Background:   Chymotrypsins, such as Chymotrypsin C (also known as pancreatic Chymotrypsin or Chymotrypsin), are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the un-reactive carbonyl group with a powerful nucleophile, the Serine 195 residue located in the active site of the enzyme, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin C is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive, but becomes active as a three polypeptide molecule that is interconnected by disulfide bonds.

Description: Rabbit polyclonal to Chymotrypsin

Immunogen: KLH conjugated synthetic peptide derived from Chymotrypsin

Specificity:  ·Reacts with Human, Mouse and Rat.

.·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 29 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.