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Recombinant Human IL-4R alpha Fc Chimera Avi-tag Protein, CF

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When Biotinylated Recombinant Human IL-4R alpha Fc Chimera Avi-tag (Catalog # AVI7700) is captured on EvenCoat Streptavidin Coated Plates (Catalog # CP004), the concentration of Recombinant Human IL-4 (Catalog ...read more
2 μg/lane of Biotinylated Recombinant Human IL-4R alpha Fc Chimera Avi-tag (Catalog # AVI7700) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity, Bioactivity
Format
Carrier-Free

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Recombinant Human IL-4R alpha Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. 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 5-30 ng/mL in the presence 0.2 ng/mL of Recombinant Human IL‑4 (Catalog # 204-IL). Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human IL-4R alpha Fc Chimera Avi-tag (Catalog # AVI7700) is captured on EvenCoat Streptavidin Coated Plates (Catalog # CP004), the concentration of Recombinant Human IL-4 (Catalog # 204-IL) that produces 50% of the optimal binding response is approximately 3-20 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-4R alpha protein
Human IL-4R alpha
(Gly24-His232)
Accession # P24394.1
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
Accession #
N-terminal Sequence
Gly24
Structure / Form

Disulfide-linked homodimer, Biotinylated via Avi-tag

Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity2
  • Bioactivity
  • Bioactivity2
Theoretical MW
52 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
73-82 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
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 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 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 Fc Chimera Avi-tag 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-4R alpha ), also known as CD124 and BSF receptor, is a widely expressed 140 kDa transmembrane glycoprotein in the class I cytokine receptor family. IL-4R 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-4R 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-4R alpha shares 51% aa sequence identity with mouse and rat IL-4R alpha . Soluble forms of IL-4R alpha , generated by alternate splicing or proteolysis, retain ligand binding properties and inhibit IL-4 bioactivity (8-11). IL-4R 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-13R 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).
  1. Wills-Karp, M. and F.D. Finkelman (2008) Sci. Signal. 1:pe55.
  2. Gordon, S. and F.O. Martinez (2010) Immunity 32:593.
  3. Kuperman, D.A. and R.P. Schleimer (2008) Curr. Mol. Med. 8:384.
  4. Li, Z. et al. (2009) Cell. Mol. Immunol. 6:415.
  5. Lee, Y.W. et al. (2010) Biomol. Ther. 18:135.
  6. Idzerda, R.L. et al. (1990) J. Exp. Med. 171:861.
  7. Galizzi, J.P. et al. (1990) Int. Immunol. 2:669.
  8. Kruse, S. et al. (1999) Int. Immunol. 11:1965.
  9. Blum, H. et al. (1996) J. Immunol. 157:1846.
  10. Jung, T. et al. (1999) Int. Arch. Allergy Immunol. 119:23.
  11. Mosley, B. et al. (1989) Cell 59:335.
  12. Kondo, M. et al. (1993) Science 262:1874.
  13. Russell, S.M. et al. (1993) Science 262:1880.
  14. Hilton, D.J. et al. (1996) Proc. Natl. Acad. Sci. 93:497.
  15. Aman, M.J. et al. (1996) J. Biol. Chem. 271:29265.
  16. Ramalingam, T.R. et al. (2008) Nat. Immunol. 9:25.
  17. Overwijk, W.W. and K.S. Schluns (2009) Clin. Immunol. 132:153.

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