Antikrein
Basic Pancreatic Trypsin Inhibitor
Kallikrein-Trypsin Inactivator
Pancreatic Trypsin Inhibitor
Trypsin-Kallikrein Inhibitor Clear, colorless to amber liquid. In 0.9% NaCl. Contains no animal-derived components. Recombinant, bovine aprotinin supplied without animal-derived components. Aprotinin is a competitive, reversible inhibitor of proteolytic and esterolytic activity. A relatively heat- and acid-stable serine protease inhibitor. Forms a tight complex, blocking the active site of the enzyme. Effective at concentrations equimolar with protease. Inhibits several proteases, including coagulation factors in the prephase of blood clotting, tissue and leukocytic proteinases, chymotrypsin, trypsin (Kd = 5 x 10-14 M), plasmin (Kd = 2.3 x 10-10 M), and kallikrein (Kd = 1 x 10-7 M). Proteases not inhibited by aprotinin include Factor Xa, thrombin, pepsin, papain, and carboxypeptidases A and B. Useful for protein purification and for extending the life of cells in culture by preventing proteolytic damage. Specific activity: >5 TIU/mg protein. One TIU (Trypsin Inhibitory Unit) is defined as the amount of aprotinin or product or inhibitor that will decrease the activity of 2 trypsin units by 50% where one trypsin unit will hydrolyze 1 µmol BAPNA per min at 25°C, pH 7.8. Purity: ≥95% by SDS-PAGE. EC 2329949, RTECS YN5080000, CAS 9087-70-1. Merck Index: 14, 757
Ref.: Deutscher, M.P., 1990. Methods Enzymol. 182, 83. |
