Chymotrypsin is a digestive enzyme that is synthesized in the pancreas and can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan and phenylalanine, all of which contain aromatic rings. Chymotrypsin uses a powerful nucleophile, namely the serine 195 residue located in its active site, to attack unreactive carbonyl groups on select amino acids. This reaction forms an enzyme-substrate intermediate that is eventually cleaved, returning Chymotrypsin to its original enzymatic state and releasing a cleaved peptide. CTRL (Chymotrypsin-like) is a 264 amino acid protein that contains one peptidase S1 domain and may exhibit Chymotrypsin-like activity. Due to its expression in pancreatic and intestinal tissue, CTRL is thought to function as a digestive enzyme that, like Chymotrypsin, may be involved in protein degradation pathways.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
recommended for detection of CTRL of human origin by WB, IP and ELISA: