Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. It is a lyophilized powder containing sucrose, sodium chloride and Tris. The predominant form of thrombin in vivo is the zymogen, prothrombin (factor II), which is produced in the liver. The concentration of prothrombin in normal human plasma is 5–10 mg/dL. Prothrombin is a glycoprotein with a glycan content of ~12%.

• Enzyme Commission Number: E.C.3.4.21.5
• Extinction coeficient: E₂₈₀1% = 18.3 (human); E₂₈₀1% = 19.5 (bovine)

12%.

Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.

Thrombin is used throughout the diagnostics industry in a variety of coagulation assays, clotting factor tests and defibrination of blood or plasma for serum controls. It is also used for site specific cleavage of recombinant fusion proteins, and in biochemical and medical research applications. It is manufactured from New Zealand-sourced bovine plasma using prothrombin activated with thromboplastin extracted from bovine lung tissue. It is lyophilized in glass vials under vacuum to optimize product performance. Low specific activity thrombin has 90 - 500 NIH units/mg and greater than 50% total protein. It has been used in a study to assess persistent hypocoagulability in patients with septic shock.