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Synthetic peptide, corresponding to 14 amino acids near the carboxy terminus of human IRF3
ab39792 is a crude synthetic peptide, purity range from 60-70%. The sequence is proprietary.
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Preservative: 0.02% Sodium Azide
Constituents: 0.1% BSA, PBS, pH 7.2
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Immunology >> Innate Immunity >> TLR Signaling
Epigenetics and Nuclear Signaling >> Transcription >> Other factors
Immunology >> Innate Immunity >> Cytokines >> Interferons
Our Abpromise guarantee covers the use of ab39792 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: Use at an assay dependent dilution. Predicted molecular weight: 47 kDa.
This peptide can be used with studies using ab25950.
This peptide usually blocks the antibody activity completely in Western blot by incubating the peptide with equal volume of antibody for 30 min at 37°C.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Mediates interferon-stimulated response element (ISRE) promoter activation. Functions as a molecular switch for antiviral activity. DsRNA generated during the course of an viral infection leads to IRF3 phosphorylation on the C-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of genes under the control of ISRE. The complex binds to the IE and PRDIII regions on the IFN-alpha and IFN-beta promoters respectively. IRF-3 does not have any transcription activation domains.
Expressed constitutively in a variety of tissues.
Belongs to the IRF family.
Contains 1 IRF tryptophan pentad repeat DNA-binding domain.
Constitutively phosphorylated on many serines residues. C-terminal serine/threonine cluster is phosphorylated in response of induction by IKBKE and TBK1. Ser-385 and Ser-386 may be specifically phosphorylated in response to induction. An alternate model propose that the five serine/threonine residues between 396 and 405 are phosphorylated in response to a viral infection. Phosphorylation, and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3.
Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation.
ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation.
Cytoplasm. Nucleus. Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm.
Target information above from: UniProt accessionQ14653
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab39792 has not yet been referenced specifically in any publications.
Publishing research using ab39792? Please let us know so that we can cite the reference in this datasheet
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