目录号 | 产品详情 | 靶点 | |
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T4S2126 | Apoptosis Wnt/beta-catenin COX STAT Autophagy | ||
Ginkgetin 是从银杏叶中分离得到的一种双黄酮,具有抗肿瘤、抗炎、神经保护、抗真菌的作用。它也是 Wnt 信号抑制剂,IC50值为 5.92 μM。 | |||
T23027 | Hedgehog/Smoothened | ||
MRT 10 是一种七跨膜平滑受体 (Smo) 拮抗剂,通过多种 Hedgehog (Hh) 测定,其IC50=0.65 μM。它与Smo 受体结合的位点是 Bodipycyclopamine。它可用于研究癌症。 | |||
T3912 | Others | ||
Saikosaponin B1 是柴胡的生物活性成分,具有抗癌作用。它能够靶向SMO 抑制 Hedgehog 通路,显著抑制髓母细胞瘤模型中的肿瘤生长。 | |||
T28073 | Dopamine Receptor | ||
MLS1547 (MLS000051547) 是一种高效的 G 蛋白偏向多巴胺 D2 受体激动剂,Ki 为 1.2 μM。 MLS1547 在钙动员试验中刺激 D2R G 蛋白介导的信号传导,EC50 为 0.37 μM。 | |||
T0760 | Estrogen Receptor/ERR MRP Endogenous Metabolite ROR | ||
Cholesterol (Cholesteryl alcohol) 属于天然产物,是哺乳动物中的主要固醇,是一种雌激素相关受体 α (ERRα) 的激动剂。Cholesterol 广泛存在于动物的细胞膜,也是合成几种重要荷尔蒙及胆酸的材料。 | |||
T21826 | Histone Methyltransferase | ||
TC-E 5003 (NSC-30176) 是选择性 PRMT1抑制剂,其 IC50值为1.5 µM。它在 TLR4 信号传导中具有抗炎特性。 | |||
T1986 | Protease-activated Receptor | ||
Atopaxar (E5555) 是一种高效、可口服的,选择性的,可逆的凝血酶受体蛋白酶激活受体-1 (PAR-1) 拮抗剂。它是一种抗血小板剂,能干扰血小板信号,可用于动脉粥样硬化血栓性疾病的研究。 | |||
T0948 | Adrenergic Receptor | ||
Adrenalone hydrochloride (Adrenalone HCl) 是一种多巴胺β氧化酶 (dopamine β oxidase) 抑制剂,结构与去甲肾上腺素转运蛋白 (NET) 配体相似,IC50=36.9 μM。它是一种肾上腺素能 (adrenergic) 激动剂,用作局部血管收缩剂和止血剂。 | |||
T6626 | Apoptosis PAK | ||
PF-3758309 (PF-03758309) 是一种可口服的、可逆的 ATP 竞争性 PAK4抑制剂。它是一种 PAK4 抑制剂,可抑制锚定独立生长、诱导凋亡、细胞骨架重塑和抑制增殖。 | |||
T1900 | ALK TGF-beta/Smad | ||
LDN-212854 (BMP Inhibitor III) 是一种新型BMP 抑制剂,抑制 ALK2 的IC50=1.3 nM,比对ALK1,ALK3,ALK4和ALK5的抑制性高2,66,1641和7135倍。 |
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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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-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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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-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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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-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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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-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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TMPY-00835 | IGFBP-3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The Insulin-like Growth Factor (IGF) signaling system plays a central role in cellular growth, differentiation, and proliferation. IGFBP3 is the most abundant IGF binding protein in human serum and is a growth inhibitory, apoptosis-inducing molecule, capable of acting via IGF-dependent and IGF-independent mechanisms. It appears to function both by cell cycle blockade and the induction of apoptosis. IGFBP3 can be transported to the nucleus by an importin beta mediated mechanism, where it has been shown to interact with the retinoid X receptor alpha and possibly other nuclear elements. IGFBP3 antiproliferative signaling appears to require an active transforming growth factor-beta (TGF-beta) signaling pathway, and IGFBP3 stimulates phosphorylation of the TGF-beta signaling intermediates Smad2 and Smad3. IGFBP3 has IGF-independent roles in inhibiting cell proliferation in cancer cell lines. Nuclear transcription factor, retinoid X receptor (RXR)-alpha, and IGFBP3 functionally interact to reduce prostate tumor growth and prostate-specific antigen in vivo. Several clinical studies have proposed that individuals with IGFBP3 levels in the upper range of normal may have a decreased risk for certain common cancers. This includes evidence of a protective effect against breast cancer, prostate cancer, colorectal cancer, and lung cancer. Moreover, IGFBP3 inhibits insulin-stimulated glucose uptake into adipocytes independent of IGF.
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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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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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