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 25°C 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 -20°C. Reconstitute with sterile 1mM HCl pH 3. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Important Note:This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Toxicity and Hazards: All products should be handled by qualified personnel only, trained in laboratory procedures.
