colon

Probable hormone. RETNLB Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 13.4 kDa and the accession number is Q9BQ08.

RPSA Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 37.7 kDa and the accession number is P08865.

Annexin A2 (ANXA2) is a member of the annexin family and has roles in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein is associated with sickle cell osteonecrosis and the expression reduce of ANXA2 is associated with osteosarcoma metastases. ANXA2 functions as an autocrine factor, it can increases osteoclast formation and bone resorption. ANXA2 is involved in muscular dystrophies. In humans, the up-regulation of ANXA2 is related with colon adenocarcinoma cell differentiation.

Chemokine (C-C Motif) Ligand 28 (CCL28) is a novel chemokine that shares the most homology with CCL27/CTACK. CCL28 shows chemotactic activity for resting CD4, CD8 T-cells and eosinophils. It Binds to CCR3 and CCR10 and induces calcium mobilization in a dose-dependent manner. CCR10 (GPR2 orphan receptor) is also the receptor for CCL27/CTACK. CCL28 is preferentially expressed by epithelial cells of diverse tissues, with highest expression level in normal and pathological colon. It is also expressed in normal and asthmatic lung tissues. Human and mouse CCL28 shares 83% sequence identity in their mature regions.

Podoplanin belongs to the podoplanin family, also known as Glycoprotein 38. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. Detected at high levels in lung and brain, at lower levels in kidney, stomach, liver, spleen and esophagus, and not detected in skin and small intestine. Expressed in epithelial cells of choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells and in endothelia of lymphatic vessels. Also expressed in stromal cells of peripheral lymphoid tissue and thymic epithelial cells. Detected in carcinoma cell lines and cultured fibroblasts. Expressed at higher levels in colon carcinomas than in normal colon tissue. It can interacts with CLEC1B; the interaction is independent of CLEC1B glycosylation and activates CLEC1B. It may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Ligand for CLEC1B, a platelet receptor. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels.

SEMA4D is a member of the semaphorin family,contains one Ig-like C2-type domain, one PSI domain and one Sema domain. SEMA4D is strongly expressed in lymphoid tissues, especially in the thymus, as well as in the nervous tissues. However, SEMA4D is expressed at lower levels in testes, brain, kidney, small intestine, prostate, heart, placenta, lung and pancreas, but not in colon and liver. SEMA4D is a cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. SEMA4D is involved in a number of fundamental biological processes such as promoting reorganization of the actin cytoskeleton, the migration of cerebellar granule cells and of endothelial cells and signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Not only these, it plays a role in axonal growth cone guidance in the developing central nervous system. Semaphorin-4D / SEMA4D may play a functional role in the immune system, as well as in the nervous system. It could induce B-cells to aggregate and improves their viability (in vitro). SEMA4D is involved in regulating dendrite and axon branching and morphogenesis and promoting interaction with PLXNB1 mediates activation of RHOA.

β-1,4-galactosyltransferase 4 (B4GALT4) is a single-pass type II membrane protein that belongs to the Glycosyltransferase 7 family. B4GALT4 consist of the following 2 domains: N-Acetyllactosamine Synthase and β-N-Acetylglucosaminyl-Glycolipid β-1,4-Galactosyltransferase. B4GALT4 is highly expressed in the heart, placenta, kidney, and pancreas; it is lowly expressed in the brain, colon, lung, muscle, ovary, testis, and uterus. B4GALT4 function is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.

ADAM DEC1 protein is expressed highly in the small intestine and appendix, moderately in lymph node, mucosal lining of the colon, thymus, spleen and very weakly in the bone marrow. ADAM DEC1 is induced during DC maturation and up-regulated in response to T-cell signals. It may play an important role in the control of the immune response and during pregnancy.

