) T-COMPLEX PROTEIN 1 SUBUNIT BETA. [MASS = 57357
Homo
sapiens (Human) ENDOPLASMIN PRECURSOR. [MASS = 92469
Homo
sapiens (Human) ISOFORM 1 OF CULLIN-ASSOCIATED NEDD8-DISSOCIATED PROTEIN 1.
Homo
sapiens (Human) ISOFORM 2 OF MICROTUBULE-ACTIN CROSSLINKING FACTOR 1,
Homo
sapiens (Human) ISOFORM 2 OF HECT, UBA AND WWE DOMAIN-CONTAINING
Homo
sapiens (Human) CREATINE KINASE B-TYPE. [MASS = 42644
Homo
sapiens (Human) KINESIN HEAVY CHAIN. [MASS = 109685
Homo
sapiens (Human) IMPORTIN BETA-1 SUBUNIT. [MASS = 97170
Homo
sapiens (Human) DNA REPLICATION LICENSING FACTOR MCM2. [MASS = 101896
Homo
sapiens (Human) STRUCTURAL MAINTENANCE OF CHROMOSOME 3. [MASS = 141542
Homo
sapiens (Human) APOLIPOPROTEIN A-I PRECURSOR. [MASS = 30778
Homo
sapiens (Human) ISOFORM M1 OF PYRUVATE KINASE ISOZYMES M1/M2. [MASS = 57931
Homo
sapiens (Human) DPYSL3 PROTEIN. [MASS = 73910
Homo
sapiens (Human) RAN BINDING PROTEIN 5. [MASS = 125545
Homo
sapiens (Human) TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE. [MASS = 89191
Homo
sapiens (Human) ALPHA-FETOPROTEIN PRECURSOR. [MASS = 68678
Homo
sapiens (Human) DIHYDROPYRIMIDINASE-RELATED PROTEIN 1. [MASS = 62184
Homo
sapiens (Human) ATP-DEPENDENT RNA HELICASE A. [MASS = 140881
Homo
sapiens (Human) MATRIN-3. [MASS = 94623
Homo
sapiens (Human) RAB GDP DISSOCIATION INHIBITOR ALPHA [MASS = 50583
Homo
sapiens (Human) APOLIPOPROTEIN E PRECURSOR. [MASS = 36154
Homo
sapiens (Human) C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC. [MASS = 101428
Homo
sapiens (Human) ISOFORM LONG OF SPLICING FACTOR, PROLINE- AND GLUTAMINE-RICH.
Homo
sapiens (Human) ATP-DEPENDENT DNA HELICASE 2 SUBUNIT 2. [MASS = 82573
Homo
sapiens (Human) ISOFORM 1 OF MICROTUBULE-ASSOCIATED PROTEIN 2. [MASS = 199539
Homo
sapiens (Human) PROTEIN DISULFIDE-ISOMERASE A4 PRECURSOR. [MASS = 72932
Homo
sapiens (Human) FIBRINOGEN BETA CHAIN PRECURSOR. [MASS = 55928
Homo
sapiens (Human) PHOSPHOGLYCERATE KINASE 1. [MASS = 44483
Homo
sapiens (Human) DNA REPLICATION LICENSING FACTOR MCM6. [MASS = 92889
Homo
sapiens (Human) ISOFORM 1 OF NUCLEAR AUTOANTIGENIC SPERM PROTEIN.
Homo
sapiens (Human) TRIPARTITE MOTIF-CONTAINING 28 PROTEIN. [MASS = 88550
Homo
sapiens (Human) ISOFORM 1 OF GENERAL TRANSCRIPTION FACTOR II-I. [MASS = 112416
Homo
sapiens (Human) NCL PROTEIN. [MASS = 51641
Homo
sapiens (Human) INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H2 PRECURSOR.
Homo
sapiens (Human) ISOFORM 5 OF INTERLEUKIN ENHANCER-BINDING FACTOR 3.
Homo
sapiens (Human) HEAT SHOCK 70 KDA PROTEIN 4. [MASS = 94300
Homo
sapiens (Human) LUPUS LA PROTEIN. [MASS = 46837
Homo
sapiens (Human) TUBULIN ALPHA-1 CHAIN. [MASS = 49924
Homo
sapiens (Human) POLY [ADP-RIBOSE] POLYMERASE 1. [MASS = 112953
Homo
sapiens (Human) LEUCYL-TRNA SYNTHETASE, CYTOPLASMIC. [MASS = 134466
Homo
sapiens (Human) PUROMYCIN-SENSITIVE AMINOPEPTIDASE. [MASS = 103276
Homo
sapiens (Human) ISOFORM 1 OF STRUCTURAL MAINTENANCE OF CHROMOSOME
Homo
sapiens (Human) ALPHA-1-ANTITRYPSIN PRECURSOR. [MASS = 46737
Homo
sapiens (Human) EUKARYOTIC INITIATION FACTOR 4A-I. [MASS = 46154
Homo
sapiens (Human) T-COMPLEX PROTEIN 1 SUBUNIT ETA. [MASS = 59367
Homo
sapiens (Human) ISOCITRATE DEHYDROGENASE (NADP) CYTOPLASMIC. [MASS = 46659
Homo
sapiens (Human) KINESIN HEAVY CHAIN ISOFORM 5C. [MASS = 109495
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U. [MASS = 88814
Homo
sapiens (Human) SPLICING FACTOR 3B SUBUNIT 1. [MASS = 145815
Homo
sapiens (Human) 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 2.
Homo
sapiens (Human) CHAPERONIN CONTAINING TCP1, SUBUNIT 8. [MASS = 59779
Homo
sapiens (Human) ATP-CITRATE SYNTHASE. [MASS = 120825
Homo
sapiens (Human) ISOFORM GAMMA-B OF FIBRINOGEN GAMMA CHAIN
Homo
sapiens (Human) ISOFORM 1 OF EXPORTIN-2. [MASS = 110417
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN
Homo
sapiens (Human) ISOFORM 2 OF FAR UPSTREAM ELEMENT-BINDING
Homo
sapiens (Human) SPLICING FACTOR 3 SUBUNIT 1. [MASS = 88886
Homo
sapiens (Human) HEAT SHOCK PROTEIN HSP 90-ALPHA 2. [MASS = 98113
Homo
sapiens (Human) 14-3-3 PROTEIN EPSILON. [MASS = 29174
Homo
sapiens (Human) ISOFORM 1 OF VINCULIN. [MASS = 116591
Homo
sapiens (Human) ALANYL-TRNA SYNTHETASE. [MASS = 106801
Homo
sapiens (Human) DNA REPLICATION LICENSING FACTOR MCM4. [MASS = 96558
Homo
sapiens (Human) ISOFORM 1 OF SPECTRIN BETA CHAIN, BRAIN 2. [MASS = 271295
Homo
sapiens (Human) FAR UPSTREAM ELEMENT-BINDING PROTEIN 2. [MASS = 72709
Homo
sapiens (Human) PROTEIN DISULFIDE-ISOMERASE A3 PRECURSOR. [MASS = 56782
Homo
sapiens (Human) RAB GDP DISSOCIATION INHIBITOR BETA. [MASS = 50663
Homo
sapiens (Human) DEAH (ASP-GLU-ALA-HIS) BOX POLYPEPTIDE 15. [MASS = 92829
Homo
sapiens (Human) LACTATE DEHYDROGENASE A. [MASS = 36689
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 10.
Homo
sapiens (Human) ISOFORM BETA OF HEAT-SHOCK PROTEIN 105 KDA. [MASS = 92116
Homo
sapiens (Human) ISOFORM 1 OF POLYADENYLATE-BINDING PROTEIN 1.
Homo
sapiens (Human) 6-PHOSPHOGLUCONATE DEHYDROGENASE,
Homo
sapiens (Human) ISOFORM 1 OF HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) DREBRIN. [MASS = 71294
Homo
sapiens (Human) EXPORTIN-1. [MASS = 123386
Homo
sapiens (Human) SMARCA4 ISOFORM 2. [MASS = 188149
Homo
sapiens (Human) HYDROXYMETHYLGLUTARYL-COA SYNTHASE,
Homo
sapiens (Human) RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE
Homo
sapiens (Human) HNRPA2B1 PROTEIN. [MASS = 28412
Homo
sapiens (Human) ENOLASE 1. [MASS = 47169
Homo
sapiens (Human) ALPHA-ACTININ-1. [MASS = 103058
Homo
sapiens (Human) DIHYDROPYRIMIDINASE-LIKE 2. [MASS = 67017
Homo
sapiens (Human) DIHYDROPYRIMIDINASE-RELATED PROTEIN 4. [MASS = 61878
Homo
sapiens (Human) INSULIN-LIKE GROWTH FACTOR 2 MRNA BINDING
Homo
sapiens (Human) ISOFORM 2 OF NEUTRAL ALPHA-GLUCOSIDASE AB
Homo
sapiens (Human) ISOFORM P150 OF DYNACTIN-1. [MASS = 141695
Homo
sapiens (Human) SPLICING FACTOR 3B SUBUNIT 2. [MASS = 100228
Homo
sapiens (Human) HEMOGLOBIN SUBUNIT EPSILON. [MASS = 16072
Homo
sapiens (Human) DNA REPLICATION LICENSING FACTOR MCM5. [MASS = 82286
Homo
sapiens (Human) FASCIN. [MASS = 54399
Homo
sapiens (Human) GLUTAMYL-PROLYL TRNA SYNTHETASE. [MASS = 170591
Homo
sapiens (Human) DNA REPLICATION LICENSING FACTOR MCM3. [MASS = 90981
Homo
sapiens (Human) UBIQUITIN-ACTIVATING ENZYME E1. [MASS = 117849
Homo
sapiens (Human) TRANSTHYRETIN PRECURSOR. [MASS = 15887
Homo
sapiens (Human) SPLICING FACTOR 3B SUBUNIT 3. [MASS = 135592
Homo
sapiens (Human) PHOSPHOFRUCTOKINASE, MUSCLE. [MASS = 85183
Homo
sapiens (Human) TUBULIN BETA-3 CHAIN. [MASS = 50433
Homo
sapiens (Human) ALPHA-ACTININ-4. [MASS = 104854
Homo
sapiens (Human) ISOFORM 1 OF GELSOLIN PRECURSOR. [MASS = 85698
Homo
sapiens (Human) MULTIFUNCTIONAL PROTEIN ADE2. [MASS = 49679
Homo
sapiens (Human) DIHYDROPYRIMIDINASE-RELATED PROTEIN 5. [MASS = 61421
Homo
sapiens (Human) ANNEXIN A5. [MASS = 35806
Homo
sapiens (Human) L-LACTATE DEHYDROGENASE B CHAIN. [MASS = 36507
Homo
sapiens (Human) CALNEXIN PRECURSOR. [MASS = 67568
Homo
sapiens (Human) ISOFORM 1 OF FIBRINOGEN ALPHA CHAIN PRECURSOR.
Homo
sapiens (Human) NON-POU DOMAIN-CONTAINING OCTAMER-BINDING PROTEIN.
