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Interleukin 6 receptor (IL-6R) alpha is a type I transmembrane glycoprotein that forms a complex with type I transmembrane signal transducer protein gp130 (CD130) and mediates the biological activities of IL-6. IL-6 binds to the membrane-bound non-signaling IL-6R alpha (mIL-6R), and the complex binds to two molecules of gp130 and leads to ‘classical’ IL-6-signal transduction, which includes activation of JAK/STAT, ERK, and PI3K signal transduction pathways (Scheller et al.). In contrast, a soluble form of IL-6R alpha (sIL-6R), which comprises the extracellular portion of the receptor, binds to the secreted IL-6 to form a complex that promotes bioavailability of IL-6. The complex of IL-6 and sIL-6R can bind to gp130 on cells that do not express the IL-6R and are unresponsive to IL-6. This process is known as trans-signaling (Hunter & Jones; Rose-John S). sIL-6R regulates both local and systemic IL-6-mediated events. Elevated levels of sIL-6R have been documented in several disease conditions such as rheumatoid arthritis, myeloma, and Crohn’s disease (Jones et al.; Mihara et al.).
(A) The biological activity of Human Recombinant IL-6R alpha was tested by its ability to inhibit the proliferation of M1 cells. Inhibition of cell proliferation was measured using a fluorometric assay method. The EC50 is defined as the effective concentration of the growth factor at which cell proliferation inhibition is at 50% of maximum. The EC50 in the example above is less than 200 ng/mL.
(B) 5 μg of Human Recombinant IL-6R alpha was resolved with SDS-PAGE under reducing (+) and non-reducing (-) conditions and visualized by Coomassie Blue staining. Human Recombinant IL-6R alpha has a predicted molecular mass of 50 - 58 kDa.
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