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Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.

Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.

ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.

ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.

STX17 is a member of to the syntaxin family and contains 1 t-SNARE coiled-coil homology domain. STX17 is involved in vesicle trafficking to lysosomes and takes part in procedures associated with cell division.

Tumor protein p53, a nuclear protein, plays an essential role in the regulation of cell cycle, specifically in the transition from G0 to G1. It is found in very low levels in normal cells, however, in a variety of transformed cell lines, it is expressed in high amounts, and believed to contribute to transformation and malignancy. p53 is a DNA-binding protein containing DNA-binding, oligomerization and transcription activation domains. It is postulated to bind as a tetramer to a p53-binding site and activate expression of downstream genes that inhibit growth and/or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Alterations of the TP53 gene occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome.

Mouse Complement 5a (C5a) is a glycoprotein which is a member of a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 77 a.a. peptide created by the C5a convertase proteolytic cleavage of C5 ? chain in the classical and alternative complement pathway (C4b2a3b, C3bBb3b). The mouse C5a has four ? helices and three intrachain disulfide bonds which form a triple loop structure. C5a functions through G-protein coupled receptor (GPCR) (C5aR/CD88). C5a is a effective chemoattractant and anaphylatoxin which functions on all classes of leukocytes and on many other cell types including endothelial, smooth muscle, kidney, liver, and neural cells. Mouse C5a also mediates IL-8 release from bronchial epithelial cells. Furthermore, it triggers an oxidative surge in macrophages and neutrophils, causing the release of histamine in basophils and mast cells. The C5a anaphylatoxin activity on hepatocytes results indirectly from interaction with nonparenchymal cell via prostanoid secretion.

PEA15 (Phospho-enriched protein in astrocytes 15kDa) is a death effector domain (DED)-containing protein mainly expressed in the central nervous system, principally in astrocytes. PEA15 is implicated in the regulation of various cellular processes including apoptosis, proliferation, glucose transport, adhesion and migration. Increased PEA15 levels have an affect tumorigenesis and cancer progression, therefore it is overexpressed in breast cancers and gliomas as well as in type 2 diabetes. PEA15 blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. PEA15 also inhibits RPS6KA3 activities by holding it in the cytoplasm. In addition, PEA15 inhibits both TNFRSF6 and TNFRSF1A mediated CASP8 activity and apoptosis.
PEA15 is ubiquitously expressed. PEA15 is most abundant in tissues such as the heart, brain, muscle and adipose tissue which use glucose as an energy source. Lower PEA15 expression is in glucose-producing tissues. Higher levels of PEA15 expression are found in tissues from individuals with type 2 diabetes than in controls.
PEA15 expression is a significant prognostic marker in ovarian cancer.

PFDN4 belongs to the prefoldin beta subunit family. PFDN4 is a heterohexameric chaperone protein that can capture unfolded actin and is a possible transcription factor. Six prefoldin polypeptides, prefoldin 1-6, are known.

PFDN6 is a subunit of the heteromeric prefoldin complex that chaperones developing actin and alpha- and beta-tubulin chains until they are transferred to the cytosolic chaperonin containing TCP1 (CCT) complex. PFDN6 binds specifically to cytosolic chaperonin (c-CPN), transfers target proteins to it and bind to developing polypeptide chain to promote folding in a setting where there are many competing pathways for nonnative proteins.

Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.

Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.

Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

CRNN is part of the "fused gene" family of proteins, which enclose N-terminus EF-hand domains and multiple tandem peptide repeats. CRNN contains two EF-hand Ca2+ binding domains in its N-terminus and two glutamine- and threonine-rich 60 amino acid repeats in its C-terminus. CRNN, also known as SEP53, which participates in the mucosal/epithelial immune response and epidermal differentiation. CRNN is a survival factor that participates in the clonogenicity of squamous esophageal epithelium cell lines, attenuates deoxycholic acid (DCA)-induced apoptotic cell death and discharge of calcium. When CRNN is over expressed in oral squamous carcinoma cell lines, it regulates negatively cell proliferation by the induction of G1 arrest.

MIG (CXCL9) is a small cytokine which is part of the CXC chemokine family. MIG, which is also recognized as monokine is induced by gamma interferon. MIG is related to 2 other CXC chemokines named CXCL10 and CXCL11, whose genes are located next to the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 obtain their chemotactic functions by interacting with the chemokine receptor CXCR3.

Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by MIG. CXCL9 is a T-cell chemoattractant. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.

HES7 belongs to the Hairy and enhancer of split family of bHLH transcription factors. The mouse ortholog of the HES7 is set by Notch signaling. The protein serves as a transcriptional repressor, and is involved in correct patterning of the axial skeleton. A mutation in HES7 has been shown to result in spondylocostal dysostosis. Multiple transcript variants encoding different isoforms have been discovered for HES7.

Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.

CD138 takes a part in cell adhesion. CD138 is expressed on the surface of pre-B cells and plasma cells but is absent from mature B cells. SDC1 is a selective marker for B cell lymphoblastic leukemia and lymphoplasmacytoid leukemia. SDC1 is missing from the apoptotic myeloma cells; therefore is a valuable marker for plasma cell and myeloma cells.

E-selectin (SELE) is a part of a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. E-selectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

Myosin is a hexameric ATPase cellular motor protein, which is composed of 2 heavy chains, 2 non-phosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains.
MYL1 gene encodes a myosin alkali light chain expressed in fast skeletal muscle. Two transcript variants have been identified for the MYL1 gene. In humans MYL1 is localized to chromosome 2q32.1-qter. The Myl1 locus encodes two alkali myosin light chains- Mlc1f and Mlc3f, from two promoters that are differentially regulated throughout development. The Mlc1f promoter is active in embryonic, fetal and adult fast skeletal muscle while the Mlc3f promoter is upregulated during fetal development and stays on in adult fast skeletal muscle.