Recombinant Human IL-6
Interleukin-6 (IL-6) is a multifunctional α-helical cytokine that regulates cell growth and differentiation of various tissues [1, 2]. Mature human IL-6 is 183 amino acids in length and shares 39% sequence identity with mouse and rat IL-6 [3]. Alternative splicing generates several isoforms with internal deletions, some of which exhibit antagonistic properties [4-7]. IL-6 induces signaling through a cell surface heterodimeric receptor complex composed of a ligand binding subunit (IL-6R alpha) and a signal transducing subunit (gp130). IL-6 binds to IL-6R alpha, triggering IL-6R alpha association with gp130 [8]. gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM [9]. Soluble forms of IL-6 R alpha are generated by both alternative splicing and proteolytic cleavage [2]. In a mechanism known as trans-signaling, complexes of soluble IL-6 and IL-6 R alpha elicit responses from gp130 -expressing cells that lack cell surface IL-6 R alpha [2]. Trans-signaling enables a wider range of cell types to respond to IL-6, as the expression of gp130 is ubiquitous, while that of IL-6 R alpha is predominantly restricted to hepatocytes, monocytes, and resting lymphocytes [2]. Soluble splice forms of gp130 block trans-signaling from IL-6/IL-6 R alpha but not from other cytokines that use gp130 as a co-receptor [2, 10]. IL-6, along with TNF-alpha and IL-1, drives the acute inflammatory response and the transition from acute inflammation to either acquired immunity or chronic inflammatory disease [1, 2]. When dysregulated, it contributes to chronic inflammation in obesity, insulin resistance, inflammatory bowel disease, arthritis, sepsis, and atherosclerosis [1, 2, 5].
Reference
[1]. Mansell, A. and B.J. Jenkins (2013) Cytokine Growth Factor Rev. 24:249.
[2]. Mihara, M. et al. (2012) Clin. Sci. (Lond.) 122:143.
[3]. Hirano, T. et al. (1986) Nature 324:73.
[4]. Kestler, D.P. et al. (1995) Blood 86:4559.
[5]. Kestler, D.P. et al. (1999) Am. J. Hematol. 61:169.
[6]. Bihl, M.P. et al. (2002) Am. J. Respir. Cell Mol. Biol. 27:48.
[7]. Alberti, L. et al. (2005) Cancer Res. 65:2.
[8]. Murakami, M. et al. (1993) Science 260:1808.
[9]. Muller-Newen, G. (2003) Sci. STKE 2003:PE40.
[10]. Mitsuyama, K. et al. (2006) Clin. Exp. Immunol. 143:125.
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Accession # |
Q75MH2 |
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Alternate Names |
IL6, B-cell differentiation factor, B-cell stimulatory factor 2, BSF2, CDF, CTL differentiation factor |
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Source |
Human embryonic kidney cell, HEK293-derived human IL-6 protein |
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Protein sequence |
Pro29-Met212 |
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M.Wt |
21.0 kDa |
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Appearance |
Solution protein. |
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Stability & Storage |
Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage. 12 months from date of receipt, -20 to -70 °C as supplied. |
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Concentration |
0. 2 mg/mL |
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Formulation |
Dissolved in sterile PBS buffer. |
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Reconstitution |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. This solution can be diluted into other aqueous buffers. |
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Biological Activity |
Measured in a cell proliferation assay using T1165.85.2.1 mouse plasmacytoma cells. The EC50 for this effect is 0.1-0.5 ng/mL |
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Shipping Condition |
Shipping with dry ice. |
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Handling |
Centrifuge the vial prior to opening. |
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Usage |
For Research Use Only! Not to be used in humans. |
Quality Control & DataSheet
- View current batch:
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Purity > 95%, determined by SDS-PAGE.
- Datasheet
Endotoxin: <0.010 EU per 1 ug of the protein by the LAL method.