Recombinant Human sIL-4 Receptor Alpha (CHO derived)(Discontinued)
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| Amount : | 20 µg |
| Purification : | Purity:>= 95% 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 Interleukin-4RAlpha , soluble IL-4 Receptor alpha, CD124 |
Source: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. The 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.
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. The 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.
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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