APAF1 polyclonal antibody

The mammalian homologs of the Ced-4 proteins, Apaf-1 (Ced-4), Nod1 (CARD4), and Nod2 contain a caspase recruitment domain (CARD) and a putative nucleotide binding domain, signified by a consensus Walker's A box (P-loop) and B box (Mg2+-binding site) . Nod1 contains a putative regulatory domain and multiple leucine-rich repeats. Nod1 is a member of a growing family of intracellular proteins which share structural homology to the apoptosis regulator Apaf-1. Nod1 associates with the CARD-containing kinase RICK and activates NFκB. The self-association of Nod1 mediates proximity of RICK and the interaction of RICK with IKKγ. In addition, Nod-1 binds to multiple caspases with long prodomains, but specifically activates caspase-9 and promotes caspase-9-induced apoptosis. Nod2 is composed of two N-terminal CARDs, a nucleotide-binding domain, and multiple C-terminal leucine-rich repeats. The expression of Nod2 is highly restricted to monocytes, and activates NFκB in response to bacterial lipopoly-saccharides.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of APAF1 pAb at 1:500 dilution Lane1:HEK293T whole cell lysate (40ug) Lane2:A549 whole cell lysate (40ug) Lane3:Jurkat whole cell lysate (40ug)