Recombinant Human IFN-alpha/beta R1 Fc Chimera Protein, CF

Recombinant Human IFN-alpha/beta R1 Fc Chimera Protein (Catalog # 11574-AB) binds Recombinant Human LRPAP (4296-LR) with an ED50 of 0.750-9.00 μg/mL.

2 μg/lane of Recombinant Human IFN-alpha/beta R1 Fc Chimera Protein (Catalog # 11574-AB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 105-120 kDa and 210-240 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

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

• Details of Functionality: Measured by its binding ability in a functional ELISA.

  Recombinant Human IFN-alpha/beta R1 Fc Chimera (Catalog # 11574-AB) binds Recombinant Human LRPAP (Catalog # 4296-LR) with an ED₅₀ of 0.750-9.00 μg/mL.

• Source: Human embryonic kidney cell, HEK293-derived human IFN-alpha/beta R1 protein
  

  Human IFNAR1 (Lys28-Lys436) Accession # AAA52730.1	GGIEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Structure / Form: Disulfide linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 74 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: 105-120 kDa, under 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 with Trehalose.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

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 Fc Chimera 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.