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The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

nterleukin 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.

Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

P-Selectin also called Platelet Alpha-Granule Membrane Protein, CD62, and Granulocyte Membrane Protein GRMP belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Pselectin is expressed transiently on the surface of activated platelets and endothelial cells. P-Selectin is a 140 kDa protein which is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Secreted P-selectin is thought to play a key role in the adhesion of platelets to monocytes and neutrophils during an inflammatory response. P-Selectin is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Levels of P-Selectin may be elevated in a number of pathological conditions.

Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.

Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppresses the ability to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

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.

TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.

Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

Protein Tyrosine Phosphatase Type IVA Member 3 (PTP4A3) is a member of a small class of prenylated protein tyrosine phosphatases (PTPs) which remove phosphate modifications from tyrosine residues on proteins. PTP4A3 enhances cell proliferation, cell motility and invasive activity. PTP4A3 functions as a protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. PTP4A3 is mostly expressed in cardiomyocytes and skeletal muscle; it is also found in the pancreas.
PTP4A3 is always overexpressed in colon cancer metastasis. PTP4A3 is notably overexpressed in liver metastasis of colorectal cancer. High levels of PTP4A3 expression are linked to tumorigenesis and metastasis; therefore it is overexpressed in metastatic colorectal, ovarian, liver and skin cancers. PTP4A3 may be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. PTP4A3 is inhibited by sodium orthovanadate and peroxovanadium compounds.

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.

Trichomonas vaginalis, an anaerobic, flagellated protozoan parasite, is most dominant protozoan causing sexual transmitted disease. T. vaginalis induced vaginal tract infection occurs as multiple steps involving interactions between host macromolecules and protozoan virulent factor. Adhension protein P65 of T. vaginalis has a vital part in assisting the penetration into vaginal tract surface.

Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI is acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and is exclusively expressed in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

CD1a is a transmembrane glycoproteins, which is structurally related to the major histocompatibility complex (MHC) proteins and form heterodimers with beta-2-microglobulin. CD1a mediates the presentation of primarily lipid and glycolipid antigens of self or microbial origin to T cells. The human genome contains five CD1 family genes organized in a cluster on chromosome 1. The CD1 family members are thought to differ in their cellular localization and specificity for particular lipid ligands. The protein encoded by this gene localizes to the plasma membrane and to recycling vesicles of the early endocytic system. Alternatively spliced transcript variants have been observed, but their biological validity has not been determined.

Tyrosyl-tRNA synthetase (YARS2) is a mitochondrial protein which catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and afterward transferred to the acceptor end of tRNA(Tyr). YARS2 gene mutations are linked with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2).

Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.

Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.