IL-4 can signal through 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.
soluble Interleukin-4Rα, soluble IL-4 Receptor alpha, CD124
GNMKVLQEPT CVSDYMSIST CEWKMNGPTN CSTELRLLYQ LVFLLSEAHT CIPENNGGAG CVCHLLMDDV VSADNYTLDL WAGQQLLWKG SFKPSEHVKP RAPGNLTVHT NVSDTLLLTW SNPYPPDNYL YNHLTYAVNI WSENDPADFR IYNVTYLEPS LRIAASTLKS GISYRARVRA WAQCYNTTWS EWSPSTKWHN SYREPFEQH
≥ 95% by SDS-PAGE gel and HPLC analyses.
The ED50 was determined by its ability to inhibit the IL-4 dependent proliferation of human TF-1 cells is ≤ 5.0 ng/ml (in the presence of 0.5 ng/ml of IL-4), corresponding to a specific activity of ≥ 2 x 105 units/mg.