目录号 | 产品详情 | 靶点 | |
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T36648 | |||
Tucatinib (Irbinitinib) hemiethanolate is a potent, orally active and selective HER2 inhibitor with an IC50 of 8 nM. Tucatinib hemiethanolate has nanomolar activity against purified HER2 enzyme and is approximately 500-fold selective for HER2 versus EGFR in cell-based assays. Tucatinib selectively inhibits the receptor tyrosine kinase HER2 relative to EGFR[1].Tucatinib blocks proliferation and the phosphorylation of HER2 and its downstream effector, Akt in HER2 overexpressing cell lines. In the EGFR overexpressing cell lines, it weakly inhibits phosphorylation and proliferation, demonstrating that Tucatinib may have potential to block HER2 signaling without causing the toxicities of EGFR inhibition[1]. Tucatinib hemiethanolate (ONT-380 hemiethanolate, 200 mg/kg/d) shows a survival benefit when each drug is dosed at the maximum-tolerated dose[1]. Tucatinib and its active metabolite causes a significant reduction in brain pErbB2 (80%)[2].Tucatinib (ARRY-380) hemiethanolate demonstrates significant dose-related tumor growth inhibition (TGI; 50% at 50 mg/kg/d and 96% at 100 mg/kg/d) with numerous partial regressions (>50% reduction from baseline size) at the higher dose level in 9/12 animals. Tucatinib (50 mg/kg/d) in combination with trastuzumab shows a 98% TGI with complete regressions in 9/12 animals and two partial regressions[3]. [1]. Moulder-Thompson S, et al. Phase 1 Study of ONT-380, a HER2 Inhibitor, in Patients with HER2+ Advanced Solid Tumors, with an Expansion Cohort in HER2+ Metastatic Breast Cancer (MBC). Clin Cancer Res. 2017 Jan 4. pii: clincanres.1496.2016.[2]. Abstract: In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 852. doi:1538-7445.AM2012-852.[3]. P. Lee, et al. In Vivo Activity of ARRY-380, a Potent, Small Molecule Inhibitor of ErbB2 in Combination with RP-56976. Cancer Research. | |||
T37452 | |||
Stephacidin B is a fungal metabolite that has been found inA. ochraceus.1Dimeric stephacidin B is rapidly converted to a monomer, avrainvillamide ,in vitro.2Stephacidin B is cytotoxic to a variety of cancer cells, including testosterone-independent PC3 and -sensitive LNCaP prostate cancer cells (IC50s = 0.37 and 0.06 μM, respectively) and estradiol-independent SK-BR-3 and -sensitive MCF-7 breast cancer cells (IC50s = 0.32 and 0.27 μM, respectively).1It induces apoptosis in HepG2 and Huh7 hepatocellular carcinoma cells when used at a concentration of 4 μM.3 1.Qian-Cutrone, J., Huang, S., Shu, Y.-Z., et al.Stephacidin A and B: Two structurally novel, selective inhibitors of the testosterone-dependent prostate LNCaP cellsJ. Am. Chem. Soc.124(49)14556-14557(2002) 2.Wulff, J.E., Herzon, S.B., Siegrist, R., et al.Evidence for the rapid conversion of stephacidin B into the electrophilic monomer avrainvillamide in cell cultureJ. Am. Chem. Soc.129(16)4898-4899(2007) 3.Hu, L., Zhang, T., Liu, D., et al.Notoamide-type alkaloid induced apoptosis and autophagy via a P38/JNK signaling pathway in hepatocellular carcinoma cellsRSC Adv.9(34)19855-19868(2019) | |||
T35897 | |||
ASK120067 is a potent and orally active inhibitor of EGFRT790M (IC50:0.3 nM) with selectivity over EGFRWT (IC50:6.0 nM). ASK120067 is a third-generation EGFR-TKI for the research of non-small cell lung cancer (NSCLC)[1]. In the in vitro kinase assay ASK120067 potently inhibits the EGFR L858R/T790M and EGFR T790M resistant mutants with IC50 values of 0.3 nM and 0.5 nM, respectively, as well as the EGFRexon19del sensitizing mutant (IC50= 0.5 nM). The 50 of ASK120067 against wild-type EGFR (EGFRWT) is 6 nM[1].ASK120067 selectively inhibits the growth of EGFR-mutant cell lines and exhibits potent antiproliferative activity in the mutant EGFR NSCLC cells, with IC50 values of 12 nM, 6 nM and 2 nM against NCI-H1975 (T790M mutation), PC-9, and HCC827 cells (sensitizing mutations), respectively. However, it shows moderate or weak anti-growth activities in A431, LoVo and A549 cells (EGFRWT), with IC50 values ranging from 338 nM to 1541 nM[1].ASK120067 (0.1-100 nM) inhibits the phosphorylation of EGFR at Tyrosine residue 1068 and its downstream signaling proteins AKT and ERK in NCI-H1975 cells (EGFRL858R/T790M) even at low dosage (0.1-1 nM). Additionally, ASK120067 inhibits p-EGFR and p-Akt and p-erk in EGFR WT A431 cell until the concentration reaches 10 to 100 nM[1]. ASK120067 (oral gavage; 5-20 mg/kg; once daily; 21 days) results in significantly regressed tumor growth, with a tumor growth inhibition (TGI) rate of 85.7%, and administration of 10 mg/kg ASK120067 causes dramatic tumor shrinkage with a TGI rate of 99.3%, exhibiting a similar potency with Osimertinib[1]. [1]. Tao Zhang, et al. Discovery of a novel third-generation EGFR inhibitor and identification of a potential combination strategy to overcome resistance. Mol Cancer. 2020 May 13;19(1):90. | |||
T38263 | |||
