1. Measured by its binding ability in a functional ELISA. 2. Immobilized recombinant mouse IL5-his at 5 μg/mL (100 μL/well) can bind biotinylated human IL5Ra-his with a linear range of 32-4000 ng/mL. 3. Measured by its ability to inhibit IL5 dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is typically 0.7-2.8 μg/mL.

Interleukin 5 receptor, alpha (IL5RA) also known as CD125 (Cluster of Differentiation 125) is a subunit of the Interleukin-5 receptor. IL5RA (CD125) is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised of a ligand-specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony-stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Six alternatively spliced transcript variants encoding three distinct isoforms have been reported. IL5RA (CD125) is a T-cell-derived cytokine that is particularly important in the development of asthma for the terminal differentiation, activation, and survival of committed eosinophil precursors.

> 85 % as determined by SDS-PAGE