Human IL-6 is an important pro-inflammatory and anti-inflammatory cytokine expressed by many cell types including: T and B cells, macrophages, endothelial cells, fibroblasts, monocytes, keratinocytes and certain tumor cells. It Is a multifunctional cytokine that modulates several physiologic processes such as hematopoiesis, stimulation of immunoglobulin synthesis, maturation and activated B cells, differentiation of T lymphocytes and regulation of the hepatic acute-phase response. IL-6 is also produced by muscle, is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance. The binding of IL-6 to its receptor triggers the association of a hetheromeric IL-6R/gp130 complex, which activates the JAK/STAT1 cascade. In a mechanism known as trans-signaling, the complex of soluble IL-6/IL-6R elicits responses from gp130-expressing cells that lack cell surface IL-6R. This enables a wider range of cell types to respond to IL-6. Recombinant human Interleukin-6 is a polypeptide chain containing 183 amino acids (30–212 of P05231 IL6_HUMAN) and a 10XHistidine-based tag. It has a predicted molecular mass of 22.2 kDa. However, as a result of potential glycosylation, the recombinant protein could migrate with an apparent molecular mass of 23-24 kDa in an SDS-PAGE gel. Human recombinant IL-6 expressed in Nicotiana benthamiana is produced by transient expression in non-transgenic plants and is purified by sequential chromatography (FPLC). This product does not contain any animal–derived components or impurities.
Human IL6 expressed in Nicotiana benthamiana
CAT# CSC-CTK0231-20 (20 μg); CAT# CSC-CTK0231-100 (100 μg)
Greater than 97% as determined by SDS-PAGE analysis.
rHu IL-6 is fully biologically active when compared to standards. The specific activity is determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erytroleukemic indicator cell line). The measured ED50 is typically less than 1 ng/ml.
Less than 0.04 EU/μg.
Lyophilized from a concentrated, sterile protein solution in 20 mM Tris-HCl buffer (pH 8.5) and 125 mM NaCl.
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 50 μg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use. At higher concentrations the solubility may be reduced and multimers generated. Optimal concentration should be determined for specific application and cell lines.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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