IRF3 Rabbit Polyclonal Antibody
- Known as:
- IRF3 Rabbit Polyclonal Antibody
- Catalog number:
- CYT-3399
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- IRF3 Rabbit Polyclonal Antibody
Related genes to: IRF3 Rabbit Polyclonal Antibody
- Gene:
- IRF3 NIH gene
- Name:
- interferon regulatory factor 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-13
- Date modifiied:
- 2017-07-07
Related products to: IRF3 Rabbit Polyclonal Antibody
Related articles to: IRF3 Rabbit Polyclonal Antibody
- Colorectal cancer (CRC) arises from a multifaceted interplay among the intestinal microbiota, chronic inflammation, and host genomic instability, with microbial dysbiosis serving as an active driver rather than a by-product of malignant transformation. Genotoxic (colibactin-positive), enterotoxigenic , and contribute to distinct stages of CRC progression by engaging the DNA-damage response and activating β-catenin-dependent Wnt signaling and NF-κB/STAT3 transcriptional programs controlling pro-inflammatory (), pro-survival (), and proliferative () gene expression.. Here, we propose a tri-axial pathogenic framework in which (i) cyclic dinucleotide-mediated activation of the cGAS-STING pathway engages TBK1-IRF3 and NF-κB signaling, driving type I interferons (β) and pro-inflammatory cytokines (α) that couple microbial genotoxic stress to innate inflammation; (ii) altered microbial metabolites, including indoles and bile acids, reprogram AhR and FXR/TGR5 signaling; and (iii) crypt-anchored biofilms spatially amplify leading to activation of STAT3, epigenetic silencing of tumor suppressors, and immune evasion. This review critically synthesizes current evidence supporting these axes and maps them onto CRC molecular subsets and tumor location. Recognition of these integrated microbial-host circuits identifies mechanistically grounded candidates for biomarker development, microbiome-based diagnostics, and targeted interventions to restore microbial and immune equilibrium, thereby providing a refined framework for the molecular classification and precision management of CRC. - Source: PubMed
Publication date: 2026/06/02
Bachir AsmaAltaie Alaa MuayadBendardaf RiyadTalaat Iman MHamoudi Rifat - TANK-binding kinase 1 (TBK1) plays a central role in the host's defense system. In this research, we identified and analyzed the TBK1 ortholog from large yellow croaker (Larimichthys crocea) and investigated its function in the host innate immunity. The obtained ORF of Lc-TBK1 is 2,172 bp and encoding a 723 aa protein. Subcellular localization analysis demonstrated that Lc-TBK1 predominantly resides in the cytoplasm. Lc-TBK1 showed broad expression across multiple tissues, and its transcript abundance was particularly high in the muscle. Its transcription was significantly upregulated after challenge with poly I:C, LPS, PGN, and Pseudomonas plecoglossicida. Overexpression of Lc-TBK1 activated IRF3, IRF7, and IFNd promoters, and such promoter activation were enhanced when Lc-TBK1 co-expressed with Lc-TRAF3 and Lc-TRIF. Co-immunoprecipitation assays confirmed direct interactions between Lc-TBK1 and several key adaptors, including Lc-TRIF, Lc-MAVS_tv1, Lc-MAVS_tv2, Lc-TRAF3, and Lc-TRAF6. Subsequent co-expression analyses revealed adaptor-specific modulation of antiviral gene transcription: Lc-TRIF and Lc-TRAF3 synergistically enhanced RSAD2, IRF3, and IRF7 expression, whereas Lc-MAVS isoforms attenuated these responses. Overall, our findings demonstrate that Lc-TBK1 signaling is differentially regulated by specific adaptor proteins, providing new insights into the evolutionary conservation and diversification of antiviral immune mechanisms in teleost. - Source: PubMed
Publication date: 2026/06/15
Li YingZha Wen QiCui Wen FengLi Meng JiaChen Yan Mi NaHuang Qiu YeYang Qiao YunShen Ying JiaWang Yi LeiJiang Yong HuaZou Peng Fei - p300 is an acetyltransferase that regulates gene expression by acetylating histones and transactivating some transcription factors such as nuclear Factor Kappa B (NF-κB) and interferon regulatory factor 3 (IRF3). p53 is an interferon (IFN)-inducible tumor suppressor that enhances antiviral responses. How p300 and p53 precisely regulate innate antiviral immunity remains incompletely understood. Herein, we report that conditional p300 knockout in alveolar epithelial cells does not suppress but rather enhances antiviral responses in mice infected with vesicular stomatitis virus (VSV) and herpes simplex virus (HSV-1). In vitro investigation reveals that A-485, a p300-specific inhibitor, and p300 knockdown suppress virus replication but promote IFN-β production in a variety of cell types by enhancing (TANK-binding kinase 1) TBK1 and IRF3 phosphorylation. p300 binds TBK1 and acetylates two lysine residues at 241 and 692 to block its activation. p300 expression is downregulated by viral infection in a p53-dependent manner. Mechanistically, viral infection increases the levels of p53, which leads to the upregulation of the seven in absentia homolog 1 (SIAH1) E3 ubiquitin ligase. SIAH1 induces p300 K48-linked polyubiquitination and subsequent proteasomal degradation. Consistently, p53 knockout inhibits, whereas SIAH overexpression enhances antiviral responses. Taken together, our study identifies p300 as an acetyltransferase that suppresses innate immunity by acetylating TBK1, and demonstrates that the p53-SIAH1 axis downregulates p300 to sustain antiviral responses. - Source: PubMed
Publication date: 2026/06/15
Yu HuidiZhan ZhihaoPan XiaoxiangZhang XinyueLiu PenggangSun JingXu Xiulong - Psoriasis is a chronic skin disease driven by skin inflammation and abnormal subcutaneous blood vessels. Yinxie Granules (YXKL) is a clinically effective traditional Chinese medicine (TCM) formula that has shown promise in psoriasis treatment, but its pharmacological mechanisms and material basis remain unclear, limiting its clinical application and co-administration with other drugs. In this study, we explored the mechanism and active components of YXKL in the treatment of psoriasis using patient samples, IMQ-induced psoriatic mice, zebrafish, and in vitro assays. We discovered that YXKL alleviated skin inflammation and restored the skin barrier by reducing M1 macrophage/Th17 infiltration, lowering pro-inflammatory cytokines (IL-6, IFN-β, IL-23, IL-17), and increasing loricrin expression. Mechanistically, we identified a dynamic transition in STING signaling during psoriasis progression. Both the STING/IRF3 and STING/NF-κB pathways were activated in moderate psoriasis, while only the STING/NF-κB pathway was hyperactivated in severe disease. YXKL specifically targeted the STING/NF-κB pathway to mitigate inflammation and vasculopathy but had no significant impact on the upstream regulators, including TRAF6, LKB1, AMPK, and ULK1. Quercetin and kaempferol were identified as the primary STING-modulating components in YXKL, binding to STING proteins and inhibiting downstream pathway activation. These flavonoid components mediate the anti-psoriatic effects of YXKL by simultaneously suppressing skin inflammation and angiogenesis while enhancing vascular integrity through STING inhibition in both keratinocytes and endothelial cells. Our results elucidated the molecular basis of YXKL for psoriasis treatment, highlighting STING/NF-κB as a pivotal therapeutic target in mitigating psoriasis development and providing natural candidate compounds as potential STING inhibitors. - Source: PubMed
Zou JueyaoHu TongyaoZhang ZhengyuHe YongWang YuxinZhou YixiaoZhu ZiyanYu SuyunZou WeiWei ZhonghongZhao YangPan YanhongChen WenxingLu Yin - Herpes simplex virus 1 (HSV-1) is a member of alphaherpesvirus that can cause some important human diseases, and type I interferon (IFN-I)-mediated antiviral effect plays a vital role in the innate immune response, whereas this reaction can be negatively regulated by some HSV-1 encoded proteins. However, it remains unknown whether additional HSV-1 factors contribute to this process. Here, we found that the HSV-1 encoded uracil-DNA glycosylase, UL2, can inhibit Sendai virus (SeV)-induced IFN-β activity. Mechanically, UL2 interacts with the components of RIG-I-like receptor (RLR) signaling pathway, including TBK1 and activated IRF3. While UL2 does not affect the ubiquitination of TBK1 or IRF3, it rather hinders the SeV-stimulated phosphorylation of IRF3 at Ser396. Simultaneously, UL2 blocks the formation of IRF3 dimer and its nuclear translocation. Therefore, these results suggested a crucial connection between UL2 and IFN-β signaling pathway, which may take considerable role in the HSV-1 evasion of the host antiviral response. - Source: PubMed
Publication date: 2026/05/22
Li MeiliChen DannaXu ChunyanChen XinruChen RuitongChen YuyuZou XingmeiZhang YixiaoWang KezhenWang ShuaiHuang WenzhuoChi JiayiPan ZhichengQin YangZhou XinyuanZhang JianPeng TaoChen ShengwenChen YongerXie XiaoleiLi LinhaiGao XinghongLv XiCai Mingsheng