IL6R polyclonal antibody

IL-6 activates intracellular signaling through binding a receptor consisting of a ligand-binding protein (IL-6Rα) and a second protein. IL-6 first binds to IL-6Rα (also known as gp80), which subsequently associates with a gp130 dimer. The active signaling complex consists of, at minimum, IL-6, IL-6Rα and a dimer of two gp130 proteins that are linked by a disulfide bond. A soluble form of IL-6Rα, namely sIL-6Rα, is generated by proteolytic cleavage of the membrane-bound precursor and can function as an agonistic molecule that can actively participate in cell-to-cell signaling. The second subunit of the IL-6 complex, gp130, also functions as a component of several additional receptor complexes, including leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF) and IL-11. LIF binds to the LIF receptor with low affinity and to a complex of the LIF receptor and gp130 with high affinity, while OSM appears to bind to gp130 with low affinity and to a complex of gp130 and the LIF receptor with high affinity.