|Description||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 which corresponds to the entire extracellular domain of IL-4Rα.|
|BiologicalActivity||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.|
|Authenticity||Verified by N-terminal and Mass Spectrometry analyses (when applicable).|
|Endotoxin||Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg).|
|Protein Content||Verified by UV Spectroscopy and/or SDS-PAGE gel.|
|Precautions||Recombinant Human sIL-4Rα is for research use only and not for use in diagnostic or therapeutic procedures.|
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