IL13RA1 forms a shared receptor component for both IL-13 and IL-4 type II signaling, making its extracellular domain (aa 22–343) a critical tool for dissecting cytokine–receptor interactions in allergic inflammation and tumor immunology. This recombinant human IL13RA1 demonstrates functional activity with an ED50 below 30 ng/mL in inhibiting IL-13-dependent proliferation of TF-1 cells, confirming that the protein retains the conformational integrity necessary for ligand engagement. Mammalian cell expression ensures native-like glycosylation and proper disulfide bond formation, supporting use in SPR- or BLI-based affinity characterization, competitive inhibition assays, and blocking antibody screening where physiologically relevant folding is essential. The C-terminal 6×His tag facilitates oriented capture on sensor chips or assay surfaces, and purity exceeding 95% paired with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based neutralization assays and therapeutic antibody epitope mapping.
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