IRAK1 Protein, Human (Sf9, GST)

IRAK1 is a serine/threonine protein kinase that initiates innate immune responses against pathogens through Toll-like receptor (TLR) and IL-1R signaling. After TLR activation, IRAK1 is recruited by MYD88 and undergoes IRAK4 phosphorylation, autophosphorylation, and kinase activation. IRAK1 Protein, Human (Sf9, GST) is the recombinant human-derived IRAK1 protein, expressed by Sf9 insect cells , with N-GST labeled tag.

IRAK1, a serine/threonine-protein kinase, assumes a crucial role in initiating the innate immune response against foreign pathogens by participating in Toll-like receptor (TLR) and IL-1R signaling pathways. Upon TLR activation, IRAK1 is swiftly recruited by MYD88 to the receptor-signaling complex, leading to its phosphorylation by IRAK4, subsequent autophosphorylation, and activation of its kinase function. IRAK1 then phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2, and PELI3), promoting pellino-mediated polyubiquitination of IRAK1. The ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1, facilitating the assembly of the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. This cascade activates IKKs (CHUK/IKKA and IKBKB/IKKB), leading to NF-kappa-B nuclear translocation and activation. Additionally, IRAK1 phosphorylates TIRAP, promoting its ubiquitination and degradation. Furthermore, IRAK1 phosphorylates interferon regulatory factor 7 (IRF7), inducing its activation and translocation to the nucleus, thereby initiating the transcriptional activation of type I IFN genes, establishing an antiviral cellular state. When sumoylated, IRAK1 translocates to the nucleus and phosphorylates STAT3.

Human

Sf9 insect cells

N-GST

P51617 (R194-S712)

3654

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.