NBP1-46086-10-10 Interleukin-6 / IL6

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Interleukin-6 / IL6


Product Description for Interleukin-6 / IL6

Interleukin-6 / IL6.
Presentation: Purified

Properties for Interleukin-6 / IL6

Product Category Proteins & Growth Factors
Target Category
Quantity 10 µg
Synonyms B-cell stimulatory factor 2, BSF-2, CDF, CTL differentiation factor, Hybridoma growth factor, IFNB2, IL-6, Interferon beta-2
Presentation Purified
Reactivity Hu
Molecular weight 29.3 kDa
Species (Protein) Human
Shipping to Not USA/Canada
PDF datasheet View Datasheet
Manufacturer Novus Biologicals Inc.

Datasheet Extract

Swiss Prot Num:
Background IL-6 is a pleotropic cytokine that regulates the development, proliferation and maturation of a number of hematopoietic cells and is essential for the maturation of B cells into immunoglobulin-secreting cells. IL-6 can also influence the growth and function of non-hematopoietic cells including the differentiation of nerve cells, metabolism of bone and induction of acute phase proteins in hepatocytes. IL-6 is predominately expressed by T cells, macrophages, fibroblasts, endothelial cells and keratinocytes. IL-6 expression can be stimulated by a number of different factors including, T cell mitogens, LPS, viruses, IL-1, TNF, IL-2, IFN-b, platelet derived growth factor (PDGF), protein kinase C, calcium ionophore A23187 and factors that increase the intracellular concentration of cAMP. IL-6 is expressed as a glycoprotein with a variable molecular mass as a result of differential glycosylation/phosphorylation patterns. At least six distinct IL-6 phosphoglycoproteins have been identified. The lower molecular weight species, 23- to 25-kDa, are O-glycosylated while the 28- to 30-kDa species are both O- and N-glycosylated. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible.
Concentration 0.02 mg/ml
General Readings Jones SA et al., (2005) J Interferon Cytokine Res. 25(5): 241-53.
Storage Store at -80C. Avoid freeze-thaw cycles.
Buffer System:
PBS with 1% human serum albumin and 10% trehalose.
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