Mouse IL-27 R alpha /WSX-1/TCCR Alexa Fluor® 647-conjugated Antibody
Mouse IL-27 R alpha /WSX-1/TCCR Alexa Fluor® 647-conjugated Antibody Summary
Gly29-Lys510
Accession # O70394
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of IL‑27 R alpha /WSX‑1/TCCR in Mouse Splenocytes by Flow Cytometry. Mouse splenocytes were stained with Rat Anti-Mouse IL-27 R alpha /WSX-1/TCCR Alexa Fluor® 647-conjugated Monoclonal Antibody (Catalog # FAB21091R, filled histogram) or isotype control antibody (Catalog # IC013R, open histogram). View our protocol for Staining Membrane-associated Proteins.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-27 R alpha/WSX-1/TCCR
IL‑27 R alpha (also known as WSX‑1 and TCCR) is a 85‑95 kDa member of the type I, group 2 cytokine receptor family (1‑6). Mature IL‑27 R alpha is a type I transmembrane glycoprotein that contains a 486 amino acid (aa) extracellular region, a 21 aa transmembrane segment and a 92 aa cytoplasmic domain. Consistent with type I cytokine receptors, the extracellular region contains four positionally conserved cysteine residues, a WSxWS motif (for receptor folding and ligand binding), and three fibronectin type III repeats. The intracellular domain contains a “box‑1” motif that may be involved with Janus kinases (3). In mouse, a soluble 33 kDa splice form that shows a 20 aa substitution for aa 251‑623 has been identified (7). The mouse IL‑27 R alpha extracellular region shares 63% amino acid identity with the human IL‑27 R alpha extracellular domain (2, 3). IL‑27 R alpha is expressed in mast cells, endothelial cells, NK cells, macrophages, monocytes, B cells, dendritic cells, and naïve T cells (1, 2, 4, 8). Typical of other class I cytokine receptor chains, the ligand binding IL‑27 R alpha molecule is known to heterodimerize with a signal‑transducing subunit (gp130) to form a functional IL‑27 receptor (9, 10). In addition, IL‑27 R alpha is reported to complex with CNTFR alpha and gp130 form a humanin receptor on neurons (7, 11), and to complex with gp130 and IL‑6 R to form a receptor for a p28:CLF heterodimeric cytokine on lymphocytes (12). Studies using IL‑27 R alpha /WSX‑1-/- mice reveal that IL‑27 has the ability to suppress T cell activity during infection, and to mediate an inhibition of both type 1 and type 2 T cell immunity (4, 13, 14). In particular, IL‑27 is known to act on naïve T cells, blocking their differentiation into a Th17 phenotype. Notably, cells committed to a Th17 phenotype, although they express a functional IL‑27 receptor, are unresponsive to the effects of IL‑27 (15). Activated T cells that are CD4+ and CD8+, and which express the IL‑27 receptor, can be induced by IL‑27 to form a double‑positive CD25+ FoxP3- IFN‑ gamma plus IL‑10 secreting phenotype that both promotes and suppresses the inflammatory response (16).
- Villarino, A.V. et al. (2004) J. Immunol. 173:715.
- Chen, Q. et al. (2000) Nature 407:916.
- Sprecher, C.A. et al. (1998) Biochem. Biophys. Res. Commun. 246:82.
- Artis, D. et al. (2004) J. Immunol. 173:5626.
- Yoshida, H. and Y. Miyazaki (2008) Int. J. Biochem. Cell Biol. 40:2379.
- Yoshida, H. and M. Yoshiyuki (2008) Immunol. Rev. 226:234.
- Hashimoto, Y. et al. (2009) Biochem. Biophys. Res. Commun. 389:95
- Holscher, C. et al. (2005) J. Immunol. 174:3534.
- Pflanz, S. et al. (2004) J. Immunol. 172:2225.
- Scheller, J. et al. (2005) Biochem. Biophys. Res. Commun. 326:724.
- Hashimoto, Y. et al. (2009) Mol. Biol. Cell 20:2864.
- Crabe, S. et al. (2009) J. Immunol. 183:7692.
- Villarino, A. et al. (2003) J. Immunol. 170:645.
- Hamano., S. et al. (2003) Immunity 19:657.
- El-behi, M. et al. (2009) J. Immunol. 183:4957.
- Fitzgerald, D.C. et al. (2007) Nat. Immunol. 8:1372.
Product Datasheets
Product Specific Notices
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.
Citation for Mouse IL-27 R alpha /WSX-1/TCCR Alexa Fluor® 647-conjugated Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Interleukin-35 Prevents Development of Autoimmune Diabetes Possibly by Maintaining the Phenotype of Regulatory B Cells
Authors: Zhengkang Luo, Sara Lundin, Mariela Mejia-Cordova, Imane Hassani, Martin Blixt, Daisy Hjelmqvist et al.
International Journal of Molecular Sciences
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