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

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When Recombinant Human IL-4 (204-IL/CF) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-4R alpha His-tag Avi-tag Protein (Catalog # AVI11165) binds with an ED50 of 70.0-560 ng/mL.
When Recombinant Human IL-4 (204-IL/CF) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-4R alpha His-tag Avi-tag Protein (Catalog # AVI11165) binds with an ED50 of 70.0-560 ng/mL.
2 μg/lane of Recombinant Human IL-4R alpha His-tag Avi-tag Protein (Catalog # AVI11165) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-4  (Catalog # 204-IL/CF) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-4R alpha His-tag Avi-tag (Catalog # AVI11165) binds with an ED50 of 70.0-560 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-4R alpha protein
Human IL-4R
(Gly24-His232)
Accession # P24394.1		6-His tagAvi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Gly24
Structure / Form
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
  • Bioactivity
Theoretical MW
26 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
39-52 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 His-tag 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-4 Ra), also known as CD124 and BSF receptor, is a widely expressed 140 kDa transmembrane glycoprotein in the class I cytokine receptor family. IL-4 Ra 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 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 (6, 7). Within the ECD, human IL-4 Ra shares 51% aa sequence identity with mouse and rat IL-4 Ra. Soluble forms of IL-4 Ra, generated by alternate splicing or proteolysis, retain ligand binding properties and inhibit IL-4 bioactivity (8-11). IL-4 Ra 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 Ra1 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). Our Avi-tag Biotinylated human IL-4R alpha features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
  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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