intestine

Cadherin 17/CDH17 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag. The predicted molecular weight is 88.24 kDa and the accession number is Q12864-1.

Cadherin-17 is a single-pass type I membrane protein that belongs to the cadherin superfamily. Cadherin-17 consists of one extracellular region containing seven cadherin domains and one transmembrane region but it lacks the conserved cytoplasmic domain. Cadherin-17 is expressed in the gastrointestinal tract and pancreatic duct. Cadherins are calcium dependent cell adhesion proteins and preferentially interact with each other in a homophilic manner in connecting cells. Cadherin-17 may have a role in the morphological organization of liver and intestine and involved in intestinal peptide transport.

Annexin A13 (ANXA13) belongs to the annexin family which plays a role in phospholipase inhibition, cytoskeletal interactions, intracellular signal transduction pathways and regulation of cellular growth. ANXA13 contains four annexin repeats and a pair of annexin repeats may form one binding site for calcium and phospholipid. ANXA13 is highly expressed in intestinal and kidney epithelial cells. The specific function of ANXA13 has not yet been determined; however it is associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes.

ANXA13 Protein, Canine, Recombinant (His) is expressed in Yeast.

Cadherin 17/CDH17 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 87 kDa and the accession number is Q12864-1.

Cadherin 17/CDH17 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 86.4 kDa and the accession number is P55281.

Cadherin 17/CDH17 Protein, Cynomolgus, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 111.8 kDa and the accession number is XP_005563762.1.

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.

Cadherin 17/CDH17 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 85.94 kDa and the accession number is XP_005563762.2.

Pancreatitis-associated protein IB, Regenerating islet-derived protein III-gamma, is a secreted protein which contains 1 C-type lectin domain. It is expressed almost exclusively in the pancreas and also expressed in testis, but not found in small intestine. This protein might be a stress protein involved in the control of bacterial proliferation.

Anterior Gradient 2 (AGR2) is an 18-21 kDa member of the PDI family of enzymes. AGR2 is widely expressed in secretory cells, such as small intestine goblet, prostate epithelium, enteroendocrine cells, and multiple carcinoma cell types. AGR2 forms transient disulfide linkages with molecules destined for secretion, possibly aiding protein folding. Expression of AGR2 shows a positive correlation with expression of estrogen receptor in breast carcinoma and a negative correlation with expression of EGF receptor. Mature human AGR2 is 155 amino acids (aa) in length (aa 21 - 175). Cys81 is presumed to participate in intermolecular bond formation. Over aa 21 - 175, human AGR2 shares 94% aa identity with mouse AGR2.

Mouse Betacellulin is a single type I membrane protein which belongs to the EGF family of cytokines. EGF family has many members including EGF, TGF-a, Amphiregulin, HB-EGF, Epiregulin, Tomoregulin and the Neuregulins. Betacellulin is characterised by a six-cysteine consensus motif that forms three intra-molecular disulfide bonds crucial for binding the ErbB receptor family. Betacellulin is expressed in several tissues and tumor cells including kidney, uterus, liver, pancreas and small intestine. Betacellulin binds and activates ErbB-1 and ErbB-4 homodimers. Betacellulin is thought to play a role in the differentiation of pancreatic beta cells.Human and mouse mature BTC protein are 80% identical at the amino acid sequence level. Betacellulin is involved in many biological processes such as stimulating gastrointestinal growth. It is proteolytically processed from a larger membrane-anchored precursor and is a potent mitogen for a wide variety of cell types.

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.

Butyrophilin-like 4, also known as BTLN4, BTN3A3 (human) and BTN3A2 (rat) is an approximately 65 kDa member of the butyrophilin family that may play a role in immune regulation. BTNL4 shows striking sequence similarity to Skint1, is also largely restricted to an epithelial tissue (the small intestine) replete with T cells, plays a role in T-cell responses in the adaptive immune response.

Liver-intestine cadherin (CDH17) has been known to function as a tumor stimulator and diagnostic marker for almost two decades.In vivo studies showed CDH17 knockout resulted in apoptotic PC tumor death through activating caspase-3 activity. Taken together, CDH17 functions as an oncogenic molecule critical to PC growth by regulating tumor apoptosis signaling pathways and CDH17 could be targeted to develop an anti-PC therapeutic approach. CDH17 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 89.2 kDa and the accession number is A0A2K5X8I8.

