Bioactive, Human IL-6Rα/gp130 Heterodimer, His and Strep Tag

Human interleukin 6 receptor (IL-6R) is a heterodimer consisting of IL-6Rα and gp130 (IL-6Rβ). Both IL-6Rα and gp130 are Type I transmembrane proteins. IL-6Rα is Type I cytokine receptor and gp130 is a member of the class of tall cytokine receptors. IL-6Rα contains an extracellular domain with an Ig-like domain, cytokine binding module (CBM) domains, and a long flexible stalk region followed by a transmembrane domain and intracellular domains. The extracellular domain of gp130 includes an N-terminal immunoglobulin-like (Ig-like) domain (D1), a cytokine-binding homology region (CHR, D2D3), and three membrane-proximal fibronectin type III domains (FNIII, D4 to D6). IL-6Rα binding to its ligand interleukin 6 (IL-6) results in homodimerization and subsequent association with gp130 homodimer resulting in higher order complexes. The interaction between IL-6 cytokine and IL-6R is crucial for immune responses, inflammation, and hematopoiesis. Dysregulation of IL-6R is implicated in many cancers and autoimmune diseases, therefore, a recombinant protein mimicking the IL-6R heterodimer conformation can be critical for immunology research and therapeutic discovery.