|Calculated MW||37 kDa|
|Other Names||Activated Factor IIa|
|Results||90-250 U/mg of lyophilized powder.|
|Application Notes||Reconstitute in sterile water (100 U/ml) with 0.9% NaCl. It forms a clear solution.|
|Storage||-20°C; Sterile filtered and lyophilized with Mannitol and Sodium Chloride.|
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Provided below are standard protocols that you may find useful for product applications.
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 188.8.131.52) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
Irwin D.M.,et al.J. Mol. Biol. 200:31-45(1988).
McGillivray R.T.A.,et al.Biochemistry 23:1626-1634(1984).
Magnusson S.,et al.(In) Hemker H.C., Veltkamp J.J. (eds.);
Irwin D.M.,et al.Biochemistry 24:6854-6861(1985).
Park C.H.,et al.Biochemistry 25:3977-3982(1986).
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