IL-17 receptor A (IL-17RA), also known as CD217, is a cytokine receptor that has roles in immunity and inflammation.1 It is composed of two extracellular fibronectin III-like domains that form the ligand-binding and receptor-dimerization domain, a transmembrane domain, an SEF/IL-17R (SEFIR) domain, a TIR-like loop (TILL), and a C/EBPβ activation domain (CBAD). IL-17RA is ubiquitously expressed and localizes to the plasma membrane.2 It also exists as a soluble form that results from alternative splicing of IL17RA pre-mRNA. IL-17RA is involved in autoimmunity, neutrophil recruitment, and host defense.1 It forms a complex with IL-17RB, IL-17RC, or IL-17RE, each of which have varying affinities for the homodimeric ligands IL-17A, IL-17E, and IL-17F, and the IL-17A/IL-17F heterodimer.1,3 Knockout of Il17ra increases mortality in mice infected with T. cruzi.4 In contrast, Il17ra-/- mice are protected against the development of collagen-induced arthritis.5 Mutations in IL17RA have been found in patients with chronic mucocutaneous candidiasis, a disease characterized by recurrent or persistent commensal Candida infections.6 Cayman's Interleukin-17RA/CD217 Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of IL-17RA fused to AVI-tagged IgG1 Fc at its C-terminus, has a calculated molecular weight of 62 kDa. As a result of glycosylation, the monomer migrates at approximately 95 kDa by SDS-PAGE under reducing conditions.WARNING This product is not for human or veterinary use.
