Measured by its ability to inhibit IL-4-dependent proliferation of TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 2‑10 ng/mL in the presence 0.2 ng/mL of Recombinant Human IL‑4 (Catalog # 204-IL) .
Source
Spodoptera frugiperda, Sf 21 (stably transfected)-derived human IL-4R alpha protein Met1-His232
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
24 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
26-39 kDa, reducing conditions
Publications
Read Publication using 230-4RB in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-4R alpha Protein, CF
CD124 antigen
CD124
IL-4 R alpha
IL-4 receptor subunit alpha
IL4R alpha
IL-4R alpha
IL-4R subunit alpha
IL4R
IL-4Ra
IL4RACD124
IL-4R-alpha
interleukin 4 receptor
interleukin-4 receptor alpha chain
interleukin-4 receptor subunit alpha
Background
Interleukin 4 Receptor alpha (IL‑4 R alpha ), also known as CD124 and BSF receptor, is a widely expressed 140 kDa transmembrane glycoprotein in the class I cytokine receptor family. IL‑4 R alpha plays an important role in Th2‑biased immune responses, alternative macrophage activation, mucosal immunity, allergic inflammation, tumor progression, and atherogenesis (1‑5). Mature human IL‑4 R alpha 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 (6, 7). Within the ECD, human IL‑4 R alpha shares 51% aa sequence identity with mouse and rat IL‑4 R alpha . Soluble forms of IL‑4 R alpha , generated by alternate splicing or proteolysis, retain ligand binding properties and inhibit IL‑4 bioactivity (8‑11). IL‑4 R alpha is a component of two distinct receptor complexes and shows species selectivity between human and mouse (6). It can associate with the common gamma chain ( gamma c) to form the IL‑4 responsive type I receptor in which gamma c increases the affinity for IL‑4 and enables signaling (12, 13). It can alternatively associate with IL‑13 R alpha 1 to form the type II receptor which is responsive to both IL‑4 and IL‑13 (14, 15). 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 gamma c (i.e. IL‑2, IL‑7, IL‑9, IL‑15, and IL‑21) (16, 17).
Wills-Karp, M. and F.D. Finkelman (2008) Sci. Signal. 1:pe55.
Gordon, S. and F.O. Martinez (2010) Immunity 32:593.
Kuperman, D.A. and R.P. Schleimer (2008) Curr. Mol. Med. 8:384.
Li, Z. et al. (2009) Cell. Mol. Immunol. 6:415.
Lee, Y.W. et al. (2010) Biomol. Ther. 18:135.
Idzerda, R.L. et al. (1990) J. Exp. Med. 171:861.
Galizzi, J.P. et al. (1990) Int. Immunol. 2:669.
Kruse, S. et al. (1999) Int. Immunol. 11:1965.
Blum, H. et al. (1996) J. Immunol. 157:1846.
Jung, T. et al. (1999) Int. Arch. Allergy Immunol. 119:23.
Mosley, B. et al. (1989) Cell 59:335.
Kondo, M. et al. (1993) Science 262:1874.
Russell, S.M. et al. (1993) Science 262:1880.
Hilton, D.J. et al. (1996) Proc. Natl. Acad. Sci. 93:497.
Aman, M.J. et al. (1996) J. Biol. Chem. 271:29265.
Ramalingam, T.R. et al. (2008) Nat. Immunol. 9:25.
Overwijk, W.W. and K.S. Schluns (2009) Clin. Immunol. 132:153.
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