| Bioactivity | E-64 (Proteinase inhibitor E 64) is a potent irreversible inhibitor against general cysteine proteases with IC50 of 9 nM for papain. | ||||||||||||
| Target | IC50: 9 nM (Papain) | ||||||||||||
| Invitro | E-64 (Proteinase inhibitor E 64) is a cathepsin B-specific inhibitor, and its binding modes with papain, actinidin, cathepsin L, and cathepsin K have been reviewed at the atomic level. E-64 has been widely used as a potent and irreversible (covalent-type) inhibitor for many cysteine proteases such as papain, ficin, actinidin, cathepsin B and L[1]. The S.cervi adult parasites are incubated in the Kreb's Ringer bicarbonate (KRB) maintenance medium for 8 h at 37°C, 5% CO2 with 5, 10, 20 and 40 μM concentration of E-64. E-64 shows a concentration and time dependent decrease in motility and viability of the parasites (EC50=16 μM)[2]. | ||||||||||||
| In Vivo | A broad spectrum of expression of CD4 and CD19 is found exists in both the islets and pancreatic lymph nodes (PLNs) and that anti-serpin B13 mAb exposure causes a significant shift that favored cells expressing low-to-intermediate amounts of these markers. However, this shift is abolished in animals that receive anti-serpin B13 mAb in the presence of the protease inhibitor E-64 (Proteinase inhibitor E 64), which maintains its blocking activity under the experimental conditions used[3]. Dahl salt-sensitive (SS) rats are fed an 8% high salt NaCl diet and intravenously infused with the irreversible cysteine cathepsin inhibitor E-64 (1 mg/day) or the vehicle (control). Both the control and E-64 infused groups develope significant hypertension and kidney damage, and no difference of the mean arterial pressure and the hypertension-associated albuminuria is observed between the groups[4]. | ||||||||||||
| Name | E-64 | ||||||||||||
| CAS | 66701-25-5 | ||||||||||||
| Formula | C15H27N5O5 | ||||||||||||
| Molar Mass | 357.41 | ||||||||||||
| Appearance | Solid | ||||||||||||
| Transport | Room temperature in continental US; may vary elsewhere. | ||||||||||||
| Storage |
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| Reference | [1]. Matsumoto K, et al. Structural basis of inhibition of cysteine proteases by E-64 and its derivatives. Biopolymers. 1999;51(1):99-107. [2]. Wadhawan M, et al. Inhibition of cathepsin B by E-64 induces oxidative stress and apoptosis in filarial parasite. PLoS One. 2014 Mar 25;9(3):e93161. [3]. Baldzizhar R, et al. Anti-serpin antibody-mediated regulation of proteases in autoimmune diabetes. J Biol Chem. 2013 Jan 18;288(3):1612-9. [4]. Blass G, et al. Chronic cathepsin inhibition by E-64 in Dahl salt-sensitive rats. Physiol Rep. 2016 Sep;4(17). pii: e12950. |