TBK1/IKKε-IN-4 is a 6-aminopyrazolopyrimidine derivative and a potent, selective TBK1 and IKKε inhibitor with IC50 values of 13 nM and 59 nM, respectively. TBK1/IKKε-IN-4 shows 100- to 1000-fold less activity against other protein kinases including PDK1, PI3K family members and mTOR[1]. TBK1/IKKε-IN-4 (Compound II; 96 hours; A549 andHCC44 cells) treatmentdisplays selective toxicity in TBK1-dependent cancer cell lines (IC50 of ~ 4.2 μM for H441 cells and IC50 of ~0.4 μM for A549 cells)[1].TBK1/IKKε-IN-4 (Compound II; 0-2 μM; 30 minutes; HCC44 cells) treatment inhibits the AKT activity[1].TBK1/IKKε-IN-4 (Compound II) inhibits LPS-induced expression of IFNβ (IC50 =62 nM), and the IFNβ target genes IP10 (IC50 =78 nM) and Mx1 (IC50=20 nM). TBK1/IKKε-IN-4 effectively blocksTLR3-dependent IRF3 nuclear translocation in cells with an IC50 under 100 nM, but does not impair TNFR1-dependent p65 NFκB nuclear translocation with doses as high as 20 μM[1]. [1]. Ou YH, et al. TBK1 directly engages Akt/PKB survival signaling to support oncogenic transformation. Mol Cell. 2011 Feb 18;41(4):458-70. | |||
T35790 | |||
Palmitic acid-13C (C1, C2, C3, and C4 labeled) is intended for use as an internal standard for the quantification of palmitic acid by GC- or LC-MS. Palmitic acid is a common 16-carbon saturated fat that represents 10-20% of human dietary fat intake and comprises approximately 25 and 65% of human total plasma lipids and saturated fatty acids, respectively.1,2Acylation of palmitic acid to proteins facilitates anchoring of membrane-bound proteins to the lipid bilayer and trafficking of intracellular proteins, promotes protein-vesicle interactions, and regulates various G protein-coupled receptor functions.1Red blood cell palmitic acid levels are increased in patients with metabolic syndrome compared to patients without metabolic syndrome and are also increased in the plasma of patients with type 2 diabetes compared to individuals without diabetes.3,4 1.Fatima, S., Hu, X., Gong, R.-H., et al.Palmitic acid is an intracellular signaling molecule involved in disease developmentCell. Mol. Life Sci.76(13)2547-2557(2019) 2.Santos, M.J., López-Jurado, M., Llopis, J., et al.Influence of dietary supplementation with fish oil on plasma fatty acid composition in coronary heart disease patientsAnn. Nutr. Metab.39(1)52-62(1995) 3.Yi, L.-Z., He, J., Liang, Y.-Z., et al.Plasma fatty acid metabolic profiling and biomarkers of type 2 diabetes mellitus based on GC/MS and PLS-LDAFEBS Lett.580(30)6837-6845(2006) 4.Kabagambe, E.K., Tsai, M.Y., Hopkins, P.N., et al.Erythrocyte fatty acid composition and the metabolic syndrome: A National Heart, Lung, and Blood Institute GOLDN studyClin. Chem.54(1)154-162(2008) | |||
T36084 | |||
PKI-179 is a potent and orally active dual PI3K/mTOR inhibitor, with IC50s of 8 nM, 24 nM, 74 nM, 77 nM, and 0.42 nM for PI3K-α, PI3K-β, PI3K-γ, PI3K-δ and mTOR, respectively. PKI-179 also exhibits activity over E545K and H1047R, with IC50s of 14 nM and 11 nM, respectively. PKI-179 shows anti-tumor activity in vivo[1][2]. PKI-179 inhibits the cell proliferation, with IC50s of 22 nM and 29 nM for MDA361 and PC3 cells, respectively[1].PKI-179 shows inhibitory activity against a panel of 361 other kinases, hERG and cytochrome P450 (CYP) isoforms at concentrations up to >30 μM, but does have activity for CYP2C8 (IC50=3 μM)[1]. PKI-179 (5-50 mg/kg; p.o. once daily for 40 days) inhibits the tumor growth and is well tolerated in nude mice bearing MDA-361 human breast cancer tumors[1].PKI-179 (50 mg/kg; p.o.) results in good inhibition of PI3K signaling in nude mice bearing MDA361 tumor xenografts[1].PKI-179 exhibits good oral bioavailability (98% in nude mouse, 46% in rat, 38% in monkey, and 61% in dog) and a high half-life (>60 min) [1]. [1]. Venkatesan AM, et, al. PKI-179: an orally efficacious dual phosphatidylinositol-3-kinase (PI3K)/mammalian target of rapamycin (mTOR) inhibitor. Bioorg Med Chem Lett. 2010 Oct 1;20(19):5869-73.[2]. Rehan M. A structural insight into the inhibitory mechanism of an orally active PI3K/mTOR dual inhibitor, PKI-179 using computational approaches. J Mol Graph Model. 2015 Nov;62:226-234. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-01174 | DKK1 Protein, Rhesus, Recombinant (N256Q, His) | Rhesus | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-01121 | DKK3 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
DKK3 (dickkopf related protein 3) is a member of the dickkopf-related family consisting of DKK1, DKK2, DKK3 and DKK4. It is a secreted protein, and also known as REIC (Reduced Expansion in Immortalized Cells). The DKK3 protein is proposed to function as a secreted tumor suppressor since it is downregulated in a number of cancer cells and prostate cancer tissue and may be a promising candidate molecule for therapeutic interference. DKK3 protein is also a negative regulator of beta-catenin and its downregulation contribute to an activation of the beta-catenin signaling pathway.
