Description

E-64 is a cysteine protease inhibitor that was isolated from the mold Aspergillus japonicus TPR-64. E-64 is also known as N-[N-(L-3-trans-carboxyoxiran-2-carbonyl)-L-leucyl]-agmatine. E-64 effectively inhibits various cysteine proteases, in particular:

cathepsin K
cathepsin L
cathepsin S

E-64 also acts against other enzymes, such as:

calpain
cathepsin B
cathepsin H
papain

Specifications

Grade	Ultra Pure
Formula	C15H27N5O5
MW	357.41
CAS	66701-25-5
Appearance	White solid
Usage	An irreversible inhibitor of cryteine proteases like papain, calpain, and cathepsin B,H,L and S
Soluble	DMSO
Working range	1~10µM
Storage	-15~-20℃

Application

E-64 is an effective ligand for affinity purification of cysteine proteases. When coupled to a thiolated affinity matrix, binding is no longer irreversible, but specificity is retained.

Biochem/physiol Actions

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.

Effective irreversible inhibitor of cysteine proteases that does not affect cysteine residues in other enzymes or react with low molecular weight thiols such as calpain and cathepsin B. Effective concentration 1-10 μM.

Documents

COA

MSDS