目录号 | 产品详情 | 靶点 | |
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T80055 | |||
Beta-glucuronidase是一种关键溶酶体酶,主要功能是参与糖胺聚糖中含有葡萄糖醛酸成分的降解过程。 | |||
T81944 | |||
LEAP-2是源自人血液的一类抗菌肽。 | |||
T8254 | Others | ||
Chrysoobtusin 是一种蒽醌衍生物,分离自决明子。其中决明子具有保肝、通便、明目的作用。 | |||
T16930 | Liver X Receptor | ||
SR9238 是有效的肝 X 受体(LXR)反向激动剂,对LXRα和LXRβ的IC50分别为 214 nM 和 43 nM。 | |||
T5178 | Liver X Receptor | ||
AZ876 是高亲和力的 LXR 激动剂。它在人的 (h)LXRα 和 hLXRβ 比 GW3965 要分别强 25 和 2.5 倍。 | |||
T11991 | P450 Antifungal | ||
Mefentrifluconazole 是一种有效的、选择性的和具有口服活性的真菌 CYP51 (Kd= 0.5 nM) 抑制剂,但对人芳香酶的抑制活性较低,IC50值为0.92 μM。它是一种新型唑类衍生物,用作农用广谱抗真菌剂。 | |||
T1801 | Liver X Receptor | ||
SR9243 是一种 liver-X-receptor 的反向激动剂,可诱导 LXR-辅阻遏物相互作用。 | |||
T15427 | Liver X Receptor | ||
GSK2033 是LXR 的有效拮抗剂,抑制LXRα和LXRβ的pIC50分别为 7 和 7.4。 | |||
T12580 | COX Epoxide Hydrolase | ||
PTUPB 是强效的sEH(IC50:0.9 μM)和COX-2(IC50:1.26 μM)的双向抑制剂。 | |||
T6347 | LPA Receptor LPL Receptor | ||
Ki16198 是一种可口服的 LPA 受体拮抗剂,是 Ki16425 的甲酯衍生物。它抑制 LPA1 和 LPA3 诱导的肌醇磷酸的Ki 值分别为 0.34 和 0.93 μM,可用于胰腺癌发生和转移的研究。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-02919 | Cadherin 17/CDH17 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
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TMPY-05352 | Cadherin 17/CDH17 Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
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TMPY-01912 | Cadherin 17/CDH17 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
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TMPY-00663 | Alkaline Phosphatase/ALPL Protein, Human, Recombinant (His) | Human | HEK293 | ||
Alkaline phosphatase (ALPL) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Alkaline phosphatases (APs) are ubiquitous in many species, from bacteria to human. Four genes encode AP isoenzymes in humans and rodents. Three AP genes are expressed in a tissue-specific manner (i.e., placental, embryonic, and intestinal AP isoenzymes). Expression of the fourth AP gene is nonspecific to a single tissue and is especially abundant in bone, liver, and kidney. This isoenzyme is also called tissue-nonspecific alkaline phosphatase (TNAP). The enzyme tissue non-specific alkaline phosphatase (TNAP) belongs to the ectophosphatase family. TNAP is present in large amounts in bone in which it plays a role in mineralization.
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TMPJ-01062 | HAMP Protein, Human, Recombinant (GST) | Human | E. coli | ||
Hepcidin(HAMP)is a secreted protein that belongs to the hepcidin family.It is expressed in liver, heart and brain. It is involved in the maintenance of iron homeostasis, and it is necessary for the regulation of iron storage in macrophages, and for intestinal iron absorption. The preproprotein is post-translationally cleaved into mature peptides of 20, 22 and 25 amino acids, and these active peptides are rich in cysteines, which form intramolecular bonds that stabilize their beta sheet structures.
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TMPY-06645 | Cadherin 17/CDH17 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
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TMPY-01878 | L-FABP Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty acid-binding protein, liver, also known as Fatty acid-binding protein 1, Liver-type fatty acid-binding protein, FABP1 and FABPL,is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP1 and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. FABP1 / FABPL binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. FABP1 / FABPL may be involved in intracellular lipid transport.
