||Batroxobin is a thrombin-like proteolytic enzyme isolated from the venom of Bothrops atrox. It splits the 16 Arg-17 Gly bond in the Aα-chain of fibrinogen and causes the release of fibrinopeptide A and the formation of fibrin I monomer or Des-AA-monomer which spontaneously aggregates into a clot of fibrin I. Batroxobin also induces the release of tPA from endothelium.
||Batroxobin is a serine protease derived from the venom of Bothrops atrox. Its molecular weight is approximately 43,000 g/mol−1. This thrombin-like proteolytic enzyme splits the 16 Arg-17 Gly bond in the A(alpha)-chain of fibrinogen, releasing fibrinopeptide A and leading to the clot formation through aggregation of formed of fibrin I monomer or Des-AA-monomer. In contrast to other anti-coagulants, it does not affect the functions of platelets. Hence, Batroxobin is used to determine fibrinogen in plasma, to measure a ''batroxobin clotting time'' as a heparin-insensitive parallel to the thrombin time, to investigate dysfibrinogenemia, and to test the contractile system of platelets.
||Thrombin-like enzyme batroxobin; EC 184.108.40.206; BX; Bothrops atrox serine proteinase; Venombin-A; Defibrase; Reptilase; Batroxobin.
||Due to its specific action on fibrinogen and its ability to clot platelet-rich plasma without affecting the integrity and functions of the platelets, and thanks to its insensitivity to thrombin inhibitors, batroxobin has found several applications as a tool in blood coagulation research and diagnosis. Batroxobin can be used to determine fibrinogen in plasma, to measure the batroxobin clotting time (Reptilase time) as a heparin-insensitive parallel to the thrombin time, to investigate dysfibrinogenemia, and to test the contractile system of platelets.
||Bothrops atrox snake venom
||May be used by the expiry date given on the label when stored unopened, protected from moisture. Avoid contamination of the reagents by micro-organisms. Shipment of product does not require cooling during the time of transportation. Store at -20°C.