Recombinant Mouse IL-13 R alpha 2 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit IL-13-dependent proliferation of TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.01‑0.03 µg/mL in the presence of 8 ng/mL of recombinant mouse IL-13.
Source
Mouse myeloma cell line, NS0-derived mouse IL-13 R alpha 2 protein
>95%, 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
63 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
85-90 kDa, reducing conditions
Publications
Read Publications using 539-IR 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
>95%, 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-13 R alpha 2 Fc Chimera Protein, CF
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 Ra2), also known as IL-13 Ra’, 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 mouse IL-13 Ra2 consists of a 313 amino acid (aa) extracellular domain with three fibronectin type-III domains, a WSxWS motif, a 21 aa transmembrane segment, and a 28 aa cytoplasmic domain (3). Within the ECD, mouse IL-13 Ra2 shares 64% and 94% aa sequence identity with human and rat IL-13 Ra2, respectively. A 40 kDa ‑ 50 kDa soluble form of mouse IL-13 Ra2 can be generated by alternate splicing or MMP-8 mediated shedding (4, 5). 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 Ra1 which then forms a signaling complex with IL-4 Ra (6, 7). IL-13 Ra2 functions as a decoy receptor by binding and internalizing IL-13 and preventing it from signaling through the IL-13 Ra1/IL-4 Ra complex (3, 8). IL‑13 Ra2 can also block IL-4 induced responses by inhibiting IL-4 bound IL-13 Ra1/IL-4 Ra receptor complexes even though it does not itself bind IL-4 (9, 10). Aside from its decoy function, IL‑13‑activated IL-13 Ra2 directly promotes the development of tissue fibrosis by inducing the transcription of TGF-beta (11). Soluble IL‑13 Ra2 retains ligand binding capability and attenuates responses to IL-13 but not to IL-4 (9, 12). The up‑regulation of transmembrane and soluble IL‑13 Ra2 during Th2-biased immune responses limits the extent of those responses (13 ‑ 15). IL‑13 Ra2 is expressed in some cancers, and its ability to block IL-13 and IL-4 contributes to tumorigenesis and metastasis (10, 16).
Wynn, T.A. (2003) Annu. Rev. Immunol. 21:425.
Tabata, Y. et al. (2007) Curr. Allergy Asthma Rep. 7:338.
Donaldson, D.D. et al. (1998) J. Immunol. 161:2317.
Tabata, Y. et al. (2006) J. Immunol. 177:7905.
Chen, W. et al. (2008) J. Allergy Clin. Immunol. 122:625.
Andrews, A.-L. et al. (2006) J. Immunol. 176:7456.
Zurawski, S.M. et al. (1995) J. Biol. Chem. 270:13869.
Caput, D. et al. (1996) J. Biol. Chem. 271:16921.
Andrews, A.-L. et al. (2006) J. Allergy Clin. Immunol. 118:858.
Rahaman, S.O. et al. (2002) Cancer Res. 62:1103.
Fichtner-Feigl, S. et al. (2006) Nat. Med. 12:99.
Zhang, J.G. et al. (1997) J. Biol. Chem. 272:9474.
Chiaramonte, M.G. et al. (2003) J. Exp. Med. 197:687.
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