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TMPY-06324 | Cadherin 17/CDH17 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
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TMPY-00446 | Alkaline Phosphatase/ALPL Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Alkaline phosphatase (ALPL) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Alkaline phosphatases (APs) are ubiquitous in many species, from bacteria to human. Four genes encode AP isoenzymes in humans and rodents. Three AP genes are expressed in a tissue-specific manner (i.e., placental, embryonic, and intestinal AP isoenzymes). Expression of the fourth AP gene is nonspecific to a single tissue and is especially abundant in bone, liver, and kidney. This isoenzyme is also called tissue-nonspecific alkaline phosphatase (TNAP). The enzyme tissue non-specific alkaline phosphatase (TNAP) belongs to the ectophosphatase family. TNAP is present in large amounts in bone in which it plays a role in mineralization.
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TMPH-02525 | Arginase-1/ARG1 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion. In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity.
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TMPY-04765 | PKLR Protein, Human, Recombinant (His) | Human | E. coli | ||
Pyruvate kinase (PKLR) is a critical erythrocyte enzyme that is required for glycolysis and production of ATP. Pyruvate kinase deficiency (PKD) is the most frequent red blood cell enzyme abnormality of the glycolytic pathway and the most common cause of hereditary nonspherocytic hemolytic anemia. Over 250 PKLR-gene mutations have been described, including missense/nonsense, splicing and regulatory mutations, small insertions, small and gross deletions, causing PKD and hemolytic anemia of variable severity. PKLR expression was increased in liver metastases as well as in primary colorectal tumors of patients with metastatic disease. PKLR protein variants may affect the frequency, and the intensity of malaria episodes induced by different Plasmodium parasites in humans living in areas of endemic malaria.
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TMPH-02524 | Arginase-1/ARG1 Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion. In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity.
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TMPY-00594 | Alkaline Phosphatase/ALPL Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Alkaline phosphatase (ALPL) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Alkaline phosphatases (APs) are ubiquitous in many species, from bacteria to human. Four genes encode AP isoenzymes in humans and rodents. Three AP genes are expressed in a tissue-specific manner (i.e., placental, embryonic, and intestinal AP isoenzymes). Expression of the fourth AP gene is nonspecific to a single tissue and is especially abundant in bone, liver, and kidney. This isoenzyme is also called tissue-nonspecific alkaline phosphatase (TNAP). The enzyme tissue non-specific alkaline phosphatase (TNAP) belongs to the ectophosphatase family. TNAP is present in large amounts in bone in which it plays a role in mineralization.
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TMPH-02561 | CES1C Protein, Mouse, Recombinant (GST) | Mouse | E. coli | ||
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant.
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TMPJ-01020 | GFER Protein, Human, Recombinant (His) | Human | E. coli | ||
GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase which belongs to the Erv1/ALR family of proteins. GFER is widely expressed in various human tissues. They are two isoforms of this protein. Isoform 1 could regenerate the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. Isoform 2 may act as an autocrine hepatotrophic growth factor promoting liver regeneration. GFER could also induce the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC). S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases play an important role in the synthesis of polyamines.
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TMPJ-01174 | Cystatin B Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Cystatin B, also called stefin B or liver thiol proteinase inhibitor, is a member of family 1 of the cystatin superfamily. Like Cystatin A, it is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as cathepsins B, H and L. Defects in Cystatin-B / CSTB are the cause of progressive myoclonic epilepsy type 1 (EPM1) which is an autosomal recessive disorder characterized by severe, stimulus-sensitive myoclonus and tonic-clonic seizures.
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TMPH-02563 | CES1C Protein, Mouse, Recombinant | Mouse | E. coli | ||
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant.
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TMPJ-00583 | CDH17 Protein, Human, Recombinant (His) | Human | Human Cells | ||
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.
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TMPY-00368 | ALR Protein, Human, Recombinant (His) | Human | HEK293 | ||
Alterations in GFER gene have been associated with progressive mitochondrial myopathy, congenital cataracts, hearing loss, developmental delay, lactic acidosis and respiratory chain deficiency in 3 siblings born to consanguineous Moroccan parents by homozygosity mapping and candidate gene approach. Using homozygosity mapping, we discovered that a mutation in the GFER gene causes an infantile mitochondrial disorder.
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TMPH-02509 | ANGPTL8 Protein, Mouse, Recombinant (E. coli, His) | Mouse | E. coli | ||
Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels. May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state. According to a report, may act by promoting ANGPTL3 cleavage. According to another study, not required for cleavage of ANGPTL3.
