Human Coagulation Factor II/Thrombin Protein, CF

Coagulation factor II/Thrombin is an essential component of the coagulation cascade in which it converts fibrinogen to fibrin, activates coagulation factors V, VII, VIII, XIII and forms complexes with protein C and thrombomodulin.(1) It also activates platelets and regulates the behavior of additional cells through protease-activated receptors (PARs) (2). It may have either protective or deleterious functions, depending on the level and location (3). Its activity is regulated by endogenous inhibitors such as anti-Thrombin III (serpin C1) or heparin cofactor II (serpin D1). A plasma serine protease, Thrombin is synthesized in the liver as a 622 amino acid precursor with a 24 amino acid signal peptide and a 19 residue pro peptide. The mature chain starting at Ala-44 can be further processed by itself or by similar enzymes into several forms including those designated as alpha-, beta‑ and gamma-Thrombin. Composed of a disulfide bond-linked dimer of the light chain (A) (residues 328-363) and the heavy chain (B) (residues 364-622), alpha-Thrombin displays the diverse functions as described above. Compared to alpha-Thrombin, the further processed B chains of beta‑ and gamma‑Thrombin have no known physiological function, but retain most of the activity towards small synthetic substrates (4). Human Thrombin purified from the plasma corresponds to the mature chain, which can be activated by treatment with thermolysin. In comparison, the recombinant human Thrombin (Catalog # http://www.rndsystems.com/product_results.aspx?k=1473-SE">1473-SE) is the active enzyme similar to the alpha- and gamma-Thrombin.