IL-10 Ultrasensitive ELISA

Human IL-10 is a non-glycosylated 18 kilodalton protein which is produced in activated populations of Th2 T cells, macrophages,
monocytes, B cells, and ultraviolet light-exposed keratinocytes. Human IL-10 exhibits both immunosuppressive and immunostimulatory
activities. By blocking the transcription of IL-1, GM-CSF, TNF-α, IL-6, IL-8, and IL-12, IL-10 serves as a potent
inhibitor of pro-inflammatory cytokine production and proliferation in Th1 cells. IL-10 is an antagonist to IFN-γ and as such is
believed to be important in regulating the switch from Th1 to Th2 immune responses. This is accomplished by acting on the
antigen presenting cells but not on B cells or dendritic cells. Cytokine synthesis by IL-2 activated NK cells is also inhibited by IL-10.
In contrast, IL-10 enhances humoral immune responses by stimulating the secretion by the B cells of IgG, IgM, and IgA. This
cytokine can also act as a co-stimulator with IL-3, IL-6, and stem cell factor for the proliferation of megakaryocytic, erythroid,
and primitive hematopoietic cells. The amino acid sequence of human IL-10 shares 84% homology with an open reading frame
from the Epstein-Barr Virus gene BCRF1, which suggests the virus acquired the mammalian IL-10 gene as a means of suppressing
the anti-viral activity of interferon-γ and macrophages.