BMP2, human

General description
The IL6 (interleukin-6) gene is mapped to human chromosome 7p15.3.[1] All the members of IL6 family have membrane glycoprotein gp130 as a common receptor.[2] IL6 (interleukin-6) induces B-cell differentiation and is a primary regulator of inflammation.[3] Application
Interleukin-6 human has been used to check its role in breast cancer metastasis.[4] It has also been used for evaluating its role in D5HS tumor sphere formation.[5] Biochem/physiol Actions
IL6 regulates tumor proliferation and inhibits apoptosis.[3] It contributes to the disease progression of coronary artery disease.[6] 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.
Preparation Note
Human IL-6, expressed in human 293 cells, is a glycosylated monomer with an apparent molecular mass of 26-30 kDa due to glycosylation, which is absent when this cytokine is expressed in E. coli. Production in human HEK 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications.
Analysis Note
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line).