| Overview |
| bs-70328r |
| AIM2 (N-terminal region) Antibody |
| WB |
| The antibody detects a 40 kDa* doublet corresponding to AIM2 in immunoblots of Jurkat cells, as well as mouse macrophages treated with IFN_ and LPS. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Rabbit |
| 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. |
| Monoclonal |
| #REF! |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| O14862 |
| PYHIN4, AIM2 |
| 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. |
| Application Dilution |
| WB |
1:300-5000 |
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