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Caspase-2 (human), (recombinant) (active)

 
ALX-201-057-U025 25 U 254.00 USD
 
ALX-201-057-U100 100 U 457.00 USD
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Product Specification

Source:Produced in E. coli. Contains an N-terminal His-tag.
 
EC:3.4.22.36
 
UniProt ID:P42575
 
Formulation:Lyophilized.
 
Purity:≥95% (SDS-PAGE)
 
Specific Activity:10’000-13’000U/mg protein. One unit is defined as the amount of enzyme that cleaves 1nmol of the caspase substrate VDVAD-pNA per hour at 37°C in reaction solution containing 50mM HEPES, pH 7.2, 50mM sodium chloride, 0.1% CHAPS, 10mM EDTA, 5% glycerol and 10mM DTT.
 
Application Notes:Useful in screening caspase inhibitors, studying enzyme regulation and kinetics, determining specificity of capase substrates, or as positive control in caspase activity assays. We recommend using 1 unit per assay for analyzing caspase activity. For a complete caspase-2 assay protocol, please refer to Caspase-2 Fluorometric Assay Kit (Prod. No. ALX-850-214).
 
Reconstitution:Reconstitute to 1U/µl with PBS containing 15% glycerol.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Handling:After reconstitution, prepare aliquots and store at -80°C.
 
Scientific Background:Caspase-2 is a member of the interleukin-1β converting enzyme (ICE) family of cysteine proteases. Similar as other caspases, caspase-2 also exists in cells as an inactive proenzyme. During apoptosis, procaspase-2 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases. The processed form of caspase-2 consists of large (19kDa) and small (12kDa) subunits which associate to form the active enzyme. The expressed caspase-2 spontaneously undergoes auto-processing to yield the subunits characteristic of the native enzyme. The active recombinant caspase-2 is routinely tested for its ability to enzymatically cleave the caspase-2 colorimetric substrate Ac-VDVAD-pNA (Prod. No. ALX-260-059). The signal can be detected by spectrophotometry.
 
201-057
Figure: Active human caspase was expressed in E. coli  and purified. The activity of recombinant caspase-2 was determined by cleaving AFC conjugates of VDVAD. The cleavage activity was effectively inhibited by the corresponding peptide inhibitor as indicated. 
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201-057

Product Literature References

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;

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