IL6ST (phospho-S782) polyclonal antibody

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.

Interleukin-6 receptor subunit beta; IL-6 receptor subunit beta; IL-6R subunit beta; IL-6R-beta; IL-6RB; CDw130; Interleukin-6 signal transducer; Membrane glycoprotein 130; gp130; Oncostatin-M receptor subunit alpha; CD130; IL6ST

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of IL6ST (phospho-S782) polyclonal antibody at 1:500 dilution Lane1:HEK293T whole cell lysate (40ug) Lane2:SGC7901 whole cell lysate (40ug) Lane3:L02 whole cell lysate (40ug) Lane4:PC12 whole cell lysate (40ug) Lane5:AML-12 whole cell lysate (40ug)