Papain

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E3132 E-64 protease inhibitor 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.
G5386 Gly-Gly-Tyr-Arg ≥97% (HPLC)  
L2023 Leupeptin trifluoroacetate salt ≥90% (HPLC), microbial Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin.1 (Loss of cochlear hair cells is believed to be mediated by calpain.)
T7254 Nα-Tosyl-L-lysine chloromethyl ketone hydrochloride ≥96% (TLC), powder Blocks the LPS- or cytokine-induced activation of nuclear factor κB (NF-κB), which, in turn, blocks the induction of iNOS and COX-2 transcription. Blocks activation of pp70s6k by all mitogens. Blocks apoptosis in cell lines by inhibiting the processing of caspases in some cell lines and to some stimuli.