IL10 is a homodimeric protein with subunits having a length of 160 amino acids. In human system 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. IL10 down-regulates the function of Th1 and Th2 cells. 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 T 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. Recombinant Human IL10 is expressed in human 293 cells as a non-covalent homodimeric glycoprotein
<1 EU/µg of recombinant protein as determined by the LAL method
Biological Activity Comment
The EC(50) as determined by the dose-dependent stimulation of the proliferation of MC/9 cells (mouse mast cell line) in the presence of 200 pg/mL IL-4 was found to be ≤1.5ng/mL.
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. Avoid repeated freeze/thaw cycles.