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PathScan® RP Phospho-IRF-3 (Ser379) Sandwich ELISA Kit #54395

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  • ELISA

Important Ordering Details

Custom Ordering Details:

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    Supporting Data

    REACTIVITY M
    Application Key:
    • ELISA-ELISA 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Description

    The rapid protocol (RP) PathScan® RP Phospho-IRF-3 (Ser379) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of IRF-3 protein phosphorylated at Ser379 in a reduced assay time of 1.5 hours. Incubation of cell lysates and detection antibody on the coated microwell plate forms a sandwich with phospho-IRF-3 (Ser379) in a single step. The plate is then extensively washed and TMB reagent is added for signal development. The magnitude of absorbance for the developed color is proportional to the quantity of phospho-IRF-3 (Ser379). Learn more about all of your ELISA kit options here.

    *Antibodies in this kit are custom formulations specific to kit.

    Protocol

    Specificity / Sensitivity

    The PathScan® RP Phospho-IRF-3 (Ser379) Sandwich ELISA Kit detects endogenous levels of mouse IRF-3 protein phosphorylated at Ser379 (equivalent to Ser386 of human IRF-3). The kit sensitivity is shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.

    Species Reactivity:

    Mouse

    Background

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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