UBE2N antibody - middle region (ARP33126_T100)
- Known as:
- UBE2N (anti-) - middle region (ARP33126_T100)
- Catalog number:
- arp33126_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- UBE2N antibody - middle region (ARP33126_T100)
Related genes to: UBE2N antibody - middle region (ARP33126_T100)
- Gene:
- UBE2N NIH gene
- Name:
- ubiquitin conjugating enzyme E2 N
- Previous symbol:
- -
- Synonyms:
- UbcH-ben, UBC13, MGC8489
- Chromosome:
- 12q22
- Locus Type:
- gene with protein product
- Date approved:
- 1997-04-16
- Date modifiied:
- 2016-11-09
Related products to: UBE2N antibody - middle region (ARP33126_T100)
Related articles to: UBE2N antibody - middle region (ARP33126_T100)
- Standard hereditary breast cancer gene panels fail to identify causative variants in some patients meeting hereditary breast and ovarian cancer (HBOC) criteria. This exploratory, hypothesis-generating study characterised germline variants in , functionally related DNA damage response genes, and selected low-evidence candidate genes in breast cancer patients with uninformative standard panel results. A total of 185 patients meeting NCCN/ACMG criteria, with normal 42-gene panel and / MLPA results, underwent second-tier targeted sequencing. Group 1 comprised and related genes (, , , , ); Group 2 consisted of Genomics England PanelApp candidates (, , , , , ). No ethnically matched control cohort was available. Variants were classified per ACMG 2015 guidelines and confirmed by Sanger sequencing. Rare variants meeting reporting criteria were identified in 20/185 patients (10.8%): one likely pathogenic (LP) frameshift deletion (c.1869_1870del) in a luminal B invasive ductal carcinoma patient, nineteen variants of uncertain significance (VUS), and one unconfirmed copy number variant. was the most frequently implicated Group 2 gene (4 patients), including a homozygous variant; variants were identified in three patients, including the only male breast cancer case. These descriptive findings identify , , , , and as candidates warranting evaluation in case-control studies with ancestry-matched cohorts, functional validation, and family segregation analysis before any consideration for panel inclusion. - Source: PubMed
Publication date: 2026/09/14
Koç AltuğAtasoy VeyselÖzer Kaya ÖzgeKeşan SelcanSaka MerveAkcan Mehmet BerkayÖzdemir Taha ReşidErdoğan Kadri MuratBoz ÖzlemÖzyılmaz BerkÜnal Olçun ÜmitÇakıroğlu UmutAkay SevalEsenkaya Mehmet Erdinç - To evaluate the therapeutic efficacy of human umbilical cord-derived mesenchymal stem cells (hUC-MSCs) in a murine model of autoimmune premature ovarian insufficiency (POI), and to investigate the association between ubiquitin-conjugating enzyme E2N (UBE2N) expression and disease progression as well as treatment response. - Source: PubMed
Li JinweiWen XianghuiZhao JiaoshiGao MinHao XubinWen ShenghuiZhou LiuzhongWu XinyuLuo XiqingCao ShuangyanWei QiujingLiu BudianFu YimanLv QingGu Jieruo - - Source: PubMed
Madigan Emily DMatos Sandro LJurczak Michael J - K63-linked ubiquitination (K63) is closely associated with the interaction, intracellular trafficking or activity of tagged proteins. However, its role during metabolic dysfunction-associated steatohepatitis (MASH) is largely unknown. Here we show that UBE2N, a ubiquitin-conjugating enzyme that specializes in creating K63, is downregulated by THAP11 in human and mouse hepatocytes with MASH. While hepatocyte-specific Ube2n deficiency exacerbates western diet-induced MASH and fibrosis via PANoptosis and impaired mitophagy, its overexpression reverses these pathological phenotypes and restores hepatic homeostasis. Mechanistically, UBE2N increases PARKIN-mediated K63-p62 at lysine 420, promoting K63-p62 translocation into damaged mitochondria for mitophagic clearance. Ube2n deficiency, conversely, induces cytoplasmic p62 accumulation and NRF2 hyperactivation, driving PANoptosis. Additional Sqstm1 deletion mitigates Ube2n deletion-induced pathologies, highlighting the importance of p62 accumulation for MASH progression. Thus, our results demonstrate that hepatocyte UBE2N is essential for regulation of metabolic stress-mediated mitophagy and PANoptosis, and that p62 is a proof-of-concept target for treating MASH and fibrosis. - Source: PubMed
Publication date: 2026/09/04
Wang FengLee JinPark Jeong-SuHuang MeizhouMa HwanSui GuoyanZhou ZixiongMatsuda MichitakaKim So YeonTsuchiya TakashiWu XuefengLee HaramOh SoohwanPark HanseulLim Key-HwanPark Chun-WoongHan Sang-BaeHong Jin TaeKarin MichaelRoh Yoon SeokSeki Ekihiro - Tumor necrosis factor receptor-associated factor 6 (TRAF6) is a central E3 ubiquitin ligase that links immune-receptor activation to nondegradative K63-linked ubiquitin signaling. Through its functional cooperation with the E2 enzyme Ubc13/UBE2N and Uev1A, TRAF6 promotes the formation of polyubiquitin scaffolds that activate TAK1, IKK, NF-κB, MAPK, inflammasome-related pathways, and multiple cancer-associated signaling networks. Because excessive or dysregulated TRAF6 activity contributes to chronic inflammation, autoimmune disease, tumor progression, metabolic reprogramming, immune evasion, and therapy resistance, the TRAF6-Ubc13 interface has emerged as an attractive but challenging target for small-molecule intervention. This review summarizes the structural and mechanistic basis of TRAF6-Ubc13-dependent ubiquitin transfer, highlighting the roles of TRAF6 RING-domain dimerization, zinc-finger support, oligomerization, and Ubc13 engagement in productive K63-linked ubiquitination. Particular emphasis is placed on C25-140, the principal validated small-molecule disruptor of the TRAF6-Ubc13 interaction, and on its ability to suppress TRAF6 E3 ligase activity and attenuate inflammatory signaling in cellular and disease models. The review also evaluates related therapeutic strategies, including Ubc13/UBE2N inhibitors, TRAF6-targeted natural products and synthetic modulators, receptor-side TRAF6 protein-protein interaction inhibitors, and emerging approaches aimed at TRAF6 oligomerization or phase-separated signaling complexes. Although current pharmacological evidence remains limited, available data support TRAF6-Ubc13 disruption as a promising strategy for selectively modulating pathological ubiquitin signaling in inflammation and cancer. Future progress will depend on improved ligand-bound structural validation, selective chemical probes, optimized pharmacological properties, and disease-specific biomarker-guided application. - Source: PubMed
Publication date: 2026/08/27
Alkhedhairi Saleh