Trypsin is a serine protease found in the digestive system of many vertebrates where it hydrolyzes proteins. Through trypsinisation, it cleaves peptides at the carboxyl side of arginine and lysine, unless they are followed by a proline.

Trypsin has an optimal operating pH of about 7.5-8.5 and optimal operating temperature of about 37°C. Unlike chymotrypsin, the activity of trypsin is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone (TPCK).

Trypsin is a serine protease that hydrolyses proteins which can be found in the digestive system. Trypsin cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues with very little or no cleavage at lysyl-proline and arginyl-proline bonds. This special cleaving activity yields peptides that are easily identified by mass spectrometry. Additionally, our Immobilized Trypsin is TPCK treated to deactivate interfering chymotrypsin, which can interfere with sequence analysis.