Homo
sapiens (Human) 116 KDA U5 SMALL NUCLEAR RIBONUCLEOPROTEIN
Homo
sapiens (Human) STRESS-INDUCED-PHOSPHOPROTEIN 1. [MASS = 62639
Homo
sapiens (Human) COATOMER SUBUNIT ALPHA. [MASS = 138332
Homo
sapiens (Human) T-COMPLEX PROTEIN 1 SUBUNIT DELTA. [MASS = 57793
Homo
sapiens (Human) ISOFORM 1 OF HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) CDNA FLJ45525 FIS, CLONE BRTHA2026311, HIGHLY SIMILAR
Homo
sapiens (Human) ATP-DEPENDENT RNA HELICASE DDX3X. [MASS = 73112
Homo
sapiens (Human) 26S PROTEASE REGULATORY SUBUNIT 6A. [MASS = 49204
Homo
sapiens (Human) GLYCOGEN PHOSPHORYLASE, BRAIN FORM. [MASS = 96565
Homo
sapiens (Human) PROTEASOME 26S NON-ATPASE SUBUNIT 11 VARIANT
Homo
sapiens (Human) DNA DAMAGE-BINDING PROTEIN 1. [MASS = 126968
Homo
sapiens (Human) RAS GTPASE-ACTIVATING-LIKE PROTEIN IQGAP1.
Homo
sapiens (Human) STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING
Homo
sapiens (Human) UBIQUITIN-ACTIVATING ENZYME E1. [MASS = 56852
Homo
sapiens (Human) ISOFORM 2 OF PROTEIN KIAA1967. [MASS = 103030
Homo
sapiens (Human) ISOFORM 2 OF MICROTUBULE-ASSOCIATED PROTEIN 4.
Homo
sapiens (Human) ISOFORM GTBP-ALT OF DNA MISMATCH REPAIR PROTEIN
Homo
sapiens (Human) 150 KDA OXYGEN-REGULATED PROTEIN PRECURSOR.
Homo
sapiens (Human) TALDO1 PROTEIN. [MASS = 35329
Homo
sapiens (Human) STATHMIN. [MASS = 17171
Homo
sapiens (Human) ISOFORM 1 OF CHROMODOMAIN HELICASE-DNA-BINDING
Homo
sapiens (Human) RUVB-LIKE 2. [MASS = 51025
Homo
sapiens (Human) PLASMA PROTEASE C1 INHIBITOR PRECURSOR. [MASS = 55154
Homo
sapiens (Human) HEAT SHOCK PROTEIN HSP 90-ALPHA 2. [MASS = 98113
Homo
sapiens (Human) PIGMENT EPITHELIUM-DERIVED FACTOR PRECURSOR.
Homo
sapiens (Human) ISOFORM LONG OF UBIQUITIN CARBOXYL-TERMINAL
Homo
sapiens (Human) PRO2275. [MASS = 13097
Homo
sapiens (Human) T-COMPLEX PROTEIN 1 SUBUNIT ZETA. [MASS = 57893
Homo
sapiens (Human) MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE.
Homo
sapiens (Human) TALIN-1. [MASS = 269767
Homo
sapiens (Human) VACUOLAR PROTEIN SORTING 35. [MASS = 91707
Homo
sapiens (Human) T-COMPLEX PROTEIN 1 SUBUNIT EPSILON. [MASS = 59671
Homo
sapiens (Human) ISOFORM 3 OF POLYPYRIMIDINE TRACT-BINDING PROTEIN 2.
Homo
sapiens (Human) ISOFORM 1 OF REGULATOR OF NONSENSE TRANSCRIPTS 1.
Homo
sapiens (Human) UBIQUITIN-LIKE 1-ACTIVATING ENZYME E1B. [MASS = 71224
Homo
sapiens (Human) ISOFORM 1 OF CLATHRIN HEAVY CHAIN 2. [MASS = 187030
Homo
sapiens (Human) SEPTIN-7. [MASS = 50809
Homo
sapiens (Human) ADENYLYL CYCLASE-ASSOCIATED PROTEIN 1. [MASS = 51542
Homo
sapiens (Human) VALYL-TRNA SYNTHETASE. [MASS = 140476
Homo
sapiens (Human) DNA MISMATCH REPAIR PROTEIN MSH2. [MASS = 104743
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN R.
Homo
sapiens (Human) FRUCTOSE-BISPHOSPHATE ALDOLASE A. [MASS = 39289
Homo
sapiens (Human) THREONYL-TRNA SYNTHETASE, CYTOPLASMIC. [MASS = 83435
Homo
sapiens (Human) STRESS-70 PROTEIN, MITOCHONDRIAL PRECURSOR.
Homo
sapiens (Human) ELONGATION FACTOR 1-DELTA. [MASS = 30991
Homo
sapiens (Human) CYTOSKELETON-ASSOCIATED PROTEIN 5. [MASS = 225509
Homo
sapiens (Human) CALRETICULIN PRECURSOR. [MASS = 48142
Homo
sapiens (Human) PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE.
Homo
sapiens (Human) ISOFORM 4 OF TUBULIN-SPECIFIC CHAPERONE D.
Homo
sapiens (Human) ISOFORM B OF ARSENITE-RESISTANCE PROTEIN 2.
Homo
sapiens (Human) ISOFORM 2 OF STRUCTURAL MAINTENANCE OF
Homo
sapiens (Human) ISOFORM 1 OF RETICULON-4. [MASS = 130102
Homo
sapiens (Human) HEMOGLOBIN SUBUNIT ZETA. [MASS = 15506
Homo
sapiens (Human) HSPC117 PROTEIN. [MASS = 55210
Homo
sapiens (Human) ISOFORM 1 OF SQUAMOUS CELL CARCINOMA ANTIGEN
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S4, X ISOFORM. [MASS = 29467
Homo
sapiens (Human) TRANSKETOLASE. [MASS = 67878
Homo
sapiens (Human) ISOFORM 2 OF NUCLEOPHOSMIN. [MASS = 29465
Homo
sapiens (Human) UNCHARACTERIZED PROTEIN C20ORF77. [MASS = 36900
Homo
sapiens (Human) T-COMPLEX PROTEIN 1 SUBUNIT ALPHA. [MASS = 60344
Homo
sapiens (Human) INTERLEUKIN ENHANCER-BINDING FACTOR 2. [MASS = 43062
Homo
sapiens (Human) 26S PROTEASE REGULATORY SUBUNIT 8. [MASS = 45626
Homo
sapiens (Human) ISOFORM 1 OF DNA REPLICATION LICENSING FACTOR
Homo
sapiens (Human) GAMMA-ENOLASE. [MASS = 47137
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP451D234. [MASS = 109187
Homo
sapiens (Human) TUBULIN, BETA 2. [MASS = 49907
Homo
sapiens (Human) ISOFORM 1 OF PROTEIN ARGININE
Homo
sapiens (Human) VILLIN 2. [MASS = 69413
Homo
sapiens (Human) RADIXIN. [MASS = 68564
Homo
sapiens (Human) ISOFORM 2 OF SWI/SNF-RELATED MATRIX-ASSOCIATED
Homo
sapiens (Human) ASPARTYL-TRNA SYNTHETASE. [MASS = 57136
Homo
sapiens (Human) D-3-PHOSPHOGLYCERATE DEHYDROGENASE. [MASS = 56519
Homo
sapiens (Human) CAD PROTEIN. [MASS = 242984
Homo
sapiens (Human) CTP SYNTHASE 1. [MASS = 66690
Homo
sapiens (Human) SERINE-THREONINE KINASE RECEPTOR-ASSOCIATED
Homo
sapiens (Human) ADENOSYLHOMOCYSTEINASE. [MASS = 47585
Homo
sapiens (Human) ELONGATION FACTOR 1-GAMMA. [MASS = 49988
Homo
sapiens (Human) CDNA FLJ45706 FIS, CLONE FEBRA2028457, HIGHLY SIMILAR
Homo
sapiens (Human) CHAPERONIN CONTAINING TCP1, SUBUNIT 3 ISOFORM B.
Homo
sapiens (Human) ENO1P PROTEIN. [MASS = 42342
Homo
sapiens (Human) PREDICTED: SIMILAR TO HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) ISOFORM SHORT OF RECEPTOR-TYPE TYROSINE-PROTEIN
Homo
sapiens (Human) 26S PROTEASE REGULATORY SUBUNIT 7. [MASS = 48503
Homo
sapiens (Human) PROTEIN DISULFIDE-ISOMERASE PRECURSOR. [MASS = 57116
Homo
sapiens (Human) FACT COMPLEX SUBUNIT SPT16. [MASS = 119914
Homo
sapiens (Human) LUMICAN PRECURSOR. [MASS = 38429
Homo
sapiens (Human) PROLIFERATION-ASSOCIATED PROTEIN 2G4. [MASS = 43656
Homo
sapiens (Human) IARS PROTEIN. [MASS = 120627
Homo
sapiens (Human) U5 SMALL NUCLEAR RIBONUCLEOPROTEIN 200 KDA
Homo
sapiens (Human) UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7.
Homo
sapiens (Human) INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN
Homo
sapiens (Human) ATP-DEPENDENT RNA HELICASE DDX1. [MASS = 82432
Homo
sapiens (Human) ISOFORM 1 OF PROBABLE ATP-DEPENDENT RNA
Homo
sapiens (Human) RNA-BINDING PROTEIN 12. [MASS = 97395
Homo
sapiens (Human) TRANSPORTIN 1. [MASS = 102355
Homo
sapiens (Human) GTP-BINDING NUCLEAR PROTEIN RAN. [MASS = 24292
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S18. [MASS = 17719
Homo
sapiens (Human) ACTIN, AORTIC SMOOTH MUSCLE [MASS = 42009
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 4
Homo
sapiens (Human) SPLICING FACTOR, ARGININE/SERINE-RICH 1. [MASS = 27745
Homo
sapiens (Human) PEROXIREDOXIN-1. [MASS = 22110
Homo
sapiens (Human) GLUTATHIONE S-TRANSFERASE P. [MASS = 23225
Homo
sapiens (Human) ACTIN, CYTOPLASMIC 1. [MASS = 41737
Homo
sapiens (Human) HEAT SHOCK 70 KDA PROTEIN 1L. [MASS = 70375
Homo
sapiens (Human) COFILIN-1. [MASS = 18371
Homo
sapiens (Human) ANGIOTENSINOGEN PRECURSOR. [MASS = 53154
Homo
sapiens (Human) TUBULIN BETA-2 CHAIN. [MASS = 49671
Homo
sapiens (Human) ISOFORM 1 OF CYTOSOLIC ACYL COENZYME A THIOESTER
Homo
sapiens (Human) HEAT SHOCK 70 KDA PROTEIN 1. [MASS = 70052
Homo
sapiens (Human) 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 12.
Homo
sapiens (Human) GAMMA-G GLOBIN (FRAGMENT). [MASS = 16969
Homo
sapiens (Human) 14-3-3 PROTEIN THETA. WASS = 27764
Homo
sapiens (Human) MALATE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR.
Homo
sapiens (Human) A-KINASE ANCHOR PROTEIN 12 ISOFORM 2. [MASS = 181690
Homo
sapiens (Human) LIVER PHOSPHOFRUCTOKINASE ISOFORM A. [MASS = 90577
Homo
sapiens (Human) 14-3-3 PROTEIN ZETA/DELTA. [MASS = 27745
Homo
sapiens (Human) ATP-DEPENDENT RNA HELICASE A. [MASS = 140881
Homo
sapiens (Human) ISOFORM C1 OF HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) NUCLEOSIDE DIPHOSPHATE KINASE A. [MASS = 17149
Homo
sapiens (Human) TRIPEPTIDYL-PEPTIDASE 2. [MASS = 138219
Homo
sapiens (Human) RCTPI1 (FRAGMENT). [MASS = 26943
Homo
sapiens (Human) ISOFORM 1 OF POLYPYRIMIDINE TRACT-BINDING PROTEIN 1.
