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Dokumenty

E0514

Sigma-Aldrich

E-64c

Calpain Inhibitor

Synonim(y):

(2S,3S)-trans-Epoxysuccinyl-L-leucylamido-3-methylbutane

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About This Item

Wzór empiryczny (zapis Hilla):
C15H26N2O5
Numer CAS:
76684-89-4
Masa cząsteczkowa:
314.38
Numer MDL:
MFCD00132882
Kod UNSPSC:
12352202
Identyfikator substancji w PubChem:
24894369

pochodzenie biologiczne

synthetic (organic)

Próba

≥98% (HPLC)

Postać

powder

rozpuszczalność

ethanol: 20 mg/mL, clear, colorless

temp. przechowywania

−20°C

ciąg SMILES

CC(C)CCNC(=O)[C@H](CC(C)C)NC(=O)[C@H]1O[C@@H]1C(O)=O

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

Klucz InChI

SCMSYZJDIQPSDI-SRVKXCTJSA-N

informacje o genach

human ... CAPN1(823)

Działania biochem./fizjol.

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.

Powiązanie

Synthetic analog of E-64
This page may contain text that has been machine translated.

Kod klasy składowania

13 - Non Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)

Certyfikaty analizy (CoA)

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Calpain Inhibitor III The Calpain Inhibitor III, also referenced under CAS 88191-84-8, controls the biological activity of Calpain. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.

Sigma-Aldrich

208722

Calpain Inhibitor III

CA-074 methyl ester ≥99% (TLC)

Sigma-Aldrich

C5857

CA-074 methyl ester

Calpeptin ≥98% (HPLC)

Sigma-Aldrich

C8999

Calpeptin

Calpain Inhibitor I N-Acetyl-Leu-Leu-norleucinal, synthetic

Roche

11086090001

Calpain Inhibitor I

Bestatin hydrochloride ≥98% (HPLC)

Sigma-Aldrich

B8385

Bestatin hydrochloride

Pepstatin A microbial, ≥90% (HPLC)

Sigma-Aldrich

P5318

Pepstatin A

Leupeptin microbial, ≥90% (HPLC)

Sigma-Aldrich

L2884

Leupeptin

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
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
Chihiro Takatsuka et al.
Plant & cell physiology, 52(12), 2074-2087 (2011-11-01)
Tobacco culture cells carry out a large-scale degradation of intracellular proteins in order to survive under sucrose starvation conditions. We have previously suggested that this bulk degradation of cellular proteins is performed by autophagy, where autolysosomes formed de novo act
L B Creemers et al.
Matrix biology : journal of the International Society for Matrix Biology, 16(9), 575-584 (1998-05-06)
The involvement of cysteine proteinases in the degradation of soft connective tissue collagen was studied in cultured periosteal explants. Using cysteine proteinase inhibitors that were active intracellularly or extracellularly (Ep453 and Ep475, respectively), it was shown that over-all collagen degradation
D A Raj et al.
Pflugers Archiv : European journal of physiology, 435(6), 804-809 (1998-06-13)
An inflammatory response triggered by neutrophil accumulation into muscle tissue is thought to occur with exercise-induced muscle damage. To investigate the relationship between Ca2+-stimulated proteolysis (calpain-like activity) and neutrophil accumulation [myeloperoxidase (MPO) activity], cardiac and plantaris muscles from rats (n
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