TGF-beta RI, also called ALK-5, is an approximately 55 kDa type I transmembrane serine/threonine receptor kinase. In the presence of TGF-beta, TGF-beta RI forms a complex with, and is phosphorylated by, TGF-beta RII. Phosphorylated TGF-beta RI can then transiently bind and phosphorylate Smad2 and Smad3. TGF-beta functions as a tumor suppressor by inhibiting the cell cycle in the G1 phase. Administration of TGF-beta is able to protect against mammary tumor development in transgenic mouse models in vivo. Disruption of the TGF-beta/SMAD pathway has been implicated in a variety of human cancers, with the majority of colon and gastric cancers being caused by an inactivating mutation of TGF-beta RII. TGF-beta RI is likely important during development, since mice deficient for TGF-beta RI die at midgestation with severe defects in vascular development of the yolk sac and placenta, and an absence of circulating red blood cells. Furthermore, TGF-beta RI appears to be involved in proper lymphatic network development.

Butyrophilin-Like Protein 9 (BTNL9) is single-pass type I membrane protein member of the BTN/MOG family that belongs to the immunoglobulin superfamily. BTNL9 consists of two domains: one B30.2/SPRY domain and one Ig-like V-type (immunoglobulin-like) domain. Human BTNL9 mRNA has been identified in adipose, lung, thymus, spleen, colon, and cardiac tissues, but its highest levels of expression were found in B cells. BTNL9 expression has also been found to be down-regulated in colon cancer tumors. BTNL9 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 60-70 KDa and the accession number is Q8BJE2.

Cathepsin V (CTSV), also known as Cathepsin L2, CTSL2, and CATL2, is a member of the peptidase C1 family. It is predominantly expressed in the thymus and testis. Cathepsin V is also expressed in corneal epithelium, and to a lesser extent in conjuctival epithelium and skin. It is a lysosomal cysteine proteinase that may play an important role in corneal physiology. It has about 75% protein sequence identity to murine cathepsin L. The fold of this enzyme is similar to the fold adopted by other members of the papain superfamily of cysteine proteases. Cathepsin V has been recently described as highly homologous to Cathepsin L and exclusively expressed in human thymus and testis. Cathepsin V is the dominant cysteine protease in cortical human thymic epithelial cells, while Cathepsin L and Cathepsin S seem to be restricted to dendritic and macrophage-like cells. Active Cathepsin V in thymic lysosomal preparations was demonstrated by active-site labeling. Recombinant Cathepsin V was capable of converting Ii into CLIP efficiently, suggesting that it is the protease that controls the generation of alphabeta-CLIP complexes in the human thymus. Cathepsin V is the third elastolytic cysteine protease which exhibits the most potent elastase activity yet described among human proteases and that it is present in atherosclerotic plaque specimens. Cathepsin L2 may play a specialized role in the thymus and testis. Expression analysis of cathepsin L2 in human tumors revealed a widespread expression in colorectal and breast carcinomas but not in normal colon or mammary gland or in peritumoral tissues. Cathepsin L2 was also expressed by colorectal and breast cancer cell lines as well as by some tumors of diverse origin, including ovarian and renal carcinomas.

FAM19A2 belongs to the FAM19/TAFA family. FAM19/TAFA family members are chemokine-like proteins. The biological functions of TAFA family members remain to be determined, but there are a few tentative hypotheses. First, TAFAs may modulate immune responses in the CNS by functioning as brain specific chemokines, and may act with other chemokines to optimize the recruitment and activity of immune cells in the CNS. Second, TAFAs may represent a novel class of neurokines that act as regulators of immune nervous cells. And third, TAFAs may control axonal sprouting following brain injury. Human FAM19A2 is 97% aa identical to mouse FAM19A2 and is expressed in the central nervous system (CNS), colon, heart, lung, spleen, kidney, and thymus, however its expression in the CNS is 50 to 1000 fold higher than in other tissues. FAM19A2 gene is a member of the TAFA family which is composed of five highly homologous genes that encode small secreted proteins.

