Recombinant Human IFN-alpha/beta R1 Fc Avi-tag Protein, CF Summary
Additional Information |
Fc Chimera |
Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated
Recombinant Human IFN-alpha / beta R1
Fc Chimera Avi-tag (Catalog # AVI11574) binds Recombinant Human IFN-alpha / beta R2 Fc Chimera (Catalog #
4015-AB) in the presence of Recombinant Human IFN-beta (Catalog #
8499-IF) with an ED 50 of 5.00-60.0 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human IFN-alpha/beta R1 protein Human IFN-A/B R1 (Gly26-Lys436) Accession # AAA52730.1 | GGIEGRMD | Human IgG1 Fc (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
N-terminal Sequence |
Gly26 |
Structure / Form |
Disulfide-linked homodimer Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
76 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 |
95-125 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 500 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 Fc Avi-tag Protein, CF
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). Our Avi-tag Biotinylated human IFN‑ alpha / beta R1 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
- Hwang, S.Y. et al. (1995) Proc. Natl. Acad. Sci. USA 92:11284.
- Takaoka, A. et al. (2000) Science 288:2357.
- Uze, G. et al. (1990) Cell 60:225.
- Lamken, P. et al. (2004) J. Mol. Biol. 341:303.
- Arduini, R.M. et al. (1999) Prot. Sci. 8:1867.
- Kalie, E. et al. (2008) J. Biol. Chem. 283:32925.
- Platanias, L.C. (2005) Nat. Rev. Immunol. 5:375.
- Claudinon, J. et al. (2009) J. Biol. Chem. 284:24328.
- Zheng, H. et al. (2011) Blood 118:4003.
- Qian, J. et al. (2011) PLoS Pathogens 7:e1002065.
- Bhattacharya, S. et al. (2010) J. Biol. Chem. 285:2318.
- Bhattacharya, S. et al. (2011) J. Biol. Chem. 286:22069.
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