Trypsin is a serine protease that specifically cleaves at the carboxyl side of lysine and arginine residues. The selectivity of this enzyme is critical for reproducible protein digestion and mass spectrometry-based protein identification. Since chymotrypsin co-purifies with trypsin derived from natural sources, Pierce Trypsin Protease has been treated with TPCK to eliminate chymotryptic activity, improving digestion specificity. Native trypsin is also subject to autolysis which can reduce enzyme stability and efficiency. To reduce autolytic degradation, Pierce Trypsin Protease is chemically modified by methylation, yielding a highly active and more stable form of the enzyme.
Trypsin is a serine protease that specifically cleaves at the carboxyl side of lysine and arginine residues. The selectivity of this enzyme is critical for reproducible protein digestion and mass spectrometry-based protein identification. Since chymotrypsin co-purifies with trypsin derived from natural sources, Pierce Trypsin Protease has been treated with TPCK to eliminate chymotryptic activity, improving digestion specificity. Native trypsin is also subject to autolysis which can reduce enzyme stability and efficiency. To reduce autolytic degradation, Pierce Trypsin Protease is chemically modified by methylation, yielding a highly active and more stable form of the enzyme.