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.

Leupeptin is a water-soluble and cell-permeable organic compound, produced by some fungal species. It is used as a protease inhibitor. Buy from Sigma-Aldrich.

Leupeptin is a tripeptide composed of N-acetylleucyl, leucyl and argininal residues joined in sequenceby peptide linkages. It is an inhibitor of the calpains, a family of calcium-activated proteases which promote cell death.

Leupeptin is a broad-spectrum, membrane-permeable protease inhibitor. Leupeptin potently inhibits serine, cysteine and threonine proteases. Leupeptin inhibits Mpro (the main protease of SARS-CoV-2) and also has anti-inflammatory activity.

The protease inhibitor leupeptin decreases protein degradation in rat skeletal and cardiac muscle incubated in vitro, while protein synthesis remains unaltered. Leupeptin also lowers protein breakdown in denervated rat muscles and affected muscles from …

Leupeptin is a naturally occurring inhibitor of various proteases, in particular serine proteases. Following its discovery, the inhibitory properties of several other peptidyl argininals have been studied.

2012年1月13日 · Leupeptin is a protease inhibitor that inhibits complete degradation of Ii (Cresswell et al., 1990; Neefjes and Ploegh, 1992). Since Ii degradation is a prerequisite for transport of MHC class II molecules to the cell surface, these inhibitors are negative regulators of class II presentation ( Amigorena et al. , 1995; Brachet et al. , 1997 ...

Leupeptin as well as other protease inhibitors such as Antipain*, Chymostatin*, Pepstatin* and phosphoramidon are useful for protection of proteins during their isolation from tissues or membranes. Not affected are α-, β-, γ- and δ-

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2020年10月5日 · Leupeptin is a bacterial small molecule that is used worldwide as a protease inhibitor. However, its biosynthesis and genetic distribution remain unknown. We identified a family of leupeptins in gammaproteobacterial pathogens, including Photorhabdus, Xenorhabdus, and Klebsiella species, amongst othe …