SUMO3 antibody
- Known as:
- SUMO3 (anti-)
- Catalog number:
- orb136332
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- SUMO3 antibody
Related genes to: SUMO3 antibody
- Gene:
- SUMO3 NIH gene
- Name:
- small ubiquitin like modifier 3
- Previous symbol:
- SMT3H1
- Synonyms:
- SMT3A
- Chromosome:
- 21q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-01-29
- Date modifiied:
- 2019-02-18
Related products to: SUMO3 antibody
Related articles to: SUMO3 antibody
- Small ubiquitin-like modifiers (SUMOs) are small peptides conjugated to proteins during post-translational modification which have been reported to modulate several aspects of the immune system, notably in auto-immune disorders. - Source: PubMed
Publication date: 2026/07/20
Giblin Sean PMoiseanu Vlad RazvanCarrington Christina JosephineNaing AudreyWatkins KillianTsuchiya TomokoKanegasaki ShiroPease James Edward - This study investigated the cytokine profiles and expression patterns of chromosome 21 genes in Saudi Arabian children with Down syndrome (DS) to identify molecular drivers of immune dysregulation and pulmonary complications. This case-control study enrolled 116 children with DS and 60 healthy controls. Cytokine levels Interleukin (), , Vascular Endothelial Growth Factor (), Tumor Necrosis Factor-alpha (), Monocyte Chemoattractant Protein-1 (), , Interferon-gamma (), and Transforming Growth Factor-beta () were measured at baseline and after lipopolysaccharide (LPS) stimulation using the Meso Scale Discovery (MSD) V-PLEX platform. Gene expression analysis was performed on a panel of immune-related (Small Ubiquitin-Like Modifier 3 (), Runt-Related Transcription Factor 1 (), Autoimmune Regulator (), and Regulator of Calcineurin 1 ()) and pulmonary genes (DNA Methyltransferase 3 Like (), Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1 A (), , , , and Integrin Subunit Beta 2 (CD18) located on chromosome 21 using quantitative real-time PCR (qRT-PCR). Children with DS exhibited elevated levels of pro-inflammatory cytokines (, , , ) and the anti-inflammatory cytokine compared to controls, both at baseline and after LPS stimulation ( < 0.05). Gene expression analysis revealed upregulation of immune-related genes (, , , ) and pulmonary genes (, , , , , ) in the DS group. and emerged as strong predictors of DS, while , , and revealed potential as biomarkers for pulmonary complications. receiver operating characteristic (ROC) analysis identified (AUC: 0.935) and (AUC: 0.890) as strong predictors of the DS immune phenotype. Furthermore, (AUC: 0.966), (AUC: 0.913), and (AUC: 0.944) demonstrated superior diagnostic accuracy as potential biomarkers for DS-associated pulmonary abnormalities. This study provides a comprehensive insight into the immune dysregulation and genetic predisposition in Saudi Arabian children with DS. The findings highlight potential biomarkers (, , , , , , , , ) and therapeutic targets for personalized medicine approaches to manage immune dysfunction and respiratory complications in this population. - Source: PubMed
Publication date: 2026/06/02
Elmetwalli AlaaEl-Sakka Samaa AhmedAlzahrani Othman RAl Balawi Aisha NawafSalama Afrah FatthiHassan Mervat GElsayed AshrafWael DaliaAlaa E Sorour HebaEl-Sewedy Tarek - SUMOylation has emerged as a key regulator of chromatin and transcription, yet its contribution to lineage reprogramming remains unclear. To explore how chromatin SUMOylation influences cellular plasticity, we studied CEBPA-driven lineage reprogramming of human leukemic B-cells into macrophage-like cells. By integrating ChIP-seq, ATAC-seq, RNA-seq and chromatin-directed proteomics, we mapped the chromatin landscape and transcriptomic changes during early reprogramming. Lineage conversion triggered a dynamic rise in SUMO2/3 chromatin occupancy at CEBPA-bound sites, revealing a coordinated regulatory mechanism. Proteomic profiling of SUMO2/3- and CEBPA-associated chromatin uncovered extensive convergence and enrichment of differentiation-related transcription factors, chromatin remodelers and coregulators. Among these, NCOA3 displayed markedly increased SUMO2/3 association upon lineage conversion. NCOA3 co-occupied CEBPA- and SUMO2/3-bound chromatin regions, implying a SUMOylation-supported coregulatory role in lineage reprogramming. Pharmacological inhibition of SUMOylation using ML-792 (SUMOi) selectively enhanced CEBPA chromatin occupancy and chromatin accessibility, altered the CEBPA association of proteins, and modified NCOA3 binding dynamics. SUMOi also reshaped gene expression, promoting loss of B-cell identity and activation of macrophage-associated programs, including lipid metabolism. Collectively, our findings highlight chromatin SUMOylation as a dynamic and context-dependent modifier that fine-tunes lineage transitions, with implications for chromatin biology and therapeutic modulation of cell identity. - Source: PubMed
Publication date: 2026/05/27
Valima EmmaManjur A B M KaiserSavinainen EeviVaris VeraLaunonen Kaisa-MariGraf ThomasVarjosalo MarkkuNiskanen Einari APalvimo Jorma J - Post-translational modifications (PTMs), such as Small Ubiquitin-like Modifier (SUMO)ylation and ubiquitination, regulate key cellular processes by covalently attaching to lysine residues. While mass spectrometry allows site-specific identification of PTMs, most existing search engines are optimized for small, non-fragmenting modifications and struggle to detect large, fragmenting protein-based modifiers. We refer to these as sequence-based modifiers (SBMs). To overcome this limitation, we developed an SBM-specific search strategy within MaxQuant that accounts for the fragmentation behavior of SBMs during peptide identification. Using publicly available datasets, we validated our approach for SUMO2/3. Our analysis identified distinct diagnostic features and characteristic mass shifts associated with SBM fragmentation, referred to in this study as d-ions (diagnostic ions) and p-ions (PTM ions). By leveraging these features, our method improved the identification of SUMOylated peptides from human cell lines by ∼13%, SUMOylation sites in mouse embryonic cells by ∼22%, and in mouse adipocytes by ∼24%. Our search method improved spectral annotation of SBMs by up to 9% increase in the median Andromeda score. Taken together, we highlight the potential of our SBM search to enhance the discovery of protein-based modifications. - Source: PubMed
Publication date: 2026/05/20
Lennartsson CarolineKyriakidou PelagiaNielsen Michael LundOlsen Jesper VelgaardCox JürgenHendriks Ivo Alexander - The receptor tyrosine kinase EphB4 is frequently overexpressed in epithelial cancers, including prostate cancer (PCa). SUMOylation is a post-translational modification that influences protein interactions, localisation and stability. This study investigated how SUMOylation regulates EphB4 localisation, stability and function in PCa. - Source: PubMed
Publication date: 2026/04/15
Maharaj Mohanan Sada NandMertens-Walker IngaLisle Jessica EHerington AdrianStephens CarsonChai MelissaMeutermans WimStephenson Sally-Anne