TRAF6 antibody - middle region (ARP30226_P050)
- Known as:
- TRAF6 (anti-) - middle region (ARP30226_P050)
- Catalog number:
- arp30226_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TRAF6 antibody - middle region (ARP30226_P050)
Related genes to: TRAF6 antibody - middle region (ARP30226_P050)
- Gene:
- TRAF6 NIH gene
- Name:
- TNF receptor associated factor 6
- Previous symbol:
- -
- Synonyms:
- RNF85
- Chromosome:
- 11p12
- Locus Type:
- gene with protein product
- Date approved:
- 1997-06-12
- Date modifiied:
- 2015-11-20
Related products to: TRAF6 antibody - middle region (ARP30226_P050)
Related articles to: TRAF6 antibody - middle region (ARP30226_P050)
- Dry eye disease (DED) is a chronic ocular surface disorder triggered by tear film imbalance, in which inflammatory disruption of immune homeostasis constitutes the core pathological mechanism. Mesenchymal stem cell-derived exosomes (MSC-Exos) offer promising anti-inflammatory therapeutic potential through immune modulation, tissue repair, and their inherently low immunogenicity. This review elucidates MSC-Exos' molecular regulation of DED inflammation, demonstrating their suppression of the TLR4/NF-κB signaling axis, the IRAK1/TRAF6/NF-κB cascade reaction, the STAT3 transcriptional regulatory network, and the NLRP3 inflammasome activation pathway, while revealing a synergistic mechanism through which MSC-Exos ameliorate the ocular surface inflammatory microenvironment by modulating the Th17/Treg immune balance via the gut-eye axis and facilitating FBXW7-mediated ubiquitination degradation pathways. Despite this therapeutic potential, clinical translation is hampered by exosomal heterogeneity, difficulties in standardization, and suboptimal delivery efficiency and long-term efficacy. Future progress will require the integration of nanotechnology and gene editing to enhance therapeutic functionality, ultimately positioning MSC-Exos as precision biologics for DED. - Source: PubMed
Publication date: 2026/09/09
Yi JiahuanLu FangfangTian YaleWang YuZhang ZiheDeng XujieWang ZhiXia ShigangZhang JiaXiao Qiguo - Tumor necrosis factor receptor-associated factor 6 (TRAF6) is a pivotal adaptor molecule in the receptor activator of nuclear factor-κB (RANK) and its ligand (RANKL) signaling pathways, which are essential for osteoclastogenesis. In this study, we identified WD40 repeat-containing protein 23 (WDR23), also known as DDB1-CUL4 associated factor 11 (DCAF11), as a novel binding partner of TRAF6. Our findings demonstrate that WDR23/DCAF11 acts as a negative feedback regulator of RANK/RANKL-induced osteoclastogenesis by promoting the autophagy-dependent degradation of TRAF6. Notably, RANKL induced the upregulation of WDR23 expression during osteoclastogenesis. WDR23 physically interacted with the TRAF domain of TRAF6 via the WD40 repeat domains 1 and 2 of WDR23, resulting in reduced TRAF6 protein stability by its autophagy-dependent degradation during osteoclastogenesis. By modulating TRAF6 protein levels, WDR23 attenuated RANKL signaling cascades, including nuclear factor-κB and mitogen-activated protein kinases, thereby downregulating the expression of osteoclastogenic markers, such as nuclear factor of activated T-cell c1, tartrate-resistant acid phosphatase, dendritic cell-specific transmembrane protein, V-ATPase subunit d2 and cathepsin K. Conversely, WDR23 knockdown or deficiency enhanced RANKL-induced osteoclastogenesis by preventing the autophagy-dependent degradation of TRAF6. WDR23-deficient mice exhibit an osteoporotic bone phenotype characterized by elevated osteoclast formation and reduced bone mass. Collectively, these results establish WDR23 as a key negative feedback regulator of RANKL-induced osteoclastogenesis via autophagy-mediated TRAF6 degradation and underscore its potential as a therapeutic target for bone disorders associated with aberrant osteoclast formation and function. - Source: PubMed
Publication date: 2026/09/10
Park Hye-WonYu JungeunYu JiyeonYou JinseonKook Yeon HeeLee Joo-YongKim TaesooLee Chul-HoChung Hee-ChungChoi Jong-SoonLee SangkyuRho Jaerang - Ischemic stroke triggers profound neuroinflammation and autophagic stress, driven predominantly by microglial overactivation. However, effective therapies targeting this pathogenesis remain elusive. Here, we report the use of 3-hydroxydehydroleucodin (3-Hyd), the primary active component from Kudiezi injection used in China for ischemic stroke patients, as a potent neuroprotective agent that markedly reduces the cerebral infarct area and improves neurological deficits in a mouse model of transient middle cerebral artery occlusion (tMCAO). Integrated bulk RNA sequencing and in vitro assays revealed that 3-Hyd significantly suppressed the microglial proinflammatory phenotype and excessive autophagic flux. Mechanistically, through chemical biology approaches, we discovered that 3-Hyd directly binds to the V51 and R128 residues of peroxiredoxin 1 (PRDX1), which physically disrupts the pathological binding of PRDX1 to its E3 ubiquitin ligase TRIM21, thus preventing the polyubiquitination of PRDX1 at the K109 residue and its subsequent proteasome degradation. Consequently, stabilized PRDX1 impedes TRAF6 ubiquitination, effectively blocking the downstream NF-κB signaling cascade. Strikingly, the anti-neuroinflammatory and cerebroprotective effects of 3-Hyd were largely abolished in microglia-specific Prdx1 conditional knockdown (Cx3cr1) mice. Together, our findings elucidate a novel TRIM21-PRDX1-TRAF6 signaling axis that governs microglial homeostasis and highlight the pharmacological stabilization of PRDX1 by 3-Hyd to block the binding of TRIM21 with PRDX1 as a promising therapeutic strategy for ischemic stroke. - Source: PubMed
Publication date: 2026/09/09
Liu KuiWang LingChen ZhuoQiu Yu-XuanGao Jia-HongXie Ting-TingLi YueHuang HeHu YangHu Li-HongPang Tao - The mitochondrial antiviral signaling protein (MAVS) is a key component of the innate immune response against RNA viruses. Its involvement in other cellular stresses is largely unknown. Here, we found that hypoxia induces MAVS aggregation, leading to the stabilization of HIF1/2α proteins and the enhancement of hypoxia signaling. Mechanistic studies revealed that MAVS enhances TRAF6 binding to ECSIT, which catalyzes ECSIT polyubiquitination. This promotes mitochondrial ROS generation and likely inhibits PHD2 enzymatic activity, thereby reducing HIF1/2α proteasomal degradation. Disrupting MAVS in both mice and zebrafish decreased the expression of hypoxia response genes and reduced the tolerance of zebrafish to hypoxia. This study reveals an unexpected role of MAVS in hypoxia signaling. - Source: PubMed
Publication date: 2026/09/09
Sun XueyiZhu ChunchunLiu WenWang ZixuanDeng HongyanJia ShukeShi ShuaiXiang YuhanLuo YimanGui Jian-FangLiu XingXiao Wuhan - Renal allograft rejection diagnosis requires invasive biopsy. We assessed whether peripheral blood mRNA of 14 Hippo, interferon (IFN) and NF-κB pathway genes and 11 serum biomarkers could distinguish acute rejection from stable graft function. - Source: PubMed
Publication date: 2026/09/08
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