IL-4 receptor alpha (CD124), soluble

IL-4 can signal through type I and type II receptor complexes, which share a common gamma chain. The type I receptor contains, in addition to the gamma chain, an IL-4R alpha subunit, whereas the type II receptor contains the IL-13R alpha. The secreted extracellular domain of IL-4R alpha, called sIL-4R alpha, binds IL-4 and antagonizes its activity. It plays an important role in regulating the differentiation of naïve CD4+ T cells and class switching to IgG1 and IgE. Recombinant Human sIL-4 Receptor alpha is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4R alpha. As a result of glycosylation, Recombinant Human sIL-4 Receptor alpha migrates with an apparent molecular mass of approximately 50-65 kDa by SDS-PAGE gel, under reducing conditions.