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Caspase-3, human recombinant

based on 17 citations in multiple journalsCaspase-3, human recombinant174.6 5
A cysteine-aspartic acid protease involved in apoptosis
Catalog #: 1083
SKU-Size Size Price Qty
1083-5 5 μg
$295.00
1083-10 10 μg
$495.00
1083-25 25 units
$140.00
1083-100 100 units
$295.00
More Sizes Get Quote

Product Details

Alternate Name Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1
Gene Symbol CASP3
Gene ID 836
Accession # P42574
Source E. coli.
Appearance Semi-Dry
Physical Form Description Semi-Dry
Molecular Weight large (17 kD) and small (11 kD) subunits
Reconstitution Instructions Reconstitute in water.
Handling Centrifuge the vial prior to opening.
Storage Conditions Shipped at -20°C. For long term storage store at -70°C.
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans

Details

Caspase-3 (also know as CPP32, Yama and apopain) is a major member of the caspase-family of cysteine proteases. Caspase-3 exists in cells as an inactive 32 kDa proenzyme. During apoptosis procaspase-3 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases, such as caspase-6 (Mch2), caspase-8 (Flice) and grazyme B. The processed form of caspase-3 consists of large (17 kD) and small (11 kD) subunits which associate to form the active enzyme. The active caspase-3 has been shown involving in the proteolysis of several important molecules, such as poly (ADP-ribose) polymerase (PARP), the sterol regulatory element binding proteins (SREBPs), focal adhesion kinase (FAK), and others. The recombinant active human caspase-3 expressed in E. coli spontaneously undergoes autoprocessing to yield subunits characteristic of the native enzyme (Full length gene Accession No. NP_004337) . The active caspase-3 preferentially cleaves caspase-3 substrates (e.g., DEVD-AFC or DEVD-pNA) and 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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Shresh Pathak, Autoimmune inner ear disease patient–associated 28-kDa proinflammatory IL-1β fragment results from caspase-7–mediated cleavage in vitro. JCI Insight., Feb. 2020;  32051334.
Samir Patel, Caspase-3 cleavage of Salmonella type III secreted effector protein SifA is required for localization of functional domains and bacterial dissemination. Gut Microbes, Feb 2019;  30727836.
Carles Solà-Riera, Orthohantaviruses belonging to three phylogroups all inhibit apoptosis in infected target cells. Sci Rep., Jan. 2019;  30696898.
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.
Nakajima, E. et. al. Calpain, Not Caspase, Is the Causative Protease for Hypoxic Damage in Cultured Monkey Retinal Cells. Invest. Ophthalmol. Vis. Sci., Sep 2011; 52: 7059 - 7067.
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