Recombinant Cynomolgus Monkey IFN-alpha/beta R1 Protein, CF Summary
Ala23-Ile439, with a C-terminal 6-His tag
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 with Trehalose.|
|Reconstitution||Reconstitute at 500 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.
When Recombinant Cynomolgus Monkey IFN‑ alpha / beta R1 His-tags protein is immobilized at 10 µg/mL (100 µL/well), Recombinant Human IFN-A2 binds with an ED50 of 1-6 ug/mL.
2 μg/lane of Recombinant Cynomolgus Monkey IFN-alpha/beta R1 Protein, CF (Catalog # 10674-AB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 80-100 kDa.
Background: IFN-alpha/beta R1
Interferon-alpha/beta receptor 1 (IFN-alpha / beta R1), also known as IFNAR1, is a member of the class II cytokine receptor family of proteins. These proteins form heterodimeric receptor complexes that mediate class II cytokine signals and subunits of the different receptor complexes are shared and serve multiple functions (1). Mature human IFN-alpha / beta R1 consists of an extracellular domain (ECD) with three tandem fibronectin type III repeats, a transmembrane segment, and a cytoplasmic domain (2). Within the ECD, human IFN-alpha / beta R1 shares 47% and 50% amino acid sequence 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, 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 (3, 4). 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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