- Catalogue N°
- 874.022.001 - 1 x 96 Discovery (plate not included)
874.022.001P - 1 x 96 Discovery (non-sterile plate)
874.022.001S - 1 x 96 Discovery (sterile plate)
874.022.005 - 5 x 96 (plates not included)
874.022.005P - 5 x 96 (non-sterile plates)
874.022.005S - 5 x 96 (sterile plates)
874.022.010 - 10 x 96 (plates not included)
874.022.010P - 10 x 96 (non-sterile plates)
874.022.010S - 10 x 96 (sterile plates)
874.022.015 - 15 x 96 (plates not included)
874.022.015P - 15 x 96 (non-sterile plates)
874.022.015S - 15 x 96 (sterile plates)
874.022.020 - 20 x 96 (plates not included)
874.022.020P - 20 x 96 (non-sterile plates)
874.022.020S - 20 x 96 (sterile plates)
- Target species
- Recognizes both natural and recombinant human IL-4 and IL-10
- 3h30 after cell stimulation
- Kit Content
- Diaclone Dual Fluorospot Sets include Capture antibody for cytokine 1, FITC-conjugated detection antibody for cytokine 1, anti-FITC antibody green fluorescence conjugate, capture antibody for cytokine 2, biotinylated detection antibody for cytokine 2, streptavidin-phycoerythrin conjugate, BSA.
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-4 is a lymphokine that co-stimulates the proliferation of activated B- and T-cells, augments the cytotoxic activity of lymphocytes and monocytes and enhances the functional activity of myeloid cells . Produced by mast cells, T-cells and bone marrow stromal cells, IL-4 regulates the differentiation of naive CD4+ cells into helper Th2 cells characterized by their cytokine secretion-profile that includes secretion of IL-4, IL-5, IL-6, IL-10 and IL-13 which favour a humoral immune response. In addition, IL-4 can inhibit the proliferation of TNF, IL-1 and IL-6 by macrophages .
IL-4 induces B-cell class switching to IgE and IgG1 isotypes, and up regulates MHC Class II production and CD23 expression .
IL-4 is a 15kDa globular glycoprotein containing 129 amino acid residues. The non-glycosylated form of the protein is fully biologically active.
Version 5 - 07.19
For research use only
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