Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free

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.

Cell permeable: no

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

Primary Target
chymotrypsin

Product does not compete with ATP.

Reversible: yes

Please refer to vial label for lot-specific concentration.

Contains no animal-derived components.

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

One TIU (Trypsin Inhibitory Unit) will decrease the activity of two trypsin units by 50% where one trypsin unit will hydrolyze 1.0 µmole of Nα-benzoyl-L-Arginine-p-Nitroanilide (L-BAPNA) per minute at pH 7.8 at 25°C.

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

Toxicity: Standard Handling (A)