Elastase

Elastase is a serine protease that catalyzes the breakdown of elastin. Produced by the pancreas, elastase can catalyze the cleavage of carboxyl groups present on small hydrophobic amino acids, such as glycine, alanine, and valine. In humans, several types of elastases are active, including neutrophil elastase, chymotrypsin C and chymotrypsin-like elastase. Neutrophil elastase can break down the outer membrane of E. coli and other Gram-negative bacteria, and has been associated with skin conditions and abdominal aortic aneurysms. Elastases have also been shown to disrupt tight junctions and cause tissue damage. Elastase has an optimal activity at a pH of 9 and can be used for protein identification, peptide mapping, and studying post-translational modifications. Visit the supplier page for more enzyme information, including units of activity and validated application.