APAF1 (ready-to-use)

IgG

Human

APAF1

PBS pH 7. 4 containing 1%BSA and 0. 1% sodium azide

Cytoplasmic Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homolog of the key cell death gene CED 4 in C. elegans was identified recently from human and mouse and designated APAF1 for Apoptosis protease-activating factor 1. APAF1 binds to Cytochrome c (APAF2) and Caspase 9 (APAF3) which leads to Caspase 9 activation. Activated Caspase 9 in turn cleaves and activates Caspase 3 that is one of the key proteases being responsible for the proteolytic cleavage of many key proteins in apoptosis. APAF1 can also associate with Caspase 4 and Caspase 8. APAF1 transcript is ubiquitously expressed in human tissues.

Monomer. Oligomerizes upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains and consecutively mature caspase-9 is released from the complex. Pro-caspase-3 is recruited into the Apaf-1-pro-caspase-9 complex via interaction with pro-caspase-9. Interacts with APIP.

Ubiquitous. Highest levels of expression in adult spleen and peripheral blood leukocytes and in fetal brain kidney and lung. Isoform 1 is expressed in heart kidney and liver.

The CARD domain mediates interaction with APIP.

Contains 1 NB-ARC domain.