Clone REA235 recognizes the CD124 antigen, a 140 kDa transmembrane glycoprotein which is also known as interleukin-4 receptor subunit alpha (IL-4Rα). CD124 is expressed on both B and T lymphocytes, and on cells of several other hematopoietic lineages, including mast cell, macrophage, and undifferentiated hematopoietic cell lines. CD124 is a receptor for both IL-4 and IL-13. The functional IL-4 receptor is formed by initial binding of IL-4 to IL-4R. Subsequent recruitment to the complex of the common γ chain, in immune cells, creates a type I receptor and, in non-immune cells, of CD213a1 (IL-13RA1) forms a type II receptor. IL-4R can also interact with the IL-13/CD213a1 complex to form a similar type II receptor. The type I IL-4 receptor complex specifically binds IL-4 whereas the type II IL-4R binds either IL-4 or IL-13. The IL-4/IL-13 responses are involved in regulating the IgE production in B cells and in alternative activation of macrophages. Binding of IL-4 to CD124 on T cells promotes differentiation of Tʜ2 cells. Clone REA235 blocks the binding of IL-4 to cells and also recognizes the soluble truncated form of CD124.

Additional information: Clone REA235 displays negligible binding to Fc receptors.