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Beschreibung

Interferon regulatory factor 3 (UniProt: Q14653, also known as IRF-3) is encoded by the IRF3 gene (Gene ID: 3661) in human. IRF-3 is a transcription factor that is constitutively expressed in a variety of tissues and plays a role in intracellular immune response against DNA and RNA viruses. It regulates the transcription of type I interferon genes (IFN-a and IFN-b) and interferon-stimulated genes by binding to an interferon-stimulated response element in their promoters. IRF-3 contains a DNA-binding domain (aa 5-111), nuclear export signal (aa 139-149), IRF-interacting domain, and a C-terminal serine-rich region that contains several phosphorylation sites. Although some of these serines are shown to be phosphorylated in the resting state, further phosphorylation of specific residues is required for its activation and nuclear translocation. In uninfected cells, IRF-3 is present in the cytoplasm, however, following infection, it undergoes phosphorylation on serine 385, serine 386, threonine 390, and serine 396. These phosphorylation events induce a conformational change that leads to its dimerization and nuclear localization where it associates with CREB binding protein to form dsRNA activated factor 1 that subsequently leads to the activation of type I interferons and ISG genes. Phosphorylation and subsequent activation of IRF-3 shown to be inhibited by vaccinia virus protein E3. Mutations in IRF3 gene have been linked to infection-induced, Herpes-specific acute encephalopathy that is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Clone AR-1 recognizes an epitope within the DNA-binding domain of IRF-3. It can detect resting IRF-3 as well as the activated form. (Ref.: Rustagi, A., et al. (2013). Methods. 59(2), 225-232, Honda, K., et al. (2006). Immunity. 25(3), 349-360).