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IL-13 is an immunoregulatory cytokine secreted predominantly by activated TH2 cells, as well as mast cells and basophils, and is a key mediator in the pathogenesis of allergic inflammation. The human IL-13 receptor (IL-13R) is a heterodimer composed of the interleukin-4 receptor a chain (IL-4Rα) and an IL-13 binding protein, IL-13Rα1.A second IL-13 binding protein, IL-13Rα2, has also been identified, which is believed to act as a “decoy” receptor. IL-13 receptors are expressed on human B cells, basophils, eosinophils, mast cells, endothelial cells, fibroblasts, monocytes, macrophages, respiratory epithelial cells, and smooth muscle cells. However, functional IL-13 receptors have not been demonstrated on human or mouse T cells.
As with other cytokine receptors, the cytoplasmic tails of IL-4 and IL-13 receptor subunits associate with tyrosine kinases of the Janus family (JAK 1
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Figure: Specificity testing of GM-1C8. BOSC cells were transiently transfected with an expression vector for the extracellular domain of IL-13Ra1 as well as an irrelevant protein. Expression of the constructs was tested with an anti-tag monoclonal antibody (B, open curves), an irrelevant monoclonal antibody served as negative control (filled curves). For specificity testing (A), GM-1C8 hybridoma supernatant was tested on both the IL-13Ra1 and the irrelevant protein transfectants. A positive signal was obtained only with IL-13Ra1-transfected cells.
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