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A two chain enzyme resulting from the cleavage of prothrombin. The primary role of thrombin in the coagulation process is to cleave fibrinogen into fibrin leading to a fibrin clot
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Prepared from factor IX isolated from pooled normal plasma. Proteolytic factor XIa activation and activator removal employing factor XIa immunoabsorbtion, to yield a heavy-chain containing the serine protease catalytic domain, the light-chain membrane binding domain and the activation glycopeptide.
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Specific factor V activator from Russell’s viper venom (RVV-V). RVV-V is a serine proteinase, which converts the single-chain coagulation factor V into a light chain (80 kDa) and a heavy chain (230 kDa) with higher coagulant activity (factor Va). Apart from factor V, no other protein substrate for R..
RVV activated factor X isolated from fresh human plasma, with subsequent removal of activator and activation peptides.The specific activity is lot dependent
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Prepared by the activation of factor XI by factor XIIa. Factor XIIa is removed from the activation mixture by immunoadsorption on a column of immobilized anti-factor XIIa.
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Human glu-plasminogen (88 kDa) is prepared from fresh human citrated plasma by lysine-Sepharose affinity chromatography in the presence of aprotinin to minimize any plasmin contamination. This is followed by gel filtration with Sephacryl 200. Treatment with aprotinin-Sepharose is carried out prior t..