AIM2 (N-terminal region) Blocking Peptide
€155.00
In stock
SKU
ECM-AX3855
Background:
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 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.
Sequence: AIM2 synthetic peptide corresponds to amino acid residues in the N-terminal region of human AIM2. This peptide sequence is highly conserved in rat and mouse AIM2
Specificity: The peptide is specifically recognized by AIM2 (N-terminal region) antibody (AP3851) in ELISA, and has been shown to block the reactivity of AP3851 in Western blot. In addition, the peptide is recommended for use in blocking AP3851 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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 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.
Sequence: AIM2 synthetic peptide corresponds to amino acid residues in the N-terminal region of human AIM2. This peptide sequence is highly conserved in rat and mouse AIM2
Specificity: The peptide is specifically recognized by AIM2 (N-terminal region) antibody (AP3851) in ELISA, and has been shown to block the reactivity of AP3851 in Western blot. In addition, the peptide is recommended for use in blocking AP3851 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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