anti-Cytochrome C, mAb (14G6)

Cytochrome c is a small heme protein consisting electron-transport chain in mitochondria and transfers electrons between complex III and IV. It is highly conserved through diverse species from unicellular microorganisms to animals and plants. Cytochrome c is also an intermediate in apoptosis. Currently, it is widely accepted that mitochondria play a key role in the regulation of apoptosis. In mammalian cells, a major caspase activation pathway is the cytochrome c-initiated pathway. In this pathway, a variety of apoptotic stimuli cause cytochrome c release from mitochondria. In the cytosol, cytochrome c interacts with its adaptor molecule, Apaf-1, resulting in the recruitment, processing and activation of pro-caspase-9 in the presence of dATP or ATP. Caspase-9, in turn, cleaves and activates pro-caspase-3 and -7; these effector caspases are responsible for the cleavage of various proteins leading to biochemical and morphological features characteristic of apoptosis. Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.