| Bioactivity | Trypsinogen, a proenzyme synthesized in the pancreas, is activated to form trypsin by enterokinase upon reaching the small intestine lumen, where it opens a hexapeptide bond at the Lys6 - Ile7 junction, leading to the production of the active enzyme. This single polypeptide chain, composed of 229 amino acids and stabilized by six disulfide bridges, further autocatalytically converts additional trypsinogen into trypsin, which is initially present as β-trypsin before undergoing autolysis at the Lys131 - Ser132 site to form α-trypsin. As a serine protease, trypsin features His46 and Ser183 at its active site and exhibits optimal enzymatic activity at a pH range of 7 to 9. |
| CAS | 9002-08-8 |
| Transport | Room temperature in continental US; may vary elsewhere. |
| Storage | Please store the product under the recommended conditions in the Certificate of Analysis. |