Recombinant Human IL-18 R beta/IL-1 R7 Fc Avi Protein, CF

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. Our Avi-tag Biotinylated IL-18 R beta/IL-1R7 Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.