| Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. Trypsin is inhibited by organophosphorous compounds such as diisopropylfluorophosphate and porcine-derived inhibitors. Used in protein sequencing and tissue disassociation. Source: Bovine pancreas Form: Supplied as a lyophilized, white powder. Unit Definition: One BAEE unit will produce a delta A253 of 0.001 per min at pH 7.6 at 25C using BAEE as substrate. Reaction volume = 3.2 ml (1cm light path). Activity: ~10,000units/mg protein Chymotrypsin: 4 BTEE units/mg protein Activators: The rate of trypsinogen conversion is enhanced by using lanthanide in place of calcium. Specificity: The protease activity of trypsin is highly specific toward positively charged side chains with lysine and arginine. Calcium ion retards trypsin autolysis and promotes activation of trypsinogen. Inhibitors: Trypsin is inhibited by DFP, TLCK, PMSF, APMSF, AEBSEF, aprotinin, leupeptin, a2-macroglobulin, a1-antitrypsin, p-aminobenzamidine, benzamidine (reversible), soybean trypsin inhibitor, lima bean inhibitor, bovine pancreas trypsin inhibitor, chicken egg white inhibitor, and turkey egg white inhibitor. Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile 1mM HCl pH 3. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. |