PDRG1, also known as C2orf126, belongs to the prefoldin subunit beta family. It is predominantly expressed in normal testis and exhibits reduced but detectable expression in other organs. PDRG1 may play a role in chaperone-mediated protein folding. PDRG1 is overexpressed in tumors relative to normal tissues. Its expression is upregulated in multiple malignancies including cancers of the colon, rectum, ovary, lung, stomach, breast and uterus when compared to their respective matched normal tissues. Thus PDRG1 is a high-value novel tumor marker that could play a role in cancer development and/or progression.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.Mouse SerpinB8, also known as Cytoplasmic antiproteinase 2, Peptidase inhibitor 8, SerpinB8, PI-8, SERPINB8 and CAP2, is a member of the Serpin superfamily. SERPINB8 was broadly expressed. In normal neuroendocrine tissues, strongest SerpinB8 expression was detected in islets of Langerhans of the pancreas. Moderate SerpinB8 expression was observed in neuroendocrine cells of the thyroid, adrenal cortex, colon, and pituitary gland. In the pancreas, SerpinB8 is specifically expressed by insulin-producing beta cells, and can be used as an additional diagnostic immunohistochemical marker. Mouse SerpinB8 distribution alters during kidney regeneration, possibly to control a prohormone convertase involved in inflammation or tissue repair.

RGS5 is a member of the RGS superfamily and acts as a negative regulator of heterotrimeric G protein-mediated signalling through G protein-coupled receptors (GPCRs). The regulator of G-protein signaling (RGS) proteins have recently been identified as signal transduction molecules which have structural homology to SST2 of Saccharomyces cerevisiae and EGL-10 of Caenorhabditis elegans. The messenger RNA of hRGS5 was abundantly expressed in heart, lung, skeletal muscle, and small intestine, and at low levels in brain, placenta, liver, colon, and leukocytes.

The netrin-1 receptor, UNC-5 Homology B, or UNC5B plays vital roles in angiogenesis, inflammation, embryonic development and carcinogenesis. Overexpression of UNC5B human colon epithelial cells suppressed dextran sodium sulfate, or DSS-induced apoptosis and caspase-3 activity. Besides, is a potential anti-neoplastic target in bladder cancer progression and inflammatory arthritis. UNC5B Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 65.7 kDa and the accession number is O08722.

GNRH2 (Gonadotropin-Releasing Hormone 2) is a Protein Coding gene. This gene is a member of the gonadotropin-releasing hormone (GnRH) gene family. Proteins encoded by members of this gene family are proteolytically cleaved to form neuropeptides which, in part, regulate reproductive functions by stimulating the production and release of the gonadotropins follicle-stimulating hormone (FSH) and luteinizing hormone (LH). 3 alternatively spliced human isoforms have been reported. The second mammalian isoform (GNRH2) is an ineffective stimulant of gonadotropin release. Given that pigs lack testicular GNRHR1, these data may indicate that GNRH2 and its receptor are involved in the autocrine or paracrine regulation of testosterone secretion. Diseases associated with GNRH2 include Colon Mucinous Adenocarcinoma and Ovarian Cancer.

Lymphocyte Antigen 6H (LY6H) is a novel member of the LY6 family of glycosylphosphatidylinositol-anchored cell surface glycoproteins. LY6H contains one UPAR/Ly6 domain. Human LY6H is synthesized as a 140 amino acid precursor that contains a 25 amino acid signal sequence, 20 amino acid propeptide that is removed in the mature form, and a 90 amino acid mature chain. LY6H is highly expressed in the brain (cerebral cortex, amygdala, hippocampus and subthalamic nucleus) and in acute human leukemic cell line MOLT-3. It is also found in lower levels in testis, pancreas, small intestine and colon. It has been shown that LY6H may play a role in both the central nervous system and the immune system.

AKR1C3, is an enzyme which belongs to the aldo/keto reductase family. It is expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. AKR1C3 catalyzes the conversion of aldehydes and ketones to alcohols. It catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2,which functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. It can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites.

