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Key Documents

A1341

Sigma-Aldrich

N-Acetyl-Glu-Ser-Met-Asp-al

≥90% (HPLC), powder

Sinonimo/i:

Ac-ESMD-CHO

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About This Item

Formula empirica (notazione di Hill):
C19H30N4O10S
Numero CAS:
Peso molecolare:
506.53
Numero MDL:
Codice UNSPSC:
12352202
ID PubChem:
NACRES:
NA.77

Saggio

≥90% (HPLC)

Forma fisica

powder

Colore

white

Solubilità

H2O: 1 mg/mL

Temperatura di conservazione

−20°C

Stringa SMILE

CSCC[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(C)=O)C(=O)N[C@@H](CC(O)=O)C=O

InChI

1S/C19H30N4O10S/c1-10(26)20-12(3-4-15(27)28)18(32)23-14(9-25)19(33)22-13(5-6-34-2)17(31)21-11(8-24)7-16(29)30/h8,11-14,25H,3-7,9H2,1-2H3,(H,20,26)(H,21,31)(H,22,33)(H,23,32)(H,27,28)(H,29,30)/t11-,12-,13-,14-/m0/s1
TVTYMGFOGZRIHG-XUXIUFHCSA-N

Descrizione generale

N-Acetyl-Glu-Ser-Met-Asp-aldehyde (Ac-ESMD-CHO) is a tetrapeptide analog that act to inhibit the activity of caspase-3 and caspase-7 proteins, which are involved in apoptosis. Ac-ESMD-CHO has been shown to block formation of the caspase-3 p17 and p12 subunits, induce accumulation of the p20 precursor peptide, inhibit 25-hydroxycholesterol-induced apoptosis in rat Sertoli cells and also to bind caspase-7.

Azioni biochim/fisiol

In the caspase-3 precursor, procaspase-3, the ESMD amino acid sequence has been identified as a cleavage site for producing the p17 and p12 subunits of mature caspase 3; Ac-ESMD-CHO has been shown to inhibit the protease that cleaves procaspase-3 at this site. Ac-ESMD-CHO binds caspase-7 and inhibits with a Ki of approximately 1300 nM, which makes it a weaker inhibitor than other inhibitor tetrapeptide analogs.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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Dominique Le Goff et al.
Reproductive toxicology (Elmsford, N.Y.), 21(3), 329-334 (2005-11-02)
The aim of the present study was to determine whether or not apoptosis occurs in Sertoli cells in presence of 25-hydroxycholesterol, an oxysterol derived from cholesterol-containing foods or endogenous oxidation. Here, we provide evidence that 25-hydroxycholesterol can induce cultured Sertoli
Johnson Agniswamy et al.
The FEBS journal, 274(18), 4752-4765 (2007-08-19)
Many protein substrates of caspases are cleaved at noncanonical sites in comparison to the recognition motifs reported for the three caspase subgroups. To provide insight into the specificity and aid in the design of drugs to control cell death, crystal
Z Han et al.
The Journal of biological chemistry, 272(20), 13432-13436 (1997-05-16)
The apoptotic cysteine protease, caspase-3, is expressed in cells as an inactive 32-kDa precursor from which 17 kDa (p17) and 12 kDa (p12) subunits of the mature caspase-3 are proteolytically generated during apoptosis. Two amino acid sequences, ESMD downward arrowS

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