THROMBIN FROM HUMAN PLASMA

General description

Thrombin is a Na⁺ activated allosteric serine protease. It belongs to chymotrypsin family. Thrombin is made of two polypeptide chains of 36 (A chain) and 259 (B chain) residues that are covalently attached with a disulfide bond.

Thrombin is a coagulation factor IIa. It is a serine endopeptidase that hydrolyzes peptide and ester bonds specifically at the carboxylic side of Arg. The enzyme converts fibrinogen to fibrin. The product contains EDTA and additional stabilizing agents.

Application

Thrombin has been used in the expression and purification of recombinant RELM (resistin-like moleculefamily members. It has also been used in platelet spreading on fibrinogen and immunostaining.

Thrombin is used in coagulation research, medical research, protein-structure analysis, and biochemical research. It has been used for the stimulation of the platelets.

Biochem/physiol Actions

Thrombin plays an important role in blood coagulation. It serve as a procoagulant factor while transforming fibrinogen into an insoluble fibrin clot. Thrombin can act as anticoagulant by the activation of protein C.

Physical form

Lyophilizate

Preparation Note

Storage conditions (working solution): -15 to -25°C

Inhibitors: DFP, TLCK, PMSF, benzamidine, α₁-antitrypsin, α₂-macroglobulin, antithrombin III heparin, hirudin, and APMSF

Reconstitution

The reconstituted solution contains 20 mM EDTA.
Important note:
Use plastic vials and pipettes because thrombin will be adsorbed to glass surfaces!

Storage and Stability

Store at 2 to 8 °C. (Store dry!)

Other Notes

For life science research only. Not for use in diagnostic procedures.