Cytochrome c is an electron transport protein from mitochondria. A primary means of caspase activation by p53 is through induction of cytochrome c release from mitochondria. Cleavage of Bid, a Bcl 2 family member, by caspase-8 produces a truncated tBid molecule which triggers mitochondria release of cytochrome c which binds to the adaptor protein Apaf-1 and procaspase-9 to form a cytosolic apoptosome complex. This event results in activation of procaspase-9 and its subsequent cleavage and activation of caspase-3 leading to the degradation of a series of cellular substrates and subsequently cell death.
- For Immunohistochemistry, Western Blot
Recognizes human, mouse, rat, bovine, guinea pig, hamster, monkey, rabbit and sheep Cytochrome c. Detects a band of ~14kDa by Western blot.