SUMO1 Antibody (N_term E67) Blocking Peptide
- Known as:
- SUMO1 Antibody (N_term E67) Blocking Peptide
- Catalog number:
- BP1222d
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SUMO1 Antibody (N_term E67) Blocking Peptide
Related genes to: SUMO1 Antibody (N_term E67) Blocking Peptide
- Gene:
- OR7E26P NIH gene
- Name:
- olfactory receptor family 7 subfamily E member 26 pseudogene
- Previous symbol:
- OR7E67P, OR7E69P, OR7E70P, OR7E68P
- Synonyms:
- OR1-51, OR1-72, OR1-73, OR912-95
- Chromosome:
- 10p13
- Locus Type:
- pseudogene
- Date approved:
- 1999-11-29
- Date modifiied:
- 2015-12-09
- 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 Antibody (N_term E67) Blocking Peptide
Related articles to: SUMO1 Antibody (N_term E67) Blocking Peptide
- 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 - Neurodegenerative diseases (NDDs) represent a growing global health burden, particularly in aging populations. These disorders primarily affect neurons and are characterized by progressive neuronal dysfunction and loss within specific regions of the central nervous system. Major NDDs include Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, Huntington's disease, multiple sclerosis, and stroke. Although each disorder exhibits distinct genetic backgrounds and pathological protein aggregates, they share common pathogenic mechanisms, including chronic neuroinflammation, impaired autophagy and mitophagy, disrupted proteostasis, telomere instability, and epigenetic alterations. A hallmark feature across NDDs is the accumulation of misfolded proteins, leading to synaptic dysfunction and neuronal degeneration. Small ubiquitin-like modifiers (SUMOs) are a family of ∼100 amino acid proteins, including SUMO1 and the closely related SUMO2/3 isoforms. SUMOylation is a dynamic posttranslational modification that regulates protein function through the covalent attachment or removal of SUMO moieties. This reversible process is mediated by SUMO-specific E1 activating, E2 conjugating, and E3 ligating enzymes and is counterbalanced by SUMO/Sentrin-specific proteases. The SUMOylation status of target proteins depends on the tightly controlled balance between conjugation and deconjugation systems. Acting as a molecular switch, SUMOylation modulates diverse cellular processes such as DNA damage repair, RNA metabolism, transcriptional regulation, and protein quality control, all of which are essential for maintaining cellular homeostasis. Accumulating evidence links dysregulated SUMOylation to the pathogenesis of multiple neurological disorders, including polyglutamine and synucleinopathies. SUMOylation influences neuroinflammation, oxidative stress, protein aggregation, neuroangiogenesis, ischemic injury, and demyelination. This review highlights recent advances in understanding the role of SUMOylation in NDDs and explores its potential as a promising therapeutic target. - Source: PubMed
Publication date: 2026/05/07
Oriquat GhalebJasim Ihsan KGajjar Tushar BHanumanthayya MalathiAbdulhameed Ahmad IsraaSingh GunjanMaharana LaxmidharBainsal Neeraj - Simian immunodeficiency viruses (SIVs) have crossed from apes to humans at least four times, but only one event gave rise to the AIDS pandemic. The host barriers that pandemic HIV-1 group M () strains overcame to spread efficiently in humans remain poorly understood. To identify such barriers, we performed CRISPR-Cas9 screens driven by the replication efficiency of SIVcpz, the chimpanzee precursor of HIV-1. Guide RNA libraries targeting more than 500 human genes encoding potential antiviral factors were inserted into the replication-competent SIVcpz MB897 molecular clone, which is phylogenetically closely related to HIV-1 group M strains. Propagation in Cas9-expressing human SupT1 T cells significantly enriched for sgRNAs targeting and . These hits only partially overlapped with those identified in analogous HIV-1-based screens, indicating virus-specific restriction profiles. Functional analyses confirmed that IFITM2 (interferon-induced transmembrane protein 2), PCED1B (PC-esterase domain-containing protein 1B), MEFV (Mediterranean fever protein, pyrin/TRIM20), and AXIN1 (Axis inhibition protein 1) restrict replication of the analyzed SIVcpz strains but not HIV-1 group M strains in primary human CD4 T cells. These findings reveal previously unrecognized host factors that limit SIVcpz replication in human cells and highlight barriers that at least some HIV-1 group M strains overcame during adaptation for pandemic spread. - Source: PubMed
Publication date: 2026/05/07
Xie QinyaWang QingxingNoettger SabrinaGosálbez GuillermoBetzler Annika CVolcic MetaKmiec DorotaKrebs StefanGraf AlexanderGülensoy DilaWeidinger GilbertSparrer Konstantin M JKirchhoff Frank - SUMOylation may be involved in preeclampsia (PE) progression. We aimed to investigate the roles of SUMOylation in PE and its underlying mechanism using animal and cell models. A rat PE model was established by dexamethasone (DEX) treatment from pregnancy day 7.5-17.5. HTR8 and BeWo trophoblasts were used as cell models. Placental RNA-seq analysis coupled with Western blotting showed upregulated SUMOylation in placentas of DEX-treated rats. SUMOylation inhibitor TAK-981 treatment robustly alleviated PE-like features including reduced blood pressure and improved renal injury, fetal weight, spiral artery remodeling and placental blood flow in DEX-treated rats. DEX increased SUMOylation in HTR8 and BeWo cells. TAK-981 reversed DEX-induced dysfunction in HTR8 and BeWo cells, such as migration, invasion and syncytialization. Mass spectrum analysis of SUMO1 immunoprecipitation coupled with functional validation showed that SUMOylated proteins related to oxidative stress caused by DEX were reversed by TAK-981 in cultured trophoblasts. TAK-981 mitigated placental oxidative stress in DEX-treated rats. GEO database combined with Western blotting showed upregulated SUMOylation in human placentas with PE. Our findings indicate that protein SUMOylation is one of the key events in PE, particularly in that associated with high glucocorticoid exposure. Targeting placental SUMOylation might be a promising therapeutic strategy for PE. - Source: PubMed
Publication date: 2026/04/11
Xiao ShuZhang YouyiTang ZhengshanChen CaiyunGuo DeweiLong JingNi Xin