IL-4 receptor alfa (CD124), oplosbaar

IL-4 can signal through type I and type II receptor complexes, which share a common gamma chain. The type I receptor contains, in addition to the gamma chain, an IL-4R alpha subunit, whereas the type II receptor contains the IL-13R alpha. The secreted extracellular domain of IL-4R alpha, called sIL-4R alpha, 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. Recombinant Human sIL-4 Receptor alpha is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4R alpha. 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.

Soluble Interleukin-4Rα, soluble IL-4 Receptor alpha, CD124

3566

P24394

NP_000409.1

NM_000418

16p12.1-p11.2

Human

Human

GNMKVLQEPT CVSDYMSIST CEWKMNGPTN CSTELRLLYQ LVFLLSEAHT CIPENNGGAG CVCHLLMDDV VSADNYTLDL WAGQQLLWKG SFKPSEHVKP RAPGNLTVHT NVSDTLLLTW SNPYPPDNYL YNHLTYAVNI WSENDPADFR IYNVTYLEPS LRIAASTLKS GISYRARVRA WAQCYNTTWS EWSPSTKWHN SYREPFEQH

< 0.1 ng/µg of protein (< 1EU/µg)

> 95% by SDS-PAGE & 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.

209

Lyophilized

23.9 kDa

CHO cells