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The **cytokine receptor common beta subunit (CSF2RB, also known as the common beta chain or βc)** is a transmembrane protein that functions as the signal-transducing subunit shared by the receptors for interleukin-3, interleukin-5, and granulocyte-macrophage colony-stimulating factor (GM-CSF)[2][3][4]. While the α subunits of these receptors confer ligand specificity, the β subunit is required for high-affinity ligand binding and intracellular signaling activation, especially involving JAK/STAT pathways[2][3]. The βc subunit is broadly expressed in hematopoietic cells and plays a critical role in eosinophil biology and the immune response, especially in conditions such as asthma and allergic inflammation[2][4]. Targeting this subunit or its associated signaling pathways is of significant therapeutic interest in the management of eosinophil-driven diseases.
Monoclonal antibodies prevent IL-5 from binding its receptor or deplete IL-5 receptor-expressing cells, thereby inhibiting downstream βc-mediated signaling and reducing eosinophil survival and activation[3]
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