E0514
E-64c
Calpain Inhibitor
别名:
(2S,3S)-trans-Epoxysuccinyl-L-leucylamido-3-methylbutane
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关于此项目
经验公式（希尔记法）:
C15H26N2O5
化学文摘社编号:
分子量:
314.38
UNSPSC Code:
12352202
PubChem Substance ID:
MDL number:
InChI
1S/C15H26N2O5/c1-8(2)5-6-16-13(18)10(7-9(3)4)17-14(19)11-12(22-11)15(20)21/h8-12H,5-7H2,1-4H3,(H,16,18)(H,17,19)(H,20,21)/t10-,11-,12-/m0/s1
SMILES string
CC(C)CCNC(=O)[C@H](CC(C)C)NC(=O)[C@H]1O[C@@H]1C(O)=O
InChI key
SCMSYZJDIQPSDI-SRVKXCTJSA-N
biological source
synthetic (organic)
assay
≥98% (HPLC)
form
powder
solubility
ethanol: 20 mg/mL, clear, colorless
storage temp.
−20°C
Gene Information
human ... CAPN1(823)
Biochem/physiol Actions
Cysteine protease inhibitor; membrane-impermeable calpain inhibitor.
Cysteine protease inhibitor; membrane-impermeable calpain inhibitor. Significantly reduces calpain-mediated depletion of microtubule-associated protein (MAP2) in an animal model of an ischemic brain.
Other Notes
Synthetic analog of E-64
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
B C Sondergaard et al.
Osteoarthritis and cartilage, 14(8), 738-748 (2006-03-28)
Both matrix metalloprotease (MMP) activity and cathepsin K (CK) activity have been implicated in cartilage turnover. We investigated the relative contribution of MMP activity and CK activity in cartilage degradation using ex vivo and in vivo models. Bovine articular cartilage
T Moldoveanu et al.
Journal of molecular biology, 343(5), 1313-1326 (2004-10-20)
The endogenous calpain inhibitor, calpastatin, modulates some patho-physiological aspects of calpain signaling. Excess calpain can escape this inhibition and as well, many calpain isoforms and autolytically generated protease core fragments are not inhibited by calpastatin. There is a need, therefore
A J Barrett et al.
The Biochemical journal, 201(1), 189-198 (1982-01-01)
1. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) at a concentration of 0.5 mM had no effect on the serine proteinases plasma kallikrein and leucocyte elastase or the metalloproteinases thermolysin and clostridial collagenase. In contrast, 10 muM-E-64 rapidly inactivated the cysteine proteinases cathepsins B, H
Eva Lindskog et al.
Applied microbiology and biotechnology, 71(4), 444-449 (2005-11-12)
Gelatin zymography revealed the presence of proteolytic activity in conditioned medium (CM) from a serum-free, non-infected Spodoptera frugiperda, Sf9 insect cell culture. Two peptidase bands at about 49 and 39 kDa were detected and found to be proform and active
Maria M M Santos et al.
Mini reviews in medicinal chemistry, 7(10), 1040-1050 (2007-11-06)
Cysteine proteases selectively catalyze the hydrolysis of peptide bonds. Uncontrolled, unregulated, or undesired proteolysis can lead to many disease states including emphysema, stroke, viral infections, cancer, Alzheimer's disease, inflammation, and arthritis. Cysteine proteases inhibitors thus have considerable potential utility for
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