Anti-Asc (Tyr-144), Phosphospecific 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. 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.

Our Asc (Tyr-144) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat Asc (Tyr-144) and is antigen affinity purified. It is great for use in WB, ICC.

Asc (Tyr-144) phospho-peptide (coupled to KLH) corresponding to amino acid residues surrounding Tyr-144 in mouse Asc. This peptide sequence is highly conserved in human and rat Asc.

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.

This antibody was cross-adsorbed to unphosphorylated Asc (Tyr-144) peptide before affinity purification using phospho-Asc (Tyr-144) peptide. The antibody detects phosphorylated Asc (Tyr-144) in the inflammasome. In J774 macrophage cells primed with LPS and treated with nigericin, the antibody colocalized with an inflammasome marker, caspase-1 inhibitor (FAM-YVAD-FMK) . In addition, the antibody detects a 20 kDa Asc protein in western blots of J774A.1 mouse macrophages treated with pervanadate.