Homo
sapiens (Human) CELLULAR RETINOIC ACID-BINDING PROTEIN 1. [MASS = 15434
Homo
sapiens (Human) MALATE DEHYDROGENASE, CYTOPLASMIC. [MASS = 36295
Homo
sapiens (Human) ESTERASE D. [MASS = 31463
Homo
sapiens (Human) ISOFORM 1 OF HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) ISOFORM SHORT OF RNA-BINDING PROTEIN FUS. [MASS = 53355
Homo
sapiens (Human) F-ACTIN CAPPING PROTEIN ALPHA-1 SUBUNIT. [MASS = 32792
Homo
sapiens (Human) PROBABLE ATP-DEPENDENT RNA HELICASE DDX48. [MASS = 46740
Homo
sapiens (Human) INORGANIC PYROPHOSPHATASE. [MASS = 32660
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A0. [MASS = 30841
Homo
sapiens (Human) ISOFORM 1 OF GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE
Homo
sapiens (Human) ELAV. [MASS = 42417
Homo
sapiens (Human) CDNA FLJ33352 FIS, CLONE BRACE2005087, WEAKLY SIMILAR
Homo
sapiens (Human) PREDICTED: SIMILAR TO ATP-DEPENDENT DNA HELICASE II,
Homo
sapiens (Human) IMPORTIN-7. [MASS = 119517
Homo
sapiens (Human) ISOFORM 1 OF CULLIN-3. [MASS = 88930
Homo
sapiens (Human) 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 6. [MASS = 45531
Homo
sapiens (Human) PROTEIN PHOSPHATASE 2C ISOFORM GAMMA. [MASS = 59272
Homo
sapiens (Human) HYPOTHETICAL PROTEIN LOC345651. [MASS = 42003
Homo
sapiens (Human) 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3. [MASS = 60978
Homo
sapiens (Human) ISOFORM 1 OF EUKARYOTIC TRANSLATION INITIATION FACTOR 3
Homo
sapiens (Human) 60S ACIDIC RIBOSOMAL PROTEIN P0. [MASS = 34274
Homo
sapiens (Human) FACT COMPLEX SUBUNIT SSRP1. [MASS = 81075
Homo
sapiens (Human) NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 4. [MASS = 43011
Homo
sapiens (Human) ISOFORM BETA-2 OF DNA TOPOISOMERASE 2-BETA. [MASS = 183267
Homo
sapiens (Human) GARS PROTEIN. [MASS = 84648
Homo
sapiens (Human) STRUCTURAL MAINTENANCE OF CHROMOSOME 1-LIKE 1 PROTEIN.
Homo
sapiens (Human) DNA-DIRECTED RNA POLYMERASE II 140 KDA POLYPEPTIDE.
Homo
sapiens (Human) NESTIN. [MASS = 177439
Homo
sapiens (Human) PREDICTED: SIMILAR TO PEPTIDYLPROLYL ISOMERASE
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D-LIKE. [MASS = 46438
Homo
sapiens (Human) ISOFORM 2C OF CYTOPLASMIC DYNEIN 1 INTERMEDIATE CHAIN 2.
Homo
sapiens (Human) CSNK2A1 PROTEIN. [MASS = 45909
Homo
sapiens (Human) PEROXIREDOXIN-6. [MASS = 24904
Homo
sapiens (Human) HIGH MOBILITY GROUP PROTEIN 1-LIKE 10. [MASS = 24218
Homo
sapiens (Human) CALMODULIN. [MASS = 16706
Homo
sapiens (Human) NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 1. [MASS = 45374
Homo
sapiens (Human) IMPORTIN-9. [MASS = 115832
Homo
sapiens (Human) ISOFORM 1 OF PROTEIN SET. [MASS = 33489
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H1. [MASS = 49229
Homo
sapiens (Human) SEPTIN-2. [MASS = 41487
Homo
sapiens (Human) ATAXIN-10. [MASS = 53489
Homo
sapiens (Human) COATOMER SUBUNIT BETA. [MASS = 107139
Homo
sapiens (Human) ISOFORM 2 OF DNA REPLICATION LICENSING FACTOR MCM7.
Homo
sapiens (Human) IRON-RESPONSIVE ELEMENT-BINDING PROTEIN 1. [MASS = 98399
Homo
sapiens (Human) TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE
Homo
sapiens (Human) 26S PROTEASE REGULATORY SUBUNIT S10B. [MASS = 44173
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP781K0743. [MASS = 105850
Homo
sapiens (Human) UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1.
Homo
sapiens (Human) ISOFORM 1 OF HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN
Homo
sapiens (Human) TUBULIN-TYROSINE LIGASE-LIKE PROTEIN 12. [MASS = 74404
Homo
sapiens (Human) ISOFORM 2 OF NUCLEAR MITOTIC APPARATUS PROTEIN 1.
Homo
sapiens (Human) ALPHA ISOFORM OF REGULATORY SUBUNIT A, PROTEIN
Homo
sapiens (Human) ISOFORM 4 OF HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) CCR4-NOT TRANSCRIPTION COMPLEX, SUBUNIT 1 ISOFORM A.
Homo
sapiens (Human) PROFILIN-1. [MASS = 14923
Homo
sapiens (Human) PROLIFERATING CELL NUCLEAR ANTIGEN. [MASS = 28769
Homo
sapiens (Human) METHIONYL-TRNA SYNTHETASE. [MASS = 101116
Homo
sapiens (Human) UBIQUITIN-LIKE 1-ACTIVATING ENZYME E1A. [MASS = 38450
Homo
sapiens (Human) ALCOHOL DEHYDROGENASE. [MASS = 36442
Homo
sapiens ,(Human) ADP-RIBOSYLATION FACTOR 1. [MASS = 20566
Homo
sapiens (Human) THIOREDOXIN-LIKE PROTEIN 1. [MASS = 32120
Homo
sapiens (Human) ISOFORM 1 OF 26S PROTEASOME NON-ATPASE REGULATORY
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 8.
Homo
sapiens (Human) VESICLE-FUSING ATPASE. [MASS = 82654
Homo
sapiens (Human) Complement component 3 precursor. [MASS = 187306
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 6.
Homo
sapiens (Human) ATP-DEPENDENT DNA HELICASE 2 SUBUNIT 1. [MASS = 69712
Homo
sapiens (Human) ISOFORM 1 OF HOST CELL FACTOR. [MASS = 208842
Homo
sapiens (Human) METASTASIS-ASSOCIATED PROTEIN MTA2. [MASS = 75023
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L ISOFORM
Homo
sapiens (Human) 26S PROTEASE REGULATORY SUBUNIT 4. [MASS = 49185
Homo
sapiens (Human) UDP-GLUCOSE CERAMIDE GLUCOSYLTRANSFERASE-LIKE 1
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 5B. [MASS = 138800
Homo
sapiens (Human) ISOFORM V0 OF VERSICAN CORE PROTEIN PRECURSOR. [MASS = 372820
Homo
sapiens (Human) TUBULIN BETA-1 CHAIN. [MASS = 50327
Homo
sapiens (Human) ISOFORM 1 OF FILAMIN-B. [MASS = 278195
Homo
sapiens (Human) CONTACTIN-2 PRECURSOR. [MASS = 113393
Homo
sapiens (Human) UBIQUITIN SPECIFIC PROTEASE 9, X-LINKED ISOFORM 4. [MASS = 290497
Homo
sapiens (Human) ISOFORM 1 OF HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN
Homo
sapiens (Human) HEMOGLOBIN SUBUNIT ALPHA: [MASS = 15126
Homo
sapiens (Human) ASTROCYTIC PHOSPHOPROTEIN PEA-15. [MASS = 15040
Homo
sapiens (Human) 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 7. [MASS = 37025
Homo
sapiens (Human) PROTEASOME SUBUNIT BETA TYPE 1. [MASS = 26489
Homo
sapiens (Human) ALPHA-CENTRACTIN. [MASS = 42614
Homo
sapiens (Human) ISOFORM 1 OF PLASMINOGEN ACTIVATOR INHIBITOR 1
Homo
sapiens (Human) CALPONIN-3. [MASS = 36414
Homo
sapiens (Human) PROTEASOME SUBUNIT ALPHA TYPE 2. [MASS = 25767
Homo
sapiens (Human) PHOSPHATIDYLETHANOLAMINE-BINDING. PROTEIN 1. [MASS = 20926
Homo
sapiens (Human) METHIONINE ADENOSYLTRANSFERASE II, BETA ISOFORM 1.
Homo
sapiens (Human) VITRONECTIN PRECURSOR. [MASS = 54306
Homo
sapiens (Human) PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE-ASSOCIATED
Homo
sapiens (Human) CONDENSIN COMPLEX SUBUNIT 3. [MASS = 114334
Homo
sapiens (Human) PEROXIREDOXIN-2. [MASS = 21761
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1
Homo
sapiens (Human) RHO GDP-DISSOCIATION INHIBITOR 1. [MASS = 23076
Homo
sapiens (Human) ISOFORM 1 OF DIPEPTIDYL-PEPTIDASE 3. [MASS = 82589
Homo
sapiens (Human) ISOFORM 1 OF ACTIN-LIKE PROTEIN 6A. [MASS = 47461
Homo
sapiens (Human) ISOFORM 2 OF NSFL1 COFACTOR P47. [MASS = 37325
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA,
Homo
sapiens (Human) ELONGATION FACTOR 1-ALPHA 2. [MASS = 50470
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP564E242. [MASS = 31424
Homo
sapiens (Human) 3-MERCAPTOPYRUVATE SULFURTRANSFERASE. [MASS = 33047
Homo
sapiens (Human) CLUSTERIN PRECURSOR. [MASS = 52495
Homo
sapiens (Human) REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT. [MASS = 68138
Homo
sapiens (Human) DYNACTIN 2. [MASS = 44820
Homo
sapiens (Human) THIOREDOXIN-LIKE PROTEIN 2. [MASS = 37432
Homo
sapiens (Human) ISOFORM 2 OF CADHERIN-11 PRECURSOR. [MASS = 76541
Homo
sapiens (Human) S-ADENOSYLMETHIONINE SYNTHETASE ISOFORM TYPE-2. [MASS = 43661
Homo
sapiens (Human) ISOFORM 1 OF ELAV-LIKE PROTEIN 3. [MASS = 39547
Homo
sapiens (Human) SIMILAR TO ANNEXIN A2 ISOFORM 1. [MASS = 38659
Homo
sapiens (Human) ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC. [MASS = 46116
Homo
sapiens (Human) NUCLEAR MIGRATION PROTEIN NUDC. [MASS = 38243
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S19. [MASS = 15929
Homo
sapiens (Human) RNA BINDING PROTEIN (FRAGMENT). [MASS = 32550
Homo
sapiens (Human) ISOFORM 1 OF DNA. [MASS = 189566
Homo
sapiens (Human) ISOFORM 2 OF SERINE/THREONINE-PROTEIN KINASE DCAMKL1.
