Human Trypsin Pan Specific (PRSS1/2/3) Biotinylated Antibody

Trypsin is a general term for any of three 24 kDa gene products that belong to the peptidase S1 family of enzymes.  Trypsin in Greek means “rubbing or friction”, and it was chosen here because the first trypsins were extracted from pancreas via a glycerin-based rubbing maceration.  Trypsin-1 (cationic), -2 (anionic) , and -3 (mesotrypsin) are synthesized as 26 kDa trypsinogens (plus a 35 kDa trypsinogen-3 isoform) that are 247 amino acids (aa) in length.  The first 15 aa constitute a signal sequence, followed by an enterokinase-cleavable eight aa propeptide, and a 224 aa mature molecule.  Asp194 is linked to enzyme activity, and Tyr154 is sulfated.  Over their mature regions, the three trypsins share 84% aa identity.  Mouse trypsin-1 shares 74% aa identity with the human trypsin consensus sequence.  Trypsin-1 and -2 cleave peptide bonds carboxylterminal to a Lys or Arg.  Trypsin-3 has limited activity on trypsin inhibitors, and thus regulates general trypsin activity.  Trypsin-1, -2, and -3 are expressed by multiple tissues, including pancreas (for general digestion), liver, lung and skin.  In blood, trypsinogen-1 and -2 circulate at ng/mL concentrations.  In pancreatic fluid, trypsin-1, -2, and -3 are found in a 58:40:2 ratio.