| Description : |
Thrombin is a "trypsin-like" serine protease protein. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the stemming of blood loss. As a result of cleaving, thrombin has two chains: a light chain (A chain, MW ~6 kDA) and a heavy chain (B chain, MW ~31 kDa). These two chains are joined by one disulfide bond. Functions of thrombin are that it converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzes many other coagulation-related reactions. Thrombin also contains g-carboxyglutamyl residues. These modified glutamyl residues are the result of carboxylation by a microsomal enzyme, vitamin Kdependent carboxylase. g-Carboxyglutamyl residues are necessary for the Ca2+-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. |
| Source : |
Procine Blood |
| Species : |
Procine |
| Form : |
Lyophilized Powder from 20 mM PBS, pH 7.4 containing 0.9% NaCl. |
| Purity : |
>95% by SDS-PAGE and HPLC analyses. |
| Optimum pH : |
Stable at neutral pH |
| Notes : |
1. Avoid keeping with heavy metal; 2. Recommended to aliquot the solutions in plastic tubes.Optimal Cleavage Sites1. A-B-Pro-Arg-||-X-Y where A and B are hydrophobic amino acids and X and Y are nonacidic amino acids 2. Gly-Arg-||-Gly |
| Storage : |
Two year when stored at -20 centigrade and stable at room temperature for 3 weeks. Avoid repeated freeze/thaw cycles. |
| Reconstitution : |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile water to a concentration of 10-100 u/ml. Stock solutions should be apportioned into working aliquots and stored at -20°C. |
