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Anti-IRF3 Antibody Picoband™ (monoclonal, 11H2)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, ICC, FC |
|---|---|
| Primary Accession | P70671 |
| Host | Mouse |
| Isotype | Mouse IgG1 |
| Reactivity | Rat, Mouse |
| Clonality | Monoclonal |
| Format | Lyophilized |
| Description | Anti-IRF3 Antibody Picoband™ (monoclonal, 11H2) . Tested in Flow Cytometry, IF, ICC, WB applications. This antibody reacts with Mouse, Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 54131 |
|---|---|
| Other Names | Interferon regulatory factor 3, IRF-3, Irf3 |
| Calculated MW | 50-55 kDa |
| Application Details | Western blot, 0.25-0.5 µg/ml, Mouse, Rat Immunocytochemistry/Immunofluorescence, 5 µg/ml, Mouse Flow Cytometry, 1-3 µg/1x10^6 cells, Mouse |
| Contents | Each vial contains 4mg Trehalose, 0.9mg NaCl and 0.2mg Na2HPO4. |
| Clone Names | Clone: 11H2 |
| Immunogen | E.coli-derived mouse IRF3 recombinant protein (Position: M1-I419). |
| Purification | Immunogen affinity purified. |
| Storage | Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles. |
| Name | Irf3 |
|---|---|
| Function | Key transcriptional regulator of type I interferon (IFN)- dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:15800576). Regulates the transcription of type I IFN genes (IFN-alpha and IFN- beta) and IFN-stimulated genes (ISG) by binding to an interferon- stimulated response element (ISRE) in their promoters (PubMed:15800576). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction (PubMed:16846591, PubMed:16979567, PubMed:20049431). Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases (PubMed:16846591, PubMed:16979567, PubMed:20049431). This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes (PubMed:16846591, PubMed:16979567, PubMed:20049431). Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages (PubMed:16846591, PubMed:16979567, PubMed:20049431). |
| Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q14653}. Nucleus {ECO:0000250|UniProtKB:Q14653}. Mitochondrion {ECO:0000250|UniProtKB:Q14653}. Note=Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm. Recruited to mitochondria via TOMM70:HSP90AA1 upon Sendai virus infection. {ECO:0000250|UniProtKB:Q14653} |
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Provided below are standard protocols that you may find useful for product applications.
Background
IRF3 (interferon regulatory factor 3) is a member of the interferon regulatory transcription factor (IRF) family. The IRF3 gene is mapped on 19q13.33. IRF3 is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. IRF3 plays an important role in the innate immune system's response to viral infection. Aggregated MAVS have been found to activate IRF3 dimerization. Although IRF3 increased transcriptional activity from an ISRE-containing promoter, expression of IRF3 as a Gal4 fusion protein did not activate expression of a chloramphenicol acetyltransferase (CAT) reporter gene containing repeats of the Gal4-binding sites. Translocation of IRF3 was accompanied by an increase in serine and threonine phosphorylation. The transcriptional activators CREBBP and EP300 coimmunoprecipitated with IRF3 only subsequent to viral infection, and the authors stated that these are also subunits of DRAF1.
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