Recombinant Human sIL-4 Receptor Alpha (HEK293 derived)(Discontinued)
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Amount : | 15 µg |
Purification : | Purity:>= 98% by SDS-PAGE gel and HPLC analyses. |
Content : | This recombinant protein is supplied in lyophilized form. |
AA sequence : | GNMKVLQEPT CVSDYMSIST CEWKMNGPTN CSTELRLLYQ LVFLLSEAHT CIPENNGGAG CVCHLLMDDV VSADNYTLDL WAGQQLLWKG SFKPSEHVKP RAPGNLTVHT NVSDTLLLTW SNPYPPDNYL YNHLTYAVNI WSENDPADFR IYNVTYLEPS LRIAASTLKS GISYRARVRA WAQCYNTTWS EWSPSTKWHN SYREPFEQH |
Alternative Name : | soluble IL-4 receptor alpha, CD124 |
Source:HEK293 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 Gamma chain 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 naive CD4 T cells and class switching to IgG1 and IgE. Recombinant Human sIL-4RAlpha is a 209 amino acid protein that corresponds to the entire extracellular domain of IL-4RAlpha .
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 Gamma chain 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 naive CD4 T cells and class switching to IgG1 and IgE. Recombinant Human sIL-4RAlpha is a 209 amino acid protein that corresponds to the entire extracellular domain of IL-4RAlpha .
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.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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