Recombinant Human UBE2V2
- Known as:
- Recombinant Human UBE2V2
- Catalog number:
- CG24
- Product Quantity:
- 10ug
- Category:
- -
- Supplier:
- Novoprotein
- Gene target:
- Recombinant Human UBE2V2
Ask about this productRelated genes to: Recombinant Human UBE2V2
- Gene:
- UBE2V2 NIH gene
- Name:
- ubiquitin conjugating enzyme E2 V2
- Previous symbol:
- -
- Synonyms:
- UEV-2, DDVit-1, EDPF-1, MMS2, UEV2, EDPF1, DDVIT1, EDAF-1
- Chromosome:
- 8q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1998-08-25
- Date modifiied:
- 2016-12-16
Related products to: Recombinant Human UBE2V2
Related articles to: Recombinant Human UBE2V2
- Oncogenic is known to induce DNA replication stress, leading to cellular senescence or death. In contrast, we found that it can also trigger polyploid ovarian nurse cells to die by inducing aberrant division stress. To explore intrinsic protective mechanisms against this specific form of cellular stress, here, we conducted a genome-wide genetic screen and identified the E2 enzyme Uev1A as a key protector. Reducing its expression levels exacerbates the nurse cell death induced by oncogenic , while overexpressing it or its human homologs, UBE2V1 and UBE2V2, mitigates this effect. Although Uev1A is primarily known for its non-proteolytic functions, our studies demonstrate that it collaborates with the E3 APC/C complex to mediate the proteasomal degradation of Cyclin A, a key cyclin that drives cell division. Furthermore, Uev1A and UBE2V1/2 also counteract oncogenic -driven tumorigenesis in diploid cells, suppressing the overgrowth of germline tumors in and human colorectal tumor xenografts in nude mice, respectively. Remarkably, elevated expression levels of UBE2V1/2 correlate with improved survival rates in human colorectal cancer patients harboring oncogenic mutations, indicating that their upregulation could represent a promising therapeutic strategy. - Source: PubMed
Publication date: 2026/03/25
Zhang QiWang YunfengFu XueliWang ZiguangZhang YangYan LizhongWang YuejiaYang MuhanSong DongzeZhang RuixingZhang HongruWu ShianZhao Shaowei - Polybrominated diphenyl ethers (PBDEs), notably decabromodiphenyl ether (BDE-209), are persistent organic pollutants widely used as flame retardants and frequently detected in electronic waste. Despite global restrictions, BDE-209 remains an environmental contaminant with bioaccumulative and potentially risk to human health. This study investigated the proteomic and phosphoproteomic effects of chronic concentration BDE-209 exposure in murine melanoma (B16-F1) cells, aiming to elucidate molecular mechanisms underlying pollutant-induced phenotypic changes of malignancy. Cells were exposed to environmentally relevant concentrations of BDE-209 (0.1 and 1 nM) for 15 days, selected based on levels previously reported in human biological samples and on prior in vitro and in vivo studies investigating chronic low-concentration exposure, followed by mass spectrometry-based analyses. A total of 3369 proteins and 4422 phosphosites were identified. BDE-209 exposure resulted in distinct proteomic signatures, including the exclusive expression in exposed cells of proteins such as PRKDC, and modulation of pathways involved in DNA repair, mRNA processing, and chromatin remodeling. PRKDC is a key kinase in DNA damage repair, and it has been associated with chemotherapy resistance and poor prognosis in several cancers, suggesting its potential as a prognostic biomarker in BDE-209-related tumor progression. Additionally, proteins involved in chromatin remodeling, SUMOylation, mRNA processing, and oncogenic signaling (e.g., YES1, DIMT1, UBE2V2) were induced. Phosphoproteomic analysis revealed differential phosphorylation of proteins linked to cancer progression, including TCOF1, IRF2BP2, and HDGFRP2. These findings demonstrate that even low-dose exposure to BDE-209 can modulate cellular signaling and promote malignancy-associated phenotypic changes, underscoring its potential role in worsening cancer prognosis and highlighting the broader health risks posed by persistent environmental contaminants. - Source: PubMed
Publication date: 2026/02/19
Ferrarini Mariana GalvãoMarchi MicheliMoggio Erick LaurentBrum HulyanaKugeratski Fernanda GBatista MichelOliveira Ribeiro Ciro AlbertoÁvila Andréa Rodrigues - In this exploratory pilot study, we profiled human periodontal ligament (PDL) transcriptomes during early orthodontic tooth movement (OTM). Early-stage (0-10 days) transcriptional dynamics under tension and compression remain insufficiently understood, and no dedicated user-friendly resource has been available for exploring large-scale human data. - Source: PubMed
Publication date: 2026/02/18
Zhang XiaoqiXing LuAi-Gumaei WaseemZhang XiaoqianWang QingxuanLi MinqiLong HuLai Wenli - The aim of this study was to investigate gene expressions related to beta cell function, and the altered protein profiles in insulinoma INS-1 cells following DB application, under both cytotoxic and non-cytotoxic conditions, with a focus on cell death and proliferation. Caspase 3 activity, LDH level, Bax, Bcl-2, PCNA, MafA, Nkx6.1, Pdx1, NeuroD1, and Pax6 gene expressions, TOS, TAS, and OSI were demonstrated. Protein profiles were analyzed using LC-MS/MS. The upstream and downstream proteins using the IPA database were determined. ERP29, UBE2V2, UBE2L6, PSMA4, TSMB10, ARF1, NUDCD2, ARF3, IRS1, PTEN, AKT, HSPA8, and Fibronectin levels were shown. The changes were observed in genes depending on pancreatic beta cell function and apoptosis. Bcl2, MafA, Nkx6.1, Pdx1, and NeuroD1 gene levels decreased, while Bax and Pax6 gene levels and TAS and TOS levels increased in the group given STZ + DB. PCNA, Bcl-2, Nkx6.1, Pdx1, and Pax6 gene levels increased, while MafA gene levels decreased in the group given DB. The protein ubiquitination pathway more predominates than the other many signaling pathways. Several proteins not previously associated, or only indirectly linked, with beta cell function, apoptosis, or proliferation were identified and characterized for the first time in insulinoma. These findings provide new insights and potential targets for the treatment of pancreatic cancer. - Source: PubMed
Publication date: 2025/10/22
Karatug Kacar Ayse - Severe preeclampsia (sPE) is a serious condition posing risks to both maternal and fetal health. Based on mass spectrometry analysis, we identified a key protein, PSME3 (proteasome activator subunit 3), an 11S proteasome activator, whose protein level was significantly downregulated in sPE placentas and whose function in sPE remains unknown. - Source: PubMed
Publication date: 2025/02/05
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