IL-6 activates intracellular signaling through binding a receptor consisting of a ligand-binding protein (IL-6Ralpha) and a second protein. IL-6 first binds to IL-6Ralpha (also known as gp80), which subsequently associates with a gp130 dimer. The active signaling complex consists of, at minimum, IL-6, IL-6Ralpha and a dimer of two gp130 proteins that are linked by a disulfide bond. A soluble form of IL-6Ralpha, namely sIL-6Ralpha, 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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
IL6R polyclonal antibody detects endogenous levels of IL6R protein.
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