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Recombinant Mouse IFN-alpha/beta R1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse IFN-alpha/beta R1 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit Limitin-mediated protection of L‑929 mouse fibroblast cells viral lysis. The ED50 for this effect is 0.3-1.2 µg/mL in the presence of 30 pg/mL of Recombinant Mouse Limitin/IFN‑ zeta (Catalog # 1535-LM).
Source
Mouse myeloma cell line, NS0-derived mouse IFN-alpha/beta R1 protein
Glu27-Thr429, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Glu27
Protein/Peptide Type
Recombinant Proteins
Gene
Ifnar1
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
  • Bioactivity
Theoretical MW
47.1 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
60-70 kDa, 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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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 IFN-alpha/beta R1 Protein, CF

  • alpha-type antiviral protein
  • AVP
  • beta-type antiviral protein
  • CRF2-1
  • Cytokine receptor class-II member 1
  • Cytokine receptor family 2 member 1
  • human interferon-alpha receptor (HuIFN-alpha-Rec)10IFRC
  • IFN-alpha/beta R1
  • IFN-alpha/beta receptor 1
  • IFN-alpha-REC
  • IFNAR
  • IFNAR1
  • IFN-aR1
  • IFNBR
  • IFNbR1
  • IFN-bR1
  • IFN-R-1
  • interferon (alpha, beta and omega) receptor 1
  • interferon alpha/beta receptor 1
  • interferon-alpha/beta receptor alpha chain
  • interferon-beta receptor 1
  • Type I interferon receptor 1

Background

Interferon‑alpha/beta receptor 1 (IFN‑ alpha / beta  R1), also known as IFNAR1, is a 100‑130 kDa member of the class II cytokine receptor family of proteins. These proteins form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions (1). IFN‑ alpha / beta  R1, in association with IFN‑ alpha / beta R2, is required for propagating anti‑microbial signal transduction triggered by the type 1 interferons such as IFN‑ alpha and IFN‑ beta (2, 3). Mature mouse IFN‑ alpha / beta  R1 consists of a 403 aa extracellular domain (ECD), a 20 aa transmembrane segment, and a 141 aa cytoplasmic domain (4). The ECD contains three tandem fibronectin type III repeats and is extensively glycosylated. Within the ECD, mouse IFN‑ alpha / beta  R1 shares 47% and 68% aa identity with human and rat IFN‑ alpha / beta  R1, respectively. IFN‑ alpha / beta  R1 interacts very weakly or not at all with type 1 interferons and does not stably interact with IFN‑ alpha / beta  R2. Ligands preferentially associate with IFN‑ alpha / beta  R2, and this complex subsequently forms a stable ternary assembly with IFN‑ alpha / beta  R1 (5‑7). IFN‑ alpha / beta ‑R1 also associates with IFN‑ gamma  R2 even in the absence of IFN‑ gamma stimulation (3). IFN‑ alpha / beta  R1 activation depends on tyrosine phoshorylation as well as palmitoylation of its cytoplasmic domain (8, 9). Rapid down‑regulation of the receptor is accomplished by ligand‑dependent or -independent pathways (e.g. VEGF R signaling, TLR signaling, or cellular stress) which induce its serine phosphorylation, ubiquitination, and degradation (10‑13).
  1. Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
  2. Hwang, S.Y. et al. (1995) Proc. Natl. Acad. Sci. USA 92:11284.
  3. Takaoka, A. et al. (2000) Science 288:2357.
  4. Uze, G. et al. (1992) Proc. Natl. Acad. Sci. USA 89:4774.
  5. Lamken, P. et al. (2004) J. Mol. Biol. 341:303.
  6. Arduini, R.M. et al. (1999) Prot. Sci. 8:1867.
  7. Kalie, E. et al. (2008) J. Biol. Chem. 283:32925.
  8. Platanias, L.C. (2005) Nat. Rev. Immunol. 5:375.
  9. Claudinon, J. et al. (2009) J. Biol. Chem. 284:24328.
  10. Zheng, H. et al. (2011) Blood 118:4003.
  11. Qian, J. et al. (2011) PLoS Pathogens 7:e1002065.
  12. Bhattacharya, S. et al. (2010) J. Biol. Chem. 285:2318.
  13. Bhattacharya, S. et al. (2011) J. Biol. Chem. 286:22069.

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Bioinformatics

Gene Symbol Ifnar1
Uniprot