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TMPH-02562 | CES1C Protein, Mouse, Recombinant (His & Myc) | Mouse | HEK293 | ||
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant.
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TMPH-02510 | ANGPTL8 Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels. May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state. According to a report, may act by promoting ANGPTL3 cleavage. According to another study, not required for cleavage of ANGPTL3.
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TMPH-01091 | CHD1L Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding.
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TMPJ-00932 | PBLD Protein, Human, Recombinant (His) | Human | E. coli | ||
Phenazine Biosynthesis-Like Domain-Containing protein (PBLD) belongs to the phenazine biosynthesis-like protein (PhzF) family, which is expressed in most tissues. PBLD takes part in the MAPK signaling pathway, and is involved in multiple basic cellular functions. The expression of PBLD can be increased in several disease processes, including insulin resistance, folate deficiency and hypotension.
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TMPJ-00868 | PFKFB1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 is an enzyme that in humans is encoded by the PFKFB1 gene. The enzyme forms a homodimer that catalyzes both the synthesis and degradation of fructose-2,6-biphosphate using independent catalytic domains. It belongs to the phosphoglycerate mutase family. Fructose-2,6-biphosphate is an activator of the glycolysis pathway and an inhibitor of the gluconeogenesis pathway. Consequently, regulating fructose-2,6-biphosphate levels through the activity of this enzyme is thought to regulate glucose homeostasis.
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TMPJ-00414 | VEGFR2/KDR Protein, Human, Recombinant (aa 20-764, His & Avi), Biotinylated | Human | Human Cells | ||
Human Vascular endothelial growth factor receptor 2(KDR, VEGFR-2) is a member of the class III subfamily of receptor tyrosine kinases (RTKs). KDR is involved in a number of fundamental biological processes such as the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. It also plays an essential role in promoting proliferation, survival, migration and differentiation of endothelial cells, reorganization of the actin cytoskeleton. VEGFR2 is identified as the receptor for VEGF and VEGFC and an early marker for endothelial cell progenitors, whose expression is restricted to endothelial cells in vivo.The adaptor protein SHB has been shown to interact with VEGFR2 in receptor tyrosine kinase signaling. In addition, VEGFR2 is able to interact with HIV-1 extracellular Tat protein upon VEGF activation, and seems to enhance angiogenesis in Kaposi's sarcoma lesions. VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis.
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TMPJ-00593 | VEGFR2/KDR Protein, Human, Recombinant (aa 20-764, His) | Human | Human Cells | ||
Human Vascular endothelial growth factor receptor 2(KDR, VEGFR-2) is a member of the class III subfamily of receptor tyrosine kinases (RTKs). KDR is involved in a number of fundamental biological processes such as the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. It also plays an essential role in promoting proliferation, survival, migration and differentiation of endothelial cells, reorganization of the actin cytoskeleton. VEGFR2 is identified as the receptor for VEGF and VEGFC and an early marker for endothelial cell progenitors, whose expression is restricted to endothelial cells in vivo.The adaptor protein SHB has been shown to interact with VEGFR2 in receptor tyrosine kinase signaling. In addition, VEGFR2 is able to interact with HIV-1 extracellular Tat protein upon VEGF activation, and seems to enhance angiogenesis in Kaposi's sarcoma lesions. VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis.
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TMPH-01212 | DNASE1L3 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends. Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells. Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity. Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation.
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TMPH-01214 | DNASE1L3 Protein, Human, Recombinant | Human | E. coli | ||
Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends. Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells. Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity. Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation.
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TMPH-01213 | DNASE1L3 Protein, Human, Recombinant (His) | Human | Baculovirus | ||
Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends. Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells. Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity. Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation.
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TMPJ-01156 | PHLDA2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Pleckstrin Homology-Like Domain Family A Member 2 (PHLDA2) is a peripheral membrane protein that belongs to the PHLDA2 family. PHLDA2 is expressed in the placenta and adult prostate gland. In the placenta, it is present in all cells of the villous cytotrophoblast. PHLDA2 plays a role in regulating placenta growth. PHLDA2 may act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids.
