Trypsin (CAS 9002-07-7)

Trypsin is a single chain serine protease polypeptide of 223 amino acid residues. The active site amino acid residues of trypsin include HIs46 and Ser183. This enzyme predominantly cleaves peptide chains at the carboxyl side of Arginine and Lysine, with an exception when either one is followed by a Proline. This property makes trypsin valuable in proteomics and protein sequencing, where it is used to digest proteins into manageable pieces for analysis. The resulting peptides can be analyzed by mass spectrometry or other analytical techniques to determine the protein′s structure, identify post-translational modifications, and elucidate complex protein networks and functions. In cell biology, trypsin is used to dissociate adherent cells from culture dishes during cell culture procedures, as its proteolytic activity helps to separate cells from each other and from the substrate to which they are attached. This is essential for passaging cells, preparing single-cell suspensions for analysis, or harvesting cells for further experiments.