Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive prot

Trypsin can be used to re-suspend cells adherent to the cell culture dish wall during the process of harvesting cells. Trypsin can also be used to dissociate dissected cells (for example, prior to cell fixing and sorting). Trypsin is commonly used in biological research during proteomics experiments to digest proteins into peptides for mass spectrometry analysis, e.g. in-gel digestion. Trypsin is particularly suited for this, since it has a very well defined specificity, asit hydrolyzes only the peptide bonds in which the carbonyl group is contributed either by an Arg or Lys residue. Trypsin can also be used to dissolve bloodclots in its microbial form and treat inflammation in its pancreatic form. During the industrial production of insulin, trypsin is necessary.

Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.