Interleukin-6, human (hIL-6) recombinant (E. coli) Roche

Recombinant IL-6, human is a growth factor for murine and human B-cells. It can be used to replace feeder cells in the preparation of murine and human hybridomas (1-3).

Primary structure
The primary structure of recombinant human IL-6 is identical to that of natural human IL-6 (one polypeptide chain, 184 amino acids), but contains an altered sequence within the first 15 amino-terminal amino acids.
Molecular Weight
20,600 Da
Specific activity/EC ₅₀
>1 x 10 ⁸  U/mg, <0.01 ng/ml (hIL-6, NIBSC, interim standard, 88/514), at least the same specific activity (EC ₅₀ ) compared to the indicated standard is guaranteed.
EC ₅₀ definition/Unit definition
The amount of hIL-6 that is required to support half-maximal stimulation of cell proliferation (MTT cleavage) with 7TD1 cells (1 unit equals ≤0.01 ng).
Species specificity
Recombinant IL-6, human is effective on mouse and human cells.

IL-6, a 26 kD protein, also known as B-cell stimulatory factor 2 (BSF-2, BCDF), interferon-β₂ (IFN-β₂), hybridoma/plasmacytoma growth factor (H(P)GF), and hepatocyte-stimulating factor is produced by many cell types (e.g., T-cells, monocytes, fibroblasts, endothelial cells) (4-11). IL-6 induces the terminal maturation of activated B-cells into antibody- producing cells (B-cell differentiation activity (12-14). The hepatic acute phase response is induced by IL-6 (hepatocyte-stimulating activity) (15,16). It was shown that IL-6 and IL-3 act synergistically to support the proliferation of hematopoietic stem cells (hemapoietic activity) (17), however, IL-6 does not have antiviral activity, although it has been called IFN-β₂ (18). High affinity receptors for IL-6 are found on many cell types.

References

1. Brakenhoff, J. P. et al. (1987) J. Immunol. 139, 4116-4121.
2. Tiebout, R. F. et al. (1987) J. Immunol. 139, 3402-3405.
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4. Sehgal, P. B. et al. (1987) Science 235, 731-732.
5. Billiau, A. (1987) Immunol. Today 8, 84-87.
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7. Kishimoto, T. & Hirano, T. (1988) BioEssays 9, 11-15.
8. Kishimoto, T. (1985) Ann. Rev. Immunol. 3, 133 -157.
9. Brooks, K., Fernandez, R., & Viletta, E. S. (1985) Methods Enzymol. 116, 372-379.
10. Gordon, J. & Guy G. R. (1987) Immunol. Today 8, 339-344.
11. O'Garra, A. et al. (1988) Immunol. Today 9, 45-54.
12. Hirano, T. et al. (1986) Nature 324, 73 -76.
13. Kikutani, H. et al. (1985) J. Immunol. 134, 990-995.
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15. Andus, T. et al. (1987) FEBS Lett. 221, 18-22.
16. Gauldie, J. et al. (1987) Proc. Natl. Acad. Sci. USA 84, 7251-7255.
17. lkebuchi, K. et al. (1987) Proc. Natl. Acad. Sci. USA 84, 9035-9039.
18. Zilberstein, A. et al. (1986) EMBO J. 5, 2529-2537.
19. Haegeman, G. et al. (1986) Eur. J. Biochem. 159, 625-632.
20. Garman, R. D. et al. (1987) Proc. Natl. Acad. Sci. USA 84, 7629 -7633.
21. Van Damme, J. et al. (1987) J. Exp. Med. 165, 915-919.
22. Van Damme, J. et al. (1987) Eur. J. Biochem. 168, 543-555.
23. Hirano, T. et al. (1987) Proc. Natl. Acad. Sci. USA 84, 228-231.
24. Van Snick, J. et al. (1986) Proc. Natl. Acad. Sci. USA 83, 9679-9683.
25. Van Snick, J. et al. (1987) J. Exp. Med. 165, 641-649.
26. Poupart, P. et al. (1987) EMBO J. 6, 1219 -1224.

200,000 U/ml (2 μg/ml) solution in PBS and 1 mg/ml BSA, filtered through a 0.2 μm pore size membrane

Purity
95% pure as determined by HPLC or SDS-PAGE [Endotoxin level: <0.1 EU/μg (LAL-test), <10 EU/ml (LAL-test).
Note: 1 EU corresponds to 0.1 ng