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CD86 type I membrane protein is a member of the immunoglobulin superfamily which is expressed by antigen-presenting cells, and acts as the ligand for two proteins at the cell surface of T cells, CD28 antigen and cytotoxic T-lymphocyte-associated protein 4. CD86 binding with CD28 protein is a co-stimulatory signal for initiation of the T-cell. CD86 binding with CTLA-4 negatively regulates T-cell activation and diminishes the immune response.

CD8 is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. CD8 acts as a co-receptor, and the T-cell receptor on the T lymphocyte recognize antigen displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional CD8 is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains.
CD8 identifies cytotoxic/suppressor t-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of t-cell mediated killing. CD8 alpha chains bind to class-I MHC molecules alpha-3 domains.

IRF5 belongs to the interferon regulatory factor (IRF) family, which is a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats.

APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines. APRIL stimulates proliferation of tumor cell lines and intensifies tumorigenicity in nude mice.

CD45 leukocyte common antigen (LCA) belongs to the family of at least four isoforms of membrane glycoproteins (220, 205, 190, 180kDa) expressed on hematopoietic cell lines but absent on non-hematopoietic cell lines, normal and malignant non-hematopoietic tissues. The intracellular portion of these molecules has protein phosphatase activity and is involved in regulation of transmembrane signals.

HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.

HSPH1 analysis is used as an indicator and as a diagnostic aid in problematic lesions. HSPH1 chaperones the responses to endoplasmic reticulum (ER) stress during its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process. HSPH1 is highly expressed in a variety of human tumors. HSPH1 is a mammalian member of the HSP105/110 family, a diverged subgroup of the HSP70 family. HSP105 has 2 isoforms, alpha and beta. Hsp105a associates with Hsp70/Hsc70 as complexes in vivo and regulates the chaperone activity of Hsp70/Hsc70 negatively in vitro and in vivo.

CD44 is a cell-surface glycoprotein that plays a role in cell-cell interactions, cell adhesion and migration. CD44 is a receptor for hyaluronic acid and also interacts with other ligands, such as osteopontin, collagens, and matrix metalloproteinases. CD44 participates in a wide variety of cellular functions such as lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. CD44 and CD49d are putative activity markers and CD44 a potential novel therapeutic target in multiple sclerosis. Increased CD44 antigen is associated with relapses in non-small cell lung cancers.

HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

Creatine kinase (CK) found mostly in skeletal muscle, heart, and brain cells which assists in producing energy. When these cells are damaged, CK is released into the bloodstream, so that a CK blood test can diagnose certain heart conditions, muscle injuries and various diseases. increased CK levels can suggest situations such as muscle damage from injury or rhabdomyolysis, heart attack, or muscular dystrophy.  Creatine kinase catalyzes the reversible reaction of creatine and ATP to form phosphocreatine and ADP. 

CD-90 plays a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain Thy-1 is the designation for a major cell surface glycoprotein characteristic to T cells,. The Thy-1 glycoproteins are constituents of thymocytes and neurons and probably are involved in cell-cell interactions. Human Thy-1 homolog maps to chromosome 11 because that is where T3D is found, in the mouse T3D and Thy-1 map to chromosome 9 along with certain other loci that are on human 11q.

Akt1, also known as Akt or else protein kinase B (PKB) is an important molecule in mammaliancellular signaling. In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. Moreover, these enzymes are members of the serine/threonine-specific protein kinase family (EC2.7.11.1). Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesis pathways, and is therefore a key signaling protein in the cellular pathways which lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a most important factor in numerous types of cancer. Akt (now also called Akt1) was at first identified as the oncogenein the transforming retrovirus, AKT8.

CD31 is a glycoprotein expressed on endothelial cells, platelets, macrophages and Kupffer cells, granulocytes, T / NK cells, lymphocytes, megakaryocytes, fibroblasts, osteoclasts, neutrophils. In humans, the gene encoding CD31 is found on chromosome 17.
CD31 is a cluster of differentiation molecule. It is also called PECAM-1 for platelet endothelial cell adhesion molecule. It plays a key role in removing aged neutrophils from the body. Both the neutrophil and the macrophage express CD31 on their membranes, and during the testing process, these CD31 molecules bind the two cells together. If the neutrophil is healthy, it will send a signal to the macrophage, and the CD31 molecules will detach.
CD31 is also expressed in certain tumors, including epithelioid hemangioendothelioma, epithelioid sarcoma-like hemangioendothelioma, other vascular tumors, histiocytic malignancies, and plasmacytomas. It is rarely found in some sarcomas and carcinomas.

This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.

Cyclin-dependent kinase 4 combines with the protein cyclin D to form a protein complex that promotes the passage of cells through the G1 checkpoint in the cell growth cycle. This cellular activity is regulated by the protein p16 produced by p16INK4a. Normally, p16 controls cell growth by inhibiting the activity of the CDK4–cyclin D complex and stopping cells at the G1 checkpoint.

IL12B is a subunit of interleukin 12 which is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. Interleukin 12 is a disulfide-linked heterodimer composed of the 40kDa cytokine receptor like subunit encoded by the IL12B gene, and a 35kDa subunit encoded by IL12A. The IL12B cytokine is expressed by activated macrophages which serve as an important inducer of Th1 cells development. The IL12B cytokine has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Overexpression of the IL12B gene was observed in the central nervous system of patients with multiple sclerosis (MS), suggesting a role of the IL12B cytokine in the pathogenesis of the disease. The promoter polymorphism of the IL12B gene has been reported to be linked to the severity of atopic and non-atopic asthma in children.

IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function. Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine,

Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.

Human HSP40 (heat shock protein with molecular size of 40kDa) is one of the mammalian homologues of bacterial DnaJ heat shock protein and regulates cellular processes by aiding in the folding, transport and assembly. HSP40 protein contains the J-domain which controls interaction with the ATPase domain of DnaK.

SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.

HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.

NRG1 is one of 4 proteins in the neuregulin family which act on the EGFR family of receptors. NRG1 was initially identified as a 44kDa glycoprotein that interacts with the ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues. In various brain areas, NRG1 is expressed at synaptic regions and its processing can be regulated by neuronal activity. The HRG-beta3variant of NRG1, along with HRG-alpha, beta1 and beta2 variants, was identified in various normal tissues and cancer cell lines.