Human IL1RAP Protein, ECD (Extracellular Domain), Fc-fusion, Biotinylated, Recombinant

Description :
IL1RAP (interleukin-1 receptor accessory protein), also known as IL1R3 (interleukin-1 receptor 3), is a single-pass, type I transmembrane glycoprotein that belongs to the interleukin-1 receptor (IL1R) family. Like other family members, IL1RAP contain 3 immunoglobulin (Ig)-like domains in the extracellular region and an intracellular TIR (Toll-like receptor/IL-1 receptor) signaling domain that is also conserved in the Toll-like receptor family. IL1RAP is identified as a co-receptor for a high-affinity IL-1 receptor type I (IL1R1) complex that mediates IL1-dependent activation of NF-κB, MAPK and other signaling pathways. IL1RAP is required for transducing the signaling events on the plasma membrane level to downstream activation of IL1-responsive genes. IL1 are pleiotropic cytokines that induce synthesis of acute phase and proinflammatory proteins during infection, tissue damage, or stress. Alternative splicing of the IL1RAP gene results in 2 transcript variants encoding two different isoforms, one membrane-bound and one soluble. The ratio of soluble to membrane-bound forms increases during acute-phase induction or stress. The soluble form of IL1RAP contributes to the antagonism of IL-1 action. When present with soluble IL1R2, soluble IL1RAP increases the IL­1 binding affinity y of IL1R2 more than 100­fold. In addition, ILRAP interacts with ST2 on mast cells and Th2 T lymphocytes to create a functional receptor complex for transducing IL33-dependent signaling activity.