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 ED 50 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 | IEGRMD | Human 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
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).
- 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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