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Papain

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Description	Biochem/physiol Actions	Product #
E-64	E-64 is an irreversible, potent, and highly selective cysteine protease inhibitor. E-64 does not react with the functional thiol group of non-protease enzymes, such as L-lactate dehydrogenase or creatine kinase. E-64 will not inhibit serine proteases (except trypsin) like other cysteine protease inhibitors, leupeptin and antipain. The trans-epoxysuccinyl group (active moiety) of E-64 irreversibly binds to an active thiol group in many cysteine proteases, such as papain, actinidase, and cathepsins B, H, and L to form a thioether linkage. E-64 is a very useful cysteine protease inhibitor for use in in vivo studies because it has a specific inhibition, it is permeable in cells and tissues and has low toxicity.	E3132
Gly-Gly-Tyr-Arg ≥97% (HPLC)		G5386
Leupeptin trifluoroacetate salt ≥90% (HPLC), microbial	Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain and cathepsin B. No inhibition found with pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM.	L2023
N_α-Tosyl-L-lysine chloromethyl ketone hydrochloride ≥96% (TLC), powder	Blocks the LPS- or cytokine-induced activation of nuclear factor κB (NFκB), which, in turn, blocks the induction of iNOS and COX-2 transcription. Blocks activation of pp70^s6k by all mitogens. Blocks apoptosis in cell lines by inhibiting the processing of caspases in some cell lines and to some stimuli.	T7254

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