The interferon regulatory factor (IRF) family of transcription factors control the expression of several interferon genes, and are involved in the JAK-STAT signaling pathway. Interferon regulatory factor-3 (IRF-3) was discovered based on its homology to IRF-1 and IRF-2. IRF3 is produced as an inactive cytoplasmic form that dimerizes and forms a complex with CREB-binding protein, after phosphorylation of Ser-386. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes. IRF-3 plays an important role in the innate immune system's response to viral infection. Double-stranded RNA (dsRNA) and toll-like receptor (TLR) signaling can also induce dimerization and phosphorylation of IRF-3. IRF-3 has been shown to induce significant apoptosis in primary macrophages.
These products are affinity-purified IgG antibodies that recognize human IRF-3 protein. The antibodies were raised in rabbit using synthetic peptides, and can be used for Western blot (WB) detection, immunohistochemical (IHC) detection, or immunoprecipitation (IP) of human IRF-3 protein.
