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Caspase-3, mouse recombinant protein

Caspase 3

     
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Product info
Primary Accession Q8BNT4
Calculated MW of large (17 kD) and small (11 kD) subunits
Additional Info
Gene ID 12367
Gene Symbol CASP3
Other Names Caspase-3, Short name=CASP-3, Apopain, Cysteine protease CPP32, Short name=CPP-32, FLICE, Protein Yama, SREBP cleavage activity 1, Short name=SCA-1
Gene Source Mouse
Source E. coli
Assay&Purity SDS-PAGE;
Assay2&Purity2 HPLC;
Recombinant Yes
Target/Specificity Caspase-3
Application Notes Reconstitute to 1 unit per µl in PBS containing 15% glycerol
Format Lyophilized powder
Storage -70°C; Lyophilized powder
Citations (0)
citation

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Background

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. 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 or Ac-DEVD-AFC

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Discontinued
Cat# PBV10028r-100
Size:

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