#79945 Phospho-IRF-3 (Ser379) (E6F7Q) Rabbit mAb
|Phospho-IRF-3 (Ser379) (E6F7Q) Rabbit mAb recognizes endogenous levels of IRF-3 protein only when phosphorylated at Ser379 in mice (equivalent to Ser386 of human IRF-3). This antibody cross-reacts wtih a 75 kDa protein of unknown origin.|
|Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser379 of mouse IRF-3 protein.|
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Western blot analysis of extracts from Raw 264.7 cells, untreated (-) or treated with cGAMP (10 μg/ml, 6 hr; +), using Phospho-IRF-3 (Ser379) (E6F7Q) Rabbit mAb (upper) or IRF-3 (D83B9) Rabbit mAb #4302 (lower).
Immunoprecipitation of Phospho-IRF-3 (Ser379) from Raw 264.7 cell extracts treated with poly(dA:dT) (2 μg/ml, 6 hr). Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is Phospho-IRF-3 (Ser379) (E6F7Q) Rabbit mAb. Western blot analysis was performed using Phospho-IRF-3 (Ser379) (E6F7Q) Rabbit mAb. Mouse Anti-rabbit IgG (Conformation Specific) (L27A9) mAb (HRP Conjugate) #5127 was used for detection.
Interferon regulatory factors (IRFs) comprise a family of transcription factors that function within the Jak/Stat pathway to regulate interferon (IFN) and IFN-inducible gene expression in response to viral infection (1). IRFs play an important role in pathogen defense, autoimmunity, lymphocyte development, cell growth, and susceptibility to transformation. The IRF family includes nine members: IRF-1, IRF-2, IRF-9/ISGF3γ, IRF-3, IRF-4 (Pip/LSIRF/ICSAT), IRF-5, IRF-6, IRF-7, and IRF-8/ICSBP. All IRF proteins share homology in their amino-terminal DNA-binding domains. IRF family members regulate transcription through interactions with proteins that share similar DNA-binding motifs, such as IFN-stimulated response elements (ISRE), IFN consensus sequences (ICS), and IFN regulatory elements (IRF-E) (2).
IRF-3 can inhibit cell growth and plays a critical role in controlling the expression of genes in the innate immune response (1-4). In unstimulated cells, IRF-3 is present in the cytoplasm. Viral infection results in phosphorylation of IRF-3 and leads to its translocation to the nucleus, where it activates promoters containing IRF-3-binding sites. Phosphorylation of IRF-3 occurs at a cluster of carboxyl-terminal serine and threonine residues (between 385 and 405), leading to its association with the p300/CBP coactivator protein that promotes DNA binding and transcriptional activity (5). During infection, IRF-3 is likely activated through a pathway that includes activation of Toll-like receptors and of a kinase complex that includes IKKε and TBK1 (6,7). IRF-3 is phosphorylated at Ser396 following viral infection, expression of viral nucleocapsid, and double stranded RNA treatment. These events likely play a role in activation of IRF-3 (8).
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