- Catalogue N°
- 874.050.001 - 1 x 96 Discovery (plate not included)
874.050.001P - 1 x 96 Discovery (non-sterile plate)
874.050.001S - 1 x 96 Discovery (sterile plate)
874.050.005 - 5 x 96 (plates not included)
874.050.005P - 5 x 96 (non-sterile plates)
874.050.005S - 5 x 96 (sterile plates)
874.050.010 - 10 x 96 (plates not included)
874.050.010P - 10 x 96 (non-sterile plates)
874.050.010S - 10 x 96 (sterile plates)
874.050.015 - 15 x 96 (plates not included)
874.050.015P - 15 x 96 (non-sterile plates)
874.050.015S - 15 x 96 (sterile plates)
874.050.020 - 20 x 96 (plates not included)
874.050.020P - 20 x 96 (non-sterile plates)
874.050.020S - 20 x 96 (sterile plates)
- Target species
- Recognizes both natural and recombinant human IL-10 and IL-2
- 3h30 after cell stimulation
- Kit Content
- Diaclone Dual ELISpot Sets include capture and detection antibodies for both of the targeted cytokines, Streptavidin-Alkaline Phosphatase conjugated, anti-FITC HRP conjugated mAb, BSA, BCIP/NTB and AEC blocking reagent.
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.
IL-2 is a powerful immunoregulatory lymphokine produced by T-Cells in response to antigenic or mitogenic activation. IL-2 stimulates growth and differentiation of B-Cells, most T-cells, NK cells, monocytes and macrophages.
Mature IL-2 is a 15.4kDa globular glycoprotein containing 133 amino acid residues including one intrachain disulfide bond between residues 58 and 105.
Apart from its most important role to mediate antigen-specific T-lymphocyte proliferation, IL-2 modulates the expression of interferon-g and major histocompatibility antigens.
Alterations in the ability of T-cell to synthesize IL-2 have been observed in physiologic and pathologic states. Currently, IL-2 is used to enhance the immune system of patients for the treatment of cancer and infectious disease.
Version 7 - 07.19
For research use only
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