E-64是一种亲和纯化半胱氨酸蛋白酶的有效配体。当耦合到硫基化的亲和基质时，结合不再是不可逆的，但保留特异性 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 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