Amphiregulin (AREG) is a single-pass membrane protein with 252 amino acids. AREG belongs to the amphiregulin family, which contains 1 EGF-like domain. AREG is expressed in a variety of tissues including ovary, placenta, lung, kidney, stomach, colon, and breast. It is related to Epidermal Growth Factor (EGF) and Transforming Growth Factor Alpha (TGF-alpha). As an EGF-related growth factor, AREG interacts with the EGF/TGF-alpha receptor to promote the growth of normal epithelial cells and inhibits the growth of certain aggressive carcinoma cell lines. AREG may also play a protective role in Bleomycin-Induced Pneumopathy.

Ubiquitin-Conjugating Enzyme E2 Variant 2 (UBE2V2) is an enzyme that belongs to the ubiquitin-conjugating enzyme family. UBE2V2 can be detected in the placenta, colon, liver, and skin. It forms a heterodimer with UBE2N. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains and which leads to protein degradation by the proteasome. UBE2V2 mediates transcriptional activation of target genes. It plays a role in the control of progress through the cell cycle and differentiation. It also plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.

The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Recently, that D614G was been found more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin.

Coats the epithelia of the intestines, airways, and other mucus membrane-containing organs. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. Major constituent of both the inner and outer mucus layers of the colon and may play a role in excluding bacteria from the inner mucus layer. Mucin-2/MUC2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 28.8 kDa and the accession number is Q02817.

Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.

Methionine aminopeptidase 1D, also known as MAP1D, is a member of the peptidase M24A family. N-terminal methionine removal is an important cellular process required for proper biological activity, subcellular localization, and eventual degradation of many proteins. The enzymes that catalyze this reaction are called Methionine aminopeptidases (MAPs). MAP1D is overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level). Downregulation of MAP1D expression by shRNA in HCT-116 colon carcinoma cells reduces anchorage-independent growth in soft agar. MAP1D binds two cobalt ions per subunit. The true nature of the physiological cofactor is under debate. MAP1D is also active with zinc, manganese, or divalent ions. MAP1D removes the amino-terminal methionine from nascent proteins. It may also play an important role in colon tumorigenesis.

S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A14, also known as S100 calciumbinding protein A14, S114 and S100A14, is a cytoplasm protein which belongs to the S-100 family. It is expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.

Secretagogin, also known as SCGN, is a secreted protein that is detectable in human serum after ischemic neuronal damage. It is a recently described calcium-binding protein. Secretagogin / SCGN is expressed at high levels in the pancreatic islets of Langerhans and to a much lesser extent in the gastrointestinal tract (stomach, small intestine and colon), the adrenal medulla and cortex and the thyroid C-cells. In the brain, the expression of Secretagogin / SCGN is restricted to distinct subtypes of neurons with highest expression in the molecular layer of the cerebellum (stellate and basket cells), in the anterior part of the pituitary gland, in the thalamus, in the hypothalamus and in a subgroup of neocortical neurons. Secretagogin / SCGN is widely expressed in prostatic adenocarcinoma as opposed to adenocarcinomas in other organs. The function of Secretagogin / SCGN is unknown, but it has been suggested in beta-cells to influence calcium-influx and has been observed downregulated in diabetes-prone BB rat islets exposed to cytokines. Secretagogin / SCGN is involved in the calcium metabolism of tumour cells and endothelial cells in a subset of neoplasms of the brain and its coverings. Secretagogin / SCGN is also a novel marker for neuroendocrine differentiation.

Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa.

Sialate O-acetylesterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. It is widely expressed with high expression in the testis, prostate, and colon. The systematic name of this enzyme class is N-acyl-O-acetylneuraminate O-acetylhydrolase. Other names in common use include N-acetylneuraminate acetyltransferase, sialate 9(4)-O-acetylesterase, and sialidase. Sialate O-acetylesterase catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. Defects in Sialate O-acetylesterase are a cause of autoimmune disease type 6 (AIS6). Individuals manifesting susceptibility to autoimmune disease type 6 can suffer from juvenile idiopathic arthritis, rheumatoid arthritis, multiple sclerosis, Sjogren syndrome, systemic lupus erythematosus, type 1 diabetes, ulcerative colitis, and Crohn disease.

