Asc (phospho Tyr-144) Blocking Peptide
€155.00
In stock
SKU
ECM-AX5635
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 (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 Caspas-1 activation.
Sequence: Asc (Tyr-144) phospho-peptide corresponding to amino acid residues surrounding Tyr-144 in mouse Asc. This peptide sequence is highly conserved in human and rat Asc.
Specificity: The peptide is specifically recognized by Asc (Tyr-144), phospho-specific antibody (AP5631) in ELISA, and has been shown to block the reactivity of AP5631 in Western blot. In addition, the peptide is recommended for use in blocking AP5631 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 (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 Caspas-1 activation.
Sequence: Asc (Tyr-144) phospho-peptide corresponding to amino acid residues surrounding Tyr-144 in mouse Asc. This peptide sequence is highly conserved in human and rat Asc.
Specificity: The peptide is specifically recognized by Asc (Tyr-144), phospho-specific antibody (AP5631) in ELISA, and has been shown to block the reactivity of AP5631 in Western blot. In addition, the peptide is recommended for use in blocking AP5631 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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