Description
Human sIL-4 Receptor alpha Recombinant Protein Lyophilized has been recombinantly produced in CHO cells.
IL-4 can signal through type I and type II receptor complexes, which share a common gamma chain (gammac). The type I receptor contains, in addition to the gammac, an IL-4Ralpha subunit, whereas the type II receptor contains the IL-13Ralpha. The secreted extracellular domain of IL-4Ralpha, called sIL-4Ralpha, 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. CHO cell-derived Recombinant Human sIL-4 Receptor alpha is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4Ralpha. 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