In humans, IL10 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. Human IL10 is a homodimeric protein that shares 73% amino acid homology with mouse IL10. IL10 inhibits the synthesis of a number of cytokines such as IFN-gamma, IL2 and TNF-beta in Th1 T helper subpopulations of T cells but not of Th2 helper cells. This activity is antagonized by IL4. The inhibitory effect on IFN-gamma production is indirect and appears to be the result of a suppression of IL12 synthesis by accessory cells. In the human system, IL10 is produced by, and down-regulates the function of Th1 and Th2 cells.
<1.0 EU/μg of recombinant protein as determined by the LAL method
Biological Activity Comment
The ED50 as determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be ≤ 2.0 ng/mL
Weight
19.0 kDa
Description
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Format
Lyophilized PowderLyophilized from a 0.2 μm filtered solution in PBS (pH 7.0)
Purity
>95% as determined by SDS-PAGE
Storage
The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.