Recombinant Mouse IL-4R alpha Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit the IL-4-dependent proliferation of HT‑2 mouse T cells. Tsang, M. et al. (1995) Cytokine 7:389. The ED50 for this effect is 0.05‑0.2 µg/mL in the presence of 3 ng/mL of recombinant mouse IL-4.
Source
Mouse myeloma cell line, NS0-derived mouse IL-4 R alpha protein
Mouse IL-4 R alpha (Ile26 - Arg233) Accession # Q544A9
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
51 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
65-85 kDa, reducing conditions
Publications
Read Publications using 530-MR 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
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse IL-4R alpha Fc Chimera 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 mouse IL-4 R alpha consists of a 208 amino acid (aa) extracellular domain (ECD) that contains a ligand binding region and one fibronectin type-III domain, a 24 aa transmembrane segment, and a 553 aa cytoplasmic domain that contains one Box 1 motif and one ITIM motif (6). Within the ECD, mouse IL-4 R alpha shares 51% and 76% aa sequence identity with human and rat IL-4 R alpha , respectively. Alternate splicing of mouse IL-4 R alpha generates a secreted isoform and an isoform that lacks the cytoplasmic region (6 - 8). Proteolytic cleavage can also release soluble IL-4 R alpha , and both these mechanisms produce a molecule which retains ligand binding properties and inhibits IL-4 bioactivity (6, 7, 9). IL-4 R alpha is a component of two distinct receptor complexes and shows species selectivity between human and mouse (10). 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 (11, 12). 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 (13, 14). 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) (15, 16).
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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.
Mosley, B. et al. (1989) Cell 59:335.
Blum, H. et al. (1996) J. Immunol. 157:1846.
Wrighton, N. et al. (1992) Growth Factors 6:103.
Jung, T. et al. (1999) Int. Arch. Allergy Immunol. 119:23.
Idzerda, R.L. et al. (1990) J. Exp. Med. 171:861.
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.
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Overwijk, W.W. and K.S. Schluns (2009) Clin. Immunol. 132:153.
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