Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human IRF3 Protein expressed in Wheat germ - ABIN2752829
Wang, Li, Dorf: NEMO binds ubiquitinated TANK-binding kinase 1 (TBK1) to regulate innate immune responses to RNA viruses. in PLoS ONE 2012
Show all 3 references for ABIN2752829
Interferon (show IFNA Proteins) regulatory factor (IRF (show TRIM63 Proteins))10 inhibits the expression of IFN1 and IFN3 to avoid an excessive immune response, a unique regulation mechanism of the IFN responses in lower vertebrates.
Hepatitis A virus protein 2B suppresses beta interferon (show IFNA Proteins) (IFN) gene transcription by interfering with IFN regulatory factor 3 activation.
MyD88 (show MYD88 Proteins) interacts with interferon (show IFNA Proteins) regulatory factor (IRF) 3 and IRF7 (show IRF7 Proteins) in Atlantic salmon (Salmo salar)
rotavirus NSP1 (show SH2D3A Proteins) (nonstructural protein 1) employs a pLxIS motif to target IRF-3 for degradation, but phosphorylation of NSP1 (show SH2D3A Proteins) is not required for its activity. These results suggest a concerted mechanism for the recruitment and activation of IRF-3 that can be subverted by viral proteins to evade innate immune responses.
Highly pathogenic Porcine reproductive and respiratory syndrome virus modulates Interferon-beta (show IFNB1 Proteins) expression mainly through attenuating IRF-3 phosphorylation.
Data suggest that molecular chaperone (show HSP90AA1 Proteins) GRP78 (show HSPA5 Proteins) contributes to toll-like receptor-3 (TLR3 (show TLR3 Proteins))-mediated, interferon regulatory factor 3 protein (IRF3)-dependent innate immune response to hepatitis C virus (HCV) in hepatocytes.
Findings suggest a common and conserved mechanism through which highly pathogenic MERS-CoV and SARS (show SARS Proteins)-CoV harness their M proteins to suppress type I IFN expression at the level of TBK1 (show TBK1 Proteins)-dependent phosphorylation and activation of IRF3 resulting in evasion of the host innate antiviral response.
observations suggest IRF3 may function as a novel regulator to modulate TGF-beta1 (show TGFB1 Proteins)-induced LX-2 proliferation, at least in part, via AKT (show AKT1 Proteins) signaling pathway
FAF1 (show FAF1 Proteins) plays a novel role in negatively regulating virus-induced IFN-beta (show IFNB1 Proteins) production and the antiviral response by inhibiting the translocation of active, phosphorylated IRF3 from the cytosol to the nucleus
the LxxLL motifs of IRF3 binds within the hydrophobic pocket of E6, precluding Ser (show SIGLEC1 Proteins)-patch phosphorylation, necessary for IRF3 activation and interferon (show IFNA Proteins) induction.
the suppression of type I IFN production by HTLV-1 Tax (show CNTN2 Proteins) through interaction with and inhibition of TBK1 (show TBK1 Proteins) kinase that phosphorylates IRF3
The authors found that Ca(2 (show CA2 Proteins)+) signaling associated with membrane perturbation and recognition of incoming viral genomes by cytosolic nucleic acid receptors are required to activate IRF3 in response to Sendai virus and human cytomegalovirus.
Study identifies crosstalk between PTEN and IRF3 in tumor suppression and innate immunity.
Amino acid residues in the N-terminal domain of Npro are involved in the stability of Npro, in interaction of Npro with IRF-3 and subsequent degradation of IRF-3, leading to downregulation of IFN-alpha (show IFNA Proteins)/beta production.
The obtained results showed that PRRSV nsp1 could inhibit Poly(I:C)-induced IFN-beta (show IFNB1 Proteins) promoter activity in MARC (show CCL7 Proteins)-145 cells by down-regulating the protein level of IRF-3 and inhibiting the phosphorylation of IRF-3.
proteasomal degradation of IRF3 is induced by a direct or indirect interaction with N(pro).
Data show that the formation of a tripartite ribosomal protein S6 kinase 1 (S6K1 (show RPS6KB1 Proteins))-STING membrane protein-TANK-binding kinase 1 (TBK1 (show TBK1 Proteins)) complex was necessary for the activation of interferon regulatory factor-3 (IRF3).
characterizes SREBP cleavage-activating protein as an essential adaptor in the STING signaling pathway
results revealed a new paradigm in which the antiviral host factor, IRF3, plays a cell-intrinsic pro-parasitic role.
Irf3/IFN activation in hematopoietic stem and progenitor cells expands multipotent progenitors fractions but inhibits HSC (show FUT1 Proteins) mobilization
find that IRF3 versus ISGF3 (show IRF9 Proteins) specificity may be critical to limiting IFN-beta (show IFNB1 Proteins) production and ISGF3 (show IRF9 Proteins) activation, temporally and spatially, but that partial overlap in their specificity is tolerable and may enhance the effectiveness of the innate-immune response
Bipartite nuclear localization signal controls nuclear import and DNA-binding activity of IRF3.
Our findings delineate a novel mechanism for the termination of IRF3 activation in nucleus through TRIM26 (show TRIM26 Proteins)-mediated IRF3 ubiquitination and degradation.
PP1 (show PPP1CC Proteins) directly interacts with IRF3 and dephosphorylates IRF3 at Ser385 and Ser396, resulting in the suppression of TLR- and RLR (show DHX58 Proteins)-triggered IFN-beta (show IFNB1 Proteins) production.
our results identify CK2 (show CSNK2A1 Proteins) as a novel regulator of TBK1 (show TBK1 Proteins) and IRF3 and suggest that targeting CK2 (show CSNK2A1 Proteins) by small molecular inhibitor may be a viable approach to prevent and treat viral infections.
The authors demonstrate that bovine herpesvirus 1 bICP0 effectively inhibits bovine IFN-beta (show IFNB1 Proteins) promoter activity and induces IRF3 degradation.
cpBVDV infection causes a marked loss of interferon regulatory factor 3 (IRF-3), a cellular transcription factor that controls interferon (show IFNA Proteins) synthesis.
This gene encodes a member of the interferon regulatory transcription factor (IRF) family. The encoded protein is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
interferon regulatory factor 3
, interferon regulatory factor 3-like