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TMPJ-00933 | PRDX5 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Peroxisomes are essential organelles that participate in multiple important metabolic processes, including the β-oxidation of fatty acids, plasmalogen synthesis, and the metabolism of reactive oxygen species (ROS). Peroxiredoxins is overexpressed in breast cancer tissues to a great extent suggesting that they has a proliferative effect and may be related to cancer development or progression. Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase that belongs to the atypical 2-Cys class of the TSA/ahpC family of peroxiredoxins. PRDX5 is a widely expressed mitochondrial antioxidant enzyme that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. In human cells, this enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus.
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TMPJ-00506 | PSG5 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Pregnancy-specific beta-1-glycoprotein 5, is a secreted protein which belongs to the immunoglobulin superfamily, CEA family. It contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain.
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TMPJ-00053 | PRL-2 Protein, Human, Recombinant (His) | Human | E. coli | ||
PTP4A2, also known as PRL2 or PTPCAAX2, is short for Protein tyrosine phosphatase type IVA 2. This protein exists in cell membrane, cytoplasm,endosome and membrane. PTP4A2 is often farnesylated during post-translational modification. Farnesylation is required for membrane targeting and for interaction with RABGGTB. The unfarnesylated forms are redirected to the nucleus and cytosol. It can stimulate progression from G1 into S phase during mitosis and promotes tumors. It also inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB.
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TMPJ-00018 | CCL16 Protein, Human, Recombinant | Human | E. coli | ||
CCL16 is a member of CC chemokine family. CCL16 cDNA encodes a 120 amino acid peptide along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. CCL16 is distantly related to other CC chemokines, showing less than 30% sequence identity. CCL16 elicits its effects on cells by interacting with cell surface chemokine receptors such as CCR1, CCR2, CCR5 and CCR8. Recombinant CCL16 has been shown to chemoattract human monocytes and THP1 cells but not resting lymphocytes nor neutrophils. CCL16 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16ninduces a calcium flux in THP1 cells that can be desensitized by prior exposure to RANTES, suggesting that CCL16 and RANTES share the same receptor in THP1 cells.
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TMPY-02956 | Apolipoprotein L/APOL1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
APOL1, also known as apolipoprotein L1, is a minor apoprotein component of HDL (High-density lipoprotein) or 'good cholesterol' which is synthesized in the liver and also in many other tissues, including pancreas, kidney, and brain. APOL1 belongs to the apolipoprotein L family. It may play a role in lipid exchange and transport throughout the body. It may also participate in reverse cholesterol transport from peripheral cells to the liver. Defects in APOL1 are the cause of focal segmental glomerulosclerosis type 4 (FSGS4). It is a renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and edema. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.
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TMPY-01567 | RBP4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Retinol-binding protein 4 (RBP4) is the specific carrier for retinol (also known as vitamin A), and is responsible for the conversion of unstable and insoluble retinol in aqueous solution into stable and soluble complex in plasma through their tight interaction. As a member of the lipocalin superfamily, RBP4 containing a β-barrel structure with a well-defined cavity is secreted from the liver, and in turn delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP4-retinol complex interacts with transthyretin (TTR), and this binding is crucial for preventing RBP4 excretion through the kidney glomeruli. RBP4 expressed from an ectopic source efficiently delivers retinol to the eyes, and its deficiency affects night vision largely. Recently, RBP4 as an adipokine, is found to be expressed in adipose tissue and correlated with obesity, insulin resistance (IR) and type 2 diabetes (T2DM).
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TMPY-00915 | Serpin A1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
SerpinA1, also known as Alpha-1 antitrypsin (AAT), is a prototype member of the Serpin superfamily of the serine protease inhibitors. This serine protease inhibitor blocks the protease, neutrophil elastase. Alpha-1 antitrypsin is mainly produced in the liver and acts as an antiprotease. Its principal function is to inactivate neutrophil elastase, preventing tissue damage. SerpinA1 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) and oxidized low-density lipoprotein (oxLDL) and conversely, enhanced by free cholesterol. Furthermore, SerpinA1/monocyte association per se depletes lipid raft cholesterol as characterized by the activation of extracellular signal-regulated kinase 2, formation of cytosolic lipid droplets, and complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). Alpha-1 antitrypsin deficiency is a recently identified genetic disease that occurs almost as frequently as cystic fibrosis. It is caused by various mutations in the SerpinA1 gene, and has numerous clinical implications. Alpha-1 antitrypsin deficiency is an inherited disease affecting the lung and liver. In the liver, alpha-1 antitrypsin deficiency may manifest as benign neonatal hepatitis syndrome; a small percentage of adults develop liver fibrosis, with progression to cirrhosis and hepatocellular carcinoma. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.
