Human Trypsin ELISA Kit

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Trypsin is a serine protease enzyme with a molecular mass around 24 kDa. Known also as "bovine trypsin" or "pancreatic trypsin" it functions primarily in the digestive system. Trypsin hydrolyzes peptide bonds specifically at the carboxyl side of the amino acids lysine and arginine. The enzyme is produced in the pancreas as an inactive precursor trypsinogen which converts to active trypsin in the small intestine.

Biological function summary

Trypsin breaks down proteins into smaller peptides facilitating digestion. It is not part of a complex but interacts with other pancreatic enzymes like chymotrypsin and elastase. Trypsin also plays a regulatory role in activating other zymogens like procarboxypeptidase and chymotrypsinogen essential in the complete protein digestion process.

Pathways

The catalytic actions of trypsin are integral to the digestive pathway in the gastrointestinal tract. It ensures the efficient breakdown and absorption of nutrients. In the trypsin activation pathway it activates other proteases which are significant for protein catabolism. This enzyme collaborates closely with anti-trypsin inhibitors that regulate its activity preventing autodigestion and maintaining homeostasis.

Associated diseases and disorders

Trypsin relates closely to pancreatitis and cystic fibrosis. Unregulated activation of trypsinogen within the pancreas causes pancreatitis a condition characterized by inflammation and damage to pancreatic cells. Alpha-1 anti-trypsin an important inhibitor of trypsin connects to conditions like emphysema and liver disease due to its dysfunctional regulation indicating a broader implication of trypsin in maintaining cellular health.