|Cell-permeable, irreversible cysteine protease inhibitor|
Sample solution is provided at 25 µL, 10mM.
|E-64d, a synthetic analog of E-64 and ethyl ester of E-64c, is an irreversible, membrane-permeable inhibitor of lysosomal and cytosolic cysteine proteases. E-64d inhibits calpain and the cysteine proteases cathepsins F, K, B, H, and L.|
|Targets||cathepsins F||cathepsins K||cathepsins B||cathepsins H||cathepsins L|
|Cas No.||88321-09-9||SDF||Download SDF|
|Chemical Name||ethyl (2S,3S)-3-[[(2S)-4-methyl-1-(3-methylbutylamino)-1-oxopentan-2-yl]carbamoyl]oxirane-2-carboxylate|
|Solubility||Soluble in DMSO||Storage||Store at -20°C|
|Shipping Condition:||Evaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
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E-64d inhibited hippocampal aberrant mossy fiber sprouting and seizure-induced up-regulation of ApoE and Clusterin in rats. A significant down-regulation of PRG-1, PRG-3, prg-5, cathepsin B amd ApoE and a up-regulation of nSMase and ANX7 were observed in hippocampus of E-64d-pretreated seizure rats.
In order to detect autophage, E-64d, a membrane-permeable cysteine protease inhibitor, was applied in culture medium where root tips from Arabidopsis seedlings were incubated.
E-64d exhibits protective effects against IRI-induced retinal apoptosis, since it inhibited IRI-induced up-regulation of m-calpain expression, the crease of m-calpain/calpastatin ratio and IRI-induced retinal damage in rats.
E-64d is a membrane permeant inhibitor of calpain that enters intact cells and inhibits proteolysis once it’s incubated with platelets before lysis.
CD-64L, CB-64D, CB-182 and CB-184 exhibited sigma 1 and sigma 2 Ki of 10.5 and 154 nM, 3063 and 16.5 nM, 27.3 and35.5 nM and 7436 and 13.4 nM respectively, where CB-64D and CB-184 displayed high sigma 2 receptor affinity and subtype selectivity.
E-64d, a membrane permeant derivative of E-64c, a thiol protease inhibitor1, was tested for ability to inhibit calpain activity in intact platelets.
E-64c or E-64d also inhibited (lanes 3-8), demonstrating their effect on calpain. When the platelets were incubated with these inhibitors for I0 min and were then washed to remove extracellular inhibitor before lysis, neither E-64c nor leupeptin inhibited proteolysis, but E-64d did inhibit. E-64d was able to penetrate the platelet and was thus not removed by washing.E-64c failed to inhibit proteolysis in intact platelets, but E-64d, the permeant inhibitor, did inhibit intracellular proteolysis.E-64c and E-64d were each able to inhibit the protease activity in lysed platelets. This protease activity has been attributed to calpain by its absolute dependence on Ca 2+and by inhibition by known inhibitors of calpain. E-64d is able to enter the intact platelet: i) after washing to remove extracellular inhibitor, there was no protease activity detected after platelet lysis, and ii) activation of platelets preincubated with E-64d, but not E-64c, resulted in inhibition of proteolysis by calpain activated in intact platelets by A23187 plus calcium.
1. M. Tamai, K. Matsumoto, S. Omura, I. Koyama, Y. Ozawa, K. Hanada J. Pharmacobio-Dyn., 9 (1986), pp. 672–677
2. E. B. McGowan, E. Becker, and T. C. Detwiler, INHIBITION OF CALPAIN IN INTACT PLATELETS BY THE THIOL PROTEASE INHIBITOR E-64d. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS , Vol. 158, No. 2, 1989