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Recombinant Human IL-13 R alpha2 Fc Alexa Fluor® 647 Protein

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Streptavidin coated beads conjugated to biotinylated anti-human IL‑13 R alpha 2 Polyclonal Antibody (BAF614) were stained with the indicated concentrations of Recombinant Human IL‑13 R alpha 2 Fc Chimera Alexa ...read more

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Summary
Reactivity HuSpecies Glossary

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Recombinant Human IL-13 R alpha2 Fc Alexa Fluor® 647 Protein Summary

Details of Functionality
Measured by flow cytometry for its ability to bind anti-human&nbsp;IL‑13&nbsp;R alpha 2&nbsp;Antibody conjugated beads. The concentration of&nbsp;Recombinant Human IL‑13&nbsp;R alpha 2 Fc&nbsp;Chimera Alexa Fluor® 647&nbsp;(Catalog # AFR7147) that produces 50% of the binding response is 1.50-15.0 ng/mL.<br /><br />
Accession #
N-terminal Sequence
Cys22
Structure / Form
Disulfide-linked homodimer
Labeled with Alexa Fluor® 647
Excitation Wavelength: 650 nm
Emission Wavelength: 668 nm
Protein/Peptide Type
Recombinant Proteins
Endotoxin Note
<1.000 EU per 1 µg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
64 kDa (monomer).
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
75-95 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Buffer
Supplied as a 0.2 μm filtered solution in PBS with BSA as a carrier protein.

Notes


This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-13 R alpha2 Fc Alexa Fluor® 647 Protein

  • cancer/testis antigen 19
  • CD213a2 antigen
  • CD213a2
  • CT19
  • IL-13 R alpha 2
  • IL-13 receptor subunit alpha-2
  • IL13BP
  • IL13R alpha 2
  • IL-13R subunit alpha-2
  • IL13R
  • IL-13R
  • IL13RA2
  • IL-13Ra2
  • IL-13R-alpha-2
  • interleukin 13 binding protein
  • interleukin 13 receptor alpha 2 chain
  • interleukin 13 receptor, alpha 2
  • interleukin-13 receptor subunit alpha-2
  • Interleukin-13-binding protein

Background

Interleukin‑13 Receptor alpha 2 (IL‑13 R alpha 2), also known as IL‑13 binding protein, and CD213a2, is a widely expressed 55 kDa cytokine receptor that plays an important role in the Th2‑polarized immune responses characteristic of a variety of pathologies, including parasitic infections and allergic asthma (1, 2). Mature human IL‑13 R alpha 2 consists of a 317 amino acid (aa) extracellular domain with three fibronectin type‑III domains, a WSxWS motif, a 20 aa transmembrane segment, and a 17 aa cytoplasmic domain (3). Within the ECD, human IL‑13 R alpha 2 shares 64% and 62% aa sequence identity with mouse and rat IL‑13 R alpha 2, respectively. In both mouse and human, a 40 kDa‑50 kDa soluble form of IL‑13 R alpha 2 can be generated by MMP‑8 mediated shedding in vitro (4).  Although this is assumed to occur in vivo in mouse, there is no evidence that shedding occurs in human (5‑7).  In mouse, alternative splicing also leads to sIL‑13 R alpha 2, but again, this phenomenon apparently does not occur in human (6‑7).  Thus, the biological effects of human IL‑13 R alpha 2 would appear to be mediated exclusively by membrane IL‑13 R alpha 2 (7). The biological effects of IL‑13 and IL‑4 are closely related in part due to a shared receptor system. IL‑13 binds to IL‑13 R alpha 1 which then forms a signaling complex with IL‑4 R alpha (8, 9). IL‑13 R alpha 2 functions as a decoy receptor by binding and internalizing IL‑13 and preventing it from signaling through the IL‑13 R alpha 1/IL‑4 R alpha complex (3, 10). IL‑13 R alpha 2 can also block IL‑4 induced responses by inhibiting IL‑4 bound IL‑13 R alpha 1/IL‑4 R alpha receptor complexes even though it does not itself bind IL‑4 (11, 12). Aside from its decoy function, IL‑13‑activated IL‑13 R alpha 2 directly promotes the development of tissue fibrosis by inducing the transcription of TGF‑ beta (13). Presumably, any human soluble IL‑13 R alpha 2, if it exists, will retain its ligand binding capability and attenuate responses to IL‑13 but not to IL‑4 (11, 14). The up‑regulation of transmembrane during Th2‑biased immune responses limits the extent of those responses (15‑17).
  1. Wynn, T.A. (2003) Annu. Rev. Immunol. 21:425.
  2. Tabata, Y. et al. (2007) Curr. Allergy Asthma Rep. 7:338.
  3. Caput, D. et al. (1996) J. Biol. Chem. 271:16921.
  4. Chen, W. et al. (2008) J. Allergy Clin. Immunol. 122:625.
  5. O’Toole, M. et al. (2008) Clin. Exp. Allergy 38:594.
  6. Chen, W. et al. (2009) J. Immunol. 183:7870.
  7. Kasaian, M.T. et al. (2011) J. Immunol. 187:561.
  8. Andrews, A.-L. et al. (2006) J. Immunol. 176:7456.
  9. Zurawski, S.M. et al. (1995) J. Biol. Chem. 270:13869.
  10. Donaldson, D.D. et al. (1998) J. Immunol. 161:2317.
  11. Andrews, A.-L. et al. (2006) J. Allergy Clin. Immunol. 118:858.
  12. Rahaman, S.O. et al. (2002) Cancer Res. 62:1103.
  13. Fichtner-Feigl, S. et al. (2006) Nat. Med. 12:99.
  14. Zhang, J.G. et al. (1997) J. Biol. Chem. 272:9474.
  15. Chiaramonte, M.G. et al. (2003) J. Exp. Med. 197:687.
  16. Morimoto, M. et al. (2009) J. Immunol. 183:1934.
  17. Zheng, T. et al. (2008) J. Immunol. 180:522.

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