The recycling of citrulline by argininosuccinate synthase 1 (ASS1) and argininosuccinate lyase (ASL) is crucial to maintain arginine availability and nitric oxide (NO) production. Nitric oxide (NO) plays an established role in numerous physiological and pathological processes, but the specific cellular sources of NO in disease pathogenesis remain unclear, preventing the implementation of NO-related therapy. Argininosuccinate lyase (ASL) is the only enzyme able to produce arginine, the substrate for NO generation by nitric oxide synthase (NOS) isoforms. Induction of endogenous NO production by enterocytes with supplements that upregulate ASL expression and complement its substrates results in improved epithelial integrity and alleviation of colitis and of inflammation-associated colon cancer.

Amphoterin-Induced Protein 2 (AMIGO2) is a single-pass type I membrane protein which belongs to the AMIGO family of immunoglobulin superfamily. Mature AMIGO2 contains an Ig-like C2-type (immunoglobulin-like) domain, 6 LRR (leucine-rich) repeats, a LRRCT domain, as well as a LRRNT domain. AMIGO2 is mainly expressed in in breast, ovary, cervix, and uterus, although lower in lung, colon, and rectum. AMIGO2 required for depolarization-dependent survival of cultured cerebellar granule neurons. AMIGO2 may mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. AMIGO2 may contribute to signal transduction through its intracellular domain, and may be required for tumorigenesis of a subset of gastric adenocarcinomas.

Phospholipase D4 (PLD4) is a newly identified protein expressed in microglia. the expression of PLD4 was located in macrophages in the colon cancer mesenchymal and lymph nodes as shown by immunohistochemical analysis. furthermore, its expression was associated with clinical staging of colon cancer. Then, THP-1 as a cell model induced into TAMs. PLD4 could be involved in the activation process of M1 phenotype macrophages. PLD4 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 51.1 kDa and the accession number is Q96BZ4.

Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with preference for phosphatidylcholines and phosphatidylglycerols over phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty acyls. Contributes to phospholipid remodeling of very low-density lipoprotein (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells. Efficiently hydrolyzes and inactivates PAF, a potent lipid mediator present in oxidized LDL. May act in an autocrine and paracrine manner. Secreted by lung epithelium, targets membrane phospholipids of infiltrating eosinophils, releasing arachidonate and boosting eicosanoid and cysteinyl leukotriene synthesis involved in airway inflammatory response. Secreted by gut epithelium, hydrolyzes dietary and biliary phosphatidylcholines in the gastrointestinal lumen, thereby regulating adipogenesis and body weight. Plays a stem cell regulator role in colon epithelium. Within intracellular compartment, mediates Paneth-like cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates the Wnt signaling pathway in ISCs and tissue regeneration. May participate in hair follicle morphogenesis by regulating phosphatidylethanolamines metabolism at the outermost epithelial layer and facilitating melanin synthesis. By generating lysophosphatidylcholines (LPCs) at sperm acrosome controls sperm cell capacitation, acrosome reaction and overall fertility. May promote neurite outgrowth in neuron fibers involved in nociception. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. In pulmonary epithelium, may contribute to host defense response against adenoviral infection. Prevents adenovirus entry into host cells by hydrolyzing host cell plasma membrane, releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and viral infection. Likely prevents adenoviral entry into the endosomes of host cells. May play a role in maturation and activation of innate immune cells including macrophages, group 2 innate lymphoid cells and mast cells.

The netrin-1 receptor, UNC-5 Homology B, or UNC5B plays vital roles in angiogenesis, inflammation, embryonic development and carcinogenesis. Overexpression of UNC5B human colon epithelial cells suppressed dextran sodium sulfate, or DSS-induced apoptosis and caspase-3 activity. Besides, is a potential anti-neoplastic target in bladder cancer progression and inflammatory arthritis. UNC5B Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 64.8 kDa and the accession number is Q8IZJ1-1.

