Purified anti-IRAK1,BioLegend,632051

The interleukin-1 receptor-associated kinase (IRAK) family of proteins are made up of serine/threonine-specific kinases which play a critical role in the response to pathogens through the induction of acute inflammation and subsequent adaptive immune responses. The mammalian IRAK molecular family consists of four members (IRAK1, IRAK2, IRAK3/IRAK-M, and IRAK4). Two are active kinases, IRAK1 and IRAK4, and two are inactive kinases, IRAK2 and IRAKM. However, all are involved in the regulation of the nuclear factor-κB (NF-κB) and mitogen-activated protein kinase (MAPK) pathways. The binding of IL-1 to IL-1 receptor type I (IL-1RI) initiates the formation of a complex that includes IL-1R1, IL-1RAcP, MyD88, and IRAKs. Currently, there are three differentially spliced variants of IRAK1: IRAK1, IRAK1b, and IRAK1c. Auto-phosphorylation plays a role in IRAK-1 activation and mediates proteasome-mediated degradation leading to IRAK1 protein loss. Meanwhile, IRAK1b lacks kinase activity and is resistant to proteasome-mediated degradation. Additionally, IRAK1c has a truncated sequence and is therefore mutated at the C-terminus of its kinase domain and acts as a negative regulator of the TLR and IL-1R signaling pathways.