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 (exc
Storage Temp
Protected from light,Store at -80°C
Shipped In
Ice chest + Ice pads
Product Description
protease inhibitor ，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
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
application：
It is used as a broad spectrum cysteine proteinase and calpain activation inhibitor. Additionally, Prevotella intermediate studies report that E-64 blocks the breakdown of methaemoglobin and the oxidation of oxyhaemoglobin by InpA. E-64 has also been used to study excystation in Giardia lamblia. E-64 is an inhibitor of Calpain, cathepsin K and cathepsin S. 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
