Anti-Chymotrypsin [Clone CHY10-103.5] - 100 μg

Chymotrypsin is a proteolytic enzyme produced by the pancreas that acts in the duodenum. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine) . These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. The proenzyme chymotrypsinogen is activated by trypsin.