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Cat. No.: TRB-100k (for 100KU)

Cat. No.: TRB-1m (for 1MU)

Description

Thrombin is a serine protease that selectively hydrolyzes the Arg-Gly peptide bond in fibrinogen, generating fibrin, releasing fibrinopeptides A and B.

Thrombin primarily exists in the form of prothrombin (Factor II) in the body, which is mainly synthesized in the liver. Prothrombin is activated by Factor X through hydrolysis, resulting in the release of active peptides and the cleavage of thrombin into light and heavy chains, forming catalytically active alpha-thrombin.
Alpha-thrombin consists of a light chain (A chain, approximately 6 kDa) and a heavy chain (B chain, approximately 31 kDa) connected by a disulfide bond.

Thrombin also contains gamma-carboxyglutamic acid residues, which are post-translationally modified glutamyl residues resulting from the carboxylation activity of vitamin K-dependent carboxylase. Thrombin is activated on the phospholipid membrane surface, where it binds the amino-terminal of prothrombin together with Factor Va and Factor Xa.

Thrombin hydrolyzes fibrinogen only at arginine residues. Its cleavage sites are not specific, and the result of cleavage produces two main products: fibrinopeptide A and fibrinopeptide B.

Under certain storage conditions, thrombin can undergo self-catalytic hydrolysis to generate type B thrombin and type y thrombin. Type B and y thrombin do not have hydrolytic activity on fibrinogen but retain activity toward synthetic peptide and protein substrates other than fibrinogen.

Product Information

• Source: Porcine plasma
• CAS No.: 9002-04-4
• Catalog Number: PE043
• Activity: ≥100 IU/mg
• Catalytic pH range: 5-10
• Molecular weight: 39 KDa

Activity Detection
Using the thrombin and fibrinogen standard, a reaction is performed with a fibrinogen solution containing 0.1% clotting substance and different potency thrombin solution at 37°C. The clotting time is observed, and the appropriate clotting time is between 14-60 seconds. A straight line regression is performed to determine the thrombin potency of the sample.

Preparation Instructions

The thrombin product is lyophilized from a solution containing NaCl and glycine at pH 6.8. When used, it is reconstituted with 0.9% NaCl solution to prepare a 10 mg/mL thrombin solution.

Storage

The storage solution can be prepared as a 0.1% (w/v) BSA solution containing thrombin at a concentration of 100 units/mL. The storage solution can retain enzymatic activity for one week at 0-5°C. The solution is most stable at pH 6.5, and the thrombin activity will significantly decrease when pH is above 7. Due to the adsorption of thrombin to glass containers, it is recommended to aliquot the thrombin solution into plastic containers. It can be stored at -20°C for more than three years.

Only for research and not intended for treatment of humans or animals

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