Liver-intestine cadherin (CDH17) has been known to function as a tumor stimulator and diagnostic marker for almost two decades.In vivo studies showed CDH17 knockout resulted in apoptotic PC tumor death through activating caspase-3 activity. Taken together, CDH17 functions as an oncogenic molecule critical to PC growth by regulating tumor apoptosis signaling pathways and CDH17 could be targeted to develop an anti-PC therapeutic approach. CDH17 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 111.73 kDa and the accession number is Q12864.

Liver-intestine cadherin (CDH17) has been known to function as a tumor stimulator and diagnostic marker for almost two decades.In vivo studies showed CDH17 knockout resulted in apoptotic PC tumor death through activating caspase-3 activity. Taken together, CDH17 functions as an oncogenic molecule critical to PC growth by regulating tumor apoptosis signaling pathways and CDH17 could be targeted to develop an anti-PC therapeutic approach. CDH17 Domain 5-7 Protein (Primary Amine Labeling), Human, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 36.79 kDa and the accession number is Q12864.

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.

Butyrophilin-like 2 (BTNL2) is a member of the BTN/MOG Ig-superfamily and functions as a negative regulator of immune cell activation. Mouse BTNL2 is type I transmembrane glycoprotein that contains an extracellular domain (ECD), a transmembrane region and a short cytoplasmic domain. The ECD features two V-type Ig-like domains, two C-type Ig-like domains, and four glycosylation sites. BTNL2 is expressed in epithelial cells of the small intestine, colonic dendritic cells, and in cells of the lymph node. BTNL2 expression is upregulated in T cells following activation, a characteristic BTNL2 shares with the homologous B7 family of costimulatory molecules. BTNL2 negatively regulates T cells by inhibiting proliferation and inflammatory cytokine secretion. It also increases the expression of FoxP3 in T cells to promote regulatory T cell development. Single nucleotide polymorphisms in BTNL2 are associated with a risk for sporadic prostate cancer, rheumatoid arthritis, sarcoidosis, ulcerative colitis, and other inflammatory diseases.

Beta-1,4-galactosyltransferase 3 (B4GALT3) belongs to the glycosyltransferase 7 family. It is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. It is highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.

Malate dehydrogenase, mitochondrial is a 338 amino acids protein that belongs to the LDH/MDH superfamily. MDH type 1 family. MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highly expressed in the adrenal system, small intestine, heart and pancreas.

Fibroblast Growth Factor Receptor-Like 1 (FGFRL1) is a single-pass type I membrane protein that belongs to the FGF receptor family. The mature human FGFRL1 consists of a 354 amino acid extracellular domain (ECD) with 3 Ig-like C2-type domains, a 21 amino acid transmembrane segment, and a 134 amino acid cytoplasmic domain. FGFR1 expressed in various tissues, preferentially in cartilaginous tissues and pancreas. It highly expressed in the liver, kidney, heart, brain and skeletal muscle, weakly expressed in the lung, small intestine and spleen. FGFRL1 has a negative effect on cell proliferation.

Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm. Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm. Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group.

Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12. Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. SORBS2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 33.1 kDa and the accession number is O94875.

MEP1B (Meprin A Subunit Beta) is a Protein Coding gene. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in the kidney and intestine. Meprins are cell membrane, oligomeric metalloendopeptidases composed of two distinct but evolutionarily related subunits, alpha, and beta. MEP1A is mapped to the short arm of chromosome 6 by the use of radiation and somatic cell hybrids. More specifically, it is localized between the centromere and GSTA2 in 6p11-p12. MEP1B mapped to chromosome 18, by the use of somatic cell hybrids, in 18q12.2-q12.3, proximal to the TTR/PALB gene. Diseases associated with MEP1B include Powassan Encephalitis and Deafness, Autosomal Dominant 31.

ASAH2 (N-acylsphingosine amidohydrolase 2), also known as neutral ceramidase, is a type II integral membrane protein that can be cleaved to produce a soluble secreted protein. The enzyme is abundant in the brush border membranes of the intestine, and also expressed in several tissues such as kidney, brain and liver. The primary structure of ASAH2/neutral ceramidase is highly conserved from bacteria to humans, however, there is a clear difference in the molecular architecture. The murine ASAH2 possesses ‘amucin box’, a Ser/Thr/Pro-rich domain glycosylated with O-glycans which is necessary to retain the enzyme on the plasma membrane as a type II integral protein. The major physiological function of ASAH2/neutral ceramidase is the metabolism of dietary sphingolipids, and thus plays a role in the generation of messenger molecules such as sphingosine and sphingosine 1-phosphate.

