Native protein purified from Bovine Pancreas. Further chemically modified to promote stability and purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity.
>=4 units per mg protein. One Unit is equivalent to one micromole of TCA soluble products, measured as tyrosine, released from 2% casein per minute, in 0.05 M Tris-HCl, pH 7.6, at 37°C, in a 30 minute reaction.
Tissue dissociation (combined with other enzymes); Cell harvesting by trypsinization; Mitochondria isolation; in vitro studies of proteins; Various hemagglutination procedures; Sample preparation for flow cytometric DNA analysis; Tryptic mapping; Fingerprinting and sequencing work; Environmental monitoring; Subculturing cells; Cleavage fusion proteins; Generating glycopeptides from purified glycoproteins.
Store at -20°C on dry atmosphere.
Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from inactive precursor zymogen, trypsinogen.