Product Details
| 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. |
| |
| Regulatory Status: | RUO - Research Use Only |
| |
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.
Please mouse over
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;
Related Products
