Protein activity determined to be > 400 units/mg. One unit of the recombinant caspase-9 is the enzyme activity that cleaves 1 nmol of the caspase substrate LEHD-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.
Reconstitute to 1 unit per μl in PBS containing 15% glycerol. Store at -80ºC.
Purity was assessed by SDS-PAGE (≥90%) 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.
APAF-3, APAF3, CASPASE-9c, ICE-LAP6, MCH6, APAF 3, ICE LAP6, Caspase 9, CASPASE 9c, ICELAP6, Caspase9, CASPASE9c
Caspase-9 is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-9 also exists in cells as an inactive proenzyme. During the initiation of apoptosis procaspase-9 is processed at aspartate residues to form active caspase-9. As one of the initiator caspases, active caspase-9 functions to trigger activation of downstream effector caspases, leading to disassembly of cell structures. The recombinant active human caspase-9 was expressed in E. coli. The active caspase-9 is routinely tested at GeneTex for its ability to enzymatically cleave these two substrates Ac-LEHD-pNA or Ac-LEHD-AFC.