epitope mapping at the C-terminus of IL-6Rα of human origin
Modification Notes
IL-6 activates intracellular signaling through binding a receptor consisting of a ligand-binding protein (IL-6Rå) and a second protein. IL-6 first binds to IL-6Rå (also known as gp80), which subsequently associates with a gp130 dimer. The active signaling complex consists of, at minimum, IL-6, IL-6Rå and a dimer of two gp130 proteins that are linked by a disulfide bond. A soluble form of IL-6Rå, namely sIL-6Rå, 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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of IL-6Rα of human origin by WB, IP, IF and ELISA also reactive with additional species, including canine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping at the C-terminus of IL-6R&alpha of human origin
Tissue Specificity
epitope mapping at the C-terminus of IL-6Rα of human origin