Interleukin-2, mouse (mIL-2) recombinant (E. coli) Roche

Recombinant murine IL-2 produced by E. coli supports the growth of murine CTLL cells, but not that of human T-cells. Recombinant murine IL-2 strongly inhibits the binding of recombinant human IL-2 to murine responder cells, but only weakly inhibits the binding to human responder cells. Murine IL-2 shares identical biological and immuno-logical activities with human IL-2 (7) and is a convenient tool for extensive studies of the pharmacological and physiological activities of IL-2 in murine models.

Preparation
Recombinant murine interleukin-2 (IL-2) is produced in E. coli and purified by standard chromatographic methods. Primary Structure One polypeptide chain (149 amino acids), identical to natural mouse IL-2, but not glycosylated (7–9). Glycosylation is not essential for biological activity.
Molecular Weight
17,200 Da
Specific activity/EC ₅₀
>2 x 10 ⁶ U/mg, <0.5 ng/ml (hIL-2, NIBSC, 1 ^st international standard, 86/504), at least the same specific activity (EC ₅₀ ) compared to the indicated standard is guaranteed.
Note: The biological activity of this product may vary in different in vitro applications. Determine the optimal concentration range for specific applications.
EC ₅₀ definition/Unit definition
The amount of mIL-2 that is required to support half-maximal stimulation of cell proliferation (XTT cleavage) with CTLL-2 cells (1 unit equals ≤0.5 ng).
Species specificity
Mouse IL-2 is effective on mouse cells but not on human cells.

Interleukin-2 (IL-2, also known as T-cell growth factor, TCGF) is a lymphokine produced by lectin- or antigen-activated T-cells. It plays an important immunoregulatory role. This factor was first identified by its ability to promote the long-term in vitro proliferation of activated T-cells. It also promotes the generation and proliferation of cytotoxic T-cells, natural killer (NK) cells, and lymphokine-activated killer (LAK) cells. IL-2 also induces other lymphokines such as interferon-g and B-cell growth factor (BCGF-1) (1–6).


References

1. Smith, K. A. (1980) Immunol. Rev. 51, 337-357.
2. Ruscetti, F. W. & Galli, R. C. (1981) Blood 57, 379-394.
3. Gillis, S. (1983) J. Clin. Immunol. 3, 1-13 .
4. Smith, K. A. (1984) Ann. Rev. Immunol. 2, 319-333.
5. Rosenberg, S. (1985) J. NatI. Canc. Inst. 75, 595-603.
6. Fletcher, M. & Goldstein, A. L. (1987) Lymphokine Res. 6, 45-47
7. Kashima, N. et al. (1987) J. Biochem. 102, 715-724.
8. Kashima, N. et al. (1985) Nature 313, 402-404.
9. Yokata, T. et al. (1985) Proc. Natl. Acad. Sci. USA 82, 68-72.

Further Reading
Gillis, S. et al. (1978) J. Immunol. 120, 2027-2032.
Gearing, A. J. H., Johnstone, A. P. &Thorpe, R. (1985) J. Immunol Methods 83, 1-27.

Recombinant murine IL-2 is >95% pure as determined by SDS-PAGE [Endotoxin level: <0.1 EU/μg (LAL-test), <10 EU/ml (LAL-test)
Note: 1 EU corresponds to 0.1 ng