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INTERLEUKIN 6 HUMAN RECOMBINANT EXPRE

Code: SCU0001-10UG D2-231

Analysis Note

The biological activity of recombinant human IL-6 was tested in culture by measuring its ability to stimulate proliferation of the IL-6 dependent mouse T1165 ce...


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£263.00 10UG
£315.60 inc. VAT

Analysis Note

The biological activity of recombinant human IL-6 was tested in culture by measuring its ability to stimulate proliferation of the IL-6 dependent mouse T1165 cells.

Biochem/physiol Actions

Interleukin-6 (IL-6) is a multifunctional protein originally discovered in the media of cells stimulated with double stranded RNA. IL-6 appears to be directly involved in the responses that occur after infection and injury and may prove to be as important as IL-1 and TNF-α in regulating the acute phase response. IL-6 is reported to be produced by fibroblasts, activated T cells, activated monocytes or macrophages, and endothelial cells. It acts upon a variety of cells, including fibroblasts, myeloid progenitor cells, T cells, B cells and hepatocytes. IL-6 induces multiple effects, as indicated by its numerous synonyms: plasmacytoma growth factor (PCT-GF), interferon-β-2 (IFN-β2), monocyte derived human B cell growth factor, B cell stimulating factor (BSF-2), hepatocyte stimulating factor (HSF), Interleukin Hybridoma/Plasmacytoma-1 (IL-HP1). In addition, IL-6 appears to interact with IL-2 in the proliferation of T lymphocytes. IL-6 also potentiates the proliferative effect of IL-3 on multipotential hematopoietic progenitors.

General description

Interleukin 6 (IL-6) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. IL-6 is a multifunctional cytokine with well-defined pro- and anti-inflammatory properties. IL-6 is secreted by T cells and macrophages to stimulate immune response, e.g. during infection and after trauma, especially burns or other tissue damage leading to inflammation. The O-linked sugar chain of IL-6 is thought to contribute to the stability of the cytokine through polymerization suppression and/or conformational changes, exemplifying the significance of its expression in a human expression system (which allows proper glycosylation).

Physical form

This product is supplied as a lyophilized powder in phosphate buffered saline (PBS), pH 7.4, with no additives or carrier proteins. It is aseptically filled.

Preparation Note

Briefly centrifuge the vial before opening. It is recommended to reconstitute the protein in sterile water to a final concentration of 100 µg/ml. Adding 0.1% recombinant human serum albumin is recommended. The product is stable for at least 2 years as supplied. After reconstitution, it is recommended to store the protein in working aliquots at –20°C.

assay≥98% (SDS-PAGE)
biological sourcehuman
colorwhite
formlyophilized powder
Gene Informationhuman ... IL6(3569)
impurities≤0.1 EU/µg protein (LAL test)
mol wtcalculated mol wt 20.8 kDa (183 amino acids glycosylated protein)
packagingvial of ≥10 µg
potency0.2-2 ng/mL EC50
Quality Level200
qualityendotoxin tested
recombinantexpressed in HEK 293 cells
storage temp.−20°C
technique(s)cell culture | mammalian: suitable
UniProt accession no.P05231
Pack10UG
This product has met the following criteria: