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Safety Information

SCP0084

Sigma-Aldrich

Caspase 3 Substrate

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Empirical Formula (Hill Notation):
C31H39N5O12
Molecular Weight:
673.67
UNSPSC Code:
12352202
NACRES:
NA.32

Assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥80%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Ac-Asp-Glu-Val-Asp-4M2NA

General description

Caspase 3 belongs to the family of cysteinyl proteases, which regulate apoptosis. It is encoded by CASP-3 gene. Caspase 3 is important for normal brain development. Caspase 3 is involved in growth stimulation of surviving tumor cells. It is associated with neuronal apoptosis in Alzheimer′s disease.

Application

Caspase 3 Substrate has been used to determine caspase activity in esophageal squamous cell carcinoma EC109 cell line.
Caspase 3, a cysteine protease activator of caspase 6 and caspase 7, metabolizes amyloid-β 4A precursor protein. Caspase 3 may be detected using a variety of chromogenic and fluorogenic peptide substrates built around the DxxD (asp-x-x-asp) sequences DMQD and DEVD such as Ac-DMQD-pNa (Acetyl-Asp-Met-Gln-Asp-p- nitroanalide), chromogenic; Ac-DMQD-AMC (Acetyl-Asp-Met-Gln-Asp- amino-4-methylcoumarin), fluorogenic and Ac-DEVD-4M2Na.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis
Kothakota S, et al.
Science, 278(5336), 294-298 (1997)
Resveratrol-induced apoptosis is enhanced by inhibition of autophagy in esophageal squamous cell carcinoma
Tang Q, et al.
Cancer Letters, 336(2), 325-337 (2013)
Caspase-3 is enriched in postsynaptic densities and increased in Alzheimer's disease
Louneva N, et al.
The American Journal of Pathology, 173(5), 1488-1495 (2008)
Caspase 3-mediated stimulation of tumor cell repopulation during cancer radiotherapy
Huang Q, et al.
Nature Medicine, 17(7), 860-860 (2011)
R U Jänicke et al.
The Journal of biological chemistry, 273(25), 15540-15545 (1998-06-23)
Although the commonly activated death protease caspase-3 appears not to be essential for apoptosis during development except in the brain, it was not shown whether substrates known to be cleaved by caspase-3 are still proteolyzed in its absence. We have

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