SUMO1 purified human protein
- Known as:
- SUMO1 enriched H. sapiens protein
- Catalog number:
- RP10299
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SUMO1 purified human protein
Related genes to: SUMO1 purified human protein
- Gene:
- SUMO1 NIH gene
- Name:
- small ubiquitin like modifier 1
- Previous symbol:
- UBL1
- Synonyms:
- PIC1, GMP1, SMT3C, SUMO-1, SMT3H3, OFC10
- Chromosome:
- 2q33.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-06-04
- Date modifiied:
- 2019-02-18
Related products to: SUMO1 purified human protein
Related articles to: SUMO1 purified human protein
- Pax6 is a critical transcription factor that regulates the development of multiple tissues, including the nervous system, ocular tissues, and pancreas. We have previously demonstrated that p32 Pax6 function is substantially regulated by protein sumoylation mediated through SUMO1 at the primary residue, Lys-91, and to a less degree at Lys-110 of the p32 Pax6 (K91/110) (Yan et al., 2010, PNAS). To further investigate the function of Pax6 sumoylation, we established stable PANC-1 pancreatic cancer cell line overexpressing p32 Pax6. Injection of these cells into immune-deficient mice promoted much enhanced tumor development than both parental and vector-transfected cells. Inhibition of Pax6 sumoylation with the sumoylation inhibitor ML-792 markedly suppressed tumor growth. Moreover, ML-792 treatment of the developed tumors also significantly suppressed tumor growth. To further study the underlying mechanisms, we generated the PANC-1 cell lines expressing K91/110R-p32 Pax6 and demonstrated that inhibition of Pax6 sumoylation through K91/110R mutations also suppressed its ability to promote tumor development in nude mice. Furthermore, K91R-p32 Pax6 knock-in mice exhibited changed cell populations in adult pancreas tissue and altered transcriptomes in the pancreas in vivo, which resembled the changes observed in PANC-1 cells expressing K91/110R-p32 Pax6 ex vivo. RNA sequencing, gel mobility shifting, chromatin immunoprecipitation, and Cut & Run assays revealed that the CXXC finger protein 4 (CXXC4) is the major downstream target directly regulated by Pax6. Silencing of CXXC4 in PANC-1 and CAPAN-1 cells expressing p32 Pax6 inhibited Pax6-induced tumor development in nude mice, exhibiting the phenotype similar to that observed in PANC-1 and CAPAN-1 cells expressing K91/110R-p32 Pax6. Together, our results demonstrated that inhibition of Pax6 sumoylation suppresses tumorigenicity of PANC-1 and CAPAN-1 pancreatic cancer cells through CXXC4. Our findings suggest that targeting Pax6 sumoylation may serve as a potential therapeutic target for pancreatic cancer treatment. - Source: PubMed
Publication date: 2026/06/25
Xiao YuanWang Jing-MiaoShan Yu-YanFu Jia-LingDeng MiWang YanZhang Jian-PingZheng Shu-YuZou MingGan Yu-WenLiang Xing-MiaoHu Xue-BinZhang LanLi David Wan-Cheng - Cataract is a major cause of blindness among patients with diabetes mellitus. The pathology underlying diabetic cataract (DC) is complex because of changes in biological processes caused by chronic hyperglycemia. O-GlcNAcylation is highly dependent on glucose availability and regulates mitochondrial functions. Dysregulation of O-GlcNAcylation has been reported in DC. Mitochondria in lens epithelial cells are key organelles for energy supply and redox homeostasis of the lens. Mitochondrial dysfunction is a hallmark of DC. However, whether O-GlcNAcylation regulates mitochondrial function underlying DC has not been fully studied. - Source: PubMed
Guo ZaoxiaLi XinnanChen XiMa XiaopanYan Hong - Inhibited acute myeloid leukemia (AML) proliferation is accompanied by downregulated peroxisome proliferator-activated receptor α (PPARα), which however can be stabilized via SUMOylation. This study investigated how PPARα SUMOylation impacts AML cell growth. - Source: PubMed
Publication date: 2025/06/08
Song XiaoluShi FangfangWang XiaogangPeng YeWang HuafangJin LaiLan Jianping - Copper (Cu) and zinc (Zn) are essential trace metal elements for vertebrates, and insufficient intake of trace metal elements can have adverse effects on animal health. Studies suggested that the interaction among trace metal elements played a crucial role in this process. Therefore, the current study was conducted to explore whether low Zn alleviated low dietary Cu-induced decrease in intestinal Cu level and identify potential mechanisms via the in vivo animal experiment and in vitro cell culture. The regulatory relationship between metal response element binding transcription factor 1 (Mtf-1) and ATPase Cu transporting alpha (Atp7a) under low Cu and low Zn was elucidated through electrophoretic mobility shift assays and chromatin immunoprecipitation analysis. The SUMOylation modification of Mtf-1 and its effects on atp7a promoter were determined through immunoprecipitation and dual-luciferase reporter assay. Compared with the control, the low dietary Cu group significantly promoted the transcriptional regulation of atp7a promoter by Mtf-1, leading to intestinal Cu metabolism disorders. However, compared with the low dietary Cu group, the low Cu + low Zn group had significantly inhibited the transcriptional regulation of atp7a promoter by Mtf-1 and alleviated intestinal Cu metabolism disorder caused by low Cu. Mechanistically, Mtf-1 was modified by SUMOylation, and Sumo1-overexpression significantly reduced atp7a promoter activity. Taken together, dietary low Zn alleviated low Cu-induced decrease in intestinal Cu level through the SUMOylated-Mtf-1 and the Mtf-1/Atp7a axis. - Source: PubMed
Zhong Chong-ChaoYang HongHogstrand ChristerSong Chang-ChunZheng HuaHuang ChaoLuo Zhi - Myocardial ischemia-reperfusion injury (MIRI) exacerbates myocardial damage, resulting in a further decline in heart function. Abnormally high TRAF6 expression was reported in MIRI. However, what actually causes the abnormally elevated expression of TRAF6 in MIRI is still unclear and needs further study.Mice underwent left anterior descending (LAD) occlusion for 30 minutes and then reperfusion for 24 hours to establish our MIRI model. Hypoxia/reoxygenation (H/R) was used to treat AC16 cells. Morphology of myocardial tissues was examined by HE staining and myocardial infarction size was measured using Evans blue/TTC staining. The levels of vital molecules were determined using RT-qPCR, ELISA, and western blot. The interactions between molecules were validated by Co-IP. Cell viability and apoptosis were evaluated using CCK-8 and flow cytometry.Our results showed higher expressions of TRAF6 and SUMO1 in MIRI models. In addition, TRAF6 protein was modified by SUMOylation, thereby enhancing TRAF6 protein stability and TRAF6 expression. Of note, TIF1β mediated TRAF6 protein SUMOylation. Moreover, TRAF6 overexpression reversed TIF1β silencing-generated enhancement of cell viability and reductions in cell apoptosis and inflammatory response in H/R-induced AC16 cells.TIF1β mediated TRAF6 protein SUMOylation to stabilize TRAF6 protein and enhance TRAF6 level, thereby facilitating MIRI through inhibiting cell viability and enhancing cell apoptosis and inflammatory response. - Source: PubMed
Nan YueZhang XuDu XinpingZuo GuoxingLu Chengzhi