Immobilized Monoclonal Anti-IL-13 R alpha 2 Antibody, Mouse IgG1 at 1 μg/mL (100 μL/well) can bind Human IL-13 R alpha 2, His Tag (Cat. No. IL2-H52H5) with a linear range of 0.4-6 ng/mL (Routinely tested).
Loaded Human IL-13, Fc Tag (Cat. No. IL3-H5256) on Protein A Biosensor, can bind Human IL-13 R alpha 2, His Tag (Cat. No. IL2-H52H5) with an affinity constant of 6.09 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
Interleukin-13 receptor subunit alpha-2 is also known as IL13Rα2, IL13Ra2 cluster of differentiation 213A2, CD213A2, CT19, IL-13R, IL13BP, and is a membrane bound protein that in humans is encoded by the IL13RA2 gene. IL13Rα2 is closely related to IL13Rα1, a subunit of the interleukin-13 receptor complex. This protein binds IL13 with high affinity, but lacks any significant cytoplasmic domain, and does not appear to function as a signal mediator. It is, however able to regulate the effects of both IL13 and IL4, despite the fact it is unable to bind directly to the latter. It is also reported to play a role in the internalization of IL13. IL13Rα2 is a component of the cell surface receptors, however, the majority exists in intracellular pools and in soluble form, and thus plays an opposite role as a potent IL13 antagonist compared with IL13Rα1. It also functions as an inhibitor of IL4-dependent pathway probably through the physical interaction between the short intracellular domain of and cytoplasmic domain of IL13Rα2 and the IL4Rα chain. In spite of the failed STAT signaling function, IL13Rα2 dose induce TGF-beta production and fibrosis. Additionally, IL13Rα2has been reported to be abundantly and specifically overexpressed in glioblastoma multiforme.