Homo
sapiens (Human) PROTEIN TRANSPORT PROTEIN SEC23A. [MASS = 86147
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L4. [MASS = 47566
Homo
sapiens (Human) PROTEASOME 26S NON-ATPASE SUBUNIT 13 ISOFORM 2. [MASS = 39871
Homo
sapiens (Human) ISOFORM 4 OF AFADIN. [MASS = 206804
Homo
sapiens (Human) DIHYDROPYRIMIDINASE-RELATED PROTEIN 2. [MASS = 62294
Homo
sapiens (Human) WUGSC:H_RG054D04.1 PROTEIN. [MASS = 29037
Homo
sapiens (Human) VACUOLAR ATP SYNTHASE CATALYTIC SUBUNIT A, UBIQUITOUS
Homo
sapiens (Human) MGEA5 PROTEIN. [MASS = 95331
Homo
sapiens (Human) GLUCOSIDASE 2 SUBUNIT BETA PRECURSOR. [MASS = 59296
Homo
sapiens (Human) CYSTEINYL-TRNA SYNTHETASE ISOFORM C.- [MASS = 94638
Homo
sapiens (Human) BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH. [MASS = 64616
Homo
sapiens (Human) HSC70-INTERACTING PROTEIN. [MASS = 41332
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S3. [MASS = 26688
Homo
sapiens (Human) GALECTIN-3-BINDING PROTEIN PRECURSOR. [MASS = 65331
Homo
sapiens (Human) ISOFORM 1 OF COMPLEMENT FACTOR B PRECURSOR (FRAGMENT).
Homo
sapiens (Human) ISOFORM 1 OF POLYADENYLATE-BINDING PROTEIN 4. [MASS = 70783
Homo
sapiens (Human) SPERMIDINE SYNTHASE. [MASS = 33825
Homo
sapiens (Human) PROTEIN DJ-1. [MASS = 19891
Homo
sapiens (Human) ISOFORM 1 OF HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN
Homo
sapiens (Human) RAB1A, MEMBER RAS ONCOGENE FAMILY. [MASS = 22678
Homo
sapiens (Human) WD40 PROTEIN. [MASS = 35079
Homo
sapiens (Human) ISOFORM B1 OF HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS
Homo
sapiens (Human) RUVB-LIKE 1. [MASS = 50228
Homo
sapiens (Human) RNA BINDING MOTIF PROTEIN, X-LINKED-LIKE 1. [MASS = 42142
Homo
sapiens (Human) PHOSPHOGLYCERATE MUTASE 2. [MASS = 28635
Homo
sapiens (Human) DNA POLYMERASE DELTA CATALYTIC SUBUNIT. [MASS = 123631
Homo
sapiens (Human) SF3B3 PROTEIN. [MASS = 30210
Homo
sapiens (Human) RETINOBLASTOMA-ASSOCIATED FACTOR 600. [MASS = 185447
Homo
sapiens (Human) TUBULIN BETA-4 CHAIN. [MASS = 49586
Homo
sapiens (Human) PROTHYMOSIN ALPHA. [MASS = 12203
Homo
sapiens (Human) 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 14. [MASS = 34577
Homo
sapiens (Human) GLYOXYLATE REDUCTASE/HYDROXYPYRUVATE REDUCTASE.
Homo
sapiens (Human) DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE. [MASS = 35423
Homo
sapiens (Human) ISOFORM 2 OF GUANINE NUCLEOTIDE-BINDING PROTEIN G(I),
Homo
sapiens (Human) ISOFORM 1 OF PROTEIN 4. 1. [MASS = 97017
Homo
sapiens (Human) ADP-SUGAR PYROPHOSPHATASE. [MASS = 24328
Homo
sapiens (Human) HISTONE H2B TYPE 2-E. [MASS = 13789
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN F. [MASS = 45672
Homo
sapiens (Human) PREDICTED: SIMILAR TO HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) NG, NG-DIMETHYLARGININE DIMETHYLAMINOHYDROLASE 2.
Homo
sapiens (Human) SERYL-TRNA SYNTHETASE. [MASS = 58646
Homo
sapiens (Human) NUCLEASE SENSITIVE ELEMENT-BINDING PROTEIN 1.
Homo
sapiens (Human) ISOFORM 1 OF CLEAVAGE AND POLYADENYLATION SPECIFICITY
Homo
sapiens (Human) POLY(RC)-BINDING PROTEIN 1. [MASS = 37498
Homo
sapiens (Human) ISOFORM B OF FIBULIN-1 PRECURSOR. [MASS = 77186
Homo
sapiens (Human) FK506-BINDING PROTEIN 3. [MASS = 25177
Homo
sapiens (Human) CTTN PROTEIN. [MASS = 70959
Homo
sapiens (Human) PREDICTED: SIMILAR TO HETEROGENEOUS NUCLEAR
Homo
sapiens (Human) PRE-MRNA-SPLICING FACTOR 19. [MASS = 55181
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S15. [MASS = 16909
Homo
sapiens (Human) GLUTAMINYL-TRNA SYNTHETASE. [MASS = 87799
Homo
sapiens (Human) PROTEIN RCC2. [MASS = 56085
Homo
sapiens (Human) DOUBLECORTEX\; LISSENCEPHALY, X-LINKED. [MASS = 49847
Homo
sapiens (Human) ISOFORM B OF MANNOSE-6-PHOSPHATE RECEPTOR-BINDING
Homo
sapiens (Human) COATOMER SUBUNIT BETA’. [MASS = 102356
Homo
sapiens (Human) HEPATOMA-DERIVED GROWTH FACTOR. [MASS = 26788
Homo
sapiens (Human) ELAV-LIKE PROTEIN 1. [MASS = 36092
Homo
sapiens (Human) PP856. [MASS = 43833
Homo
sapiens (Human) RAS-RELATED PROTEIN RAB-2A. [MASS = 23546
Homo
sapiens (Human) ISOFORM 2 OF PROTEIN ENABLED HOMOLOG. [MASS = 63924
Homo
sapiens (Human) ISOFORM 1 OF BETA-CATENIN. [MASS = 85497
Homo
sapiens (Human) AP-2 COMPLEX SUBUNIT ALPHA-2. [MASS = 104150
Homo
sapiens (Human) EEF1A1 PROTEIN. [MASS = 47869
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S17. [MASS = 15419
Homo
sapiens (Human) 14-3-3 PROTEIN GAMMA. [MASS = 28171
Homo
sapiens (Human) RAS-GTPASE-ACTIVATING PROTEIN-BINDING PROTEIN 1. [MASS = 52164
Homo
sapiens (Human) POLY(RC)-BINDING PROTEIN 2 ISOFORM B. [MASS = 38222
Homo
sapiens (Human) EXPORTIN-T. [MASS = 109964
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 2C 1. [MASS = 97214
Homo
sapiens (Human) PREDICTED: STRUCTURAL MAINTENANCE OF CHROMOSOMES
Homo
sapiens (Human) PREGNANCY ZONE PROTEIN PRECURSOR. [MASS = 163836
Homo
sapiens (Human) ISOFORM 1 OF LIM AND SH3 DOMAIN PROTEIN 1. [MASS = 29717
Homo
sapiens (Human) SIMILAR TO NESTIN. [MASS = 175922
Homo
sapiens (Human) ISOFORM 1 OF FILAMIN-C. [MASS = 291293
Homo
sapiens (Human) MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER 1.
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S13. [MASS = 17091
Homo
sapiens (Human) MITOGEN-ACTIVATED PROTEIN KINASE 1. [MASS = 41259
Homo
sapiens (Human) UDP-GLUCOSE 6-DEHYDROGENASE. [MASS = 55024
Homo
sapiens (Human) PROBABLE ATP-DEPENDENT RNA HELICASE DDX5. [MASS = 69148
Homo
sapiens (Huirian) ISOFORM 1 OF SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 3.
Homo
sapiens (Human) HSP90 CO-CHAPERONE CDC37. [MASS = 44468
Homo
sapiens (Human) AMBP PROTEIN PRECURSOR. [MASS = 38999
Homo
sapiens (Human) CGI-150 PROTEIN. [MASS = 55012
Homo
sapiens (Human) PRE-MRNA-PROCESSING FACTOR 6 HOMOLOG. [MASS = 106925
Homo
sapiens (Human) TAR DNA-BINDING PROTEIN 43. [MASS = 44740
Homo
sapiens (Human) ISOFORM 1 OF KH DOMAIN-CONTAINING, RNA-BINDING, SIGNAL
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP451P021. [MASS = 117896
Homo
sapiens (Human) KH-TYPE SPLICING REGULATORY PROTEIN. [MASS = 73115
Homo
sapiens (Human) ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL
Homo
sapiens (Human) 182 KDA TANKYRASE 1-BINDING PROTEIN. [MASS = 181816
Homo
sapiens (Human) CONDENSIN COMPLEX SUBUNIT 1. [MASS = 157169
Homo
sapiens (Human) ISOFORM 1 OF ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN
Homo
sapiens (Human) SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2. [MASS = 13527
Homo
sapiens (Human) FUSE-BINDING PROTEIN-INTERACTING REPRESSOR ISOFORM A.
Homo
sapiens (Human) COP9 SIGNALOSOME COMPLEX SUBUNIT 6. [MASS = 36163
Homo
sapiens (Human) ACETYL-COA CARBOXYLASE 1. [MASS = 265040
Homo
sapiens (Human) ISOFORM 2 OF SUPPRESSOR OF G2 ALLELE OF SKP1 HOMOLOG.
Homo
sapiens (Human) ISOFORM 5 OF DYNAMIN-1-LIKE PROTEIN. [MASS = 79123
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L5. [MASS = 34231
Homo
sapiens (Human) PREDICTED: SIMILAR TO RIBOSOMAL PROTEIN L13 ISOFORM 1.
Homo
sapiens (Human) INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE 2. [MASS = 55805
Homo
sapiens (Human) ISOFORM 1 OF PHOSPHOSERINE AMINOTRANSFERASE. [MASS = 40423
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C-LIKE 1.
Homo
sapiens (Human) UBIQUITIN-CONJUGATING ENZYME E2 N. [MASS = 17138
Homo
sapiens (Human) PROTEIN KINASE C-BINDING PROTEIN NELL2 PRECURSOR.
