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.
{{Chembox | Verifiedfields = changed | Watchedfields = changed | verifiedrevid = 443919723 | ImageFile = Leupeptin.svg | ImageClass = skin-invert-image | ImageFile_Ref = | ImageName = Stereo, skeletal formula of leupeptin | IUPACName = N-Acetyl-leucyl-N-{[5-[(diaminomethylidene)amino]-1-oxopentan-2-yl}-leucinamide |Section1= |Section2= |Section3= }} 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, many of which are contained within lysosomes, are released. These proteases, if freely present in the lysate, would destroy any products from the reaction being studied, and make the experiment uninterpretable. For example, leupeptin could be used in a calpain extraction to keep calpain from being hydrolyzed by specific proteases. The suggested concentration is 1-10 μM (0.5-5 μg/ml).
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).