Sulfotransferase family cytosolic 1B member 1, also known as Sulfotransferase 1B1, Sulfotransferase 1B2, Thyroid hormone sulfotransferase, SULT1B1 and ST1B2, is a cytoplasm protein that belongs to the sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. SULT1B1 is highly expressed in the liver, peripheral blood leukocytes, colon (mucosal lining), small intestine (jejunum) and spleen. A lesser expression of SULT1B1 was observed in the lung, placenta and thymus. SULT1B1 catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. SULT1B1 sulfates dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine.

Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) is a member of the IGF-II mRNA-binding protein (IMP) family. IGF2BP2 is a member of a family of mRNA binding proteins that, collectively, have been shown to bind to several different mRNAs in mammalian cells, including one of the mRNAs encoding insulin-like growth factor-2. Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) is involved in the stimulation of insulin action. IGF2BP2 / IMP2 is expressed in oocytes, granulosa cells of small and growing follicles, Leydig cells, spermatogonia, and semen (at protein level). It is also expressed in testicular cancer (at protein level). It is expressed weakly in the heart, placenta, skeletal muscle, bone marrow, colon, kidney, salivary glands, testis, and pancreas. IGF2BP2 binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. This binding is isoform-specific. IGF2BP2 may regulate the translation of target mRNAs.

Chloride intracellular channel protein 4, also known as Intracellular chloride ion channel protein p64H1 and CLIC4, is a member of the chloride channel CLIC family. It contains oneGST C-terminal domain. CLIC4 is a member of a family of intracellular chloride channels. It is regulated by p53, c-Myc, and tumor necrosis factor-alpha. CLIC4 is detected in epithelial cells from colon, esophagus and kidney (at protein level). CLIC4 has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. CLIC4 could promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis). Expression of CLIC4 is prominent in heart, kidney, placenta and skeletal muscle. Overexpression of CLIC4 in cancer cells inhibits tumor growth. Conversely, overexpression of CLIC4 in tumor stromal cells stimulates tumor growth. Thus, CLIC4 participates in normal and pathological processes and may serve as a useful target for therapies in disturbances of homeostasis and neoplastic transformation. Loss of CLIC4 in tumor cells and gain in tumor stroma is common to many human cancers and marks malignant progression. Up-regulation of CLIC4 in tumor stroma is coincident with myofibroblast conversion, generally a poor prognostic indicator. Reactivation and restoration of CLIC4 in tumor cells or the converse in tumor stromal cells could provide a novel approach to inhibit tumor growth.

Harmonin, also known as Antigen NY-CO-38 / NY-CO-37, Autoimmune enteropathy-related antigen AIE-75, Protein PDZ-73, Renal carcinoma antigen NY-REN-3, Usher syndrome type-1C protein and USH1C, is a protein that is expressed in small intestine, colon, kidney, eye and weakly in pancreas. USH1C is expressed also in vestibule of the inner ear. USH1C contains 3 PDZ (DHR) domains. USH1C may be involved in protein-protein interaction. Defects in USH1C are the cause of Usher syndrome type 1C (USH1C), also known as Usher syndrome type I Acadian variety. USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa and sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). Defects in USH1C are also the cause of deafness autosomal recessive type 18 (DFNB18) which is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.