Homo
sapiens (Human) ISOFORM 1 OF DYNAMIN-2. [MASS = 98064
Homo
sapiens (Human) NEURONAL PROTEIN NP25. [MASS = 24893
Homo
sapiens (Human) SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE
Homo
sapiens (Human) PROLYL ENDOPEPTIDASE. [MASS = 80764
Homo
sapiens (Human) 60S ACIDIC RIBOSOMAL PROTEIN P2. [MASS = 11665
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S7. [MASS = 22127
Homo
sapiens (Human) ISOFORM 1 OF DNA-BINDING PROTEIN A. [MASS = 40090
Homo
sapiens (Human) ISOFORM EWS-B OF RNA-BINDING PROTEIN EWS. [MASS = 61217
Homo
sapiens (Human) THYMIDYLATE SYNTHASE. [MASS = 31759
Homo
sapiens (Human) NASCENT POLYPEPTIDE-ASSOCIATED COMPLEX SUBUNIT
Homo
sapiens (Human) HISTIDINE-RICH GLYCOPROTEIN PRECURSOR. [MASS = 59578
Homo
sapiens (Human) ISOFORM 1 OF PROTEASOME SUBUNIT ALPHA TYPE 7. [MASS = 27887
Homo
sapiens (Human) 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE
Homo
sapiens (Human) SPLICEOSOME RNA HELICASE BAT1. [MASS = 48991
Homo
sapiens (Human) PREDICTED: SIMILAR TO PHOSPHOGLYCERATE MUTASE 1
Homo
sapiens (Human) CRK-LIKE PROTEIN. [MASS = 33777
Homo
sapiens (Human) RNA-BINDING PROTEIN MUSASHI HOMOLOG 1. [MASS = 39125
Homo
sapiens (Human) FLAP ENDONUCLEASE 1. [MASS = 42593
Homo
sapiens (Human) ISOFORM C OF FIBULIN-1 PRECURSOR: [MASS = 74462
Homo
sapiens (Human) TUBA6 PROTEIN. [MASS = 37021
Homo
sapiens (Human) BA395L14.12. [MASS = 28403
Homo
sapiens (Human) ISOFORM SHORT OF TATA-BINDING PROTEIN-ASSOCIATED
Homo
sapiens (Human) LUNG-CANCER ONCOGENE 7. [MASS = 37889
Homo
sapiens (Human) DNAJ HOMOLOG SUBFAMILY A MEMBER 1. [MASS = 44868
Homo
sapiens (Human) CLASS III ALCOHOL DEHYDROGENASE 5 CHI SUBUNIT. [MASS = 41601
Homo
sapiens (Human) DYNC1H1 PROTEIN. [MASS = 22182
Homo
sapiens (Human) ISOFORM 2 OF SERINE/THREONINE-PROTEIN KINASE PAK 1. [MASS = 61632
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L21. [MASS = 18434
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U ISOFORM A
Homo
sapiens (Human) HISTONE H4. [MASS = 11236
Homo
sapiens (Human) SCC-112 PROTEIN. [MASS = 150830
Homo
sapiens (Human) WW DOMAIN-BINDING PROTEIN 11. [MASS = 69998
Homo
sapiens (Human) ISOFORM 2 OF PUTATIVE GTP-BINDING PROTEIN PTD004. [MASS = 27584
Homo
sapiens (Human) PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, ISOFORM IB,
Homo
sapiens (Human) ISOFORM II OF UBIQUITIN-PROTEIN LIGASE E3A. [MASS = 100646
Homo
sapiens (Human) BRAIN ACID SOLUBLE PROTEIN 1. [MASS = 22562
Homo
sapiens (Human) ACTIN-LIKE PROTEIN 2. [MASS = 44761
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 5. [MASS = 49223
Homo
sapiens (Human) 14-3-3 PROTEIN ETA. [MASS = 28088
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1.
Homo
sapiens (Human) ISOFORM DELTA-1 OF SERINE/THREONINE-PROTEIN PHOSPHATASE 2A
Homo
sapiens (Human) UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10. [MASS = 87692
Homo
sapiens (Human) PDCD6IP PROTEIN. [MASS = 96818
Homo
sapiens (Human) PROTEIN FAM98B. [MASS = 37191
Homo
sapiens (Human) ISOFORM 1 OF 40S RIBOSOMAL PROTEIN S24. [MASS = 15423
Homo
sapiens (Human) ADENYLOSUCCINATE SYNTHETASE ISOZYME 2. [MASS = 50097
Homo
sapiens (Human) ISOFORM 1 OF MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY
Homo
sapiens (Human) EXPORTIN-7. [MASS = 123776
Homo
sapiens (Human) PHOSPHOLIPASE A-2-ACTIVATING PROTEIN. [MASS = 87157
Homo
sapiens (Human) ISOFORM 1 OF PHOSPHOLIPID TRANSFER PROTEIN PRECURSOR.
Homo
sapiens (Human) CERULOPLASMIN PRECURSOR. [MASS = 122205
Homo
sapiens (Human) RAS-RELATED PROTEIN RAB-7. [MASS = 23490
Homo
sapiens (Human) SERINE/THREONINE-PROTEIN PHOSPHATASE 2A CATALYTIC SUBUNIT
Homo
sapiens (Human) ISOFORM 1 OF DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11A.
Homo
sapiens (Human) ADENYLATE KINASE ISOENZYME 1. [MASS = 21635
Homo
sapiens (Human) GPI-ANCHORED PROTEIN P137. [MASS = 72752
Homo
sapiens (Human) ALPHA-2-ANTIPLASMIN PRECURSOR. [MASS = 55064
Homo
sapiens (Human) PLASMA RETINOL-BINDING PROTEIN PRECURSOR. [MASS = 23010
Homo
sapiens (Human) ISOFORM 4 OF SAPS DOMAIN FAMILY MEMBER 3. [MASS = 88952
Homo
sapiens (Human) AP-1 COMPLEX SUBUNIT MU-1. [MASS = 48456
Homo
sapiens (Human) ALPHA-SOLUBLE NSF ATTACHMENT PROTEIN. [MASS = 33247
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA, 1
Homo
sapiens (Human) PROTEASOME SUBUNIT ALPHA TYPE 6. [MASS = 27399
Homo
sapiens (Human) QUINONE OXIDOREDUCTASE. [MASS = 35207
Homo
sapiens (Human) SPLICING FACTOR 3A SUBUNIT 3. [MASS = 58849
Homo
sapiens (Human) GMP SYNTHASE. [MASS = 76715
Homo
sapiens (Human) ISOFORM 2 OF NMDA RECEPTOR-REGULATED PROTEIN 1. [MASS = 61602
Homo
sapiens (Human) EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 2.
Homo
sapiens (Human) PROTEIN C14ORF166. [MASS = 28068
Homo
sapiens (Human) FARNESYL DIPHOSPHATE SYNTHASE. [MASS = 48275
Homo
sapiens (Human) COATOMER SUBUNIT GAMMA-2. [MASS = 97622
Homo
sapiens (Human) FIBRILLARIN. [MASS = 33784
Homo
sapiens (Human) NUCLEAR CAP-BINDING PROTEIN SUBUNIT 1. [MASS = 91839
Homo
sapiens (Human) PROTEASOME SUBUNIT BETA TYPE 4 PRECURSOR. [MASS = 29192
Homo
sapiens (Human) CALCIUM-BINDING PROTEIN 39. [MASS = 39869
Homo
sapiens (Human) PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN. [MASS = 66130
Homo
sapiens (Human) PROTEIN FAM49B. [MASS = 36748
Homo
sapiens (Human) 47 KDA HEAT SHOCK PROTEIN PRECURSOR. [MASS = 46267
Homo
sapiens (Human) PEPTIDYLPROLYL ISOMERASE B PRECURSOR. [MASS = 23743
Homo
sapiens (Human) ISOFORM 1 OF EXPORTIN-5. [MASS = 136311
Homo
sapiens (Human) CADHERIN-2 PRECURSOR. [MASS = 99851
Homo
sapiens (Human) ISOFORM 3 OF DREBRIN-LIKE PROTEIN. [MASS = 49042
Homo
sapiens (Human) 16 KDA PROTEIN. [MASS = 16122
Homo
sapiens (Human) PROBABLE ATP-DEPENDENT RNA HELICASE DDX23. [MASS = 95647
Homo
sapiens (Human) CORONIN-1C. [MASS = 53249
Homo
sapiens (Human) SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN. [MASS = 14544
Homo
sapiens (Human) TROPOMYOSIN 1 ALPHA CHAIN ISOFORM 2. [MASS = 32678
Homo
sapiens (Human) VON HIPPEL-LINDAU BINDING PROTEIN 1. [MASS = 26535
Homo
sapiens (Human) ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC. [MASS = 41351
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L19. [MASS = 23466
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S2. [MASS = 31324
Homo
sapiens (Human) ISOFORM 1 OF MELANOMA-ASSOCIATED ANTIGEN D2. [MASS = 64954
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L3. [MASS = 45978
Homo
sapiens (Human) UBIQUITIN AND RIBOSOMAL PROTEIN S27A PRECURSOR.
Homo
sapiens (Human) PREDICTED: SIMILAR TO RAN-SPECIFIC GTPASE-ACTIVATING
Homo
sapiens (Human) SEPTIN 9. [MASS = 63633
Homo
sapiens (Human) SPERMATID PERINUCLEAR RNA-BINDING PROTEIN. [MASS = 73765
Homo
sapiens (Human) PROBABLE ATP-DEPENDENT RNA HELICASE DDX46. [MASS = 117461
Homo
sapiens (Human) RAS-RELATED PROTEIN RAB-14. [MASS = 23766
Homo
sapiens (Human) MARCKS-RELATED PROTEIN. [MASS = 19398
Homo
sapiens (Human) GCN1-LIKE PROTEIN 1. [MASS = 292930
Homo
sapiens (Human) KINESIN LIGHT CHAIN 1 ISOFORM 2. [MASS = 65310
Homo
sapiens (Human) ISOFORM 2 OF AT-RICH INTERACTIVE DOMAIN-CONTAINING
Homo
sapiens (Human) TROPOMYOSIN 4. [MASS = 28522
Homo
sapiens (Human) EARLY ENDOSOME ANTIGEN 1. [MASS = 162466
Homo
sapiens (Human) RETICULOCALBIN-1 PRECURSOR. [MASS = 38890
Homo
sapiens (Human) ISOFORM 1 OF APOPTOSIS INHIBITOR 5. [MASS = 57561
Homo
sapiens (Human) ISOFORM 1 OF FOCAL ADHESION KINASE 1. [MASS = 119233
Homo
sapiens (Human) TUBULIN-SPECIFIC CHAPERONE B. [MASS = 27326
Homo
sapiens (Human) HSPC121. [MASS = 44423
Homo
sapiens (Human) SEPTIN-11. [MASS = 49267
Homo
sapiens (Human) NEUROCAN CORE PROTEIN PRECURSOR. [MASS = 142973
Homo
sapiens (Human) LYSYL-TRNA SYNTHETASE. [MASS = 68048
Homo
sapiens (Human) 6-PHOSPHOGLUCONOLACTONASE. [MASS = 27547
Homo
sapiens (Human) SPLICING FACTOR, ARGININE/SERINE-RICH 2. [MASS = 25345
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L7A. [MASS = 29864
Homo
sapiens (Human) GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT
Homo
sapiens (Human) ISOFORM LONG OF 60 KDA SS-A/RO RIBONUCLEOPROTEIN.
Homo
sapiens (Human) SUPERKILLER VIRALICIDIC ACTIVITY 2-LIKE 2. [MASS = 117805
Homo
sapiens (Human) ISOFORM LONG OF TRIFUNCTIONAL PURINE BIOSYNTHETIC
Homo
sapiens (Human) HEPARIN COFACTOR 2 PRECURSOR. [MASS = 60178
Homo
sapiens (Human) APOLIPOPROTEIN A-II PRECURSOR. [MASS = 11175
Homo
sapiens (Human) MYOSIN-11. [MASS = 227339
Homo
sapiens (Human) HISTONE H1.2. [MASS = 21234
Homo
sapiens (Human) HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN G. [MASS = 42332
Homo
sapiens (Human) GLUCOSAMINE-6-PHOSPHATE ISOMERASE. [MASS = 32669
Homo
sapiens (Human) DNA LIGASE 1. [MASS = 101736
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L18A. [MASS = 20762
Homo
sapiens (Human) CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 73 KDA
Homo
sapiens (Human) PROTEASOME ACTIVATOR COMPLEX SUBUNIT 1. [MASS = 28723
Homo
sapiens (Human) ACYLAMINO-ACID-RELEASING ENZYME. [MASS = 81225
Homo
sapiens (Human) 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL PRECURSOR.