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TMPY-04811 | DKK1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPH-00221 | Agouti-signaling Protein, Bovine, Recombinant (His) | Bovine | Baculovirus | ||
Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment).
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TMPY-00775 | DKK1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-04753 | IRE1 Protein, Human, Recombinant (aa 465-977) | Human | Baculovirus-Insect Cells | ||
Endoplasmic reticulum stress and hypoxia are necessary components of malignant tumors growth and suppression of ERN1 (from endoplasmic reticulum to nuclei-1) signalling pathway, which is linked to the apoptosis and cell death processes, significantly decreases proliferative processes. An enhanced expression of TP53 gene in ERN1 knockdown glioma cells correlates with the decreased level of ubiquitin ligase MDM2 and increased expression level of USP7 which deubiquitinates TP53 and MDM2 and induces TP53-dependent cell growth repression and apoptosis. Thus, the expression of genes encoding TP53 and related to TP53 factors depends upon the endoplasmic reticulum stress signaling as well as on hypoxia, and correlates with suppression of glioma growth under ERN1 knockdown. The dependence of insulin-like growth binding proteins as well as IGF2BP3 and HTRA1 gene expressions in U87 glioma cells on ERN1 signaling enzyme function and hypoxia, indicating its participation in the regulation of metabolic and proliferative processes via IGF/INS receptors, because endoplasmic reticulum stress is an important component of tumor growth and metabolic diseases.
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TMPY-04413 | IRE1 Protein, Human, Recombinant (aa 465-977, His & GST) | Human | Baculovirus-Insect Cells | ||
Endoplasmic reticulum stress and hypoxia are necessary components of malignant tumors growth and suppression of ERN1 (from endoplasmic reticulum to nuclei-1) signalling pathway, which is linked to the apoptosis and cell death processes, significantly decreases proliferative processes. An enhanced expression of TP53 gene in ERN1 knockdown glioma cells correlates with the decreased level of ubiquitin ligase MDM2 and increased expression level of USP7 which deubiquitinates TP53 and MDM2 and induces TP53-dependent cell growth repression and apoptosis. Thus, the expression of genes encoding TP53 and related to TP53 factors depends upon the endoplasmic reticulum stress signaling as well as on hypoxia, and correlates with suppression of glioma growth under ERN1 knockdown. The dependence of insulin-like growth binding proteins as well as IGF2BP3 and HTRA1 gene expressions in U87 glioma cells on ERN1 signaling enzyme function and hypoxia, indicating its participation in the regulation of metabolic and proliferative processes via IGF/INS receptors, because endoplasmic reticulum stress is an important component of tumor growth and metabolic diseases.
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TMPY-05797 | DKK1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-03179 | CNPY4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CNPY4 belongs to the canopy family. CNPY4 interacts with toll-like receptor 4 (TLR4) and plays a role in the regulation of the cell surface expression of TLR4. Toll-like receptors (TLRs) recognize microbial products and induce immune responses. Lipopolysaccharide is recognized by the receptor complex consisting of TLR4 and MD-2. As CNPY4, PRAT4B also regulates cell surface expression of TLR4. PRAT4B has a signal peptide followed by a mature peptide. It is associated with the hypoglycosylated, immature form of TLR4 but not with MD-2 or TLR2.
