Apaf-1, Human (Apoptosis Protease Activating Factor-1) Control Peptide
Description
Highly purified. 17-aa peptide from human APAF1. Apoptosis or programmed cell death is a fundamental cellular process that is essential for normal tissue development and abnormal growth. Apoptosis is driven by two classes of specialized proteases known as caspases (Cysteine Aspartase). The initiator caspases can be activated by self-cleavage. The effector caspases are then activated in an amplification cascade. Several key factors are released from the mitochondria that regulate apoptosis. The first such factor (Cytochrome-C) to be described binds to a cytoplasmic scaffolding protein called Apaf-1 (Apoptosis Protease activating factor-1), a homolog of C. elegans Ced-4. Both Apaf-1 and Ced-4 are composed of an N-terminal Caspase Recrutiment domain (CARD) linked to a Nuceoltide-bidning domain (NBD), also known as NB-ARC or NOD domain. Ced-4 and Apaf-1 self-associate via the NBD and activate Casp-3 and -9. The C-terminal region of Apaf-1 lacks homology with Ced-4 and contains 12 WD-40 rep