Recombinant Rhesus Macaque IL-13 Protein

IL-13 is a 17 kDa immunoregulatory cytokine that plays a key role in the pathogenesis of allergic asthma and atopy. It is secreted by Th1 and Th2 CD4⁺ T cells, NK cells, visceral smooth muscle cells, eosinophils, mast cells, and basophils (1, 2). IL-13 circulates as a monomer with two internal disulfide bonds that contribute to a bundled four alpha-helix configuration (3, 4). Mature rhesus IL-13 shares 94%, 58%, and 60% amino acid sequence identity with human, mouse, and rat IL-13, respectively. Despite the low homology, it exhibits cross-species activity between human, mouse, and rat (5, 6). IL-13 has diverse activities on numerous cell types (7). On macrophages, IL-13 suppresses the production of proinflammatory cytokines and other cytotoxic substances. On B cells, IL-13 induces immunoglobulin class switching to IgE, upregulates the expression of MHC class II, CD71, CD72, and CD23, and costimulates proliferation. IL-13 upregulates IL-6 while downregulating IL-1 and TNF-alpha production by fibroblasts and endothelial cells. IL-13 binds with low affinity to IL-13 R alpha1, triggering IL-13 R alpha1 association with IL-4 R alpha. This high affinity receptor complex also functions as the type 2 IL-4 receptor complex (8, 9). Additionally, IL-13 binds with high affinity to IL-13 R alpha2 which is expressed intracellularly, on the cell surface, and as a soluble molecule (10 - 13). IL-13 R alpha2 regulates the bioavailability of both IL-13 and IL-4 and is overexpressed in glioma and several bronchial pathologies (9, 14, 15). Compared to wild type IL-13, the atopy-associated R110Q variant of IL-13 elicits increased responsiveness from eosinophils that express low levels of IL-13 R alpha2 (16).