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TMPY-04918 | CNPY4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CNPY4 belongs to the canopy family. CNPY4 interacts with toll-like receptor 4 (TLR4) and plays a role in the regulation of the cell surface expression of TLR4. Toll-like receptors (TLRs) recognize microbial products and induce immune responses. Lipopolysaccharide is recognized by the receptor complex consisting of TLR4 and MD-2. As CNPY4, PRAT4B also regulates cell surface expression of TLR4. PRAT4B has a signal peptide followed by a mature peptide. It is associated with the hypoglycosylated, immature form of TLR4 but not with MD-2 or TLR2.
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TMPY-01175 | DKK1 Protein, Rhesus, Recombinant (N256Q, mFc) | Rhesus | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-00627 | SLAM/CD150 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
CD150/signaling lymphocytic activation molecule (SLAM) is a cell surface sialylated phosphoglycoprotein and belongs to the CD2 subset of the Ig superfamily of type I transmembrane glycoproteins. The CD150 receptor is expressed on thymocytes, activated and memory T cells, B cells, platelets, natural killer T cells, and mature dendritic cells, and is also detected on tumor cells of Hodgkin's lymphoma (HL) and diffuse large B-cell lymphoma with an activated B cell phenotype. Additionally, it is the immune cell receptor for measles virus (MV). As a self-ligand, CD150 performs diverse immunologic functions including T/B-cell costimulation, induction of interferon γ (IFN-γ) in Th1 T-cell clones, redirection of Th2 clones to a Th1 or Th0 phenotype, and inhibition of apoptosis in B cells. Furthermore, CD150 was shown to be the second receptor for measles virus in addition to CD46, and the distribution of SLAM on various cell lines is consistent with their susceptibility to clinical isolates of measles virus.
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TMPY-03667 | SLAM/CD150 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
CD150/signaling lymphocytic activation molecule (SLAM) is a cell surface sialylated phosphoglycoprotein and belongs to the CD2 subset of the Ig superfamily of type I transmembrane glycoproteins. The CD150 receptor is expressed on thymocytes, activated and memory T cells, B cells, platelets, natural killer T cells, and mature dendritic cells, and is also detected on tumor cells of Hodgkin's lymphoma (HL) and diffuse large B-cell lymphoma with an activated B cell phenotype. Additionally, it is the immune cell receptor for measles virus (MV). As a self-ligand, CD150 performs diverse immunologic functions including T/B-cell costimulation, induction of interferon γ (IFN-γ) in Th1 T-cell clones, redirection of Th2 clones to a Th1 or Th0 phenotype, and inhibition of apoptosis in B cells. Furthermore, CD150 was shown to be the second receptor for measles virus in addition to CD46, and the distribution of SLAM on various cell lines is consistent with their susceptibility to clinical isolates of measles virus.
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TMPY-06377 | DKK3 Protein, Human, Recombinant | Human | HEK293 | ||
DKK3 (dickkopf related protein 3) is a member of the dickkopf-related family consisting of DKK1, DKK2, DKK3 and DKK4. It is a secreted protein, and also known as REIC (Reduced Expansion in Immortalized Cells). The DKK3 protein is proposed to function as a secreted tumor suppressor since it is downregulated in a number of cancer cells and prostate cancer tissue and may be a promising candidate molecule for therapeutic interference. DKK3 protein is also a negative regulator of beta-catenin and its downregulation contribute to an activation of the beta-catenin signaling pathway.
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TMPY-03261 | CNPY2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CNPY2 is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain. CNPY2 enhances migration of C6 glioma cells through phosphorylation of the myosin regulatory light chain. It is expressed in different tissues, including brain. Overexpression of CNPY2 enhanced the motility of glioma cells measured in matrigel invasion chambers and using a scratch assay. Downregulation of CNPY2 by RNA interference significantly decreased glioma cell migration and phosphorylation of MRLC. Inhibition of the corresponding MRLC kinase by ML-7 did not affect migration of CNPY2-overexpressing cells.
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TMPY-05479 | DKK1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-01016 | SLAM/CD150 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD150/signaling lymphocytic activation molecule (SLAM) is a cell surface sialylated phosphoglycoprotein and belongs to the CD2 subset of the Ig superfamily of type I transmembrane glycoproteins. The CD150 receptor is expressed on thymocytes, activated and memory T cells, B cells, platelets, natural killer T cells, and mature dendritic cells, and is also detected on tumor cells of Hodgkin's lymphoma (HL) and diffuse large B-cell lymphoma with an activated B cell phenotype. Additionally, it is the immune cell receptor for measles virus (MV). As a self-ligand, CD150 performs diverse immunologic functions including T/B-cell costimulation, induction of interferon γ (IFN-γ) in Th1 T-cell clones, redirection of Th2 clones to a Th1 or Th0 phenotype, and inhibition of apoptosis in B cells. Furthermore, CD150 was shown to be the second receptor for measles virus in addition to CD46, and the distribution of SLAM on various cell lines is consistent with their susceptibility to clinical isolates of measles virus.
