Thrombin Active from human plasma

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 3.4.21.5) that catalyzes many coagulation-related reactions. It is primarily associated with blood clotting.

Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. It also induces inflammation. 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.

Lyophilized from a buffer composed of 20 mM Bis-Tris, 150 mM NaCl and 0.1% PEG 8000, pH 6.5.

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.

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.