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E-64
Chemischer Name: L-trans-Epoxysuccinyl-Leu-4-guanidinobutylamide // Synonyme: L-trans-Epoxysuccinyl-Leu-agmatine, L-trans-3-Carboxyoxiran-2-carbonyl-L-leucylagmatine, N-[N-(L-3-Trans-carboxirane-2-carbonyl)-L-leucyl]-agmatine, protease inhibitor E-64
- Art-Nr.:LS-3890
- CAS Nr.:66701-25-5
- Lagertemperatur:-20°C
- Formel:C15H27N5O5
- Molare Masse:357,41 g/mol
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description
Irreversible, highly selective inhibitor of cysteine proteases. Shows no inhibition against serine proteases with except for trypsin. Interacts with the Sn-subsites of proteases. For in vivo studies, the use of E-64 as a cysteine protease inhibitor is highly recommended because of its specificity, cell and tissue permeability, as well as its low toxicity. Inhibits activation-induced programmed cell death and restores defective immune responses in HIV+ donors.
references
K. Hanada, M. Tamai, M. Yamagishi, S.Ohmura, J. Sawada & I. Tanaka (1978) Isolation and Characterization of E-64, a New Thiol Protease Inhibitor. Agric. Bioi. Chem., 42 (3),
523-528.
A. J. Barrett, A. A. Kembhavi, M. A. Brown, H. Kirschke, C. G. Knight, M. Tamai, K.
Hanada (1982) L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem J.,
201(1), 18998.
K. Matsumoto, K. Mizoue, K. Kitamura, W. C. Tse, C. P. Huber, T. Ishida (1999) Structural basis of inhibition of cysteine proteases by E-64 and its derivatives. Biopolymers,
51(1), 99107.
Isolation and Characterization of E-64, a New Thiol Protease Inhibitor; K. Hanada, M. Tamai, M. Yamagishi, S. Ohmura, J. Sawada and I. Tanaka; Agricultural and Biological Chemistry 2014; 42: 523-528. doi:10.1080/00021369.1978.10863014
Structural basis of inhibition of cysteine proteases by E-64 and its derivatives; K. Matsumoto, K. Mizoue, K. Kitamura, W. C. Tse, C. P. Huber and T. Ishida; Biopolymers 1999; 51: 99-107. doi:10.1002/(SICI)1097-0282(1999)51:1<99::AID-BIP11>3.0.CO;2-R
L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L; A. J. Barrett, A. A. Kembhavi, M. A. Brown, H. Kirschke, C. G. Knight, M. Tamai and K. Hanada; Biochemical Journal 1982; 201: 189-198. doi:10.1042/bj2010189
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