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TMPY-00138 | CNPY3 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
CNPY3 Protein, Human, Recombinant (hFc) is expressed in HEK293 with hFc tag. The predicted molecular weight is 53.7 kDa. Accession number: Q9BT09-1
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TMPY-00950 | WISP1/CCN4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CCN4/Wnt-induced secreted protein 1 (WISP1) is a secreted, cysteine-rich, heparin-binding glycoprotein, belonging to the CCN (CTGF/CYR61/NOV) family of growth factors, and is involved in diverse biological functions such as cell growth, adhesion, migration, angiogenesis, tissue repair, and regulation of extracellular matrix. Members of the CCN family demonstrate high structural homology sharing four conserved cysteine-rich modular domains: an IGFBP (insulin-like growth factor-binding) domain, a von Willebrand type C domain, a thrombospondin domain and a C-terminal cysteine -knot domain. WISP1 is a putative downstream effector of the Wnt/Frizzled pathway that mediates diverse developmental processes, was identified as an oncogene regulated by the Wnt-1-beta-catenin pathway. Thus WISP1 may contribute to Wnt-1-mediated tumorigenesis and malignance. Expression of WISP1 in some cells results in transformation and tumorigenesis. WISP1 acts to block cell death at a late stage in the p53-mediated apoptosis pathway. It was reported that WISP1 interacts with sulfated glycoconjugates, decorin and biglycan in the ECM of connective tissue, and possibly prevents their inhibitory activity in tumor cell proliferation.
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TMPY-05005 | CNPY3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CNPY3 Protein, Human, Recombinant (His) is expressed in HEK293 with His tag. The predicted molecular weight is 28.5 kDa. Accession number: A0A7U3JW12
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TMPY-02924 | RGS1 Protein, Human, Recombinant (His) | Human | E. coli | ||
RGS1 (regulator of G-protein signaling 1) has been associated with multiple autoimmune disorders including type I diabetes. RGS1 desensitizes the chemokine receptors CCR7 and CXCR4 that are critical to the localization of T and B cells in lymphoid organs. RGS1 expression may be a prognostic marker for risk stratification and a promising target for the development of a new Multiple myeloma (MM) therapy. The markers in the RGS1 gene might be in linkage disequilibrium with a protective allele that reduces the risk of anxiety and depressive disorders.
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TMPJ-00223 | SLAMF1 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Human Cells | ||
SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAM signaling are likely to exist: one in which the inhibitor SH2D1A acts as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates.
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TMPY-00226 | CNPY3 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
CNPY3 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 with hFc tag. The predicted molecular weight is 53.9 kDa. Accession number: Q9DAU1-1
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TMPH-00909 | ASIP Protein, Human, Recombinant (GST & His) | Human | E. coli | ||
ASIP Protein, Human, Recombinant (GST & His) is expressed in E. coli.
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TMPY-00596 | CNPY3 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CNPY3 Protein, Mouse, Recombinant (His) is expressed in HEK293 with His tag. The predicted molecular weight is 28.6 kDa. Accession number: Q9DAU1-1
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TMPJ-00226 | SLAMF1 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Signaling lymphocyte activation molecule (SLAM), is a self-ligand glycoprotein which exists not only found on the surface of activated and memory T cells, but also on the surface of activated B cells, dendritic cells, and macrophages. SLAM consists of a extracellular domain (ECD) with two Ig-like domains,transmembrane segment, and cytoplasmic domain with three immunoreceptor tyrosine switch motifs (ITSM). SLAM is thought to play an important role in adhesion between T cells and APCs and has been shown to act as a coreceptor in TCR-dependent responses. SLAM, together with CD46, is one of the two receptors for measles virus. SLAM is a cell surface receptor that, like the B cell receptor, CD40, and CD95, can transmit positive or negative signals. SLAM can associate with the SH2-containing inositol phosphatase (SHIP), the SH2-containing protein tyrosine phosphatase (SHP-2), and the adaptor protein SH2 domain protein 1A. It’s upregulated on activated B cells and CD4+ and CD8+ T cells, but downregulated on Th2 polarized cells. Also, it can Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4-/CD8- T-cells.
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TMPY-02194 | SOCS3 Protein, Human, Recombinant (His & Trx) | Human | E. coli | ||
Suppressor of cytokine signaling 3, also known as SOCS-3, Cytokine-inducible SH2 protein 3, CIS-3, STAT-induced STAT inhibitor 3, SOCS3 and CIS3, is a protein which is widely expressed with high expression in heart, placenta, skeletal muscle, peripheral blood leukocytes, fetal and adult lung, and fetal liver and kidney. SOCS3 / CIS3 contains one SH2 domain and one SOCS box domain. SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 / CIS3 is involved in negative regulation of cytokines that signal through the JAK / STAT pathway. SOCS3 / CIS3 inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp13, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity. SOCS3 / CIS3 suppresses fetal liver erythropoiesis. It regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. SOCS3 / CIS3 regulates IL-6 signaling. SOCS3 / CIS3 interacts with multiple activated proteins of the tyrosine kinase signaling pathway including IGF1 receptor, insulin receptor and JAK2. SOCS3 / CIS3 could be used as a possible therapeutic agent for treating rheumatoid arthritis.
