Protease Activated Receptor (PAR) Activator
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Protease Activated Receptor (PAR) Activator (7)
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Trypsin
0 ImagesTrypsin is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin activates PAR2 and PAR4. Trypsin induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin also promotes cell proliferation and differentiation. Trypsin can be used in the research of wound healing and neurogenic inflammation.
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Human α-Thrombin (Lyophilized)
0 ImagesCat. No.: HY-114164HCAS No.: 9002-04-4Synonyms: EC 3.4.21.5 (Lyophilized); Human Alpha Thrombin (Lyophilized)Human α-Thrombin (EC 3.4.21.5; Human Alpha Thrombin) (Lyophilized) is a terminal serine protease in the coagulation cascade, as well as a potent physiological platelet agonist and fibrin-generating enzyme in vivo. Human α-Thrombin catalyzes the conversion of fibrinogen to fibrin for blood clot formation, and activates platelet aggregation by cleaving the protease-activated receptors PAR1 (major) (Kd = 1 nM) and PAR4 (minor) on the platelet surface to expose tethered ligands. Human α-Thrombin also amplifies coagulation via positive feedback by activating coagulation factors V, VIII, XI (FV/FVIII/FXI), and switches to activate protein C to exert anticoagulant effects after binding to thrombomodulin.
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Trypsin (MS grade)
0 ImagesCat. No.: HY-129047ACAS No.: 9002-07-7Trypsin MS grade is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin MS grade activates PAR2 and PAR4. Trypsin MS grade induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin MS grade also promotes cell proliferation and differentiation. Trypsin MS grade can be used in the research of wound healing and neurogenic inflammation.
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TRAP-7
0 ImagesTRAP-7 is a thrombin receptor (PAR) activating peptide. TRAP-7 stimulates total inositol phosphate (IP) accumulation and phosphorylation of a specific endogenous substrate for activated PKC. TRAP-7 can be used in cardiovascular disease research.
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Cathepsin G
0 ImagesCat. No.: HY-P3012CAS No.: 107200-92-0Cathepsin G is a pH-dependent serine protease. Cathepsin G hydrolyzes diverse synthetic and protein substrates and remodels extracellular matrix. Cathepsin G exerts immunomodulatory effects via recruiting phagocytes, enhancing T cell motility, activating ERK1/2 and p38 MAPK signaling, and mediating PKCζ membrane translocation. Cathepsin G regulates inflammatory responses by cleaving inflammatory mediators. Cathepsin G participates in vascular regulation by converting angiotensin I to angiotensin II. Cathepsin G induces PAR4-dependent platelet activation, facilitates platelet-neutrophil aggregation, and mediates VITT-related NETosis, thrombus formation. Cathepsin G can be used for the research of immune thrombotic thrombocytopenia, cardiovascular disease, and select autoimmune and inflammatory diseases.
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Murine Thrombin
0 ImagesCat. No.: HY-114164GCAS No.: 9002-04-4Murine Thrombin is a murine serine protease that plays a central role in blood coagulation. Murine Thrombin stimulates macrophages to polarize into a unique phenotype characterized by anti-inflammatory and pro-repair properties. Murine Thrombin activates PAR1, induces the production of MCP-1, MMP3 and VEGF in mouse intervertebral discs, and causes degradation of the cartilage matrix and destruction of intervertebral disc structure. Murine Thrombin activity increases significantly in paraoxon-induced status epilepticus.
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Apoptosis inducer 28
0 ImagesCat. No.: HY-169124Apoptosis Inducer 28 (Compound X1) is an apoptosis-inducing agent with anticancer activity in vitro. Apoptosis Inducer 28 can arrest the cell cycle at the G1 phase, promote cell death, and induce apoptosis by disrupting mitochondrial membrane potential. Apoptosis inducer 28 can also decrease the production of reactive oxygen species, downregulate the gene expression of BAX, Bcl-xL, and Bcl-2, while upregulating the gene expression of PAR-4.
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