Chymotrypsin protease is a purified native endoproteinase validated for maximum activity and selectivity in proteomic applications.

• Cleaves at the carboxyl side of tyrosine, phenylalanine, tryptophan and leucine therby increasing sequence coverage
• Treated with TLCK to eliminate trypsin activity for better specificity
• High activity of greater than 45 units/mg protein

Applications include in-solution digestions and in-gel digestion of proteins from from 1-D or 2-D gels.

MS-grade endoproteinase isolated from bovine pancreas. Two predominant forms of chymotrypsin protease, A and B, are found in equal amounts in bovine pancreas. They are similar proteins (80% homology) but have different proteolytic characteristics. Chymotrypsin Protease can tolerate mild denaturing conditions, such as 0,1% SDS, 2 M urea, 2 M guanidine·HCl, 1% CHAPS, and 30% acetonitrile, with optimal activity at pH 7,5 to 8,5. This lyophilised enzyme has a mass of 25 kDa and is stable for one year when stored at –20 °C.