Homo
sapiens (Human) THO COMPLEX SUBUNIT 4. [MASS = 27558
Homo
sapiens (Human) SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1. [MASS = 13282
Homo
sapiens (Human) FRUCTOSE-BISPHOSPHATE ALDOLASE C. [MASS = 39325
Homo
sapiens (Human) ALPHA-2-HS-GLYCOPROTEIN PRECURSOR. [MASS = 39325
Homo
sapiens (Human) IMPORTIN ALPHA-4 SUBUNIT. [MASS = 57887
Homo
sapiens (Human) GTP BINDING PROTEIN 1. [MASS = 72454
Homo
sapiens (Human) ISOFORM 1 OF DAZ-ASSOCIATED PROTEIN 1. [MASS = 43383
Homo
sapiens (Human) VACUOLAR PROTEIN SORTING 26A. [MASS = 38170
Homo
sapiens (Human) CYTOPLASMIC FMR1 INTERACTING PROTEIN 1 ISOFORM A.
Homo
sapiens (Human) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
Homo
sapiens (Human) ACONITATE HYDRATASE, MITOCHONDRIAL PRECURSOR.
Homo
sapiens (Human) LUNG CANCER ONCOGENE 7. [MASS = 37889
Homo
sapiens (Human) F-ACTIN CAPPING PROTEIN ALPHA-2 SUBUNIT. [MASS = 32818
Homo
sapiens (Human) ISOFORM DUT-M OF DEOXYURIDINE 5′-TRIPHOSPHATE
Homo
sapiens (Human) ISOFORM 1 OF ALPHA-ADDUCIN. [MASS = 80955
Homo
sapiens (Human) ISOFORM 1 OF PROTEIN PHOSPHATASE 1 REGULATORY
Homo
sapiens (Human) BM-010. [MASS = 36153
Homo
sapiens (Human) PROTEIN TYROSINE PHOSPHATASE,-RECEPTOR-TYPE, ZETA1
Homo
sapiens (Human) ISOFORM 3 OF UDP-N-ACETYLGLUCOSAMINE-PEPTIDE N-
Homo
sapiens (Human) HIV TAT SPECIFIC FACTOR 1. [MASS = 85853
Homo
sapiens (Human) UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG B.
Homo
sapiens (Human) PNAS-125. [MASS = 23755
Homo
sapiens (Human) IGKV1-5 PROTEIN. [MASS = 26234
Homo
sapiens (Human) HEMOGLOBIN SUBUNIT GAMMA-1. [MASS = 16009
Homo
sapiens (Human) EXOSOME COMPLEX EXONUCLEASE RRP42. [MASS = 31835
Homo
sapiens (Human) ISOFORM 2 OF TRANSCRIPTION FACTOR BTF3. [MASS = 17699
Homo
sapiens (Human) HISTONE-BINDING PROTEIN RBBP4. [MASS = 47525
Homo
sapiens (Human) SERINE/THREONINE-PROTEIN KINASE MRCK BETA.
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP68610180 (FRAGMENT).
Homo
sapiens (Human) THYMOPOIETIN ISOFORM BETA. [MASS = 50670
Homo
sapiens (Human) DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT.
Homo
sapiens (Human) FACTOR VII ACTIVE SITE MUTANT IMMUNOCONJUGATE.
Homo
sapiens (Human) TUBULIN-SPECIFIC CHAPERONE A. [MASS = 12724
Homo
sapiens (Human) TRYPTOPHANYL-TRNA SYNTHETASE. [MASS = 53165
Homo
sapiens (Human) ISOFORM 1 OF SYMPLEKIN. [MASS = 141148
Homo
sapiens (Human) SERINE/THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC
Homo
sapiens (Human) ANTITHROMBIN III VARIANT. [MASS = 52692
Homo
sapiens (Human) UBIQUITIN-ACTIVATING ENZYME E1. [MASS = 25052
Homo
sapiens (Human) PREDICTED: SIMILAR TO CHLORIDE INTRACELLULAR CHANNEL
Homo
sapiens (Human) ISOFORM 1 OF TRANSCRIPTION ELONGATION FACTOR SPT5.
Homo
sapiens (Human) EUKARYOTIC INITIATION FACTOR 5A ISOFORM I VARIANT A.
Homo
sapiens (Human) ISOFORM 3 OF DNA REPAIR PROTEIN RAD50. [MASS = 138432
Homo
sapiens (Human) COP9 SIGNALOSOME COMPLEX SUBUNIT 5. [MASS = 37448
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP547J2313. [MASS = 18829
Homo
sapiens (Human) CORTICOSTEROID-BINDING GLOBULIN PRECURSOR. [MASS = 45141
Homo
sapiens (Human) PROFILIN 2 ISOFORM A. [MASS = 15046
Homo
sapiens (Human) ISOFORM GAMMA-1 OF SERINE/THREONINE-PROTEIN PHOSPHATASE
Homo
sapiens (Human) ISOFORM 1 OF UBIQUITIN-PROTEIN LIGASE BRE1B. [MASS = 113678
Homo
sapiens (Human) ISOFORM 1 OF RAS GTPASE-ACTIVATING PROTEIN 1. [MASS = 116403
Homo
sapiens (Human) ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 1A. [MASS = 41569
Homo
sapiens (Human) CADHERIN-5 PRECURSOR. [MASS = 87516
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S14. [MASS = 16142
Homo
sapiens (Human) LETHAL GIANT LARVAE HOMOLOG 1. [MASS = 115388
Homo
sapiens (Human) LEUCINE ZIPPER TRANSCRIPTION FACTOR-LIKE 1. [MASS = 34592
Homo
sapiens (Human) MEPRIN A SUBUNIT ALPHA PRECURSOR. [MASS = 84368
Homo
sapiens (Human) WD REPEAT PROTEIN 61. [MASS = 33581
Homo
sapiens (Human) TRIPARTITE MOTIF-CONTAINING PROTEIN 2. [MASS = 81530
Homo
sapiens (Human) ISOFORM 1 OF ATP-DEPENDENT RNA HELICASE DDX19B.
Homo
sapiens (Human) SORTING NEXIN 1 ISOFORM C. [MASS = 53304
Homo
sapiens (Human) HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT.
Homo
sapiens (Human) SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT
Homo
sapiens (Human) HEAT SHOCK 70 KDA PROTEIN 4L. [MASS = 94486
Homo
sapiens (Human) AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2. [MASS = 39589
Homo
sapiens (Human) D-DOPACHROME DECARBOXYLASE. [MASS = 12581
Homo
sapiens (Human) THIMET OLIGOPEPTIDASE. [MASS = 78709
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L38. [MASS = 8087
Homo
sapiens (Human) ALDEHYDE DEHYDROGENASE 16 FAMILY, MEMBER A1.
Homo
sapiens (Human) CYTOCHROME B5 REDUCTASE ISOFORM 1. [MASS = 34235
Homo
sapiens (Human) NETRIN RECEPTOR DCC PRECURSOR. [MASS = 158457
Homo
sapiens (Human) ISOPENTENYL-DIPHOSPHATE DELTA ISOMERASE. [MASS = 32485
Homo
sapiens (Human) PHOSPHATIDYLINOSITOL TRANSFER PROTEIN, BETA.
Homo
sapiens (Human) HIGH MOBILITY GROUP PROTEIN B2. [MASS = 23903
Homo
sapiens (Human) TUMOR PROTEIN, TRANSLATIONALLY-CONTROLLED 1.
Homo
sapiens (Human) BLEOMYCIN HYDROLASE. [MASS = 52562
Homo
sapiens (Human) ALPHA-ENOLASE, LUNG SPECIFIC. [MASS = 49477
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L12. [MASS = 17819
Homo
sapiens (Human) CELL DIVISION CYCLE 5-LIKE PROTEIN. [MASS = 92251
Homo
sapiens (Human) ISOFORM 2 OF UBIQUITIN CARBOXYL-TERMINAL
Homo
sapiens (Human) COMPLEMENT C5 PRECURSOR. [MASS = 188331
Homo
sapiens (Human) ISOFORM 1 OF CYTOPLASMIC LINKER PROTEIN 2. [MASS = 115837
Homo
sapiens (Human) THIOREDOXIN REDUCTASE 1, CYTOPLASMIC PRECURSOR.
Homo
sapiens (Human) HISTONE H1X. [MASS = 22487
Homo
sapiens (Human) ISOFORM GTBP-N OF DNA MISMATCH REPAIR PROTEIN
Homo
sapiens (Human) BILIVERDIN REDUCTASE A PRECURSOR. [MASS = 33428
Homo
sapiens (Human) LAMINA-ASSOCIATED POLYPEPTIDE 2 ISOFORM ALPHA.
Homo
sapiens (Human) SYNAPTIC VESICLE MEMBRANE PROTEIN VAT-1
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L8. [MASS = 27893
Homo
sapiens (Human) PHYTANOYL-COA HYDROXYLASE INTERACTING
Homo
sapiens (Human) CONDENSIN COMPLEX SUBUNIT 2. [MASS = 82535
Homo
sapiens (Human) HIGH-MOBILITY GROUP BOX 1. [MASS = 15185
Homo
sapiens (Human) SELENIDE, WATER DIKINASE 1. [MASS = 42911
Homo
sapiens (Human) APOLIPOPROTEIN M. [MASS = 21253
Homo
sapiens (Human) HYPOTHETICAL PROTEIN DKFZP686M09245. [MASS = 61598
Homo
sapiens (Human.) ISOFORM 1 OF EXOSOME COMPLEX EXONUCLEASE RRP44.
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L10A. [MASS = 24700
Homo
sapiens (Human) ECHINODERM MICROTUBULE-ASSOCIATED.PROTEIN-LIKE 4.
Homo
sapiens (Human) CALPAIN-1 CATALYTIC SUBUNIT. [MASS = 81890
Homo
sapiens (Human) 55 KDA PROTEIN. [MASS = 55183
Homo
sapiens (Human) ZYXIN. [MASS = 67285
Homo
sapiens (Human) DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 1.
Homo
sapiens (Human) TYROSYL-TRNA SYNTHETASE, CYTOPLASMIC. [MASS = 59012
Homo
sapiens (Human) PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2.
Homo
sapiens (Human) U4/U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 1. [MASS = 90255
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S21. [MASS = 9111
Homo
sapiens (Human) DNAJ HOMOLOG SUBFAMILY C MEMBER 7. [MASS = 56441
Homo
sapiens (Human) CALSYNTENIN 1 ISOFORM 2. [MASS = 108643
Homo
sapiens (Human) TWINFILIN ISOFORM 1. [MASS = 43918
Homo
sapiens (Human) CENTROSOMAL PROTEIN 170 KDA ISOFORM ALPHA.
Homo
sapiens (Human) ISOFORM 1 OF 26S PROTEASE REGULATORY SUBUNIT 6B.
Homo
sapiens (Human) U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A. [MASS = 31148
Homo
sapiens (Human) PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A. [MASS = 17881
Homo
sapiens (Human) PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2.
