Human α-Thrombin  (Synonyms: EC 3.4.21.5; Human Alpha Thrombin)

Human α-thrombin is a multifunctional serine protease that plays a pivotal role in the coagulation pathway. Human α-thrombin cleaves fibrinogen and converts it into fibrin. Human α-thrombin can stimulate platelet activation and stabilize fibrin polymers^[1].

Product Information
α-thrombin is composed of a light chain (A chain) (Mw~6,000) and a heavy chain (B chain) (Mw~31,000) connected by disulfide bonds. In some cases, α-thrombin will undergo autolysis to generate β-thrombin and γ-thrombin. This product is obtained by homogenizing human prothrombin through activation of factor Xa, factor Va and phospholipids. SDS-PAGE detection ensures the complete activation of prothrombin, and the activity is not less than 2,700 NIH units/mg with reference to the NIH thrombin standard.

Instructions
Thrombin has different cleavage efficiencies for different fusion proteins. It is recommended to conduct a small-scale enzyme cleavage test first. For example, fix 10 μg of fusion protein, set a gradient addition amount of thrombin (such as 0.1 U, 0.2 U, 0.5 U, 1 U, etc.), and perform the test at a temperature gradient (such as 4°C, 25°C, 37°C, etc.). It is recommended to find the optimal conditions before conducting the enzymatic digestion experiment.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9002-04-4

Liquid

Colorless to light yellow

[Human a-Thrombin]

Shipping with dry ice.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Troisi R, et, al. Molecular dynamics simulations of human α-thrombin in different structural contexts: evidence for an aptamer-guided cooperation between the two exosites. J Biomol Struct Dyn. 2021 Apr;39(6):2199-2209.  [Content Brief]