Recombinant active Human caspase-3 expressed in E. coli spontaneously undergoes autoprocessing to yield subunits characteristic of the native enzyme. The active caspase-3 preferentially cleaves caspase-3 substRates (e.g., DEVD-AFC or DEVD-pNA) and is routinely tested for its ability to enzymatically cleave these two substRates Ac-DEVD-pNA or Ac-DEVD-AFC.
Protein activity determined to be 300000 units/mg. One unit of the recombinant caspase-3 is the enzyme activity that cleaves 1 nmol of the caspase substrate DEVD-pNA (pNA: pnitroanaline) per hour at 37ºC in a reaction solution containing 50 mM HEPSE (pH 7.2), 50 mM NaCl, 0.1% Chaps, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.
Reconstitute with PBS, 15% Glycerol to 1 unit/μl.
Store at -20ºC or below. After reconstitution, keep as concentrated solution. Aliquot and avoid freeze-thaw cycles.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
This gene encodes a protein that belongs to a highly conserved family of cysteinyl aspartate-specific proteases that function as essential regulators of programmed cell death through apoptosis. Members of this family contain an N-terminal pro-domain and require cleavage at specific aspartate residues to become mature. The protein encoded by this gene belongs to a subgroup of cysteinyl aspartate-specific proteases that are activated by initiator caspases and that perform the proteolytic cleavage of apoptotic target proteins. Mice defective for this gene exhibit a variety of phenotypes including reduced neuronal apoptosis resulting in hyperplasias, hearing loss, attenuated osteogenic differentiation of bone marrow stromal stem cells, and pre- and post-natal lethality. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]