IL-13 His Tag Protein, Human

IL-13 (interleukin 13) is a type I cytokine secreted by activated Th2 cells, mast cells, and basophils, belonging to the four-helix bundle cytokine family. Its protein structure consists of four α-helices (A, B, C, D) stabilized by two disulfide bonds forming a compact globular conformation, and recombinant expression with His-tag technology facilitates purification and structural studies. This cytokine activates the JAK1/TYK2-STAT6 signaling pathway through type I receptors (IL-13Rα1/IL-4Rα heterodimer), regulating B cell IgE class switching, mucus production, and eosinophil chemotaxis; concurrently, binding to IL-13Rα2 (decoy receptor) participates in inflammatory modulation and tissue fibrosis. In clinical medicine, IL-13 serves as a core driver of type 2 inflammatory diseases, with biologics targeting the IL-4/IL-13 pathway such as dupilumab approved for treating moderate-to-severe asthma, atopic dermatitis, and chronic rhinosinusitis with nasal polyps. Furthermore, IL-13 receptor α2 is highly expressed in solid tumors including glioblastoma, emerging as a novel tumor target for CAR-T cells and bispecific antibodies, demonstrating broad clinical application prospects spanning from inflammatory regulation to cancer immunotherapy.