Golgi membrane protein 1, also known as Golgi membrane protein GP73, Golgi phosphoprotein 2, and GOLM1, is a protein that belongs to the GOLM1 / CASC4 family. GOLM1 is widely expressed. It is highly expressed in the colon, prostate, trachea, and stomach. It is expressed at a lower level in testis, muscle, lymphoid tissues, white blood cells, and spleen. It is predominantly expressed by cells of the epithelial lineage. GOLM1 is expressed at a low level in the normal liver. Expression significantly increases in virus (HBV, HCV) infected liver. Expression of GOLM1 does not increase in liver disease due to non-viral causes (alcohol-induced liver disease, autoimmune hepatitis). Increased expression in hepatocytes appears to be a general feature of advanced liver disease. In liver tissue from patients with adult giant-cell hepatitis (GCH), GOLM1 is strongly expressed in hepatocyte-derived syncytial giant cells. GOLM1 is constitutively expressed by biliary epithelial cells but not by hepatocytes.

Beta-defensin 3 is a member of the defensin family. Defensin family is comprised by microbicidal and cytotoxic peptides made by neutrophils. Members of the beta-defensin 3 family are highly similar in protein sequence. Beta-defensin 3 shows antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Beta-defensin 3 is abundantly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. It is also expressed in salivary gland, bone marrow, colon, stomach, polyp and larynx. However, in small intestine, it cannot be detected. Defensin has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense. Beta-defensin 3 kills multiresistant S.aureus and vancomycin-resistent E.faecium. It has no significant hemolytic activity.

IDO2 belongs to the indoleamine 2,3-dioxygenase family. Indoleamine 2,3-dioxgyenase (IDO), is a cytosolic haem protein which, together with the hepatic enzyme tryptophan 2,3-dioxygenase, catalyzes the conversion of tryptophan and other indole derivatives to kynurenines. In addition to classic IDO (IDO1), a new variant, IDO2, has recently been described. IDO2 is expressed in the liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon. IDO is widely distributed in human tissues, its physiological role is not fully understood but is of great interest. IDO can be up-regulated via cytokines such as interferon-gamma, and can thereby modulate the levels of tryptophan, which is vital for cell growth. In humans and mice, the IDO1 and IDO2 genes are present tandemly in a tail-to-head arrangement on chromosome 8. In lower vertebrates such as zebrafish and toads, only a single IDO gene may be present that may be more IDO2-like in structure. This closer relationship to IDO2 suggests that IDO2 may be the ancestor of the better characterized IDO1 gene and that IDO1 might have been generated by gene duplication of IDO2 before the origin of tetrapods in mammalian evolutionary history. IDO2 catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism.

SULT1A3 belongs to the sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. They are different in their tissue distributions and substrate specificities while their gene structure (number and length of exons) is similar. SULT1A3 gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. It is the most centromeric of the four sulfotransferase genes. Exons of this gene overlap with exons of a gene that encodes a protein containing GIY-YIG domains (GIYD1). SULT1A3 is expressed in liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte. SULT1A3 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.

MMP19, also known as RASI-1, is a member of the peptidase M1A family. It contains 4 hemopexin-like domains and is expressed in the mammary gland, placenta, lung, pancreas, ovary, small intestine, spleen, thymus, prostate, testis colon, heart, and blood vessel walls. It is a matrix metalloproteinase (MMP). Proteins of the MMP family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP19 may play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 is frequent in RA patients.

Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B) also known as DcR3(Decoy Receptor 3) and M68 is the tumor necrosis factor receptor superfamily. DcR3/TNFRSF6B belongs to the tumor necrosis factor receptor superfamily. The encoded protein is postulated to play a regulatory role in suppressing FasL- and LIGHT-mediated cell death. It acts as a decoy receptor that competes with death receptors for ligand binding. Over-expression of this gene has been noted in gastrointestinal tract tumors. Read-through transcription into this gene from the neighboring upstream gene, which encodes regulator of telomere elongation helicase 1 (RTEL1), generates a non-coding transcript. DcR3/TNFRSF6B is detected in fetal lung, brain and liver. DcR3/TNFRSF6B is also detected in adult stomach, spinal cord, lymph node, trachea, spleen, colon and lung. This protein is highly expressed in several primary tumors from colon, stomach, rectum, esophagus and in SW480 colon carcinoma cells.

