Leupeptin, also known as N-acetyl-L-leucyl-L-leucyl-L-argininal, is a naturally occurring protease inhibitor that can inhibit cysteine, serine and threonine peptidases. It is often used during in vitro experiments when a specific enzymatic reaction is being studied. When cells are lysed for these studies, proteases,...

Leupeptin is a reversible inhibitor of cysteine, serine, and threonine proteases that is produced naturally by Streptomyces. It has been reported to inhibit cathepsin B (Ki = 6 nM), calpain (Ki = 10 nM), trypsin (Ki = 35 nM), plasmin (Ki = 3.4 µM), and kallikrein (Ki = 19 µM), and has no effect against chymotrypsin,...

Potent, competitive and reversible cysteine, serine and threonine protease inhibitor. Inhibits calpain, kallikrein, trypsin, plasmin, papain and cathepsin B. Does not inhibit pepsin, elastase, renin, cathepsins A and D, thrombin or alpha-chymotrypsin. Used to protect against hearing loss caused by acoustic...

Protease inhibitor.

Leupeptin is a reversible competitive inhibitor of serine and thiol proteases that, competes with substrate for the active site of the enzyme. It has been reported to, inhibit calpain, cathepsin B and trypsin, for example. Leupeptin is often used for the inhibition of plasmin, trypsin, papain, kallikrein and...