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)
- 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 - Tumor necrosis factor-related apoptosis-induced ligand (TRAIL) selectively induces apoptosis in cancer cells. However, many cancer cells are resistant to TRAIL because of downregulation of death receptors (DRs) and overexpression of anti-apoptotic proteins. Ubiquitin-conjugating enzyme E2N (UBE2N), also known as Ubc13, plays a central role in ubiquitin-mediated cellular activities. In this study, we aimed to explore the sensitization effect of UBE2N inhibition in TRAIL-mediated apoptosis in cancer cells. NSC697923 (a potent inhibitor of UBE2N) alone and TRAIL alone did not induce apoptosis in renal carcinoma Caki cells. However, combined treatment with NSC697923 and TRAIL significantly enhanced apoptotic cell death in cancer cells, but not in normal cells. Mechanistically, NSC697923 induced upregulation of DR5 mRNA and protein levels through CHOP-mediated DR5 transcriptional activation and ubiquitin-mediated DR5 stabilization. NSC697923-mediated DR5 mRNA upregulation was regulated by upregulation of CHOP expression, a key transcriptional factor of DR5. CHOP siRNA treatment inhibited NSC697923-mediated DR5 protein expression. Moreover, NSC697923 generated ROS, and pretreatment with ROS scavengers inhibited DR5 upregulation and NSC697923 plus TRAIL-mediated cell death. These findings suggest that UBE2N inhibitor enhances TRAIL-induced apoptosis by DR5 upregulation and UBE2N inhibition may serve as a potential strategy to overcome TRAIL resistance in cancer therapy. - Source: PubMed
Publication date: 2026/07/13
Jeong Yu JinWoo Seon MinSeo Seung UnSong So RaeKwon Taeg Kyu - Type 2 diabetes mellitus (T2DM) and sarcopenia demonstrate a significant comorbidity, particularly in the elderly, yet the molecular mechanisms linking them, especially through oxidative stress, remain incompletely understood. This study aimed to identify oxidative stress-related hub genes involved in T2DM-associated sarcopenia (T2DS) by integrating single-cell RNA sequencing (scRNA-seq) and bulk RNA-seq data with machine learning. We analyzed scRNA-seq datasets (GSE244515, GSE268953) to characterize cellular heterogeneity and bulk RNA-seq datasets (GSE202295, GSE226151) for differential expression. Cell type annotation revealed key involvement of neuromuscular junctions and myofibers. Functional enrichment analyses highlighted pathways like the proteasome, TNF signaling, and ubiquitin-mediated proteolysis. From an initial set of oxidative stress-related genes, a comprehensive machine learning framework comprising 127 algorithm combinations was employed. The Lasso+Stepglm[both] model identified 12 candidate genes. Subsequent Protein-Protein Interaction (PPI) network analysis refined this to seven core hub genes: TNFRSF1B, PSMA2, UBE2D1, UBE2N, HSP90AA1, RAD23A, and DNAJB1. These genes are functionally interconnected, primarily implicating TNFRSF1B-mediated inflammatory signaling that activates the ubiquitin-proteasome system, leading to enhanced protein degradation-a key pathway in muscle atrophy. ROC curve analysis confirmed the strong diagnostic value of these hub genes across training, test, and external validation sets. Our findings systematically reveal novel oxidative stress-related hub genes and mechanisms in T2DS, providing potential biomarkers and therapeutic targets for this debilitating condition. - Source: PubMed
Publication date: 2026/07/07
Zhu GuangwenZou KaiLiang YiXie LitingChen Qiu - Microglia contribute to detrimental neuroinflammation under pathological conditions and thereby drive the pathogenesis and development of various diseases of the central nervous system (CNS). Here, the deubiquitinating enzyme OTUB1 is identified as a regulator of microglial activation and CNS inflammation. In mice, microglia-specific OTUB1 deletion significantly ameliorates ischemic brain injury by reducing the pro-inflammatory activation of microglia. OTUB1 enhances Toll-like receptor (TLR) signaling through stabilizing UBC13 and TAB2, leading to the increased induction of cytokines. Notably, OTUB1 reduces the proteasomal degradation of TAB2 by reducing its K48 ubiquitination in a catalytic activity-independent manner. Moreover, microglia-confined OTUB1 deficiency also alleviates lipopolysaccharide-induced sickness behavior and experimental autoimmune encephalomyelitis in mice due to decreased neuroinflammation. Pharmacological inhibition of OTUB1 significantly mitigated ischemic stroke injury in mice. These findings reveal an important role of OTUB1 in potentiating microglial activation and neuroinflammation, providing a proof-of-principle observation for targeting OTUB1 in the treatment of TLR-associated neuroinflammatory diseases. - Source: PubMed
Publication date: 2026/07/02
Cao ZijunZhu ZhenhuZeng PingMei FuqiWang DeqiXu JunXu YanqiChen KangminWei ChushanShen JiangyunJin KeshuoChen JiaqingLi ZhongdingLiu BaohuaSchlüter DirkHuang JingyongWang Xu - Myelodysplastic neoplasms (MDS) are clonal hematopoietic disorders defined by ineffective hematopoiesis, cytopenias, and variable risk of progression to acute myeloid leukemia. Although genomic and epigenomic studies have provided insight into disease pathogenesis, reliable biomarkers for diagnosis and prognosis remain limited. Proteomics offers an important advantage because it reflects the functional protein state and captures post-translational modifications, making it highly relevant for risk assessment and therapy guidance. Recent studies have identified several groups of candidate biomarkers. Kinases and signal transduction proteins such as CAMK1D, PRKCZ, KIT, MAST4, PAK6, PTK7, and NTRK1 are dysregulated in MDS and associated with poor outcomes, immune evasion, and aberrant stem cell signaling. Oncofetal proteins like IGF2BP3 and signaling regulators such as RBP4 further highlight proteomic signatures linked to chemoresistance and subtype specificity. In the transplant setting, immune regulators including CSK, FGR, CRTAM, GP1BA, UBE2N, and STAT1 may serve as predictors of graft rejection and relapse. Cytoskeletal and extracellular matrix proteins such as CEP55, Talin-1, Kindlin-3, Vinculin, THBS1, LRG1, SPARC, SAA1, Clusterin, and PRDM16 underscore the role of bone marrow microenvironmental remodeling and adhesion defects in disease progression. Finally, metabolic enzymes such as LDHA reflect altered energy metabolism and correlate with more aggressive disease biology. Collectively, these proteomic candidates illustrate the complex interplay of signaling, immune regulation, bone microenvironment, and metabolism in MDS. Their validation in clinical cohorts could enable early detection, refined risk stratification, and new therapeutic avenues, positioning proteomics as a central tool in the future management of MDS. - Source: PubMed
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