Recombinant Human IL-13Rα

Interleukin 13 receptor alpha 1 (IL13Rα1), also known as CD213A1, is a subunit of the IL-13 receptor, and binds IL-13 with a low affinity by itself. IL-13 is capable of binding two types of receptor (1). One is the heterodimer composed of the IL13Rα1 and the IL4Rα , which transduces the IL-13 signals. The other is IL13Rα2 which acts as a non-signaling "decoy" receptor (2). IL13Rα1 forms a functional receptor complex for IL-13 with IL4Rα, a subunit shared by IL-13 and IL-4 receptors, transducing an IL13-dependent proliferative signal (3). IL13Rα1 also has also been shown to serve as an alternate accessory protein to the common cytokine receptor gamma chain for IL-4 signaling, but cannot replace the function of gamma C in allowing enhanced IL-2 binding activity (4). IL13Rα1 can bind tyrosine kinase TYK2, and thus may mediate the signaling processes that lead to the activation of JAK1, STAT3 and STAT6 induced by IL-13 and IL-4 (5). Overexpression of IL13Rα1 may play some roles in the pathogenesis of chronic stage of psoriasis.