Recombinant Human IL-6
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BackgroundIL-6 is a pleotropic 26 kD protein that can act as both a pro-inflammatory cytokine and an anti-inflammatory myokine, a form of cytokine produced in muscle cells that participates in tissue regeneration and repair, maintenance of healthy bodily functioning, and homeostasis within the immune system. IL-6 plays a part in the immune, endocrine, nervous, and hematopoietic systems, in addition to bone metabolism, regulation of blood pressure and inflammation. Osteoblasts secrete IL-6 to stimulate osteoclast formation. Smooth muscle cells in the tunica media of many blood vessels also produce IL-6 as a pro-inflammatory cytokine. Furthermore, IL-6 is an important mediator of fever and of the acute phase response which is the body's rapid attempt to restore homeostasis after tissue injury, infection, neoplastic growth, or immunological disturbance. In addition, IL-6 can be released into circulation in response to various stimuli including PAMPs (pathogen-associated molecular patterns) and cortisol, a hormone produced by the human body under psychologically stressful conditions. In its role as an anti-inflammatory myokine, IL-6 precedes the appearance of other cytokines in the circulation, is notably elevated with exercise, and is mediated by both its inhibitory effects on TNF-α and IL-1, and activation of IL-1ra and IL-10. IL-6 signals through a cell-surface type I cytokine receptor complex formed by the binding of IL-6 to IL-6R, forming a binary complex, which in turn combines with GP130 to transduce extracellular signaling by the activation STAT3. Hence, it is thought that blocking the interaction between IL-6 and GP130 may have therapeutic potential via the inhibition of the IL-6/GP130/STAT3 signaling pathway. Moreover, IL-6 initiates the inflammatory and auto-immune processes in many diseases such as diabetes, atherosclerosis, depression, Alzheimer's disease, rheumatoid arthritis, cancer, and various others. Thus, there is an interest in the therapeutic potential of anti-IL-6 mAbs. Protein DetailsPurity ≥95% by SDS Page Endotoxin Level < 1.0 EU/mg as determined by the LAL method Biological Activity The biological activity of Human IL-6 was determined in a cell proliferation assay using a factor dependent murine plasmacytoma cell line, T1165.85.2.1 (Nordan, R.P., Pumphrey, J.G., and B. Rudikoff. 1987. J. Immunol. 139:813). The expected ED<sub>50</sub> for this effect is typically 0.2 - 0.8 ng/ml. Protein Accession No. Amino Acid Sequence pv ppgedskdva aphrqpltss eridkqiryi ldgisalrke tcnksnmces skealaennl nlpkmaekdg cfqsgfneet clvkiitgll efevyleylq nrfesseeqa ravqmstkvl iqflqkkakn ldaittpdpt tnaslltklq aqnqwlqdmt thlilrsfke flqsslralr qm
N-terminal Sequence Analysis Pro29 State of Matter Lyophilized Predicted Molecular Mass The predicted molecular weight of Recombinant Human IL-6 is Mr 20.3 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is 21 kDa. Predicted Molecular Mass 20.3 Formulation This recombinant protein was 0.2 µm filtered and lyophilized from aqueous solution containing 10mM sodium phosphate, pH 7.5 Storage and Stability This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions. Country of Origin USA Shipping Next Day Ambient References & Citations1. Jumming, L. et al. (1988) Lab. Invest. 61:588 2. Pederson, BK. et al. (2005) Exerc. Sport Sci. Rev. 33:114 3. Satoh, T. et al. (1988) Mol. Cell. Biol. 8:3546 4. Perkins, SL. et al. (1997) Am. J. Physiol. Endocrinol. Metab. 272:461 5. Baier, M. et al. (1997) Proc. Nat. Acad. Sci. (USA) 94:5273 Certificate of AnalysisIMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein. |
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