Human IL-10 Platinum ELISA

Description: The human IL-10 ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human IL-10. The human IL-10 ELISA is for in vitro diagnostic use. Not for use in therapeutic procedures.

Interleukin-10 is a pleiotropic cytokine playing an important role as a regulator of lymphoid and myeloid cell function. In humans IL-10 is produced by activated CD8(+) peripheral blood T-cells, by T-helper CD4(+) T-cell clones.
Due to the ability of IL-10 to block cytokine synthesis and several accessory cell functions of macrophages this cytokine is a potent suppressor of the effector functions of macrophages, T-cells and NK cells. In addition, IL-10 participates in regulating proliferation and differentiation of B-cells, mast cells and thymocytes. The primary structure of human IL-10 has been determined by cloning the cDNA encoding the cytokine. The corresponding protein exerts 160 amino acids with a predicted molecular mass of 18.5 kDa. Based on its primary structure, IL-10 is a member of the four a-helix bundle family of cytokines. In solution human IL-10 is a homodimer with an apparent molecular mass of 39 kDa. Although it contains an N-linked, glycosylation site, it lacks detectable carbohydrates. Recombinant protein expressed in E. coli thus retains all known biological activities. The human IL-10 gene is located on chromosome 1 and is present as a single copy in the genome. The human IL-10 exhibits strong DNA and amino acid sequence homology to the murine IL-10 and an open reading frame in the Epstein-Barr virus genome, BCRF1 which shares many of the cellular cytokine's biological activities and may therefore play a role in the host-virus interaction. The immunosuppressive properties of IL-10 suggest a possible clinical use of IL-10 in suppressing rejections of grafts after organ transplantations. IL-10 can furthermore exert strong anti-inflammatory activities.

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