Biochem/physiol Actions

Cell permeable: no

Reversible: yes

Primary Targetchymotrypsin

Product does not compete with ATP.

Kd = 5 x 10-14 M, 2.3 x 10-10 M, 1 x 10-7 M against trypsin, plasmin, and kallikrein, respectively

General description

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 (K_d = 5 x 10^-14 M), plasmin (K_d = 2.3 x 10^-10 M), and kallikrein (K_d = 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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

Deutscher, M.P., 1990. Methods Enzymol.182, 83.

Packaging

25 mg in Glass bottle

1, 5 mg in Plastic ampoule

Please refer to vial label for lot-specific concentration.

Physical form

Contains no animal-derived components.

Unit Definition

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.

Warning

Toxicity: Standard Handling (A)