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Caspase-7 (human), (recombinant)

BML-SE177-5000 5000 U 531.00 USD
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Product Details

Alternative Name:Mch3, CMH-1
MW:~20 + 12kDa
Source:Produced in E. coli. Human caspase-7 (aa 24-303). Genbank Accession No. U40281.
UniProt ID:P55210
Formulation:Liquid. In 50mM HEPES, pH 7.4, containing 100mM sodium chloride, 0.5% CHAPS, 1mM EDTA, 10% glycerol and 10mM DTT.
Purity:≥95% (SDS-PAGE)
Activity:100 U/µl
Specific Activity:One U=1 pmol/min at 30°C using Ac-DEVD-pNA (200µM; Prod. No. ALX-260-033) as substrate.
Application Notes:Useful tool to study enzyme regulation and kinetics, cleave target substrates, screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:After initial defrost, aliquot product into individual tubes and refreeze at -80°C. Avoid repeated freeze/defrost cycles.
Scientific Background:Caspase-7 acts as an effector caspase in apoptosis and has substrate preferences similar to caspase-3. It displays an affinity for ADP-ribose polymers and automodification of PARP-1 (ADP-ribosylation) makes it a better caspase-7 substrate.
Regulatory Status:RUO - Research Use Only

Product Literature References

GSDMEa-mediated pyroptosis is bi-directionally regulated by caspase and required for effective bacterial clearance in teleost: H. Xu, et al.; Cell Death Dis. 13, 491 (2022), Abstract;
A whole cell assay to measure caspase-6 activity by detecting cleavage of lamin A/C: R. Mintzer, et al.; PLoS One 7, e30376 (2012), Abstract; Full Text
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35: I.L. Brand, et al.; Cell Death Dis. 2, e242 (2011), Abstract; Full Text

General Literature References

Cif (Cytochrome c efflux-inducing factor) activity is regulated by Bcl-2 and caspases and correlates with the activation of Bid.: Z. Han et al.; Mol. Cell. Biol. 19, 1381 (1999),
Signaling pathway activated during apoptosis of the prostate cancer cell line LNCaP: overexpression of caspase-7 as a new gene therapy strategy for prostate cancer.: M. Marcelli et al.; Cancer Res. 59, 382 (1999),
Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver.: J.M. Chandler et al.; J. Biol. Chem. 273, 10815 (1998),
Granzyme B mimics apical caspases. Description of a unified pathway for trans-activation of executioner caspase-3 and -7.: X. Yang et al.; J. Biol. Chem. 273, 34278 (1998),
Biochemical characteristics of caspases-3, -6, -7, and -8.: H.R. Stennicke & G.S. Salvesen; J. Biol. Chem. 272, 25719 (1997),
Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells.: L. Faleiro et al.; EMBO J. 16, 2271 (1997),
Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32.: J.A. Lippke et al.; J. Biol. Chem. 271, 1825 (1996),
Mch3, a novel human apoptotic cysteine protease highly related to CPP32.: T. Fernandes-Alnemri et al.; Cancer Res. 55, 6045 (1995),

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