SUMO1 293T Cell Transient Overexpression Lysate(Denatured)
- Known as:
- SUMO1 293T Cell Transient Overexpression Lysate(Denatured)
- Catalog number:
- H00007341-T02
- Product Quantity:
- 100 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- SUMO1 293T Cell Transient Overexpression Lysate(Denatured)
Related genes to: SUMO1 293T Cell Transient Overexpression Lysate(Denatured)
- 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 293T Cell Transient Overexpression Lysate(Denatured)
Related articles to: SUMO1 293T Cell Transient Overexpression Lysate(Denatured)
- 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 - Atherosclerosis (AS)-associated cardiovascular disease is the main cause of global mortality. The excessive retention of glycated low-density lipoprotein (G-LDL) under the vascular endothelium promotes AS. In addition, G-LDL supports a role in promoting the expression of scavenger receptor A (SR-A), increasing SR-A-mediated transcytosis of G-LDL in endothelial cells (ECs), consequently accelerating the progression of atherosclerosis. However, the underlying mechanism used by G-LDL to promote SR-A expression has not been elucidated, thus representing the aim of this work. - Source: PubMed
Publication date: 2026/05/30
Shu MengCheng WenzhuoYu FangyangZhang LiyinWang LiShu YanWang RuonanXue BaoruiJin Si - Hypoxia-ischaemia and reperfusion (HI/R) damage is a result stemming from any event that interrupts the brain's blood supply, such as the occlusion of a blood vessel. In neurons, the molecular mechanisms involved in the HI/R cascade are diverse in nature, ranging from proteomic, genomic, and transcriptomic alterations in the cells. Many of these changes are governed by post-translational modifications such as SUMOylation, which can quickly and reversibly alter the fate of key proteins. This review summarises current evidence regarding the role of SUMOylation in key molecular pathways in major in vivo and in vitro models of cerebral HI/R. Our review reinforces the concept of SUMOylation being a dynamic and time-dependent process that functions as a rapid molecular switch, affecting major pathways across different cell types and cellular compartments. Moreover, the context-dependent pathological and neuroprotective action of SUMOylation in different pathways involved in HI/R is explored. It sheds light on a novel notion placing aberrant SUMO-1 conjugation as the main culprit in reperfusion damage, whereas SUMO-2/3 principally serves as a compensatory mechanism during ischaemia to prevent damage. Nevertheless, it also highlights important gaps in the current scientific evidence regarding the role of SUMO, underscoring the need for further investigation. - Source: PubMed
Gissoni João MCampos Kiara FVieira Helena L ANetto Carlos AlexandreDurán-Carabali Luz ElenaCimarosti Helena I - Lung cancer remains a leading cause of cancer-related death, highlighting the urgent need for new treatment strategies. SUMOylation, a post-translational modification that regulates DNA repair, replication, and cell cycle progression, is often increased in cancers and is a promising therapeutic target. Previously, we identified alternative splicing events affecting the SUMO transcripts, resulting in variant mRNAs coding for both non-conjugatable (SUMO1α and SUMO2α) and conjugatable (SUMO3α) isoforms-potentially helping to regulate overall cellular SUMOylation. In this study, we investigated whether increasing the levels of the transcripts coding for the non-conjugatable isoforms could decrease SUMOylation and improve chemotherapy efficacy in non-small cell lung cancer (NSCLC). To test this, we designed two sets of exon-skipping morpholinos called SUM2IN and SUMO1IN, targeting the pre-mRNAs of SUMO2 and SUMO1, respectively, and tested them in A549 and HCC827 cell lines. While treatment with SUM2IN significantly increased SUMO2α mRNA and reduced overall SUMO1 and SUMO2 conjugation in all tested cell lines, SUM1IN affected the proportion of SUMO1 mRNA variants and overall SUMO conjugation in a cell-type-specific manner. Still, both SUM2IN and SUM1IN altered cell cycle progression, decreased cell growth, and enhanced the cytotoxic effects of cisplatin and etoposide in A549 and HCC827 cells, while having a notably smaller impact on these parameters in the non-malignant lung fibroblast cell line HEL-299. Therefore, SUM2IN and SUM1IN display chemosensitizing activity against NSCLC and provide a strong foundation for developing SUMO-targeted chemosensitizers for NSCLC and other aggressive human cancers. - Source: PubMed
Publication date: 2026/05/05
Garcia-Morin AndreaOrozco-Sepulveda RebecaJuarez-Vargas YeseniaBanuelos ClaudiaGutierrez-Zubiate IsabelRosas-Acosta German - Acute severe ulcerative colitis (ASUC) now imposes an increasing global burden, yet lacks broadly effective therapeutic options. While organoid transplantation represents a promising approach for intestinal injuries, its efficacy for ASUC treatment remains suboptimal. Here, we elucidate the intrinsic mechanism of RIPK1 involvement in necroptosis initiation, and further develop an organoid-based dual-axis therapeutic paradigm for ASUC. We identified that RIPK1 undergoes PIAS1-catalyzed SUMO1 modification at lysine 305, which promotes its compartmentalization within phase-separated structures, thereby serving as nucleation platforms for accelerating RIPK3 amyloid fibril assembly. Interfering with phase separation of RIPK1 suppresses necroptosis in intestinal cells and colonic organoids in vitro, as well as alleviates intestinal injury and reduces mortality in vivo. Notably, while colonic organoid transplantation showed limited therapeutic efficacy in ASUC, a synergistic therapy combining necroptosis blockade and organoid transplantation effectively reduced inflammatory damage and enhanced epithelial regeneration by reprogramming the intestinal microenvironment. These findings suggest that the SUMO1-RIPK1 axis functions as a druggable checkpoint governing necroptotic cell fate and presents a clinically actionable strategy to potentiate regenerative medicine paradigms in ASUC pathogenesis. - Source: PubMed
Publication date: 2026/05/13
Deng QifengLiu JiruShen JianYang SidiZhao XinWang WenruLu JianruLiu LihongZhou LiangCai SihuiZeng LinsenZhou XiaoqianCui Jun