目录号 | 产品详情 | 靶点 | |
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T1996 | FAK | ||
Defactinib (VS-6063) 是新型的 FAK 抑制剂,能够时间和剂量依赖性的抑制 FAK 在 Tyr397 位点磷酸化。 | |||
T3122 | Apoptosis FAK HIV Protease Autophagy | ||
Fangchinoline (Tetrandrine B) 是从Stephaniatetrandra 中分离出来的,一种具有广泛生物学活性的天然产物。它是新型HIV-1抑制剂,通过损害 gp160 蛋白水解过程来抑制 HIV-1 复制。它靶向Focal adhesion kinase (FAK)并抑制肿瘤细胞中 FAK 介导的的信号传导途径。 | |||
T2609 | Apoptosis FAK c-Fms FGFR Bcr-Abl PDGFR Src c-Kit Hck | ||
Masitinib (AB1010) 是生物口服可利用的选择性 c-Kit 抑制剂 (对于人重组c-Kit,IC50=200 nM),它还抑制PDGFRα/β(IC50s=540/800 nM),Lyn(对 LynB 的IC50=510 nM),Lck,较小程度上抑制FGFR3和FAK。它有抗增殖,促凋亡活性,且毒性低。 | |||
T6177 | FAK PYK2 CDK | ||
PF-562271 besylate (PF-00562271 Besylate) 是一种可逆的,有效的,ATP 竞争性的 FAK(IC50:1.5 nM)和 Pyk2 (IC50:13 nM)激酶抑制剂。 | |||
T2465 | FAK PYK2 CDK | ||
PF-562271 是一种可逆的,有效的,ATP 竞争性的 FAK (IC50:1.5 nM)和 Pyk2 (IC50:13 nM)激酶抑制剂。 | |||
T24730 | FAK p53 | ||
Roslin 2 bromide (Benzylhexamethylenetetramine bromide) 是一种 p53 再激活剂,可破坏 FAK 和 p53 的结合。 Roslin 2 bromide 具有抗癌作用。 | |||
T21768 | FAK PYK2 CDK | ||
PF-562271 hydrochloride (PF-562271 HCl) 是一种可逆的,有效的,ATP 竞争性的 FAK (IC50:1.5 nM)和 Pyk2 (IC50:13 nM)激酶抑制剂。 | |||
T1950 | Apoptosis FAK | ||
PND-1186 (VS-4718) 是一种高特异性的FAK 可逆抑制剂,IC50为 1.5 nM。它选择性促进肿瘤细胞凋亡。 | |||
T1918 | Apoptosis FAK c-Met/HGFR PYK2 IGF-1R | ||
NVP-TAE 226 (TAE226) 是一种具有 ATP 竞争性的双重FAK 和IGF-1R 抑制剂,IC50分别为 5.5 nM、140 nM。它还抑制Pyk2、胰岛素受体,IC50分为 3.5 nM、40 nM。 | |||
T3041 | FAK ALK | ||
ALK inhibitor 2 是嘧啶类 ALK 的有效抑制剂。它是一种睾丸特异性丝氨酸/苏氨酸激酶 2 (TSSK2;IC50=37 nM) 和粘着斑激酶 (FAK;IC50=5 nM) 抑制剂。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPK-00676 | Osteopontin Protein, Human, Recombinant (aa 17-300, His) | Human | HEK293 | ||
Ovarian cancer is one of the most lethal malignant tumors in women. Secreted phosphoprotein 1 (SPP1) plays an important role in some cancer types. The expression of SPP1 was higher in epithelial ovarian cancer tissues than in normal ovarian tissues. Silencing SPP1 decreased the cell proliferation, migration, and invasion. Ectopic expression of SPP1 increased the cell proliferation, migration, and invasion. Silencing SPP1 prevented ovarian cancer growth in mice. Silencing SPP1 inhibited Integrin β1/FAK/AKT pathway.
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TMPH-02922 | SRPX2 Protein, Mouse, Recombinant (His & Myc) | Mouse | Baculovirus | ||
Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF. Promotes synapse formation. Required for ultrasonic vocalizations.
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TMPH-02923 | SRPX2 Protein, Mouse, Recombinant (His & Myc & SUMO) | Mouse | E. coli | ||
Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF. Promotes synapse formation. Required for ultrasonic vocalizations.
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TMPK-00538 | Osteopontin Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Ovarian cancer is one of the most lethal malignant tumors in women. Secreted phosphoprotein 1 (SPP1) plays an important role in some cancer types. The expression of SPP1 was higher in epithelial ovarian cancer tissues than in normal ovarian tissues. Silencing SPP1 decreased the cell proliferation, migration, and invasion. Ectopic expression of SPP1 increased the cell proliferation, migration, and invasion. Silencing SPP1 prevented ovarian cancer growth in mice. Silencing SPP1 inhibited Integrin β1/FAK/AKT pathway.
