IL-6 R α - Fc Chimera

 

 

 

A DNA sequence encoding the signal peptide and extracellular domain of human Interleukin 6 receptor alpha chain (aa 1-354) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Symansis IL-6Ra(1-354aa)-FcHCX™ migrates as a wide band ~98.6-96.5 kDa while the unmodified MW is predicted to be 64.6 kDa. on SDS-PAGE because of post-translation modifications particularly glycosylation.

Symansis IL-6Ra(1-354aa)-FcHCX™ Theoretical pI: 7.87 ≥ 95% purity as determined by SDS-PAGE and visualized by silver stainBackground Information Dysregulated production of IL-6 and its receptor (IL-6R) are implicated in the pathogenesis of multiple myeloma, autoimmune diseases and prostate cancer. The IL-6R complex comprises two molecules each of IL-6, IL-6R, and the signaling molecule, gp130.terleukin IL-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. The complex then binds to two molecules of gp130 and leads IL-6-signal transduction, which includes activation of JAK/STAT, ERK, and PI3K signal transduction pathways. 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. sIL-6R regulates both local and systemic IL-6-mediated events. Symansis’ IL-6Rα-Fc HCX™ is a fusion protein of IL-6Rα and human Fc and is useful in IL-6 drug interaction studies and IL-6 mediated signalling studies, as well as studies of sIL-6R.