|Calculated MW||37 kDa|
|Other Names||Activated Factor IIa|
|Results||>3000 units/mg protein.|
|Application Notes||A working stock solution can be prepared by adding 1 mL buffered saline, pH 7.4 (ex. 25 mM HEPES, 150 mM NaCl, 0.1% PEG 8000, pH 7.4). Further dilution should be made in buffer containing a suitable stabilizing agent such as 0.1%-1% Prionex, BSA, or PEG.|
|Storage||-20°C; Lyophilized from a buffer composed of 20 mM Bis-Tris, 150 mM NaCl and 0.1% PEG 8000, pH 6.5.|
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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.
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Suzuki Y.,et al.Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
Degen S.J.F.,et al.Biochemistry 22:2087-2097(1983).
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