Human IL‑18 R beta /IL‑1 R7 Biotinylated Antibody

IL-18, originally described as an interferon-gamma inducing factor (IGIF), is a member of the IL-1 family of cytokines that has multiple immunoregulatory functions. It has potent IFN-gamma inducing activities and plays a key role in the activation of T helper type 1 (Th1) responses. The functional IL-18 receptor complex consists of two components, the IL‑18 R alpha (IL-1 R5) and IL-18 R beta (also termed IL-1 R7 and AcPL) subunits. Both subunits are members of the IL-1 receptor superfamily. Although IL‑18 R alpha by itself binds IL-18 with low-affinity and IL-18 R beta does not bind IL-18 in vitro, co-expression of IL‑18 R alpha and IL-18 R beta is required for high-affinity binding and IL-18 responsiveness. Human IL-18 R beta cDNA encodes a 599 amino acid (aa) residue precursor type I membrane protein with a 14 aa signal peptide, a 342 aa extracellular region containing three immunoglobulin-like domains, a single transmembrane domain and a 222 aa cytoplasmic domain. Human and mouse IL-18 R beta share 65% aa sequence identity. The expression of IL-18 R beta parallels that of IL-18 R alpha and is detected in numerous tissues including lung, spleen, leukocytes and colon.