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Caspase-7, human recombinant

based on 7 citations in multiple journalsCaspase-7, human recombinant74.1 4
A cysteine protease involved in apoptosis 
Catalog #: 1087
SKU-Size Size Price Qty
1087-25 25units
$215.00
1087-100 100 units
$370.00
More Sizes Get Quote

Product Details

Alternate Name Caspase-7, CASP-7, Apoptotic protease Mch-3, CMH-1, ICE-like apoptotic protease 3
Gene Symbol CASP7
Gene ID 840
Accession # P55210
Source E. coli.
Appearance Lyophilized powder
Physical Form Description Lyophilized powder
Purity by SDS-PAGE ≥90%
Reconstitution Instructions Reconstitute to 1 unit per µl in water.
Handling Centrifuge the vial prior to opening.
Storage Conditions -70°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans

Details

Caspase-7 (also know as Mch3, ICE-LAP3, CMH-1) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-7 also exists in cells as an inactive proenzyme. During apoptosis procaspase-7 is processed at aspartate residues by self-proteolysis and/or cleavage by another caspase. The processed active form of caspase-7 consists of large and small subunits which associate to form the active enzyme. Active caspase-7 has been shown involving in the proteolysis of PARP (poly ADP-ribose polymerase), an enzyme that is involved in DNA repair and genomic maintenance. The recombinant active human caspase-7 was expressed in E. coli. The active caspase-7 is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-DEVD-pNA (Cat. #1008-200) or Ac-DEVD-AFC (1007-200).


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Zhou et al., Changes in phosphatidylinositol 3-kinase 55 kDa gamma expression and subcellular localization may be caspase 6 dependent in paraquat-induced SH-SY5Y apoptosis. Human and Experimental Toxicology, Jul 2014; 33: 761 - 771.
Xia et al., Differential Regulation of c-Jun Protein Plays an Instrumental Role in Chemoresistance of Cancer Cells. J. Biol. Chem., Jul 2013; 288: 19321 - 19329.
Murakami, E. et. al. Mechanism of Activation of PSI-7851 and Its Diastereoisomer PSI-7977. J. Biol. Chem., Nov 2010; 285: 34337 - 34347.
Cheng F. et. al. The Capsid Proteins of Aleutian Mink Disease Virus Activate Caspases and Are Specifically Cleaved during Infection J. Virol., Mar 2010; 84: 2687 - 2696.
Chen H et al (2009) Mol. Cell. Biol.; 29: 3657 - 3664.
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