| 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. Activity: ~180 units per mg protein. Protein: As Reported Chymotrypsin: As Reported Virus Testing: Mycoplasma, BVD, Parvovirus, Adenovirus, Rabies, Blue Tongue, Respiratory Synctial, Reovirus Unit Definition: 1 unit hydrolyzes 1umole of p-toluene-sulfonyl-L-arginine methyl ester (TAME) per minute at 25C, pH 8.2, in the presence of 0.01M calcium ion. Quality Control: SDS-PAGE Certificate of Origin: Trypsin is derived from animal products of North American origin, collected in USDA-approved facilities and inspected to be free of disease. Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile buffer or media. 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. Further dilutions can be made in assay buffer. |
