Protein activity determined to be 10,000 – 13,000 units/mg. One unit of the recombinant caspase-2 is the enzyme activity that cleaves 1 nmol of the caspase substrate VDVAD-pNA (pNA: pnitroanaline) per hour at 37ºC in a reaction solution containing 50 mM Hepes, pH 7.2, 50 mM NaCl, 0.1% Chaps, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.
two large (19 kDa) and two small (12 kDa) subunits kDa. ( Note
Reconstitute to 1 unit per μl in PBS containing 15% glycerol. Store at -80ºC.
Purity was assessed by SDS-PAGE (≥95%) and by HPLC.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
CASP-2, ICH-1L, ICH-1S, ICH1, NEDD-2, NEDD2, CASP 2, ICH 1L, ICH 1S, NEDD 2, Caspase 2, CASP2, ICH1L, ICH1S, Caspase2
Caspase-2 (also know as Ich-1, Nedd-2) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-2 also exists in cells as an inactive proenzyme. During apoptosis pro-caspase-2 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases. The processed active caspase-2 is a heterotetramer consisting of two large (19 kDa) and two small (12 kDa) subunits.The recombinant active human caspase-2 was expressed in E. coli. The active caspase-2 preferentially cleaves caspase-2 substrates (e.g., VDVAD-AFC or VDVAD-pNA) and is routinely tested at GeneTex for its ability to enzymatically cleave these two substrates Ac-VDVAD-pNA or Ac-VDVAD-AFC.