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TMPJ-01345 | TCblR Protein, Human, Recombinant (His) | Human | Human Cells | ||
CD320 antigen is also known as 8D6 antigen,FDC-signaling molecule 8D6,Transcobalamin receptor and 8D6A. It is a single-pass type I membrane protein and containing two LDL-receptor class A domains. CD320 has been recently discovered and reported as a follicular dendritic cell (FDC) protein. CD320 can augments the proliferation of plasma cells precursors generated by IL-10. CD320 also founctions a receptor for the cellular uptake of transcobalamin bound cobalamin. Defects in CD320 are the cause of methylmalonic aciduria type TCblR (MMATC) which is a metabolic disorder.
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TMPJ-01344 | TCblR Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
CD320 antigen is also known as 8D6 antigen,FDC-signaling molecule 8D6,Transcobalamin receptor and 8D6A. It is a single-pass type I membrane protein and containing two LDL-receptor class A domains. CD320 has been recently discovered and reported as a follicular dendritic cell (FDC) protein. CD320 can augments the proliferation of plasma cells precursors generated by IL-10. CD320 also founctions a receptor for the cellular uptake of transcobalamin bound cobalamin. Defects in CD320 are the cause of methylmalonic aciduria type TCblR (MMATC) which is a metabolic disorder.
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TMPH-01189 | CISH Protein, Human, Recombinant (GST) | Human | E. coli | ||
CISH Protein, Human, Recombinant (GST) is expressed in E. coli.
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TMPY-04058 | RGS5 Protein, Human, Recombinant (His) | Human | E. coli | ||
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.
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TMPJ-00455 | SLAMF5 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
CD84, also called SLAMF5, is a member of the CD2 subgroup of the immunoglobulin receptor superfamily. Members of this CD2 subgroup mediate signal transduction through the interaction of its immunoreceptor tyrosine-based switch motifs (ITSM) in the intracellular region and the SH2 domain of adaptor molecules SAP (SLAM-associated protein) and EAT-2 (EWS-activated transcript 2), and accordingly modulate both adaptive and innate immune responses. CD84 expression has been documented on several hematopoietic cell types, including monocytes, macrophages, dendritic cells, B lymphocytes, and platelets. Activation of cell surface CD84 initiates a signaling cascade involving its intra-cytoplasmic tyrosine residues that results in Bcl-2 upregulation, which in turn enhances cell survival. Either immunoneutralization or blockade of CD84 with a CD84 extracellular domain protein fragment induces cell death in vitro and in vivo.
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TMPJ-00229 | SLAMF5 Protein, Human, Recombinant (His) | Human | Human Cells | ||
SLAM family member 5 (SLAMF5/CD84) is a type I transmembrane protein in the SLAM subgroup of the CD2 family. SLAM family proteins regulate multiple aspects of immune system function. Mature human CD84 consists of a 204 amino acid (aa) extracellular domain (ECD) with two Iglike domains,a 21 aa transmembrane segment, and a 99 aa cytoplasmic domain with two immunoreceptor tyrosinebased switch motifs (ITSMs). CD84 exhibits homophilic binding which is mediated by the N-terminal Ig-like domain. Ligation induces tyrosine phosphorylation in the cytoplasmic ITSMs which then recruit the signaling adaptor molecules SAP (SLAM-associated protein) and EAT-2(EWS/Fli1-activated transcript 2).CD84 signaling inhibits Fc epsilon RI-induced mast cell activation but enhances platelet activation. LPS-induced macrophage activation,T cell proliferation and IFN-γproduction, and the interactions between T cells and B cells that are required for germinal center formation.
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TMPJ-01129 | SMAD1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
SMAD Family Member 1 (SMAD1) is a member of the dwarfin/SMAD family. SMAD1 has the highest expression in the heart and skeletal muscle, containing one MAD homology 1 domain and one MAD homology 2 domain, As a transcriptional modulator SMAD 1 is activated by bone morphogenetic proteins type 1 receptor kinase. Defects in SMAD1 may cause primary pulmonary hypertension (PPH1), characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure and death.
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TMPJ-00228 | SLAMF5 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Human Cells | ||
SLAM family member 5 (SLAMF5/CD84) is a type I transmembrane protein in the SLAM subgroup of the CD2 family. SLAM family proteins regulate multiple aspects of immune system function. Mature human CD84 consists of a 204 amino acid (aa) extracellular domain (ECD) with two Iglike domains,a 21 aa transmembrane segment, and a 99 aa cytoplasmic domain with two immunoreceptor tyrosinebased switch motifs (ITSMs). CD84 exhibits homophilic binding which is mediated by the N-terminal Ig-like domain. Ligation induces tyrosine phosphorylation in the cytoplasmic ITSMs which then recruit the signaling adaptor molecules SAP (SLAM-associated protein) and EAT-2(EWS/Fli1-activated transcript 2).CD84 signaling inhibits Fc epsilon RI-induced mast cell activation but enhances platelet activation. LPS-induced macrophage activation,T cell proliferation and IFN-γproduction, and the interactions between T cells and B cells that are required for germinal center formation.
