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Caspase-6 (human), (recombinant)

Highly, active caspase-6 for the study of enzyme kinetics or screening of inhibitors
BML-SE170-5000 5000 U 528.00 USD
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Product Details

Alternative Name:Mch2
MW:18 + 11 kDa subunits
Source:Produced in E. coli.
UniProt ID:P55212
Formulation:Liquid. In 50mM HEPES, pH 7.4, containing 100mM sodium chloride, 0.5% CHAPS, 1mM EDTA, 10% glycerol and 10mM DTT.
Purity:≥80% (SDS-PAGE)
Activity:100 U/µl
Specific Activity:One U=1 pmol/min at 30°C using Ac-VEID-pNA (200mM; Prod. No. BML-P437) 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 the remaining, unused enzyme quickly by snap-freezing in a dry/ice ethanol bath or liquid nitrogen, if possible.
Handling:Avoid freeze/thaw cycles.
Scientific Background:Effector caspase responsible for the cleavage of nuclear lamins in apoptosis. Caspase-6 cleavages of various other protein targets have been implicated in the pathogenesis of neurodegenerative diseases, including Alzheimer’s disease (b-amyloid precursor protein), Huntington’s disease (huntingtin).
Regulatory Status:RUO - Research Use Only
Caspase-6 (human), (recombinant) SDS-PAGE
SDS-PAGE Analysis - Lane 1: MW Marker, Lane 2: 1 µg Caspase-6.
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Caspase-6 (human), (recombinant) SDS-PAGE

Product Literature References

Characterization of calpain and caspase-6 generated glial fibrillary acidic protein breakdown products follow ing traumatic brain injury and astroglial cell injury: Z. Yang, et al.; Int. J. Mol. Sci. 23, 8960 (2022), Abstract;
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;
Huntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1: R.J. Harding, et al.; Commun. Biol. 4, 1374 (2021), Abstract;
Activation of caspase-6 is promoted by a mutant huntingtin fragment and blocked by an allosteric inhibitor compound: D.E. Ehrnhoefer, et al.; Cell Chem. Biol. 26, 1295 (2019), Abstract; Full Text
Quantification of Total and Mutant Huntingtin Protein Levels in Biospecimens Using a Novel alphaLISA Assay: B. Baldo, et al.; eNeuro 5, ENEURO.0234-18.2018 (2018), Abstract; Full Text
Laquinimod decreases Bax expression and reduces caspase-6 activation in neurons: D. Ehrnhoefer, et al.; Exp. Neurol. 283A, 121 (2016), Application(s): Caspase-6 inhibition (in vitro), Abstract;
Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment: J. Gafni, et al.; J. Neurosci 32, 7454 (2012), Abstract;
Induction of the C-terminal proteolytic cleavage of AβPP by statins: O. Descamps, et al.; J. Alzheimers Dis. 25, 51 (2011), Abstract;
Identification and Evaluation of Novel Small Molecule Pan-Caspase Inhibitors in Huntington’s Disease Models: M.J. Leyva, et al.; Chem. Biol. 17, 1189 (2010), Abstract;

General Literature References

Caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis: K. Samejima, et al.; J. Biol. Chem. 274, 4335 (1999), Abstract;
Biochemical characteristics of caspases-3, -6, -7, and -8: H.R. Stennicke & G.S. Salvesen; J. Biol. Chem. 272, 25719 (1997), Abstract;
Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells: L. Faleiro, et al.; EMBO J. 16, 2271 (1997), Abstract;
Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis: A. Takahashi, et al.; PNAS 93, 8395 (1996), Abstract;
The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A: K. Orth, et al.; J. Biol. Chem. 271, 16443 (1996), Abstract;
Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family: T. Fernandes-Alnemri, et al.; Cancer Res 55, 2737 (1995), Abstract;

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