Pierce Trypsin Protease, MS Grade, is a serine protease derived from porcine pancreatic extracts. The enzyme is TPCK-treated to eliminate chymotryptic activity and methylated to improve stability during protein digestion.

Features of Trypsin Protease, MS Grade:

• Exceptional selectivity—cleaves at the carboxyl side of lysine and arginine residues with greater than 95% specificity
• High purity—no detectable chymotrypsin activity
• Enhanced stability—chemically modified for reduced autolytic activity

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

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.

In addition to possessing high specific activity and being resistant to autolytic digestion, Pierce Trypsin Protease can tolerate commonly used partially denaturing conditions, such as 0.1% SDS, 1M urea and 10% acetonitrile. Pierce Trypsin Protease is most active in pH ranges pH 7 to 9 and can be reversibly inactivated at pH < 4. Both the liquid and lyophilized forms of the enzyme are stable for > 1 yearr when stored at -20°C.