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TMPJ-01086 | CD244 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Natural killer cell receptor 2B4 (2B4/CD244)is a 66 kDa type I transmembrane glycoprotein in the SLAM subgroup of the CD2 protein family. SLAM family proteins have an extracellular domain (ECD) with two or four Ig-like domains and at least two cytoplasmic immunoreceptor tyrosine-based switch motifs (ITSMs). 2B4 interacts with CD48, while other SLAM family proteins interact in a homophilic manner. The mouse 2B4 cDNA encodes a 397 amino acid (aa) precursor that includes a 19 aa signal sequence, a 207 aa ECD with one Ig-like V-type and one C2-type Ig-like domain, a 21 aa transmembrane segment, and a 150 aa cytoplasmic domain with four ITSMs. Within the ECD, mouse 2B4 shares 46% and 68% aa sequence identity with human and rat 2B4, respectively. 2B4/CD48 signaling cooperates with other receptor systems to either promote or inhibit NK and CD8+ T cell activation. The inhibitory activities are distinct from those of MHC I restricted inhibitory NK cell receptors. Ligation of 2B4 with antibodies or CD48 constructs can directly trigger inhibitory signaling or disrupt an inhibitory interaction, leading to cellular activation. 2B4 can also induce signaling through CD48.
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TMPJ-01154 | SLAMF3 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
CD229(SLAMF3) is a type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family. Mature mouse CD229 consists of a 406 aa extracellular domain (ECD) with two Ig-like V-set and two Ig-like truncated C2-set domains, a 21 aa transmembrane segment, and a 180 aa cytoplasmic domain with two immunoreceptor tyrosinebased switch motifs ITSMs. Within the first two Ig-like domains that are common to all SLAM proteins, mouse CD229 shares 22%-36% aa sequence identity with mouse 2B4, BLAME, CD2F10,CD84, CRACC, NTBA, and SLAM. CD229 is expressed on T, B, and NK cells, thymocytes and monocytes. Homophilic binding between CD229 molecules is mediated by the N-terminal Ig-like domain. Human and mouse CD229 exhibit crossspecies binding. Antigen stimulation of lymphocytes induces CD229 clustering to sites of T cell-B cell contact. Antibody ligation of CD229 can inhibit T cell activation, but CD229 knockout mice show impaired T cell immune responses, suggesting a potential role for CD229 in T cell activation or costimulation.
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TMPJ-00359 | SLAMF3 Protein, Human, Recombinant (His) | Human | Human Cells | ||
SLAMF3 (CD229) is a type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family. Mature human SLAMF3 consists of a 407 amino acid (aa) extracellular domain (ECD) with two Ig-like V-set and two Ig-like truncated C2-set domains. The ECD of human SLAMF3 shares 57% - 59% aa sequence identity with mouse and rat SLAMF3. Within the first two Ig-like domains that are common to all SLAM proteins, human SLAMF3 shares 24% - 39% aa sequence identity with human 2B4, BLAME, CD2F-10, CD84, CRACC, NTB-A, and SLAM. It is expressed on T and B cells, thymocytes, and more weakly on NK cells. It may participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. SLAMF3 may be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. It also disable autoantibody responses and inhibit IFN-gamma secretion by CD4+ T-cells and negatively regulate the size of thymic innate CD8+ T-cells and the development of invariant natural killer T (iNKT) cells.
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TMPY-05081 | Notch 1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
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TMPY-01147 | R-Spondin 1/RSPO1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
RSPO1 gene is a member of the R-spondin family. It encodes RSPO1 which is known as a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. In mice, RSPO1 induces the rapid onset of crypt cell proliferation and increases intestinal epithelial healing, providing a protective effect against chemotherapy-induced adverse effects. This protein is an activator of the beta-catenin signaling cascade, leading to TCF-dependent gene activation. RSPO1 acts both in the canonical Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway, probably by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. It also acts as a ligand for frizzled FZD8 and LRP6.
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TMPY-02115 | R-Spondin 3/RSPO3 Protein, Human, Recombinant (aa 1-146, His) | Human | HEK293 | ||
R-spondin 3 (RSPO3) is a member of the R-Spondin (RSPO) family in vertebrates that activate Wnt/beta-catenin signaling, plays a key role in these processes. The RSPO family of secreted Wnt modulators is involved in development and disease and holds therapeutic promise as stem cell growth factors. The four members have high structural homology. RSPO2 and RSPO3 are more potent than RSPO1, whereas RSPO4 is relatively inactive. All RSPO members require Wnt ligands and LRP6 for activity and amplify signaling of Wnt3A, Wnt1, and Wnt7A, suggesting that RSPO proteins are general regulators of canonical Wnt signaling. RSPO3/PCP signaling during gastrulation requires Wnt5a and is transduced via Fz7, Dvl, and JNK. RSPO3 functions by inducing Sdc4-dependent, clathrin-mediated endocytosis. RSPO3 is a novel, evolutionarily conserved angiogenic factor in embryogenesis. RSPO3 has a key role in the interaction between chorion and allantois in labyrinthine development.