Alanine aminotransferase (ALT), also known as glutamate pyruvate transaminase (Gpt), is a pyridoxal enzyme that catalyzes the reversible interconversion of L-alanine and 2-oxoglutalate to pyruvate and L-glutamate and plays a key role in the intermediary metabolism of glucose and amino acids. As a key enzyme for gluconeogenesis, Gpt is a widely-used serum marker for liver injury. Two ALT isoenzymes have been identified, ALT1 and ALT2 (GPT1 and GPT2), which are encoded by separate genes and share significant sequence homology, but differ in their expression patterns. Gpt1 is widely distributed and mainly expressed in the intestine, liver, fat tissues, colon, muscle, and heart, in the order of high to low expression level, whereas Gpt2 expression is more restricted, mainly in the liver, muscle, brain, and white adipose tissue. It has been reported that hepatic ALT2 protein is approximately four times higher in male rats than in female rats.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. Mouse SerpinB12 is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. It is expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine. SerpinB12 inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.

MLN (Motilin) is a Protein Coding gene. 3 alternatively spliced human isoforms have been reported. This gene encodes a small peptide hormone that is secreted by cells of the small intestine to regulate gastrointestinal contractions and motility. The encoded protein belongs to the motilin family. Proteolytic processing of the secreted protein produces the mature peptide and a byproduct referred to as motilin-associated peptide (MAP). MLN plays an important role in the regulation of Interdigestive Gastrointestinal Motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle. Diseases associated with MLN include Gastroparesis and Duodenogastric Reflux. Among its related pathways are RET signaling and Signaling by GPCR.

Cardiotrophin-1, also known as CT-1 and CTF1, is a member of the IL-6 superfamily. It is a sreted cytokine that is expressed in heart, skeletal muscle, prostate and ovary, and to lower levels in lung, kidney, pancreas, thymus, testis and small intestine. The protein exerts its cellular effects by interacting with the glycoprotein 130 (gp130)/leukemia inhibitory factor receptor beta (LIFR) heterodimer. In addition, CT-1 activates phosphatidylinositol 3-kinase (PI-3 kinase) in cardiac myocytes and enhances transcription factor NF-κB DNA -binding activities.

CD160 antigen is a Lipid-anchor that exists as a disulfide-linked homomultimer. CD160 contains one Ig-like V-type domain. The human CD160 precursor is a cysteine-rich, glycosylphosphatidylinositol-anchored protein of 181 amino acids with a single Ig-like domain. It is weakly homologous to KIR2DL4. CD160 is expressed in the spleen, peripheral blood, and small intestine. Its expression is tightly associated with peripheral blood NK cells and CD8 T lymphocytes with cytolytic effector activity. CD160 is a receptor showing broad specificity for both classical and non-classical MHC class I molecules.

Chymotrypsin-Like Elastase Family Member 3A (CELA3A) is an enzyme that contains one peptidase S1 domain. ELA3A belongs to the peptidase S1 family of the Elastase subfamily. ELA3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. ELA3A may also function in the intestinal transport and metabolism of cholesterol. ELA3A is efficient protease with alanine specificity but only little elastolytic activity. ELA3A preferentially cleaves proteins after alanine residues.

Serpin B12 is a member of the serpin family. Serpins are the largest and most diverse family of serine protease inhibitors. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. Serpin B12 is expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine. Serpins 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. SerpinB12 inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.

Liver-intestine cadherin (CDH17) has been known to function as a tumor stimulator and diagnostic marker for almost two decades.In vivo studies showed CDH17 knockout resulted in apoptotic PC tumor death through activating caspase-3 activity. Taken together, CDH17 functions as an oncogenic molecule critical to PC growth by regulating tumor apoptosis signaling pathways and CDH17 could be targeted to develop an anti-PC therapeutic approach. CDH17 Domain 6-7 Protein, Human, Recombinant (mFc) is expressed in HEK293 mammalian cells with C-mFc tag. The predicted molecular weight is 50.18 kDa and the accession number is Q12864.

APOA5 is probably the gene with the strongest effect on triglyceride (TG) metabolism. APOA5 is almost exclusively expressed in the liver, and its product apoAV has a very low circulating concentration. New physiological roles of apoAV have been recently elucidated, such as control of chylomicron production in the intestine and TG accumulation in adipose tissue.The key role of APOA5 in TG metabolism has been largely shown through genetic studies in association with either severe or moderate hypertriglyceridemia.

This enzyme, isolated from small intestine, specifically inactivates the apo forms of a certain group of intracellular pyridoxal phosphate-requiring enzymes. It has chymotrypsin-like specificity towards small substrates. Mcpt2 Protein, Rat, Recombinant (His & Myc) is expressed in E. coli expression system with N-6xHis and C-Myc tag. The predicted molecular weight is 30.5 kDa and the accession number is P00770.

Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in the blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. The mucosal mast cell (MMC) granule-specific beta-chymase, mouse mast cell protease-1 (mMCP-1), is released systemically into the bloodstream early in nematode infection before parasite-specific IgE responses develop and TGF-beta1 induces the constitutive release of mMCP-1 by homologs of MMC in vitro. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.

Poly(rC)-binding protein 1, also known as Heterogeneous nuclear ribonucleoprotein E1, Alpha-CP1, Nucleic acid-binding protein SUB2.3 and PCBP1, is a family member of heterogeneous nuclear ribonucleoproteins (hnRNPs) that belong to RNA-binding proteins and bear three KH domains. PCBP1 is loosely bound in the nucleus. It may shuttle between the nucleus and the cytoplasm. It is abundantly expressed in skeletal muscle, thymus and peripheral blood leukocytes while a lower expression is observed in prostate, spleen, testis, ovary, small intestine, heart, liver, adrenal and thyroid glands. PCBP1 is widely expressed in many human tissues and involved in the regulation of transcription, transportation process, and function of RNA molecules. PCBP1 plays a pivotal role in post-transcriptional regulation for RNA metabolism and RNA function in gene expression. PCBP1 acts as a negative regulator of CD44 variants splicing in HepG2 cells, and loss of PCBP1 in human hepatic tumor contributes to the formation of a metastatic phenotype.

Myelin P2 protein, also known as PMP2, is a cytosolic protein found primarily in peripheral nerves. It Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. It is similar in amino acid sequence and tertiary structure to fatty acid binding proteins found in the liver, adipocytes, and intestine, its expression is limited to the nervous system. PMP2 is detected only in myelin-producing cells of the central and peripheral nervous systems, the oligodendrocytes and Schwann cells, respectively. PMP2 may play a role in lipid transport protein in Schwann cells. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

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.

Endothelin-converting enzyme 1, also known as ECE-1, is a single-pass type II membrane protein which belongs to thepeptidase M13 family. ECE-1 converts big endothelin-1 to endothelin-1. ECE-1 is a membrane metalloprotease that generates endothelin from its direct precursor big endothelin. Four isoforms of ECE-1 are produced from a single gene through the use of alternate promoters. These isoforms share the same extracellular catalytic domain and contain unique cytosolic tails, which results in their specific subcellular targeting.All isoforms of ECE-1 are expressed in umbilical vein endothelial cells, polynuclear neutrophils, fibroblasts, atrium cardiomyocytes and ventricles. Isoforms A, B and C of ECE-1 are also expressed in placenta, lung, heart, adrenal gland and phaeochromocytoma; isoforms A and C of ECE-1 in liver, testis and small intestine; isoform B, C and D of ECE-1 in endothelial cells and umbilical vein smooth muscle cells; isoforms C and D in saphenous vein cells, and isoform C in kidney. Defects in ECE1 are a cause of Hirschsprung disease, cardiac defects and autonomic dysfunction. It is a form of Hirschsprung disease with skip-lesions defects, craniofacial abnormalities and other dysmorphic features, and autonomic dysfunction.

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.

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.

C1D nuclear receptor corepressor belongs to the C1D family. It is a DNA binding and apoptosis-inducing protein.C1D nuclear receptor corepressorinteracts with TSNAX and DNA-PKcs. It acts as a corepressor for the thyroid hormone receptor. It is thought that C1D nuclear receptor corepressor regulates TRAX/Translin complex formation. It is expressed in kidney, heart, brain, spleen, lung, testis, liver and small intestine. It plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. It potentiates transcriptional repression by NR1D1 and THRB. C1D nuclear receptor corepressorcan activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. It also can induce apoptosis in a p53/TP53 dependent manner.

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.

PNLIP is an enzyme that belongs to the lipase family. Secreted from the pancreas, PNLIP is the primary lipase that hydrolyzes dietary fat molecules in the human digestive system, converting triglyceride substrates found in ingested oils to monoglycerides and free fatty acids. Bile salts secreted from the liver and stored in gallbladder are released into the duodenum where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal.

GATE-16, also known as ATG8, belongs to the MAP1 LC3 family. It is expressed at high levels in the brain, heart, prostate, ovary, spleen and skeletal muscle. GATE-16 is expressed at very low levels in lung, thymus and small intestine. GATE-16 is involved in intra-Golgi traffic. It modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1.