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IRF-1 Antibody #4966

Inquiry Info. # 4966

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    Product Specifications

    REACTIVITY
    SENSITIVITY Endogenous
    MW (kDa) 48
    SOURCE Rabbit

    Product Information

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Specificity / Sensitivity

    IRF-1 Antibody detects endogenous levels of IRF-1. This antibody does not cross-react with other family members at physiological levels.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser149 of IRF-1. Antibodies are purified by protein A and peptide affinity chromatography.

    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).

    The IRF-1 transcription factor was originally identified as a regulator of virus-inducible enhancer-like elements of the IFN-β gene (3). IRF-1 is widely expressed and upregulated by viral infection or interferon stimulation and other cytokines. IRF-1 is serine-phosphorylated by casein kinase II (CKII ) at two clustered sites, one in the DNA binding domain (amino acids 138-150) and another in the transactivation domain (amino acids 219-231) (4). Mutation analysis of the latter site suggest that these phosphorylation sites help regulate IRF-1 activity. Tyrosine phosphorylation has also been shown to be important in IFN-γ-mediated differentiation of myeloid cell lines (5). C-terminal SUMOylated IRF-1 inhibits apoptosis in tumor cells by repression of its transcriptional activity (6).

    Alternate Names

    Interferon regulatory factor 1; IRF-1; IRF1; MAR

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