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 -20°C,Argon charged
Shipped In
Ice chest + Ice pads
Note
Wherever possible, you should prepare and use solutions on the same day. However, if you need to make up stock solutions in advance, we recommend that you store the solution as aliquots in tightly sealed vials at -20°C. Generally, these will be useable for up to one month. Before use, and prior to opening the vial we recommend that you allow your product to equilibrate to room temperature for at least 1 hour. Need more advice on solubility, usage and handling? Please visit our frequently asked questions (FAQ) page for more details.
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
1.Limei Cai, Xiaoming Liu, Zhiqiang Tian, J.P. Michaud, Zhongjian Shen, Zhen Li, Songdou Zhang, Xiaoxia Liu. (2022) Safety of Bacillus thuringiensis Cry1Ah and Vip3Aa toxins for the predatory stink bug Arma custos (Hemiptera: Pentatomidae). SCIENCE OF THE TOTAL ENVIRONMENT, 851 (158120). [PMID:35987246][10.1016/j.scitotenv.2022.158120]
2.Jiandong Shen, Wei Zhang, Qixing Jiang, Pei Gao, Yanshun Xu, Wenshui Xia. (2022) The role of cathepsin L on structural changes of collagen fibers involved in textural deterioration of chilled grass carp (Ctenopharyngodon idella) fillets. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 102 (13):(5858-5866). [PMID:35426126][10.1002/jsfa.11935]
3.Yunhua Zhang, Jinyun Ji, Xiao Zhao, Ruoheng Jin, Jianhong Li, Hu Wan. (2017) Expression, purification and enzymatic properties of a β-N-acetylhexosaminidase from brown planthopper, Nilaparvata lugens. JOURNAL OF ASIA-PACIFIC ENTOMOLOGY, 20 (1340). [PMID:][10.1016/j.aspen.2017.10.005]
References
1.Limei Cai, Xiaoming Liu, Zhiqiang Tian, J.P. Michaud, Zhongjian Shen, Zhen Li, Songdou Zhang, Xiaoxia Liu. (2022) Safety of Bacillus thuringiensis Cry1Ah and Vip3Aa toxins for the predatory stink bug Arma custos (Hemiptera: Pentatomidae). SCIENCE OF THE TOTAL ENVIRONMENT, 851 (158120). [PMID:35987246][10.1016/j.scitotenv.2022.158120]
2.Jiandong Shen, Wei Zhang, Qixing Jiang, Pei Gao, Yanshun Xu, Wenshui Xia. (2022) The role of cathepsin L on structural changes of collagen fibers involved in textural deterioration of chilled grass carp (Ctenopharyngodon idella) fillets. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 102 (13):(5858-5866). [PMID:35426126][10.1002/jsfa.11935]
3.Yunhua Zhang, Jinyun Ji, Xiao Zhao, Ruoheng Jin, Jianhong Li, Hu Wan. (2017) Expression, purification and enzymatic properties of a β-N-acetylhexosaminidase from brown planthopper, Nilaparvata lugens. JOURNAL OF ASIA-PACIFIC ENTOMOLOGY, 20 (1340). [PMID:][10.1016/j.aspen.2017.10.005]
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