Description
Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes and dissociating at pH >10.0 or <3.0. Effective concentration is equimolar with protease.
Activity
> 3.0 EPU/mg protein
Purity
Single band (≥92%) by SDS-PAGE
Unit Definition
One trypsin inhibitor unit (EPU) will inhibit the activity of one
trypsin unit hydrolyze 1umol of N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) per second at pH 8.0 at 25 °C.
Each EPU of aprotinin is equivalent to 1,800 KIU.
Storage
Recombinant aprotinin should be stored under -20°C or below in sealed container. It is stable within 24 months.
Synonyms
Trypsin Inhibitor; 9087-70-1; aprotinin; Trasylol