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SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

4-1BBR is a member of the TNF-receptor superfamily. 4-1BB receptor contributes to the clonal expansion, survival, and development of T cells.4-1BBRcan also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.

Bcl-2–associated X protein (Bax) belongs to the Bcl-2 protein family.
Bax is a pro-apoptotic Bcl-2 protein containing BH1, BH2 and BH3 domains.
Bax accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor bcl2 or its adenovirus homolog e1b 19k protein. Bax induces the release of cytochrome c, activation of casp3, and thereby apoptosis. Bax is expressed in a wide variety of tissues, with highest levels in the testis and ovary.
Tumor suppressor protein p53 upregulates the expression of BAX. Bax has been shown to be involved in p53-mediated apoptosis.

Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.

Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.

RAB3A Interacting Protein Like 1 (RAB3IL1) is a 382 amino acid protein which is a member of the SEC2 family. RAB3IL1 is a guanine nucleotide exchange factor (GEF) for Rab3A. RAB3IL1 competes for interaction with Rab3A and IHPK1 via its coiled coil domain, which doesn’t involve IHPK1 kinase activity.

HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

Rho-related GTP-binding protein RhoB (RhoB) belongs to the Rho GTP-binding protein family. RhoB facilitates apoptosis in neoplastically transformed cells after DNA damage. RhoB has a negative role in tumorigenesis since deletion causes tumor formation.

Chlamydia is a common term for infection with any bacterium belonging to the phylum Chlamydiae. This term derives from the name of the bacterial genus Chlamydiain the family Chlamydiaceae, order Chlamydiales, class and phylum Chlamydiae. There are two genera in Chlamydiaceae: Chlamydia and Chlamydophila. The genus Chlamydia includes three species: C. trachomatis, C. muridarum, and C. suis.

Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 aa, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 aa, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. Four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.

S100 calcium binding protein A5 (S100A5) belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A5 has a Ca2+ affinity 20-100 fold higher than the other S100 proteins investigated under identical conditions. Furthermore, S100A5 protein binds Zn2+ and Cu2+, and Cu2+ strongly which harms the binding of Ca2+. S100A5 is expressed in very limited regions of the adult brain.

S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.

MTHSFD, also known as Methenyltetrahydrofolate Synthetase Domain Containing protein, is linked to Pancreas, Annular and Gastrointestinal Defects. It has also been associated with Immunodeficiency Syndrome. Some of the Gene Ontology annotations that are related to the MTHSFD gene are nucleic acid binding and nucleotide binding.

SEPSECS catalyzes the last step of sec synthesis by way of converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.

Serpin Peptidase Inhibitor, Clade B Member 3, also known as SERPINB3 is a papain-like cysteine protease inhibitor which modulates the host immune response versus tumor cells. SERPINB3 is a protein coding gene which acts as an inhibitor of UV-induced apoptosis by suppressing the activity of c-Jun NH(2)-terminal kinase (JNK1).

DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.
DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques.

SIRT5 belongs to the Sirtuin family of proteins, homologs to the yeast Sir2 protein. Sirtuin family members hold a sirtuin core domain and grouped into four classes. The protein encoded by this gene is included in class III of the sirtuin family. Human sirtuins functions were not yet determined; still, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies propose that human sirtuin could operate as intracellular regulatory protein with mono-ADP-ribosyltransferase activity.

Asialoglycoprotein Receptor 2 (ASGR2) is a hetero-oligomeric protein comprised of major and minor subunits, encoded by different genes. ASGR2 is a subunit of the asialoglycoprotein receptor; it is the less abundant minor subunit. The ASGR2 receptor is a transmembrane protein, which has a crucial role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

GGPS1 is PART of the prenyltransferase family. GGPS1 is widely expressed in testis, heart and skeletal muscle, GGPS1 is localized in the cytoplasm and catalyzes the formation of geranylgeranyl pyrophosphate, a precursor of geranylgeranylated proteins and carotenoids. GGPS1 is a significant enzyme that is responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor.