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Recombinant Human IFN-alpha/beta R1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IFN-alpha / beta R1 is present at 10 μg/mL, it binds to Recombinant Human IFN‑ alpha / beta  R2 Fc Chimera (Catalog # 4015-AB) in the presence of recombinant human IFN-alpha 2. The concentration of Recombinant Human IFN-alpha / beta R2 Fc Chimera that produces 50% of the optimal binding response is approximately 0.5-1.5 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human IFN-alpha/beta R1 protein
Gly26-Lys436
Accession #
N-terminal Sequence
Gly26
Protein/Peptide Type
Recombinant Proteins
Gene
IFNAR1
Purity
>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
47.2 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
70-90 kDa, reducing conditions
Publications
Read Publication using
245-AB in the following applications:

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 under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human 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 human IFN‑ alpha / beta  R1 consists of a 409 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 100 aa cytoplasmic domain (4). The ECD contains three tandem fibronectin type III repeats and is extensively glycosylated. Within the ECD, human IFN‑ alpha / beta  R1 shares 47% and 50% aa identity with mouse and rat  IFN‑ alpha / beta  R1, respectively. Alternative splicing generates two additional isoforms that lack the transmembrane segment and either all or a portion of the cytoplasmic domain. 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. (1990) Cell 60:225.
  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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245-AB
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Applications: Bioactivity

Publications for IFN-alpha/beta R1 (245-AB)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol IFNAR1
Uniprot