Product Details
| Source: | Produced in E. coli. Contains an N-terminal His-tag. |
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| EC: | 3.4.22.36 |
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| UniProt ID: | P42575 |
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| Formulation: | Lyophilized. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Specific Activity: | >5,000U/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. |
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| 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). |
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| Reconstitution: | Reconstitute to 1U/µl with PBS containing 15% glycerol. |
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| Shipping: | Shipped on Dry Ice |
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| Long Term Storage: | -80°C |
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| Handling: | After reconstitution, prepare aliquots and store at -80°C. |
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| 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. |
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| Regulatory Status: | RUO - Research Use Only |
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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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Product Literature References
GSDMEa-mediated pyroptosis is bi-directionally regulated by caspase and required for effective bacterial clearance in teleost: H. Xu, et al.; Cell Death Dis.
13, 491 (2022),
Abstract;
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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