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TMPY-05300 | Syndecan-4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
SDC4 (Syndecan-4), also known as Syn4, is a transmembrane heparan sulfate proteoglycan that co-operates with integrins during cell-matrix interactions for the assembly of focal adhesions and actin stress fibers and in the phosphorylation of focal adhesion kinase (FAK) on Tyr397. Syndecan-4 plays roles in the formation of focal adhesions and stress fibers. The cytoplasmic domain of syndecan-4 interacts with several signalling and structural proteins, and both extracellular and cytoplasmic domains are necessary for regulated activation of associated transmembrane receptors. Syndecan-4/SDC4 is a heparan sulfate proteoglycan and works as a coreceptor for various growth factors. SDC4 deficiency limits neointimal formation after vascular injury by regulating vascular smooth muscle cells (VSMCs) proliferation and vascular progenitor cells (VPCs) mobilization. Therefore, SDC4 may be a novel therapeutic target for preventing arterial restenosis after angioplasty.
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TMPY-03440 | Sts1 Protein, Human, Recombinant (His) | Human | E. coli | ||
UBASH3B contains a ubiquitin associated domain at the N-terminus, an SH3 domain, and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. UBASH3B was found to inhibit endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor. UBASH3B interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. It promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. UBASH3B exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP7. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.
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TMPY-03576 | Syndecan-4 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
SDC4 (Syndecan-4), also known as Syn4, is a transmembrane heparan sulfate proteoglycan that co-operates with integrins during cell-matrix interactions for the assembly of focal adhesions and actin stress fibers and in the phosphorylation of focal adhesion kinase (FAK) on Tyr397. Syndecan-4 plays roles in the formation of focal adhesions and stress fibers. The cytoplasmic domain of syndecan-4 interacts with several signalling and structural proteins, and both extracellular and cytoplasmic domains are necessary for regulated activation of associated transmembrane receptors. Syndecan-4/SDC4 is a heparan sulfate proteoglycan and works as a coreceptor for various growth factors. SDC4 deficiency limits neointimal formation after vascular injury by regulating vascular smooth muscle cells (VSMCs) proliferation and vascular progenitor cells (VPCs) mobilization. Therefore, SDC4 may be a novel therapeutic target for preventing arterial restenosis after angioplasty.
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TMPY-02392 | Syndecan-4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
SDC4 (Syndecan-4), also known as Syn4, is a transmembrane heparan sulfate proteoglycan that co-operates with integrins during cell-matrix interactions for the assembly of focal adhesions and actin stress fibers and in the phosphorylation of focal adhesion kinase (FAK) on Tyr397. Syndecan-4 plays roles in the formation of focal adhesions and stress fibers. The cytoplasmic domain of syndecan-4 interacts with several signalling and structural proteins, and both extracellular and cytoplasmic domains are necessary for regulated activation of associated transmembrane receptors. Syndecan-4/SDC4 is a heparan sulfate proteoglycan and works as a coreceptor for various growth factors. SDC4 deficiency limits neointimal formation after vascular injury by regulating vascular smooth muscle cells (VSMCs) proliferation and vascular progenitor cells (VPCs) mobilization. Therefore, SDC4 may be a novel therapeutic target for preventing arterial restenosis after angioplasty.
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TMPH-01086 | CSPG4 Protein, Human, Recombinant (His & Myc) | Human | HEK293 | ||
Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades.
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TMPY-04084 | ANGPTL1 Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
Angiopoietin-like protein 1 (ANGPTL1) has been reported to suppress migration and invasion in lung and breast cancer, acting as a novel tumor suppressor candidate. Downregulation of tumor suppressor signaling plays an important role in the pathogenesis of hepatocellular carcinoma (HCC).The downregulation of the angiopoietin-like protein ANGPTL1 is associated with vascular invasion, tumor thrombus, metastasis, and poor prognosis in HCC. Ectopic expression of ANGPTL1 in HCC cells effectively decreased their in vitro and in vivotumorigenicity, cell motility, and angiogenesis. shRNA-mediated depletion of ANGPTL1 exerted opposing effects. ANGPTL1 promoted apoptosis via inhibition of the STAT3/Bcl-2-mediated antiapoptotic pathway and decreased cell migration and invasion via downregulation of transcription factors SNAIL and SLUG. Furthermore, ANGPTL1 inhibited angiogenesis by attenuating ERK and AKT signaling and interacted with integrin α1β1 receptor to suppress the downstream FAK/Src-JAK-STAT3 signaling pathway. Taken together, these results suggest ANGPTL1 as a prognostic biomarker and novel therapeutic agent in HCC. ANGPTL1 expression was down-regulated in CRC tissues and inversely correlated with poor survival. ANGPTL1 repressed migration and invasion of CRC cells, and microRNA-138 was involved in this process. Angiopoietin-like protein 1 (ANGPTL1) has been shown to act as a tumor suppressor by inhibiting angiogenesis, cancer invasion, and metastasis.
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TMPY-04383 | CSK Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.References
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TMPY-04760 | CSK Protein, Mouse, Recombinant | Mouse | Baculovirus-Insect Cells | ||
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.References
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TMPY-04444 | CSK Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus-Insect Cells | ||
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.References
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