AIM2 (N-terminal region) Antibody

Host- and pathogen-associated cytoplasmic double-stranded DNA triggers the activation of a NALP3-independent inflammasome, which activates caspase-1, leading to maturation of pro-interleukin-1beta and inflammation. Several studies have isolated AIM2 (absent in melanoma 2) as a candidate cytoplasmic-DNA-sensing protein that contains an N-terminal pyrin domain and C-terminal oligonucleotide binding domain. A screen for transcripts induced by interferon-beta identified AIM2 gene expression. AIM2 protein bound double-stranded DNA, recruited the inflammasome adaptor ASC, and localized to ASC containing speckles. AIM2 and ASC form a pyroptosome, which induces pyroptotic cell death mediated by caspase-1. RNA-mediated suppression of AIM2 expression impairs DNA-induced maturation of interleukin-1beta in THP-1 human monocytic cells, as well as abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus. Thus, AIM2 is a DNA-sensing protein for the activation of the caspase-1 inflammasome.

AIM2 synthetic peptide (coupled to KLH) corresponds to amino acid residues in the N-terminal region of human AIM2. This peptide sequence is highly conserved in rat and mouse AIM2.