Trypsin, Bovine Pancreas, TPCK-Treated, Sterile, Irradiated

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.\n\nUsed in protein sequencing and tissue disassociation.\n\nActivity:\n~180 units per mg protein. \n\nProtein: \nAs reported\n\nChymotrypsin: \nAs reported\n\nVirus Testing:\nMycoplasmsa, BVD, Parvovirus, Adenovirus, Rabies, Blue Tongue, Respiratory Synctial, Reovirus.\n\nUnit Definition:\n1 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. \n\nQuality Control:\nSDS-PAGE\n\nCertificate of Origin:\nTrypsin is derived from animal products of North American origin, collected in USDA-approved facilities and inspected to be free of disease.\n\nStorage and Stability: Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile buffer or media. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. 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.

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SPECIFICATIONS

Catalog Number

T8675

Size

100mg

Form

Supplied as a lyophilized powder. Trypsin has been treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity. Trypsin is also irradiated and tested for the absence of mycoplasma and extraneous virus. Reconstitute with 10ml of sterile buffer or media (Hanks, Earles, BSS, PBS, etc.).

References

Kostka, V., and Carpenter, F. H., Jour. Bio. Chem, 239:1799 (1964)\nAbita, J., and Lazdunski, M.: On the Structural and Functional Role of Carboxylates in Chymotrypsinogen A: A Comparison with Chymotrypsin, Trypsinogen and Trypsin, Biochem. Biophys.\nRes. Comm., 35, 707 (1969).\n\nAbuchowski, A., and Davis, F.: Preparation and Properties of Polyethylene Glycol-Trypsin Adducts, Biochim. Biophys. Acta, 578, 41 (1979).\n\nAnson, M.: The Estimation of Pepsin, Trypsin, Papain and Cathepsin with Hemoglobin, J. Gen. Physiol., 22, 79 (1938).\n\nAntonini, E., and Ascenzi, P.: The Mechanism of Trypsin Catalysis at Low pH. Proposal for a Structural Model, J. Biol. Chem., 256, 12449 (1981).\n\nArakawa, T., Hung, L., Mcginley, M., Rohde, M., and Narhi, L.: Induced Resistance of Trypsin to Sodium Dodecylsulfate upon Complex Formation with Trypsin Inhibitor, J. Protein Chem., 11,\n171 (1992).\n\nArnon, R., and Neurath, H.: An Immunological Approach to the Study of Evolution of Trypsins, Proc. Natl. Acad. Sci., 64, 1323 (1969).\n\nAscenzi, P., Amiconi, G., Bolognesi, M., Menegatti, E., and Guarneri, M.: Trypsin Activation. Effect of the Ile-Val Dipeptide Concentration on Kazal Inhibitor Binding to Bovine Trypsinogen,\nBiochim. Biophys. Acta, 832, 1985 (1985).\n\nAscenzi, P., Bolognesi, M., Guarneri, M., Menegatti, E., and Amiconi, G.: Benzamidine as a Spectroscopic Probe for the Primary Specificity Subsite of Trypsin-like Proteinases, Mol. Cell.\nBiochem., 64, 139 (1984).\n\nAscenzi, P., Menegatti, E., Bortolotti, F., Guarneri, M., and Antonini, E.: Steady-state and Pre-steady-state Kinetics of the Trypsin-catalyzed Hydrolysis of a-CBZ-L-Lysine-p-nitrophenyl Ester,\nBiochim. Biophys. Acta, 658, 158 (1981).\n\nAsgeirsson, B., Fox, J., and Bjarnason, J.: Purification and Characterization of Trypsin from the Poikilotherm Gladus morhua, Eur. J. Biochem., 180, 85 (1989).\n\nAtassi, P.: Surface-simulation Synthesis of the Substrate-binding Site of an Enzyme. Demonstration with Trypsin, Biochem. J., 226, 477 (1985).\n\nBaines, N., Baird, J., and Elmore, D.: The Kinetics of Hydrolysis of Derivatives of Arginine, Homoarginine and Ornithine by Trypsin, Biochem. J., 90, 470 (1964).\n\nBalls, A.: Concerning Trypsinogen, Proc. Natl. Acad. Sci., 53, 392 (1965).\n\nBar-Eli, A., and Katchalski, E.: Water-Insoluble Trypsin Derivative and its Use as a Trypsin Column, Nature, 188, 856 (1960).\n\nBartholomew, J., Handley, C., and Lowther, D.: The Effects of Trypsin Treatment on Proteoglycan Biosynthesis of Bovine Articular Cartilage, Biochem. J., 227, 429 (1985).\n\nBeardslee, R., and Zahnley, J.: A Simple Preparation of [[beta]]-Trypsin Based on a Colorimetric Study of the Thermal Stabilities of [[alpha]] and [[beta]] Trypsin, Arch. Biochem. Biophys., 158,\n806 (1973).\n\nBerezin, I., Kazanskaya, N., Klyosov, A., and Svedas, V.: The Mechanism of the [[alpha]]-Chymotrypsin and Trypsin-Catalyzed Hydrolysis of Amides. Evidence for the Participation of the Active\nSerine in the Amidase Activity of Trypsin, Eur. J. Biochem., 38, 529 (1973).\n\nBergmann, M., and Fruton, J.: in Advances in Enzymology, 63 (1941).\n\nBerlin, I., and Neujahr, H.: Studies of Controlled Lysis of Washed Cell Suspensions of Lactobacillus fermenti and Preparation of Membrane-like Fragments by a Combined Trypsin-Lysozyme\nTreatment, Acta Chem. Scand., 22, 2972 (1969).\n\nBerliner, L., and Wong, S.: Evidence Against Two \"pH-locked\" Conformations of Phosphorylated Trypsin, J. Biol. Chem., 248, 1118 (1973).\n\nBerliner, L., and Wong, S.: Spin-Labeled Sulfonyl Fluorides as Active Site Probes of Protease Structure. I. Comparison of the Active Site Environments in [[alpha]]-Chymotrypsin and Trypsin, J.\nBiol. Chem., 249, 1668 (1974).\n\nBier, M., and Nord, F.: Arch. Biochem. Biophys., 33, 320 (1951).\n\nBorovsky, D., and Schlein, Y.: Quantitative Determination of Trypsin-like and Chymotrypsin-like Enzymes in Insects, Arch. Insect Biochem. Physiol., 8, 249 (1988).\n\nBricteux -Gr