Invitrogen™ IL-10 Human Matched Antibody Pair

Description

The Human IL-10 Antibody Pair Kit comes with pre-matched antibody pairs, standards, and streptavidin-HRP to develop your own enzyme linked immunosorbent assays (ELISA) to detect and quantify protein levels of human IL-10. Buffer reagents needed to complete the ELISA reaction are sold separate as a Buffer Kit for Antibody Pairs (Catalog No. CNB0011). The Assay Buffer included in this Buffer Kit can be used as a blocking reagent for ELISA plates as well as a diluent for ELISA standards and samples, detection antibody, and HRP conjugate. Principle of the method ELISAs are designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody is coated to the bottom of the wells of a microplate, which is an overnight process. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. A sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen.

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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