Recombinant Mouse IL-6/IL-6R alpha Protein Chimera


Recombinant Mouse IL-6/IL-6R alpha complex (Catalog #9038-SR) inhibits M1 mouse myeloid leukemia cell proliferation. The ED50 for this effect is 2‑12 ng/mL.

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Recombinant Mouse IL-6/IL-6R alpha Protein Chimera Summary

Details of Functionality
Measured by its ability to inhibit M1 mouse myeloid leukemia cell proliferation. The ED50 for this effect is 2‑12 ng/mL.
Mouse myeloma cell line, NS0-derived mouse IL-6/IL-6R alpha Complex protein
Mouse IL-6R alpha
Accession # P22272
Accession # P08505
Accession #
N-terminal Sequence
Leu20 (major), Leu28 (minor)
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
60 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
70-87 kDa, reducing conditions
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9038-SR in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse IL-6/IL-6R alpha Protein Chimera

  • IL-6/IL-6R alpha Complex


Interleukin-6 (IL-6) is a pleiotropic, alpha -helical, 22-28 kDa phosphorylated and variably glycosylated cytokine that plays important roles in the acute phase reaction, inflammation, hematopoiesis, bone metabolism, and cancer progression. 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 (1-5). When dysregulated, it contributes to chronic inflammation in obesity, insulin resistance, inflammatory bowel disease, arthritis, sepsis, and atherosclerosis (1-3). IL-6 can also function as an anti-inflammatory molecule, as in skeletal muscle where it is secreted in response to exercise (2). In addition, it enhances hematopoietic stem cell proliferation and the differentiation of Th17 cells, memory B cells, and plasma cells (1, 6). 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-6 R alpha , triggering IL-6 R alpha association with gp130 and gp130 dimerization (7). gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM (8). Soluble forms of IL-6 R alpha are generated by both alternative splicing and proteolytic cleavage (3). 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 (3). 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, 3). 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 (3, 9). Mature mouse IL-6 shares 39% and 85% amino acid (aa) sequence identity with human and rat IL-6, respectively (10-12). Within the extracellular domain, mouse IL-6 R alpha shares 51% and 89% aa sequence identity with human and rat IL-6 R alpha , respectively (13).
  1. Mansell, A. and B.J. Jenkins (2013) Cytokine Growth Factor Rev. 24:249.
  2. Schuett, H. et al. (2009) Thromb. Haemost. 102:215.
  3. Hunter, C.A. and S.A. Jones (2015) Nat. Immunol. 16:448.
  4. Erta, M. et al. (2012) Int. J. Biol. Sci. 8:1254.
  5. Garbers, C. et al. (2012) Cytokine Growth Factor Rev. 23:85.
  6. Cerutti, A. et al. (1998) J. Immunol. 160:2145.
  7. Murakami, M. et al. (1993) Science 260:1808.
  8. Muller-Newen, G. (2003) Sci. STKE 2003:PE40.
  9. Mitsuyama, K. et al. (2006) Clin. Exp. Immunol. 143:125.
  10. Chiu, C.P. et al. (1988) Proc. Natl. Acad. Sci. USA 85:7099.
  11. Simpson, R.J. et al. (1988) Eur. J. Biochem. 176:187.
  12. Van Snick, J. et al. (1988) Eur. J. Immunol. 18:193.
  13. Sugita, T. et al. (1990) J. Exp. Med. 171:2001.

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