CHYMOTRYPSIN ENDOPROTEINASE MS GRADE, 4 X 25 UG，90056，赛默飞世尔

Thermo Scientific Chymotrypsin Protease, MS Grade, is a purified native endoproteinase validated for maximum activity and selectivity in proteomic applications.

Features of Chymotrypsin Protease, MS Grade:

• Increased sequence coverage—cleaves at the carboxyl side of tyrosine, phenylalanine, tryptophan and leucine
• Better specificity—treated with TLCK to eliminate trypsin activity
• High activity—greater than 45 units/mg protein

This Chymotrypsin is a mass spectrometry (MS)-grade serine protease isolated from bovine pancreatic extracts. This chymotrypsin is TLCK-treated to eliminate tryptic activity. The selectivity of this enzyme is important for reproducible protein digestion and mass spectrometry-based protein identification. Chymotrypsin-digestion typically generates a larger number of shorter peptides compared to trypsin. This mass spectrometry-grade Chymotrypsin is packaged lyophilized (convenient 4 x 25 µg).

Applications
• In-solution digestions
• In-gel digestion of proteins from 1-D or 2-D gels

Product Details
The endoproteinase chymotrypsin specifically cleaves at the carboxyl side of tyrosine, phenylalanine, tryptophan and leucine. Two predominant forms of chymotrypsin, A and B, are found in equal amounts in bovine pancreas. They are similar proteins (80% homology), but have different proteolytic characteristics. Both forms of chymotrypsin are present in Thermo Scientific Chymotrypsin. Since trypsin may co-purify with Chymotrypsin derived from natural sources, Thermo Scientific Chymotrypsin has been treated with TLCK to eliminate potential tryptic activity, improving digestion specificity. Chymotrypsin can tolerate mild denaturing conditions, such as 0.1% SDS, 2M urea, 2M guanidine·HCl, 1% CHAPS, and 30% acetonitrile with optimal activity in the pH range 7.5 to 8.5. This lyophilized enzyme has a mass of 25 kDa and is stable for 1 year when stored at -20°C.