rmIFN-a/b R1, CF (50 ug)

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 mouse IFN‑ alpha / beta  R1 consists of a 403 aa extracellular domain (ECD), a 20 aa transmembrane segment, and a 141 aa cytoplasmic domain (4). The ECD contains three tandem fibronectin type III repeats and is extensively glycosylated. Within the ECD, mouse IFN‑ alpha / beta  R1 shares 47% and 68% aa identity with human and rat IFN‑ alpha / beta  R1, respectively. 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).