- Catalogue N°
- 856.031.001 - 1 x 96 Discovery (plate not included)
856.031.001P - 1 x 96 Discovery (non-sterile plate)
856.031.001S - 1 x 96 Discovery (sterile plate)
856.031.005 - 5 x 96 (plates not included)
856.031.005P - 5 x 96 (non-sterile plates)
856.031.005S - 5 x 96 (sterile plates)
856.031.010 - 10 x 96 (plates not included)
856.031.010P - 10 x 96 (non-sterile plates)
856.031.010S - 10 x 96 (sterile plates)
856.031.015 - 15 x 96 (plates not included)
856.031.015P - 15 x 96 (non-sterile plates)
856.031.015S - 15 x 96 (sterile plates)
856.031.020 - 20 x 96 (plates not included)
856.031.020P - 20 x 96 (non-sterile plates)
856.031.020S - 20 x 96 (sterile plates)
- Target species
- Recognizes natural human IL-10
- 3h after cell stimulation
- Cross Reaction
- No cross reactivity with other human cytokines. Cross reactivity with simian IL-10. No cross reactivity with viral IL-10.
- Kit Content
- Diaclone ELISpot Sets include capture and detection antibodies, Streptavidin - Alkaline Phosphatase conjugated, BSA, BCIP/NTB and blocking reagent.
- Additional Information
- Spots read visually or with reader
Interleukin-10 is a pleiotropic cytokine playing an important role as a regulator of lymphoid and myeloid cell function. 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 exists at 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-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.
IL-10 in disease
IL-10 expression was shown to be elevated in parasite infections like in Schistosoma mansoni , Leishmania, Toxoplasma gondii and Trypanosoma infection.
Furthermore, high IL-10 expression was detected in mycobacterial infections as shown for Mycobacterium leprae, Mycobacterium tuberculosis and Mycobacterium avium infections.
High expression levels of IL-10 are also found in retroviral infections inducing immunodeficiency.
Version 10 - 07.19
For research use only
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