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TMPY-00834 | IGF1R/CD221 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The insulin-like growth factor-1 receptor (IGF1R) is a transmembrane tyrosine kinase involved in several biological processes including cell proliferation, differentiation, DNA repair, and cell survival. This a disulfide-linked heterotetrameric transmembrane protein consisting of two α and two β subunits, and among which, the α subunit is extracellular while the β subunit has an extracellular domain, a transmembrane domain, and a cytoplasmic tyrosine kinase domain. The IGF1R signaling pathway is activated in the mammalian nervous system from the early developmental stages. Its major effect on developing neural cells is to promote their growth and survival. This pathway can integrate its action with signaling pathways of growth and morphogenetic factors that induce cell fate specification and selective expansion of specified neural cell subsets. Modulation of cell migration is another possible role that IGF1R activation may play in neurogenesis. In the mature brain, IGF-I binding sites have been found in different regions of the brain, and multiple reports confirmed a strong neuroprotective action of the IGF-IR against different pro-apoptotic insults. IGF1R is an important signaling molecule in cancer cells and plays an essential role in the establishment and maintenance of the transformed phenotype. Inhibition of IGF1R signaling thus appears to be a promising strategy to interfere with the growth and survival of cancer cells. IGF1R is frequently overexpressed by tumors and mediates proliferation and apoptosis protection. IGF signaling also influences hypoxia signaling, protease secretion, tumor cell motility, and adhesion, and thus can affect the propensity for invasion and metastasis. Therefore, IGF1R is now an attractive anti-cancer treatment target.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02361 | VEGFR2/KDR Protein, Human, Recombinant (His) | Human | HEK293 | ||
VEGFR2 also called KDR or Flk-1, 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. VEGFR2 was shown to be the primary signal transducer for angiogenesis and the development of pathological conditions such as cancer and diabetic retinopathy. It has been shown that VEGFR2 is expressed mainly in the endothelial cells, and the expression is upregulated in the tumor vasculature. Thus the inhibition of VEGFR2 activity and its downstream signaling are important targets for the treatment of diseases involving angiogenesis. VEGFR2 transduces the major signals for angiogenesis via its strong tyrosine kinase activity. However, unlike other representative tyrosine kinase receptors, VEGFR2 does not use the Ras pathway as major downstream signaling but rather uses the phospholipase C-protein kinase C pathway to signal mitogen-activated protein (MAP)-kinase activation and DNA synthesis. VEGFR2 is a direct and major signal transducer for pathological angiogenesis, including cancer and diabetic retinopathy, in cooperation with many other signaling partners; thus, VEGFR2 and its downstream signaling appear to be critical targets for the suppression of these diseases. VEGF and VEGFR2-mediated survival signaling are critical to endothelial cell survival, maintenance of the vasculature and alveolar structure, and regeneration of lung tissue. Reduced VEGF and VEGFR2 expression in emphysematous lungs has been linked to increased endothelial cell death and vascular regression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPJ-01463 | IL-2 Protein, Human, Recombinant (E. coli) | Human | E. coli | ||
Interleukin-2(IL-2) is an interleukin, a type of cytokine signaling molecule in the immune system,belongs to the IL-2 family. It is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes.
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TMPY-03626 | R-Spondin 1/RSPO1 Protein, Human, Recombinant | Human | CHO | ||
RSPO1 gene is a member of the R-spondin family. It encodes RSPO1 which is known as a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. In mice, RSPO1 induces the rapid onset of crypt cell proliferation and increases intestinal epithelial healing, providing a protective effect against chemotherapy-induced adverse effects. This protein is an activator of the beta-catenin signaling cascade, leading to TCF-dependent gene activation. RSPO1 acts both in the canonical Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway, probably by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. It also acts as a ligand for frizzled FZD8 and LRP6.
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TMPY-03197 | R-Spondin 1/RSPO1 Protein, Mouse, Recombinant (His) | Mouse | CHO | ||
RSPO1 gene is a member of the R-spondin family. It encodes RSPO1 which is known as a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. In mice, RSPO1 induces the rapid onset of crypt cell proliferation and increases intestinal epithelial healing, providing a protective effect against chemotherapy-induced adverse effects. This protein is an activator of the beta-catenin signaling cascade, leading to TCF-dependent gene activation. RSPO1 acts both in the canonical Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway, probably by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. It also acts as a ligand for frizzled FZD8 and LRP6.
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TMPY-01321 | DLL4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPK-00474 | IL-22RA1 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
IL-22 receptor, also known as IL-22 R alpha 1 and CRF2-9, is an approximately 65 kDa transmembrane glycoprotein in the type II cytokine receptor family (CRF).Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
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TMPY-04803 | DLL4 Protein, Human, Recombinant | Human | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-01337 | DLL4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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