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Oligodendrocyte-myelin glycoprotein (OMG) is a cell membrane protein which contains 8 leucine-rich repeats. The OMG protein is expressed on the surface of oligodendrocytes and on large projection neurons, including Purkinje cells of the cerebellum, pyramidal cells of the hippocampus, motoneurons of the brainstem and anterior horn cells of the spinal cord. The neurite outgrowth inhibitory activities of all three myelin-derived proteins are mediated by binding to a joint receptor complex consisting of the Nogo receptor and the p75 neurotrophin receptor.

CCNB2 is a member of the cyclin family. CCNB2 is vital for regulation of the cell cycle at the G2/M (mitosis) transition. CCNB2 cooperates with the CDK1 protein kinase to create a serine/threonine kinase holoenzyme complex recognized as maturation promoting factor (MPF).

PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.

POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.

Lysosomal-Associated Membrane Protein 3, also known as LAMP3 is part of the lysosome-associated membrane protein family. LAMP3 and CD68 share an extremely similar predicted structure. LAMP3 performs in dendritic cell function and in adaptive immunity as well. Furthermore, LAMP3 overexpression is actively involved in tumor invasion via increased migration into lymph-vascular spaces.

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, also known as CEACAM3, is a member of the immunoglobulin super family. The genes in this family encode cell adhesion proteins, which are expressed at higher levels in tumorous tissues rather than in normal tissues. CEACAM3 plays a significant part in the clearance of pathogens through the innate immune system. In addition, CEACAM3 is accountable for RAC1 stimulation in the course of pathogen phagocytosis.

Proteasome subunit beta type-9 (PSMB9) belongs to the proteasome B-type family which is a 20S core beta subunit. PSMB9 is positioned in the class II region of the MHC (major histocompatibility complex). Expression of the PSMB9 protein is induced by INFG and this gene product replaces catalytic subunit 1 (proteasome beta 6 subunit) in the immunoproteasome.

MAEA is a 396aa widely expressed adhesion protein which has 5 alternatively spliced isoforms. MAEA holds one CTLH domain and one LisH domain. MAEA forms a complex with F-actin, which takes part in regulating actin distribution in erythroblasts and macrophages and is known to assist in cell division and nuclear architecture. MAEA is confined with condensed chromatin at prophase, nuclear spindle poles at metaphase and in the contractile ring throughout cytokinesis phase and telophase.

Mago-Nashi Homolog B (MAGOHB) is a member of the mago nashi family. MAGOHB involved in mRNA splicing and in the nonsense-mediated decay (NMD) pathway. MAGOHB interacts with RBM8A and is a part of the exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, UPF3B, UPF2 and ALYREF/THOC4.

CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli.
RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.

C1q is the first component of the classical pathway of complement activation. C1q along with the enzymatically active components C1r and C1s forms the C1 complex. When C1 binds to immunoglobulins in the form of immune complexes, it leads to activation of C1r and C1s proteases and a further activates the classical pathway of complement. C1q is a glycoprotein that belongs to the collectin family, having a molecular weight of about 410-462 kDa. C1q is a hexamer composed of globular heads attached to collagen-like triple-helix tails. The globular heads of C1q exclusively bind to the CH2 domain of IgG molecules or the CH3 domain of IgM. Each heavy chain of the immunoglobulin molecule contains a single binding site for C1q. Given that C1q must bind to no less than two heavy chains in order to alter its conformation and activate C1r and C1s, its activation follows only after binding to immunoglobulins in the form of immune complexes bound to multivalent antigens. C1q’s main physiological role is in the clearance of immune complexes and apoptotic bodies from the organism. Interruption of this process may lead to development of autoimmunity. Individuals with genetic deficiencies of C1q or other components of the classical pathway are at risk to develop SLE. C1q specifically binds to apoptotic bodies of human keratinocytes, vascular endothelial cells and lymphocytes. Complement components C1q and bound C3 mediate the clearance of apoptotic bodies. Hence, C1q may advance the clearance of autoantigens, avoiding stimulation of the immune system. Nonetheless, an extended exposition of the immune system to the neoepitope exposed on C1q molecules bound to immune complexes or apoptotic bodies could ultimately lead to an autoimmune response against C1q itself and to an altered complement function. C1q deficiency may also lead to disruption of the negative selection of autoreactive B cells. C1q along with other specific recognition proteins bind to the highly conserved lupus antigens (dsDNA and nuclear proteins) and activate the complement system. Autoantibodies against C1q (anti-C1q) are found in a number of autoimmune and infectious diseases like glomerulonephritis (GN) and lupus erythematosus (SLE), these antibodies are significant in clinical practice due to their negative predictive value.

WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.

B2M is a part of the MHC class I family that participates in the presentation of peptide antigens to the immune system. B2M is localized on the surface of numerous cells and abundant on the surface of white blood cells. High production or destruction of these cells causes B2M levels in the blood to raise. This increase is observed in people with cancers involving white blood cells, but it is mainly significant in people newly diagnosed with multiple myeloma. B2M Testing is done primarily when evaluating a person for certain kinds of cancer affecting white blood cells including chronic lymphocytic leukemia, non-Hodgkin''s lymphoma, and multiple myeloma or kidney disease.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

Clathrin light chain B (CLTB) is a member of the clathrin light chain family. Clathrin is a protein that has a key role in the formation of coated vesicles. CLTB functions as the key structural component of the lattice-type cytoplasmic face of coated pits and vesicles which capture certain macromolecules during receptor-mediated endocytosis. CLTB forms a triskelion form comprised of 3 clathrin heavy chains and 3 light chains. When the triskelia interact they form a polyhedral pattern which encircles the vesicle. CME (Clathrin-mediated endocytosis) controls numerous cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission.

CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

Chloride channels are various group of proteins that control fundamental cellular processes including stabilization of cell membrane potential, transepithelial transport, regulation of intracellular pH, and maintenance of cell volume. CLIC1 is part of the p64 family and is localized to the cell nucleus. CLIC1 displays both nuclear and plasma membrane chloride ion channel activity. CLIC1 inserts into membranes and forms chloride ion channels. CLIC1 channel activity depends on the pH. CLIC1 membrane insertion is redox-regulated and happens under oxydizing conditions.

RAB11A is part of the small GTPase superfamily, Rab family. RAB11A is related with both constitutive and regulated secretory pathways, and takes part in protein transport. RAB11A is a well-known marker for protein trafficking, sorting, and recycling in the endosomal pathway. RAB11A is a main regulator of membrane delivery during cytokinesis.

Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.

CA14 is a part of the Carbonic anhydrases family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They present wide variety in tissue distribution and in their subcellular localization. CA14 is a type I membrane protein which shares highest sequence similarity with the other transmembrane CA isoform, CA XII. Nevertheless, they have different patterns of tissue-specific expression and therefore take different physiologic parts.

Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.