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MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin

Pregnancy Specific Beta-1-Glycoprotein 1 (PSG1) is a member of a subgroup of transcription factors which are phosphorylated upon binding to promoter sequences. PSGs belong to the carcinoembryonic antigen (CEA) family and function as early biochemical markers of syncytiotrophoblast formation. Furthermore, PSG1 is assumed to mediate placental vascular morphogenesis by enhancing VEGF-A production and endothelial tube formation. PSG1 is a major product of the syncytiotrophoblast, reaching concentrations of 100- 290 mg/l at term in the serum of pregnant women.

Family With Sequence Similarity 19 Member-A5 (FAM19A5) belongs to the TAFA family which is comprised of 5 highly homologous genes encoding small secreted proteins. These proteins have conserved cysteine residues at fixed positions, and are remotely related to MIP-1alpha, which is a member of the CC-chemokine family. The TAFA proteins are primarily expressed in specific regions of the brain, and are assumed to serve as brain-specific chemokines or neurokines which act as regulators of immune and nervous cells.

GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

The Argonaute protein is part of the RISC or RNA-induced silencing complex, as so, the protein has a key part in the slicing processes of RNA. The RNA interference (RNAi) is being held by RISC. Small non-coding RNA fragments bond to the Argonaute proteins, through base pairing, eventually leads to the cleavage of messenger RNA or translation suppression.

The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virusof the herpes family(which includes Herpes simplex virusand Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expressionwhich can be broadly categorized as being lytic cycle or latent cycle. The lytic cycleor productive infection results in staged expression of a host of viral proteinswith the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cellas EBV virions are produced by budding from the infected cell. The latent cycle(lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen(EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins(LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs(EBERs).

ST13 is an adaptor protein (co-chaperone) that mediates the association of HSP70 & HSP90 and appears in early receptor complexes. ST13 plays a role in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of ST13 is downregulated in colorectal carcinoma tissue signifying that is candidate tumor suppressor gene. Through common binding to both Hsp70 and Hsp90, ST13 functions as an adaptor that can integrate Hsp70 and Hsp90 interactions. The expression of ST13 decreases in colorectal cancer tissue compared with that in adjacent normal tissue. ST13 is mostly expressed in colorectal epithelia and adenocarcinoma cells. ST13 functions to promote the efficiency of glucocorticoid receptor maturation in cells. The expression levels of the ST13 gene were significantly decreased in primary tumors compared with adjacent mucosa.

RAB13 is a member of the small GTPase superfamily which are nontransforming monomeric GTP-binding proteins that hold 4 extremely conserved regions that take part in GTP binding and hydrolysis. In addition, RAB proteins have a vital role in the endocytic pathways. The GTPase Rab13 regulates the assembly of functional epithelial tight junctions (TJs) and is expressed in every phase of preimplantation development.

MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

JAM3 belongs to the junctional adhesion molecule protein family and functions as a receptor for another member of this family. JAM3 plays a part in cell-cell adhesion. The soluble form of JAM3 is a mediator of angiogenesis. JAM3 is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). A mutation in an intron of the JAM3 gene is linked with hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts.

Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) , is part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.

M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.

GINS4, a member of the GINS4/SLD5 family, has a key part in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is significant for GINS complex assembly. GINS complex connects favorably to singlestranded DNA. Recombinant human GINS4 protein, fused to His-tag at N-terminus was purified by using conventional chromatography techniques.

C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.

V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.

HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.

Signal-Regulatory Protein Gamma (SIRPG) belongs to the signal-regulatory protein (SIRP) family whose members are receptor-type transmembrane glycoproteins which negatively regulate the receptor tyrosine kinase-coupled signaling processes. SIRPG is also a part of the immunoglobulin superfamily.

LIM domain only 1 (LMO1) is a protein-coding gene. LMO1 encodes a transcriptional regulator which contains two cysteine-rich LIM domains but lacks a DNA-binding domain. LIM domains might play a part in protein interactions; hence the protein may regulate transcription by competitively binding to specific DNA-binding transcription factors.

A fusion tag called FLAG consists of eight amino acids (AspTyrLysAspAspAspAspLys) including an enterokinase-cleavage site. FLAG is specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions. Several antibodies against this peptide have been developed. One antibody denoted as M1 binds the peptide in the presence of bivalent metal cations preferably Ca(+). Elution is effected by chelating agents. Another strategy is competitive elution with excess of free Flag Peptide. The FLAG peptide purifies and detects recombinant fusion proteins. FLAG peptide is useful in Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure, and protein localization. Flag peptide is a hydrophilic tag which significantly improves the detection and purification of recombinant fusion proteins.

ATPaseTransporting Beta 3 (ATP1B3) is a member of the X(+)/potassium ATPases subunit beta family. ATP1B3 is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The beta subunit controls, by way of assembly of alpha/beta heterodimers, the quantity of sodium pumps transported to the plasma membrane. The precise role of the beta-3 subunit is unknown.