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TMPY-03014 | Osteoactivin/GPNMB Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
GPNMB belongs to the PMEL / NMB family, also known as Osteoactivin and Hematopoietic growth factor-inducible neurokinin 1 ( HGFIN ), is a transmembrane glycoprotein that is expressed in numerous cells, including osteoclasts, macrophages, dendritic cells, and tumor cells. It is suggested to influence osteoblast maturation, cell adhesion, and migration. GPNMB protein acts as a downstream mediator of BMP-2 effects on osteoblast differentiation and function. GPNMB participates in bone mineralization and functions as a negative regulator of inflammation in macrophages. Osteoactivin is expressed at high levels in normal and inflammatory liver macrophages suggesting a significant role in acute liver injury. The early-phase upregulation of Osteoactivin expression in the tubular epithelium in response to renal injury might play a role in triggering renal interstitial fibrosis via activation of matrix metalloproteinase expression and collagen remodeling in rats. Osteoactivin is a protein that is expressed in aggressive human breast cancers and is capable of promoting breast cancer metastasis to bone.
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TMPY-00907 | RBP4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Retinol-binding protein 4 (RBP4) is the specific carrier for retinol (also known as vitamin A), and is responsible for the conversion of unstable and insoluble retinol in aqueous solution into stable and soluble complex in plasma through their tight interaction. As a member of the lipocalin superfamily, RBP4 containing a β-barrel structure with a well-defined cavity is secreted from the liver, and in turn delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP4-retinol complex interacts with transthyretin (TTR), and this binding is crucial for preventing RBP4 excretion through the kidney glomeruli. RBP4 expressed from an ectopic source efficiently delivers retinol to the eyes, and its deficiency affects night vision largely. Recently, RBP4 as an adipokine, is found to be expressed in adipose tissue and correlated with obesity, insulin resistance (IR) and type 2 diabetes (T2DM).
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TMPK-00114 | C-Reactive Protein /CRP Protein, Human, Recombinant (His) | Human | HEK293 | ||
C-reactive protein (CRP) is a polypeptide molecule belonging to the family of pentraxins. CRP is synthesized primarily by the liver in response to certain pro-inflammatory cytokines. It plays an important role in innate immunity, opsonization by its properties, complement activation and immunoglobulins receptor binding. CRP is a protein of the acute systemic inflammation and is, therefore, a prime marker of inflammation.The CRP is quantified by immunonephelometry or immunoturbidimetry.
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TMPY-02509 | Alpha-fetoprotein Protein, Human, Recombinant (His) | Human | HEK293 | ||
Alpha-fetoprotein (AFP) is classified as a member of the albuminoid gene superfamily consisting of albumin, AFP, vitamin D (Gc) protein, and alpha-albumin. AFP is a glycoprotein of 591 amino acids and a carbohydrate moiety. AFP is one of the several embryo-specific proteins and is a dominant serum protein as early in human embryonic life as one month, when albumin and transferrin are present in relatively small amounts. It is first synthesized in the human by the yolk sac and liver(1-2 months) and subsequently predominantly in the liver. A small amount of AFP is produced by the GI tract of the human conceptus. It has been proved that AFP may reappear in the serum in elevated amounts in adult life in association with normal restorative processes and with malignant growth. Alpha-fetoprotein (AFP) is a specific marker for hepatocellular carcinoma (HCC), teratoblastomas, and neural tube defect (NTD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00443 | EPO/Erythropoietin Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Erythropoietin is a member of the EPO / TPO family. It is a secreted, glycosylated cytokine composed of four alpha helical bundles. Erythropoietin can be found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. It also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals. Genetic variation in erythropoietin is associated with susceptbility to microvascular complications of diabetes type 2. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. It has a longer circulating half-life in vivo. Erythropoietin is being much misused as a performance-enhancing drug in endurance athletes.
