IL-4 can signal through type I and type II receptor complexes, which share a common γ chain (γc). The type I receptor contains in addition to the γ chain 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 naive CD4 T cells and class switching to IgG1 and IgE. Recombinant Human sIL-4Rα is a 209 amino acid protein that corresponds to the entire extracellular domain of IL-4Rα.
Source: HEK293 cells
Synonyms: soluble IL-4 receptor alpha, CD124
AA Sequence: GNMKVLQEPT CVSDYMSIST CEWKMNGPTN CSTELRLLYQ LVFLLSEAHT CIPENNGGAG CVCHLLMDDV VSADNYTLDL WAGQQLLWKG SFKPSEHVKP RAPGNLTVHT NVSDTLLLTW SNPYPPDNYL YNHLTYAVNI WSENDPADFR IYNVTYLEPS LRIAASTLKS GISYRARVRA WAQCYNTTWS EWSPSTKWHN SYREPFEQH
Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.
Biological Activity: 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.
Note:
100μg is the largest vial size for this product. Larger sizes supplied as multiple 50μg and/or 100μg vials.
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