Human IL-27 R alpha /WSX-1/TCCR Antibody

Catalog # Availability Size / Price Qty
AF1479
AF1479-SP
Product Details
Citations (2)
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Human IL-27 R alpha /WSX-1/TCCR Antibody Summary

Species Reactivity
Human
Specificity
Detects human IL-27 R alpha /WSX‑1/TCCR in direct ELISAs and Western blots. In direct ELISAs, approximately 20% cross‑reactivity with recombinant mouse TCCR is observed.
Source
Polyclonal Goat IgG
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. See Certificate of Analysis for details.
*Small pack size (-SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human IL-27 R alpha /WSX‑1/TCCR Fc Chimera (Catalog # 1479-TC)
Immunohistochemistry
5-15 µg/mL
Immersion fixed paraffin-embedded sections of human lymph node

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.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.

Background: IL-27 R alpha/WSX-1/TCCR

IL‑27 R alpha (also known as WSX‑1 and TCCR) is a 96‑100 kDa member of the type I, group 2 cytokine receptor family (1, 2, 3, 4, 5, 6). Mature IL‑27 R alpha  is a type I transmembrane glycoprotein that contains a 484 amino acid (aa) extracellular region, a 21 aa transmembrane segment and a 99 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). One potential alternate splice form has been hypothesized that involves a 58 aa addition to the cytoplasmic domain and, based on mouse, a soluble 33 kDa splice form that shows a 20 aa substitution for aa 257‑636 may also occur in human (3, 7). The human IL‑27 R alpha extracellular region shares 63% amino acid identity with the mouse 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).

References
  1. Villarino, A.V. et al. (2004) J. Immunol. 173:715.
  2. Chen, Q. et al. (2000) Nature 407:916.
  3. Sprecher, C.A. et al. (1998) Biochem. Biophys. Res. Commun. 246:82.
  4. Artis, D. et al. (2004) J. Immunol. 173:5626.
  5. Yoshida, H. & Y. Miyazaki (2008) Int. J. Biochem. Cell Biol. 40:2379.
  6. Yoshida, H. & M. Yoshiyuki (2008) Immunol. Rev. 226:234.
  7. Hashimoto, Y. et al. (2009) Biochem. Biophys. Res. Commun. 389:95.
  8. Holscher, C. et al. (2005) J. Immunol. 174:3534.
  9. Pflanz, S. et al. (2004) J. Immunol. 172:2225.
  10. Scheller, J. et al. (2005) Biochem. Biophys. Res. Commun. 326:724.
  11. Hashimoto, Y. et al. (2009) Mol. Biol. Cell 20:2864.
  12. Crabe, S. et al. (2009) J. Immunol. 183:7692.
  13. Villarino, A. et al. (2003) J. Immunol. 170:645.
  14. Hamano., S. et al. (2003) Immunity 19:657.
  15. El-behi, M. et al. (2009) J. Immunol. 183:4957.
  16. Fitzgerald, D.C. et al. (2007) Nat. Immunol. 8:1372.
Long Name
Interleukin-27 Receptor Subunit alpha
Entrez Gene IDs
9466 (Human); 50931 (Mouse)
Alternate Names
class I cytokine receptor; CRL1IL-27R; Cytokine receptor-like 1; IL-27 R alpha; IL27R alpha; IL27R; IL27RA; IL-27Ra; IL-27R-alpha; interleukin 27 receptor, alpha; interleukin-27 receptor subunit alpha; TCCR; TCCRIL-27 receptor subunit alpha; T-cell cytokine receptor type 1; Type I T-cell cytokine receptor; WSX-1; WSX1IL-27R subunit alpha; zcytor1

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Citations for Human IL-27 R alpha /WSX-1/TCCR 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.

2 Citations: Showing 1 - 2
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  1. A soluble form of IL-27Ralpha is a natural IL-27 antagonist.
    Authors: Dietrich C, Candon S, Ruemmele F, Devergne O
    J Immunol, 2014-04-25;192(11):5382-9.
    Species: Primate - Chlorocebus aethiops (African Green Monkey)
    Sample Types: Cell Lysates
    Applications: Immunoprecipitation
  2. IL-27 abrogates receptor activator of NF-kappa B ligand-mediated osteoclastogenesis of human granulocyte-macrophage colony-forming unit cells through STAT1-dependent inhibition of c-Fos.
    Authors: Furukawa M, Takaishi H, Takito J, Yoda M, Sakai S, Hikata T, Hakozaki A, Uchikawa S, Matsumoto M, Chiba K, Kimura T, Okada Y, Matsuo K, Yoshida H, Toyama Y
    J. Immunol., 2009-07-20;183(4):2397-406.
    Species: Human
    Sample Types: Whole Cells
    Applications: ICC

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