Expression of REG3B was sufficient to inhibit cytokine-induced activation of STAT3 in IECs. The human REG3beta protein, the functional counterpart of mouse REG3B, inhibited STAT3 activity in human 293T cells, and its expression level in colorectal tumors correlated inversely with pSTAT3 level and survival times of patients. REG3B negatively regulates cytokine-induced activation of STAT3 in colon epithelial cells. This pathway might be targeted in patients with colitis to reduce carcinogenesis.

The netrin-1 receptor, UNC-5 Homology B, or UNC5B plays vital roles in angiogenesis, inflammation, embryonic development and carcinogenesis. Overexpression of UNC5B human colon epithelial cells suppressed dextran sodium sulfate, or DSS-induced apoptosis and caspase-3 activity. Besides, is a potential anti-neoplastic target in bladder cancer progression and inflammatory arthritis. UNC5B Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 39.2 kDa and the accession number is Q8IZJ1-1.

Tribbles homolog 3, also known as Neuronal cell death-inducible putative kinase, p65-interacting inhibitor of NF-kappa-B, SINK and TRIB3, is a Nucleus protein that belongs to the protein kinase superfamily and CAMK Ser/Thr protein kinase family and Tribbles subfamily. Highest expression Of TRIB3 is in liver, pancreas, peripheral blood leukocytes and bone marrow. It is also highly expressed in a number of primary lung, colon and breast tumors. TRIB3 is expressed in spleen, thymus, and prostate and is undetectable in other examined tissues, including testis, ovary, small intestine, colon, leukocyte, heart, brain, placenta, lung, skeletal muscle, and kidney. TRIB3 disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. TRIB3 may bind directly to and mask the 'Thr-38' phosphorylation site in AKT1. It binds to ATF4 and inhibits its transcriptional activation activity. TRIB3 interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. It interacts with MAPK kinases and regulates activation of MAP kinases. It may play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. TRIB3 does not display kinase activity.

Angiotensin-Converting Enzyme 2 (ACE-2) is an integral membrane protein and a zinc metalloprotease of the ACE family, the ACE family includes somatic and germinal ACE. ACE-2 cleaves angiotensins I and II as a carboxypeptidase, ACE-2 converts angiotensin I to angiotensin 1-9, and angiotensin II to angiotensin 1-7. ACE-2 is also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. ACE-2 can be high expressed in testis, kidney and heart, in colon, small intestine and ovary at moderate levels. Captopril and lisinopril as the classical ACE inhibitor don’t inhibit ACE-2 activity. ACE-2 may play an important role in regulating the heart function.

CD254, also known as RANKL, TNFSF11, TRANCE, OPGL and ODF, is a type II membrane protein of the tumor necrosis factor (TNF) superfamily, and affects the immune system and control bone regeneration and remodeling. RANKL is the ligand of nuclear factor (NF)-κB (RANK). When RANKL binds to RANK, it will undergo trimerization and then bind to an adaptor molecule TNF receptor-associated factor 6 (TRAF6). This results in the activation of several downstream signaling cascades, including the NFκB, mitogen-activated protein kinases (MAPK), activating protein 1 (AP-1), and nuclear factor of activated T cells (NFATc1), resulting in the formation of multinucleated bone-resorbing osteoclasts. RANKL is widely expressed in skeletal muscle, thymus, liver, colon, small intestine, adrenal gland, osteoblast, mammary gland epithelial cells, prostate and pancreas.

β-Defensin 4A is a membrane-active cationic peptide that functions in inflammation and innate immune responses. There are at least 30 β-Defensins, which are distinguished from α-Defensins by the connectivity pattern of their three intermolecular disulfide bonds. Members of the Defensin family are highly similar in protein sequence. This gene encodes Defensin, DEFB4;, which has broad-spectrum antimicrobial activity and may play an important role in innate epithelial defense. They are highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. β-Defensin 4A has low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine. The 45 amino acid mature human BD3 shares 38% and 33% amino acid sequence identity with mouse and rat BD3, respectively.