Recombinant Human IL-10

IL-10 is a homodimeric, anti-inflammatory cytokine of 17-21 kD with various, pleiotropic, effects in immunoregulation and inflammation. It increases antibody production, in addition to enhancing B cell survival and proliferation. IL-10 inhibits both the synthesis of pro-inflammatory cytokines and the actions of NK cells during the immune response to viral infection. Moreover, IL-10 is involved in peripheral T cell tolerance to allergens, autoantigens, transplantation antigens and tumor antigens. IL-10 can also block NF-κB activity, and is involved in the regulation of the JAK-STAT signaling pathway. In mice, lack of IL-10 has been shown to cause inflammation and pain via COX activation resulting in vascular endothelial and cardiac dysfunctions. Additionally, IL-10 is linked to myokines, a form of cytokine produced in muscle cells that participates in tissue regeneration and repair, maintenance of healthy bodily functioning, and homeostasis in the immune system. Exercise is known to increase circulating levels of IL-10. Hence, it is thought that physical exercise promotes an environment of anti-inflammatory cytokines. Furthermore, knockout studies of IL-10 suggest this cytokine is crucial for counteracting the hyperactive immune response in the intestinal tract. It has been reported that treatment with recombinant IL-10 producing bacteria has been beneficial in patients with Crohn's disease.

The biological activity of Human IL-10 was determined by a cell proliferation assay using the murine mast cell line, MC/9-2 (Thompson-Snipes, L. et. al., 1991, J. Exp. Med. 173:507). The expected ED₅₀ for this effect is typically 0.15 - 0.75 ng/ml. The cell number is assessed in a fluorometric assay using the redox senstitive dye, Resazurin.

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Ser19

Lyophilized

The predicted molecular weight of Recombinant Human IL-10 is Mr 18.6 kDa.

18.6

This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives present.

This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.

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3. Kotenko, SV. et al. (1997) EMBO J. 16:5894
4. Vieira, P. et al. (1991) Proc. Nat. Acad. Sci. 88:1172
5. Ho, AS. et al. (1993) Proc. Nat. Acad. Sci. 90:11267