Recombinant Human IFN-alpha/beta R1 Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: IFN-alpha/beta R1
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).
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- 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.
Citation for Recombinant Human IFN-alpha/beta R1 Protein, CF
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.
1 Citation: Showing 1 - 1
Human Interferon-ε and interferon-? exhibit low potency and low affinity for cell surface IFNAR and the poxvirus antagonist B18R
Authors: BD Harris, J Schreiter, M Chevrier, JL Jordan, MR Walter
J. Biol. Chem., 2018;0(0):.
Sample Types: Whole Cells
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