Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.
Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to assess an expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization.
Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.
Activity is expressed in NIH units, and is measured by direct comparison to an NIH thrombin reference standard.
When reconstituted with 1 mL water, vial contains stated activity in 0.15 M sodium chloride and 0.05 M sodium citrate, pH 6.5.
The NIH assay procedure uses 0.2 mL of diluted plasma (1:1 with saline) as a substrate and 0.1 mL of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of Biggs. Only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations.
Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard, Lot K.