epitope corresponding to phosphorylated Ser 782 of Ser 782 of human origin
recommended for detection of Ser 782 phosphorylated IL-6Rβ of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
IL-6Rβ Background Information IL-6 activates intracellular signaling through binding a receptor consisting of a ligand-binding protein (IL-6R) and a second protein. IL-6 first binds to IL-6R which subsequently associates with a gp130 dimer. The active signaling complex consists of at minimum IL-6, IL-6R and a dimer of two gp130 proteins that are linked by a disulfide bond. A soluble form of IL-6R 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. Ser-782 as the major phosphorylated serine residue in human gp130, regulating cell surface expression of the receptor polypeptide.
