Recombinant Human sIL-4 Receptor α (CHO derived)

IL-4 can signal thro μgh type I and type II receptor complexes, which share a common gamma chain (γc). The type I receptor contains, in addition to the γc, an IL-4Rα subunit, whereas the type II receptor contains the IL-13Rα. The secreted extracellular domain of IL-4Rα, called sIL-4Rα, 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. PeproTech's CHO cell-derived Recombinant Human sIL-4 Receptor α is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4Rα. As a result of glycosylation, Recombinant Human sIL-4 Receptor α migrates with an apparent molecular mass of approximately 50-65 kDa by SDS-PAGE gel, under reducing conditions.