Anti-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.

Our AIM2 (N-terminal region) rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat AIM2 (N-terminal region) and is antigen affinity purified. It is great for use in WB.

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.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.