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. Asc can be phosphorylated at Tyr-144 in a Syk and JNK-dependent manner. This phosphorylation is critical for Asc speck formation and Caspase-1 activation.
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Bürckstümmer, T. et al. (2009). Nat Immunol. 10(3):266.
*For more information, see UniProt Accession Q9EPB4
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Yu, SH et al. (2019) J Ethnopharmacol. 239:111917. (WB: mouse bone marrow macrophages)
Dubois, EC et al. (2019) PLoS Pathog. 15(4):e1007709. (WB: mouse macrophage)
Furuya, MY et al. (2018) Arthritis Res Ther. 20(1):196. (WB: human neutrophils)
Kwak, SB et al. (2018) Mediators Inflamm. 2018:6054069. (WB: mouse J774A.1, BMDMs)
Hoyt, L.R. et al. (2016) J Immunol. 197:1322. (WB: mouse macrophage, LPS)
This kit contains: