|Other Names||Interleukin-1 receptor-associated kinase 1, IRAK-1, IRAK1, IRAK|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP3139a was selected from the region of human Phospho-IRAK1-S376. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cytoplasm. Nucleus. Lipid droplet. Note=Translocates to the nucleus when sumoylated RSAD2/viperin recruits it to the lipid droplet (By similarity)|
|Tissue Location||Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2.|
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Provided below are standard protocols that you may find useful for product applications.
IRAK1 binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. Isoform 1 binds rapidly but is then degraded allowing isoform 2 to mediate a slower, more sustained response to the cytokine. Isoform 2 is inactive suggesting that the kinase activity of this enzyme is not required for IL-1 signaling. Once phosphorylated, IRAK1 recruits the adapter protein PELI1. This protein is partially responsible for IL1-induced upregulation of the transcription factor NF-kappa B.
De Nardo, D., et al., J. Biol. Chem. 280(11):9813-9822 (2005).Siedlar, M., et al., Int. J. Cancer 114(1):144-152 (2005).Huang, Y., et al., J. Biol. Chem. 279(49):51697-51703 (2004).Noubir, S., et al., J. Biol. Chem. 279(24):25189-25195 (2004).Cuschieri, J., et al., Shock 21(2):182-188 (2004).
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