Product Name: IL-6Rα/gp130
Predicted Molecular Weight: 122 kDa
SDS PAGE Molecular Weight: The migration range of the heterodimer protein with glycosylation under non-reducing condition is ~190 kDa and under reducing condition ~120 for IL-6Rα chain and ~85 kDa for gp130 (IL-6Rβ) chain on SDS PAGE.
Protein Construct: IL-6R heterodimer protein contains an IL-6Rα extracellular domainand gp130 extracellular domainfused with a proprietary dimer motif followed by a His tag at the IL-6Rα C-terminus and a Strep tag at the gp130 C-terminus.
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.