- Tel: 858.663.9055
- Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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In mammalian cells, the highly conserved cytochrome C protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e. cytochrome in the mitochondria with heme attached).
Optimal dilution of the recombinant Cytochrome C antibody should be determined by the researcher.
A human partial protein corresponding to amino acids 81-104 of pigeon Cytochrome C was used as the immunogen for this recombinant Cytochrome C antibody. The epitope has been localized to amino acids 93-104.
Store the recombinant Cytochrome C antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
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