Homo
sapiens (Human) RAS-RELATED PROTEIN RAB-5C. [MASS = 23483
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S8. [MASS = 24074
Homo
sapiens (Human) PERIPHERIN. [MASS = 53878
Homo
sapiens (Human) NUCLEOSIDE DIPHOSPHATE KINASE B. [MASS = 17298
Homo
sapiens (Human) SEC31L1 PROTEIN. [MASS = 121651
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S16. [MASS = 16314
Homo
sapiens (Human) UROPORPHYRINOGEN DECARBOXYLASE. [MASS = 40787
Homo
sapiens (Human) 114 KDA PROTEIN. [MASS = 113977
Homo
sapiens (Human) COLLAGEN ALPHA-1(V) CHAIN PRECURSOR. [MASS = 183560
Homo
sapiens (Human) CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 2.
Homo
sapiens (Human) CYTOSOLIC AMINOPEPTIDASE P. [MASS = 74798
Homo
sapiens (Human) ISOFORM 2 OF SPLICING FACTOR 1. [MASS = 68502
Homo
sapiens (Human) PREDICTED: SIMILAR TO BASIC LEUCINE ZIPPER AND W2
Homo
sapiens (Human) ISOFORM 1 OF URIDINE 5′-MONOPHOSPHATE SYNTHASE.
Homo
sapiens (Human) DEAD BOX POLYPEPTIDE 42 PROTEIN. [MASS = 102975
Homo
sapiens (Human) ISOFORM C OF NEURAL CELL ADHESION MOLECULE 1, 120
Homo
sapiens (Human) COLD-INDUCIBLE RNA-BINDING PROTEIN. [MASS = 18648
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L18. [MASS = 21503
Homo
sapiens (Human) ISOFORM 1 OF JMJC DOMAIN-CONTAINING.HISTONE
Homo
sapiens (Human) RCC1 PROTEIN. [MASS = 48146
Homo
sapiens (Human) LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47. [MASS = 63473
Homo
sapiens (Human) ISOFORM 1 OF RNA-BINDING PROTEIN NOVA-1. [MASS = 52056
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S10. [MASS = 18898
Homo
sapiens (Human) SPLICING FACTOR U2AF 65 KDA SUBUNIT. [MASS = 53501
Homo
sapiens (Human) ISOFORM SHORT OF PROTEASOME SUBUNIT ALPHA TYPE 1.
Homo
sapiens (Human) ALPHA-1-ACID GLYCOPROTEIN 2 PRECURSOR. [MASS = 23603
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S23. [MASS = 15676
Homo
sapiens (Human) DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN
Homo
sapiens (Human) HYPOTHETICAL PROTEIN LOC387104. [MASS = 103199
Homo
sapiens (Human) PROTEIN TRANSPORT PROTEIN SEC24C. [MASS = 118315
Homo
sapiens (Human) THIOREDOXIN. [MASS = 11606
Homo
sapiens (Human) CYTOSOLIC PURINE 5′-NUCLEOTIDASE. [MASS = 64970
Homo
sapiens (Human) PREDICTED: SIMILAR TO RIBOSOMAL PROTEIN S3A ISOFORM 1.
Homo
sapiens (Human) ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S25. [MASS = 13742
Homo
sapiens (Human) ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 3. [MASS = 20456
Homo
sapiens (Human) CYSTATIN B. [MASS = 11140
Homo
sapiens (Human) PHOSPHOGLUCOMUTASE-2-LIKE 1. [MASS = 70456
Homo
sapiens (Human) 40S RIBOSOMAL PROTEIN S9. [MASS = 22460
Homo
sapiens (Human) ANKYRIN REPEAT AND FYVE DOMAIN CONTAINING 1
Homo
sapiens (Human) ISOFORM LONG OF COLD SHOCK DOMAIN-CONTAINING
Homo
sapiens (Human) DEAD (ASP-GLU-ALA-ASP) BOX POLYPEPTIDE 39, ISOFORM 2.
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L23A. [MASS = 17695
Homo
sapiens (Human) ALPHA-INTERNEXIN. [MASS = 55391
Homo
sapiens (Human) ISOFORM 3 OF ANAMORSIN. [MASS = 32213
Homo
sapiens (Human) SPLICING FACTOR, ARGININE/SERINE-RICH 4. [MASS = 56678
Homo
sapiens (Human) DEBRANCHING ENZYME HOMOLOG 1. [MASS = 61555
Homo
sapiens (Human) ISOFORM 2 OF PROTEASOME SUBUNIT ALPHA TYPE 3. [MASS = 27516
Homo
sapiens (Human) MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN LARGE SUBUNIT
Homo
sapiens (Human) ISOFORM B OF NEURONAL-SPECIFIC SEPTIN-3. [MASS = 40100
Homo
sapiens (Human) 60S RIBOSOMAL PROTEIN L28. [MASS = 15616
Homo
sapiens (Human) PREDICTED: SIMILAR TO HETEROGENEOUS NUCLEAR
CSF was collected from the lateral ventricle of E12.5, E14.5, and E17.5 rat embryos and from the fourth ventricle of E14.5 rat embryos. CSF from two litters (approximately 20-24 rat embryos) was pooled for each time point and was separated by 1-D SDS-PAGE and the proteins were visualized with Coomassie blue stain.
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) FATTY
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) BA1-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) DA1-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) HEAT
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) GPI-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) ACTIN,
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 284 KDA
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 170 KDA
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) IRON-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) SP120-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) IKAP,
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) ATP-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) INTER-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) HEAT
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat) HEAT
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) MAMA.
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) TLN
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 14-3-3
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) FAR
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) VALYL-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 14-3-3
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) L-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) RAT T-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) T-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) HEAT-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) LAR
Rattus norvegicus (Rat) IG
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) IG
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) POLY
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 26S
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) FETUB
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) RAB
Rattus norvegicus (Rat) L-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 40S
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) DNA
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) L-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 60S
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) L-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) NON-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) D-3-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) AMBP
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) RAB
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) ALPHA
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) L-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) IGH-1A
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) ALPHA
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) RAT
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) GPI-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) T-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) FATTY
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) GM2
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) SSB
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) HEAT
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) HEAT
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 1-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) BETA-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) T-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) BETA-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) M-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 14-3-3
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 14-3-3
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) ZERO
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) GTP-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) T-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 60S
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) LOW-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) 40S
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) DNA
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) AC2-
Rattus norvegicus (Rat)
Rattus norvegicus (Rat) PRX
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
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Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Rattus norvegicus (Rat)
Parada et al (J Proteome Res, 2005. 4:2420-8) identified 31 proteins within the rat e-CSF finding an abundance of extracellular matrix proteins, enzymes, and enzyme regulators, consistent with our study. We identified a much larger number of proteins within the CSF while identifying 24 of the 31 previously identified proteins. The 7 proteins that we did not find are the following: calreticulin, DJ-1, EEf1 g, laminin receptor 1, malate dehydrogenase 1, set beta isoform, and tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta polypeptide. The differences between our study and the study by Parada et al appear a consequence of methodology rather than sample differences. Parada et al chose for mass spectrometry the most prominent silver-stained e-CSF proteins resolved by two-dimensional electrophoresis, whereas we performed an analysis of the entire e-CSF separated by one-dimensional electrophoresis. Our one-dimensional approach enabled a more comprehensive analysis (one which would be unwieldy for an entire two dimensional gel), the study by Parada et al is complementary with this one as some proteins resolved in two dimensions would have a reduced likelihood of becoming suppressed due to co-migration in one dimension with abundant protein species such as albumin.
Our analyses are semi-quantitative, and we identified interesting differences between our various rat e-CSF samples. Apolipoprotein M is found in both E14.5 LV and E14.5 4thV but our analysis did not identify it in either E12.5 LV or E17.5 LV, phosphatidylethanolamine binding protein was found only in the E17.5 LV, collagen alpha I (XI) was identified in E14.5 and E17.5 LV, and phosphatase 2 (alpha isoform of regulatory subunit A) was found in E12.5 LV. Also, apolipoprotein D, an apolipoprotein that was not identified by Parada et al was identified only in the E14.5 4thV.
In a comparison of proteins found in the human e-CSF to the proteins found in the rat e-CSF, we found that of the 188 proteins identified in the human e-CSF, 135 human proteins were identified in any one of the four samples of embryonic rat CSF. 83 of those proteins were present in all four samples of embryonic rat CSF. Table 1 includes the human proteins found common to rat CSF. We have indicated the specific rat samples in which each protein was identified. Out of the top 50 proteins found in the human CSF, 45 were also found in the rat CSF.
Proteins common to human and rat CSF presumably represent proteins related to fundamental CSF functions. For example, e-CSF contains many transport and carrier proteins including transferrin, albumin, alpha-fetoprotein, transthyretin, ceruloplasmin, and plasma retinol-binding protein that are all involved in either metal ion or vitamin transport through fluid or across cell membranes. There are a number of apolipoproteins involved in the transport and metabolism of lipids and fatty acids in the CSF as reported in this paper and by Parada et al (supra). There are also a large number of enzymes and protease inhibitors in the CSF that are involved in regulating immune response and maintaining homeostasis.
Other proteins common to rat and human CSF may play more specific roles in neurogenesis. One factor in the e-CSF is Amyloid Beta A4 Protein Precursor (APP), which we identified in rat CSF at E12.5, E14.5, and E17.5 and human CSF at CS20. This protein is normally present in brain and a soluble form is known to circulate in adult CSF (Palmert et al., Proc Natl Acad Sci USA, 1989. 86:6338-42). The soluble form of APP has been shown to stimulate proliferation of embryonic neural stem cells as well as adult neural progenitor cells from the subventricular zone (Caille et al., Development, 2004. 131:2173-81; Hayashi et al., Biochem Biophys Res Commun, 1994. 205:936-43; Ohsawa et al., Eur J Neurosci, 1999. 11:1907-13). APP may play a role during neurogenesis not only within the cell but may be released in the extracellular space and taken up in the CSF in order to diffuse throughout the CSF a play a function at more distant sites. Similarly, Tenascin, which we found in all CSF samples from rat and human from CS 20, is a secreted extracellular matrix glycoprotein implicated in axon guidance during development and regeneration (von Hoist et al., J Biol Chem, 2007. 282: 9172-81), which was recently shown to be expressed in progenitor cells in the ventricular zone of the developing brain. CSF contains multiple critical extracellular matrix factors including fibronectin, laminin, tenascin, fibulin, versican, and neurocan core protein. Because many of these factors can support or orient neuronal migration, they may be acting in the CSF as external cues for proliferating and differentiating neuronal progenitor cells.
Few proteins were identified that may be exclusive to rat or human e-CSF. The protein Pigment Epithelium Derived Factor (PEDF) was only found in the human e-CSF and is known to circulate in the adult CSF and is significantly decreased in CSF of patients with frontotemporal dementia (Davidsson et al., Brain Res Mol Brain Res, 2002. 109:128-33). This secreted serine protease inhibitor, known to be released by retinal pigment cell into the matrix, is a known neurotrophic protein involved in survival and potentially differentiation of specific neurons (Houenou et al., J Comp Neurol, 1999. 412:506-14). PEDF is known to act on photoreceptor cells but also may play a role in spinal motor neuronal survival. It is likely that PEDF is released by the photoreceptor cells into the matrix and taken up by the CSF and may act on cell types and neurons by diffusion through the CSF. Similarly, the Neuronal Cell Adhesion Molecule L1-Like Protein, also found only in the human e-CSF is known to play important roles in neurite outgrowth and neuronal survival (Hillenbrand et al., Eur J Neurosci, 1999. 11:813-26; Montag-Sallaz et al., Mol Cell Biol, 2002. 22:7967-81; Nishimune et al., J Neurosci Res, 2005. 80:593-9).
