582J;IL4R;CD124;IL-4RA;IL4RA;IL-4 receptor subunit alpha;IL-4-binding protein;IL4-BP;IL-4R subunit alpha;IL-4R-alpha;Interleukin-4 receptor subunit alpha;582J2.1;IL-4RαIL 4R alpha;IL4R nirs variant 1;IL4RA;Interleukin 4 receptor;Interleukin 4 receptor alpha chain;sIL4Ralpha/prot;Soluble IL-4 receptor subunit alpha;Soluble IL-4R-alpha;Soluble interleukin-4 receptor subunit alpha

HEK293 Cells

Met26-Gln231

P24394

Human

50.2 kDa

60-70 kDa

C-Fc

Measured by its ability to inhibit IL-4-dependent proliferation of TF‑1 human erythroleukemic cells. The ED50 for this effect is 5-20 ng/ml.

> 95 % as determined by reducing SDS-PAGE.

< 1.0 EU per μg of the protein as determined by the LAL method.

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

This product is provided as lyophilized powder which is shipped with ice packs.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.

Please refer to the printed manual for detailed information.

Interleukin 4 Receptor alpha (IL4-Ra) is a widely expressed 140 kDa transmembrane glycoprotein in the class I cytokine receptor family. Mature human IL4-Ra consists of a 207 amino acid (aa) extracellular domain (ECD) that contains a cytokine binding region and one fibronectin type III domain; a 24 aa transmembrane segment; and a 569 aa cytoplasmic domain that contains one Box 1 motif and one ITIM motif. IL4-Ra plays an important role in Th2-biased immune responses; alternative macrophage activation; mucosal immunity; allergic inflammation; tumor progression; and atherogenesis. Soluble forms of IL4-Ra; generated by alternate splicing or proteolysis; retain ligand binding properties and inhibit IL-4 bioactivity. IL4-Ra is a component of two distinct receptor complexes and shows species selectivity between human and mouse. It can associate with the common gamma chain (γc) to form the IL-4 responsive type I receptor in which γc increases the affinity for IL-4 and enables signaling. It can alternatively associate with IL13-Ra1 to form the type II receptor which is responsive to both IL-4 and IL-13. The use of shared receptor components contributes to the overlapping biological effects of IL-4 and IL-13 as well as other cytokines that utilize γc.