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TMPJ-00235 | TPO Protein, Human, Recombinant (His) | Human | Human Cells | ||
Thrombopoietin (TPO) is a glycoprotein hormone which belongs to the EPO/TPO family. It produced by the liver and kidney which regulates the production of platelets. TPO stimulates the production and differentiation of megakaryocytes, the bone marrow cells that bud off large numbers of platelets. Lineage-specific cytokine affects the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets.
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TMPY-01633 | SOST Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Sclerostin, the protein product of the SOST gene, is a potent inhibitor of bone formation. Sclerostin protein is widely expressed at low levels with highest levels in bone, cartilage, kidney, liver, bone marrow and primary osteeoblasts differentiated for 21 days, and was originally identified as an important regulator of bone remodeling, homeostasis, and links bone resorption and bone apposition. Recent studies have revealed that Sclerostin protein inhibits the bone growth probably by binding to the extracellular domain of the Wnt coreceptors LRP5 and LRP6 and disrupting Wnt-induced Frizzled-LRP complex formation.
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TMPY-00639 | EPO/Erythropoietin Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Erythropoietin is a member of the EPO / TPO family. It is a secreted, glycosylated cytokine composed of four alpha helical bundles. Erythropoietin can be found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. It also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals. Genetic variation in erythropoietin is associated with susceptbility to microvascular complications of diabetes type 2. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. It has a longer circulating half-life in vivo. Erythropoietin is being much misused as a performance-enhancing drug in endurance athletes.
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TMPY-00925 | SOST Protein, Human, Recombinant (His) | Human | HEK293 | ||
Sclerostin, the protein product of the SOST gene, is a potent inhibitor of bone formation. Sclerostin protein is widely expressed at low levels with highest levels in bone, cartilage, kidney, liver, bone marrow and primary osteeoblasts differentiated for 21 days, and was originally identified as an important regulator of bone remodeling, homeostasis, and links bone resorption and bone apposition. Recent studies have revealed that Sclerostin protein inhibits the bone growth probably by binding to the extracellular domain of the Wnt coreceptors LRP5 and LRP6 and disrupting Wnt-induced Frizzled-LRP complex formation.
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TMPY-03274 | CXCL11 Protein, Human, Recombinant | Human | E. coli | ||
I-TAC, also known as CXCL11, is a small cytokine belonging to the CXC chemokine family. It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells. The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
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TMPY-01883 | EPOR Protein, Human, Recombinant (His) | Human | HEK293 | ||
Erythropoietin (EPO) is the major glycoprotein hormone regulator of mammalian erythropoiesis, and is produced by kidney and liver in an oxygen-dependent manner. The biological effects of EPO are mediated by the specific erythropoietin receptor (EPOR/EPO Receptor) on bone marrow erythroblasts, which transmits signals important for both proliferation and differentiation along the erythroid lineage. EPOR protein is a type â… single-transmembrane cytokine receptor, and belongs to the homodimerizing subclass which functions as ligand-induced or ligand-stabilized homodimers. EPOR signaling prevents neuronal death and ischemic injury. Recent studies have shown that EPO and EPOR protein may be involved in carcinogenesis, angiogenesis, and invasion.
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TMPY-01032 | CD299 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
C-type lectin domain family 4, member M, also known as DC-SIGNR and CLEC4M, is a type II integral membrane protein that is 77% amino acid identical to DC-SIGN, an HIV gp120-binding protein. Though the encoded gene located in the same chromosome, DC-SIGN is expressed solely on dendritic cells, while DC-SIGNR is predominantly found in liver sinusoidal endothelial cells and lymph node, as well as placental endothelium. DC-SIGNR exists as a homotetramer, and the tandem repeat domain, also called neck domain, mediates oligomerization. DC-SIGNR is regarded as a pathogen-recognition receptor involved in peripheral immune surveillance in liver, and probably mediates the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. DC-SIGNR appears to selectively recognize and bind many viral surface glycoproteins containing high mannose N-linked oligosaccharides in a calcium-dependent manner, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S, as well as the cellular adhesion protein ICAM3. DC-SIGNR has been thought to play an important role in establishing HIV infection by enhancing trans-infection of CD4(+)T cells in the regional lymph nodes. It may affect susceptibility to HIV infection by a mechanism that is different in females and males. DC-SIGNR can bind to hepatitis C virus (HCV), and its polymorphism might affect HCV loads supporting the concept that DC-SIGNR contributes to HCV replication efficacy.
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