Introduction 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. 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.Source Bovine Blood.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized freeze dry powder formulated with Tris buffer and sodium chloride.
Solubility It is recommended to reconstitute the lyophilized Thrombin in sterile 18MΩ-cm H2O.
Stability Lyophilized Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IPF1 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Biological Activity 2000 NIH U/mg.
Usage CHI's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.