Recombinant Human IL-18 R alpha/IL-1 R5 Fc Avi-tag, CF

IL-18 Receptor alpha (IL-18 Ra), also known as IL-18 R1, IL-1 R5, and IL-1 Rrp, is a transmembrane component of the IL-18 Receptor (1). It associates with IL‑18 Rb/IL‑1 R7 to form the high affinity receptor complex for IL-18 and confer cellular responsiveness to IL-18 (2, 3). IL-18 is a member of the IL-1 family of cytokines and shares numerous immunoregulatory functions with IL-12. Mature human IL-18 Ra consists of a 308 amino acid (aa) extracellular domain (ECD) with three immunoglobulin-like domains, a 21 aa transmembrane segment, and a 191 aa cytoplasmic domain (4). Within the ECD, human IL-18 Ra shares 56% aa sequence identity with mouse and rat IL-18 Ra. IL-18 Ra is widely expressed on epithelial cells as well as on B cells, NK cells, CD4+ and CD8+ T cells, and dendritic cells (5-8). Signaling through the IL-18 receptor promotes a Th1 biased immune response and NK cell cytolytic activity (6, 7, 9-11). It also contributes to cigarette smoke-induced airway inflammation and epithelial damage (12). Our Avi-tag Biotinylated human IL-18 Ra features biotinylation at a single site contained within the avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound the streptavidin-coated surface due to the precise control of biotinylatin and the rest of the protein in changed so there is no interference in the protein's bioactivity.