Conversely, we only observed the Extracellular Superoxide Dismutase, a protein known to remove free radicals that can be toxic to cells in rat e-CSF. One of the functions of the e-CSF may be the removal of toxins and toxin metabolic byproducts, and therefore it would important to have proteins within the CSF that help neutralize some of the toxic products released into the CSF. Additionally, we found in the rat e-CSF Mannose 6-phosphate/Insulin-like Growth Factor II Receptor (IGF2R), a soluble form of the receptor has been found in the serum, amniotic fluid and urine of both rodents and humans, affecting organ size based on its interaction with IGF2 and other factors (Causin et al., Biochem J, 1988. 252:795-9; Kiess et al., Proc Natl Acad Sci USA, 1987. 84:7720-4; MacDonald et al., J Biol Chem, 1989. 264:3256-61; Xu et al., J Clin Endocrinol Metab, 1998. 83:437-42; Zaina et al., J Biol Chem, 1998. 273:28610-6). Confirmation of these apparent differences would require Western blotting, and may lead to studies of their intriguing biological potential in the e-CSF.
Subcellular Localization of e-CSF Proteins
To compare the e-CSF of human and rat further we analyzed the 188 proteins found in the human e-CSF and the 137 proteins in the rat e-CSF present in all samples based on subcellular localization, molecular function, and biological process. The subcellular localization of each protein in the CSF is shown in Tables 1 and 3. The majority of proteins found in the human (
We used the PANTHER protein ontology database to classify the proteins into distinct categories of molecular function and biological process. Panther identified 180 out of 188 proteins with a total number of 237 functional hits for the human e-CSF, 119 out of 137 proteins with a total number of 155 functional hits for the rat e-CSF, and 191 out of 200 proteins with a total number of 234 functional hits for embryonic mouse brain. Table 1 shows the percentage of proteins assigned to each functional category in the embryonic human CSF, embryonic rat CSF, and E16.5 embryonic mouse brain.
Panther analysis of molecular function reveals the majority of proteins found within the human and rat CSF share similar functional categories (Table 4,
Panther analysis reveals distinct functional groups of proteins present in the CSF as compared to embryonic tissue. Protein categories in the embryonic human and rat CSF are quite similar and to control for random similarity in categorization based on molecular function we compared the CSF protein samples to a sample of 200 most abundant proteins in embryonic E16.5 mouse brain (Table 4). The comparison of relevant protein categories in each sample is shown in
Panther analysis of proteins based on biological process reveals strong similarity between the embryonic human and rat CSF and differences between the CSF and the embryonic brain (Table 6,
The similarities between the embryonic human and rat CSF are apparent when the proteins are classified into groups and analyzed on the basis of subcellular localization, molecular function, and biological process. Based on the functional characteristics of the proteins found in the e-CSF, the CSF is a heterogeneous mixture of many types of classes of proteins with varying functions. The e-CSF is far more complex than previously thought. This may be due to active secretion from the choroid plexus into the CSF, or from the contents within the extracellular membrane bound particles that are present in the rodent CSF during development, or potentially to aposomes budding from the choroid plexus and floating within the CSF that have been shown previously to support protein translation (Saunders et al., Cell Mol Neurobiol, 2000. 20:29-40; Agnew et al., Cell Tissue Res, 1980. 208:261-81; Gudeman et al., J Neurosci Res, 1989. 24:184-91).
Although we did not find the growth factor FGF-2 as reported by Martin et al (Dev Biol, 2006. 297:402-16), many growth factors are in low abundance and are of smaller molecular weight making them more challenging to identify by multiple peptide assignments using mass spectrometry on a complex mixture.
Cortical Explants in e-CSF
Cortical explants can survive and proliferate in the presence of e-CSF. Embryonic day 16 (E16) rat cortical explants cultured with 100% E17 CSF for 24 hours, without additional exogenous media or factors, retained tissue architecture, cell proliferation, and cell viability, approximating in vivo E17 rat cortex (
Comparison of E13 and E17 Rat e-CSF
The primary source of CSF is the choroid plexus, a highly vascularized secretory epithelial tissue that extends into the ventricles. To determine if the embryonic choroid-plexus-derived-CSF provides support and instructive cues to the developing cortex we compared CSF from E13 embryos (pre choroid plexus formation) with that from E17 embryos (post choroid plexus formation). E17 CSF increased the frequency of PH3-labeled proliferating cells in E16 cortical explants compared to explants cultured with E13 CSF (E17 mean: 44.1±±1.43; E13 mean: 25±4.2; n=4; p<0.05) (
CSF was then determined to maintain and stimulate proliferation of primary dissociated cortical progenitors cultured as neurospheres, an in vitro experimental model for neural stem cells. Primary neurospheres derived from E14 rat embryos were dissociated, plated at clonal density, and cultured with CSF collected from E13 or E17 embryos. Both E13 and E17 CSF supported the generation of small neurospheres composed primarily of GLAST-positive-staining cells in the absence of supplemental FGF and EGF for 10 days in vitro (DIV) (
Both E13 and E17 CSF maintain viable GLAST-positive-staining neurospheres (
We next characterized the embryonic CSF proteome to determine how the CSF drives the proliferation of cortical progenitor cells. Total CSF protein concentration increased from E12 on, peaked at birth (P0) and declined into adulthood (
To investigate the distinct effects of embryonic CSF at different developmental stages, we performed extensive LC-MS/MS analyses on increased volumes of E17 CSF. From these E17 rat proteome analyses, we identified several peptides corresponding to Insulin-like growth factor 2 (IGF2) in the CSF (
Drosophila)-like 1
To test if CSF could serve as a vehicle for IGF signaling, we assessed the expression of IGF1 and IGF2 mRNA in the developing cortex. IGF2 mRNA was highly expressed in the choroid plexus of E17 rat embryos, as well as in vascular endothelial cells and the leptomeninges of both E14 and E17 rat brain (
To determine if CSF-borne IGF2 has the capacity to stimulate IGF signaling in the developing cortex, we first examined the localization of the IGF1 receptor (IGF1R) in the developing cortex. IGF1R, which binds IGF2 and is essential for the proliferative response to IGF signaling (references), localized to the apical, ventricular surface of radial neuroepithelial cells that contacts the CSF (
We then tested whether Igf2 could maintain GLAST-positive cortical progenitor cells in vitro by culturing primary neurosphere dissociated cells with Igf2 (
The following methods were used to perform the above described experiments.
Cortical Explants
Rat embryos were removed from extra-embryonic membranes and placed in sterile Hanks Balanced Salt Solution (HBSS). The lateral wall of the developing cortex was dissected using a fine scalpel and demarcated in the rostral-caudal direction by the width of the lateral ganglionic eminence, in the dorsal direction by the in-fold of the medial cortical wall, and in the lateral direction by the border with the lateral ganglionic eminence. The dissected cortex was transferred to a polycarbonate membrane (Whatman; 13 mm, 8.0 um) using a platinum wire loop. Explants were then cultured for 24 hours in conditions described in text. Artificial CSF (ACSF) was made fresh for each use. ACSF consisted of NaCl 119 mM, KCl 2.5 mM, NaHCO3 26 mM, NaH2PO4 1 mM, Glucose 11 mM, MgCl2 2 mM, CaCl2 2.8 mM. Supplemental IGF2 (US Biologicals) was added to ACSF at a final concentration of 2 ng/ml. 15 μg of IGF2 neutralization antibody in 15 μl of PBS (Millipore) was incubated with 100% E17 CSF for 1 hour rotating at 4° C. As a control, 15 μl of PBS was incubated with 100% E17 CSF. For BrdU labeling, explants were pulsed with BrdU for 30 minutes immediately prior to fixation. Explants were fixed (60% methanol, 30% chloroform, and 10% acetic acid) for 5-10 minutes, washed with 70% ethanol, embedded in paraffin, and sectioned at 5 um. Explant integrity was visualized by Hematoxylin and Eosin staining (data not shown).
Immunohistochemical and Immunoblot Analysis
The following antibodies were purchased: mouse anti-Tuj 11:250 (Covance), rat anti-BrdU 1:400 (AbD Serotec), rabbit anti-PH3 1:400 (Upstate), mouse anti-Vimentin 4A4 1:100 (Assay Designs), guinea pig anti-GLAST 1:100 (Company name), anti-phospho-Histone H3 1:400 (Upstate), rabbit P-AKT 1:100 (Cell Signaling), rabbit P-IGF1R, 1:100 (Cell Signaling), HRP conjugated anti-albumin 1:10,000 (Immunology Consultants Laboratory, Inc.), HRP conjugated anti-transferrin 1:1000 (Immunology Consultants Laboratory, Inc.), rabbit anti-Cystatin C 1:1000 (abeam), rabbit anti-Cathepsin B 1:1000 (abeam), rabbit anti-IGF2 1:100 (Santa Cruz Biotechnology), rabbit anti-FGF2 1:100 (Santa Cruz Biotechnology), rabbit anti-EC-SOD 1:1000 (Stressgen), mouse anti-APP 1:100 (Chemicon International).
Cortical Neurospheres
E14 rat cortex was dissected in sterile HBSS followed by gentle trituration. Primary spheres were generated in DMEM/F12 supplemented with heparin, N2, FGF (10 ng/ml), and EGF (20 ng/ml) and collected after 7-9 days in vitro (DIV). Primary spheres were then re-suspended in media without EGF or FGF, dissociated into single cells, plated at a final density of 2,500 cells/cm2, and cultured in various media conditions. Fresh media was supplemented on day 4 of incubation. Cells were fixed in 4% Paraformaldehyde and stained for GLAST after 10 DIV.
Cortical Cell Cultures
Cultures of mixed cortical progenitor cells and neurons were prepared. Briefly, mouse embryonic E13.5 cortices were isolated and dissociated by Papain Dissociation System according to the manufacturer's instructions (Worthington Biochem. Corp). Cells were cultured in NBM supplemented with 1% penicillin-streptomycin, 1% glutamine, N2, and bFGF (10 ng/ml). The following day, cells were deprived of growth factors for 6 hours, followed by a 5 minute pulse of ACSF, embryonic CSF, or Igf2 (20 ng/ml).
In Situ Hybridization
Non-radioactive in situ hybridization was performed as described (Berger et al., J Comp Neurol 433, 101-14 (2001)), using a digoxigenin (DIG)-labelled cRNA probe generated from a TA vector (Invitrogen) clone of IGF1 or IGF2 cDNA and frozen rat brain sections.
All patents, patent applications, and publications mentioned in this specification, including U.S. Provisional Application No. 60/963,211, filed Aug. 3, 2007, are hereby incorporated by reference to the same extent as if each independent patent, patent application, or publication was specifically and individually indicated to be incorporated by reference.
This invention was made with U.S. government support under grants HG00041, 2 RO1 NS032457, and P20 RR16462 awarded by National Institutes of Health. The Government has certain rights to this invention.
Filing Document | Filing Date | Country | Kind | 371c Date |
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PCT/US08/09405 | 8/4/2008 | WO | 00 | 5/24/2011 |
Number | Date | Country | |
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60963211 | Aug 2007 | US |