Recombinant mouse Cleaved Caspase-3 protein (ab52071)
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Overview
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Product nameRecombinant mouse Cleaved Caspase-3 protein
See all Cleaved Caspase-3 proteins and peptides -
Protein lengthFull length protein
Description
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NatureRecombinant
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SourceEscherichia coli
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Amino Acid Sequence
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Accession
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SpeciesMouse
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Specifications
Our Abpromise guarantee covers the use of ab52071 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Biological activity
SPECIFIC ACTIVITY: 300,000 units/mg. One unit of the recombinant caspase-3 is the enzyme activity that cleaves 1 nmol of the caspase substrate DEVD-pNA (pNA: pnitroanaline) per hour at 37°C.
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FormLyophilised
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Additional notes
The lyophilized caspase-3 is stable for 1 year at –70degC. Following reconstitution in PBS, the enzyme should be aliquoted and immediately stored at –70degC. Avoid multiple freeze/thaw cycles as activity might decrease.
Cleaved caspase-3 is useful in studying enzyme regulation, determining target substrates, screening caspase inhibitors, or as a positive control in caspase activity assays. We recommend using 1 unit/assay for analyzing caspase activity.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
pH: 7.20
Constituents: 0.154% DTT, 1.19% HEPES, 0.292% EDTA, 5% Glycerol, 0.29% Sodium chloride, 0.1% CHAPSThis product is an active protein and may elicit a biological response in vivo, handle with caution.
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ReconstitutionReconstitute to 1 unit per µl in PBS containing 15% glycerol.
General Info
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Alternative names
- active caspase 3
- Apopain
- CASP 3
see all -
FunctionInvolved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-
-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. -
Tissue specificityHighly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.
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Sequence similaritiesBelongs to the peptidase C14A family.
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Post-translational
modificationsCleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.
S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol. -
Cellular localizationCytoplasm.
- Information by UniProt
Datasheets and documents
References
ab52071 has not yet been referenced specifically in any publications.
