Anti-IRAK (CT) Antibody

Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. {PubMed:11397809, PubMed:12860405, PubMed:14684752, PubMed:15084582, PubMed:15465816, PubMed:15767370, PubMed:17997719, PubMed:20400509}.

Immunoblotting: use at 1:1,000-1:2,000 dilution. <br><br>Immunoprecipitation: use 2-4 ug antibody per sample. <br><br>Positive control: Whole cell lysate from HeLa cells or THP-1 cells.

Nuclear factor kappa B (NF-kappaB) is a ubiquitous transcription factor and key mediator of gene expression during immune and inflammatory responses. NF-kappaB activates numerous genes in response to extracellular stimuli, such as IL-1, TNFalpha, LPS, oxidative stress, and mitogens. NF-kappaB is associated with IkappaB in cytoplasm. After stimulation, 1kappaB is phosphorylated and dissociates from NF-kappaB. NF-kappaB enters cell nuclei where it activates an array of genes. A serine/threonine protein kinase associated with IL-1 receptor (IRAK) mediates a signaling cascade leading to NF-kappaB activation. IRAK is associated with IL-1 receptor subunits IL-1RI and IL-1RacP and serves as a signaling molecule to mediate IL-1 responses. IRAK also mediates IL-18-induced NF-kappaB activation.