The mammalian homologues of the key cell death gene CED-4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease-activating factor 1) (1,2). 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. Recently, Cho et al have identified a new Apaf-1 Interactiong Protein (APIP) also known as CG129 and MMRP19, as a negative regulator of ischemic injury. APIP competes with Caspase-9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N-terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
APimmunoprecipitation antibody can be used in ELISA, Western Blot, immunohistochemistry starting at 5 μg/mL, and immunofluorescence starting at 10 μg/mL.
Protein G Column
PBS, 0.2% gelatin, 0.05% sodium azide.
Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.