Thrombin

Thrombin, a glycosylated sodium-activated type II enzyme, is also called coagulation factor IIa. It contains two anion-binding exosites, ABE-I and ABE-II. Thrombin exists as α, β, and γ isoforms at different stages of its generation. Bovine a-thrombin consists of a light chain (A chain) and a heavy chain (B chain). These two chains are joined by one disulfide bond.

Thrombin has been used in flow cytometry analysis to investigate the basal activation level of circulating platelets in mice. It has also been used to coagulate the plasma and allow the organotypic slice to adhere to the coverslip during culturing.

Thrombin is a serine protease critical in the blood clotting process and activates clotting factors V, VIII, XI, and XII. It mediates the conversion of inactive plasma protein fibrinogen (factor I) into biologically active fibrin. Thrombin acts as a pro-coagulant and promotes platelet aggregation. It can also produce anti-coagulant effects. It is used to treat bleeding from capillaries and small venules. During vascular injury, thrombin is crucial for controlling the macrophages, neutrophils, monocytes, SMC, and dendritic cells.

Appearance (colour): almost white
Appearance (description): powder
Activity (fibrinogen; pH 7.6; 37 °C): ≥ 50 U/mg