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Rabbit Polyclonal Phospho-IRF-3 (S396) antibody (STJ90486)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:20000;
Recommended protocols: check protocols
Click or hover above images to see image description for IRF-3 (phospho Ser396) Polyclonal Antibody.
Check alternative names for the antibodyExpand
IRF3 antibody,|Interferon regulatory factor 3 antibody|IRF 3 antibody|IRF-3 antibody|IRF3 antibody|IRF3_HUMAN antibody|MGC94729 antibody|Anti-IRF3 antibody [EPR2418Y] (ab68481)
SCBT cat No: sc-15991|sc-376455|sc-9082|sc-33641|sc-33642|
IRF-3 (phospho Ser396) Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Phospho-IRF-3 (S396) Polyclonal Antibody detects endogenous levels of IRF-3 protein only when phosphorylated at S396.
Synthesized phospho-peptide derived from IRF-3 (phospho Ser396) at AA range 340-420
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:20000;
|Molecular weight|| |
IRF-3 (phospho Ser396) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
IRF-3 (phospho Ser396) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Interferon regulatory factor 3 antibody, IRF-3 antibody
|Protein names|| |
Interferon regulatory factor 3 , IRF-3
|Protein 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. 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. 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. 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. 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. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages. / In the absence of viral infection, maintained as a monomer in an autoinhibited state and phosphorylation disrupts this autoinhibition leading to the liberation of the DNA-binding and dimerization activities and its nuclear localization where it can activate type I IFN and ISG genes.
|Protein tissue specificity|| |
Expressed constitutively in a variety of tissues.
|Involvement in disease|| |
Herpes simplex encephalitis 7 (HSE7) [MIM:616532]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. . Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
|Protein sequence and domain|| |
Belongs to the IRF family. / Contains 1 IRF tryptophan pentad repeat DNA-binding domain.
|Protein post-translational modifications|| |
Constitutively phosphorylated on many Ser/Thr residues. C-terminal serine/threonine cluster is phosphorylated in response of induction by IKBKE and TBK1. Phosphorylated at Ser-396 by IKBKE upon ssRNA viral infection. Ser-385 and Ser-386 may be specifically phosphorylated in response to induction. Phosphorylation at Ser-386 by TBK1 results in oligomerization. An alternate model propose that the five serine/threonine residues between 396 and 405 are phosphorylated in response to a viral infection. / (Microbial 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.
|Protein cellular localization|| |
Cytoplasm / Nucleus
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St John’s Laboratory Ltd.
|Product type|| |
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