Human Interleukin-10 Recombinant

IL-10 is produced by mouse Th2-cells following their stimulation by lectins. The main source for B-cell derived IL-10 in mice are Ly1 B-cells that express CD5 (Ly1) and CD11. In humans IL-10 is produced by activated CD8 (+) peripheral blood T-cells, by T-helper CD4 (+) T-cell clones after both antigen-specific and polyclonal activation, by B- cell lymphomas, and by monocytes following cell activation by bacterial lipopolysaccharides and mast cells. IL-10 is a homodimeric protein with subunits having a length of 160 amino acids. Human Interleukin-10 shows 73% amino acid homology with mouse Interleukin-10. The murine IL-10 receptor has been cloned. This receptor is a protein of approximately 110 kDa that binds murine IL-10 specifically. This receptor is structurally related to receptors for IFN. The CD nomenclature for this receptor is CDw210. IL-10 inhibits the synthesis of a number of cytokines such as IFN-gamma, IL-2 and TNF-beta in Th1 T-helper subpopulations of T-cells but not of Th2 T-helper cells. This activity is antagonized by IL-4. The inhibitory effect on IFN- gamma production is indirect and appears to be the result of a suppression of IL-12 synthesis by accessory cells. In the human system, IL-10 is produced by, and down-regulates the function of Th1 and Th2 cells.

Reconstitute at 0.1-1.0 mg/ml in distilled water. This solution can then be diluted into other buffers. To maximize product collection from vial surface, vortex briefly and then spin down to recollect the liquid.

The lyophilized protein is stable for at least 2 years from date of receipt when stored at -20°C. Upon reconstitution, store in working aliquots at +4°C for up to one month, or at -20°C for up to six months, in the presence of a carrier protein. Avoid repeated freeze/thaw cycles.