Recombinant IRAK1 protein (His tag)

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Recombinant Human Interleukin-1 receptor-associated kinase 1 (IRAK-1) Fragment (residues 197-526) is a high-purity protein encompassing the complete kinase domain, essential for studying innate immune signaling pathways. This fragment enables targeted investigation of IRAK-1's serine/threonine kinase activity in Toll-like receptor and IL-1 receptor-mediated responses.

IRAK-1 is a critical serine/threonine-protein kinase (EC 2.7.11.1) that initiates innate immune responses against pathogens through Toll-like receptor (TLR) and IL-1 receptor signaling pathways. Upon TLR activation, IRAK-1 is recruited by MYD88 to receptor complexes where it undergoes phosphorylation by IRAK-4, leading to autophosphorylation and kinase activation. Activated IRAK-1 phosphorylates E3 ubiquitin ligases Pellino proteins, promoting polyubiquitination events that facilitate the assembly of signaling complexes involving MAP3K7/TAK1-TRAF6 and NEMO-IKKA-IKKB, ultimately leading to NF-kappa-B nuclear translocation and activation. Additionally, IRAK-1 phosphorylates interferon regulatory factor 7 (IRF7) to activate type I IFN antiviral responses and, when sumoylated, translocates to the nucleus to phosphorylate STAT3. The protein localizes primarily to the cytoplasm but can translocate to the nucleus when sumoylated and is also recruited to lipid droplets by RSAD2/viperin.