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Snake venom metalloproteinase-disintegrin-like mocarhagin

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Snake venom zinc metalloproteinase that inhibits platelet aggregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu-298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to GPIBA. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1/SELPLG) at Tyr-51/Asp-52, and completely abolishes the binding of PSGL-1 to P-selectin. Anionic amino acid sequences containing sulfated tyrosines are needed for cleavages. Inhibits the thrombin-induced platelet aggregation, and the thrombin-induced release of ATP and ADP. Has lectin activity (inhibited by heparin).

Below are the list of possible Snake venom metalloproteinase-disintegrin-like mocarhagin products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Snake venom metalloproteinase-disintegrin-like mocarhagin

 Snake venom metalloproteinase-disintegrin-like mocarhagin ELISA Kit
 Snake venom metalloproteinase-disintegrin-like mocarhagin Recombinant
 Snake venom metalloproteinase-disintegrin-like mocarhagin Antibody
Also known as Snake venom metalloproteinase-disintegrin-like mocarhagin (MOC) (Mocarhagin-1) (SVMP) (Zinc metalloproteinase mocarhagin).
Snake venom zinc metalloproteinase that inhibits platelet ag
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gregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu-298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to GPIBA. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1/SELPLG) at Tyr-51/Asp-52, and completely abolishes the binding of PSGL-1 to P-selectin. Anionic amino acid sequences containing sulfated tyrosines are needed for cleavages. Inhibits the thrombin-induced platelet aggregation, and the thrombin-induced release of ATP and ADP. Has lectin activity (inhibited by heparin).
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