Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. Trypsin is a pancreatic serine endoprotease which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. The enzyme also exhibits esterase and amidase activities. Trypsin has an average molecular mass of 23.29 kDa and a pH optimum near 8.0. This product is prepared from recombinant trypsin, porcine sequence and the lysine residues have been dimethylated to further restrict autolysis. It is naturally devoid of chymotryptic activity. This high quality trypsin is suitable for proteomics use. Specific activity: >= 10,000 BAEE units per mg protein.
Synonyms: Mass Spectrometry Trypsin
Purity: >=10,000 unit/mg
Storage: 2-8C