Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved 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).