Trypsin, MS approved is designed for in-gel or in-tube digestion of proteins of interest for subsequent mass spectrometric analysis of the resulting, trypsin-digestion typical peptides. The enzyme has a very high specificity, the sequence coverage is significantly over 80 %. Based on excellent and proprietary production procedures, Trypsin, MS approved is of unique stability. It is modified by reductive methylation and purified by chromatography, yielding a highly active molecule that is extremely resistant to autolytic digestion.

Trypsin, MS approved is a highly purified enzyme preparation that is free of activity from other proteases. The absence of chymotryptic activity is verified by purity and function control which is carried out for each lot.

• Each lot is QC-tested by MS
• Modified by reductive methylation
• Premium purity, high specificity, superior stability
• Purified from porcine pancreas

Trypsin, MS approved is a serine endopeptidase which specifically cleaves peptide bonds at the carboxyl side of lysine, arginine and S-aminoethyl cysteine residues. There is little or no cleavage at arginyl-proline or lysyl-proline bonds. Cleavage may also be considerably reduced when acidic residues are present on either side of a potentially susceptible bond.

Trypsin, MS approved is supplied as lyophilisate.