SUMO3 Monoclonal Antibody
- Known as:
- SUMO3 Monoclonal Antibody
- Catalog number:
- AM1201a
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SUMO3 Monoclonal Antibody
Related genes to: SUMO3 Monoclonal 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 Monoclonal Antibody
Related articles to: SUMO3 Monoclonal Antibody
- 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 - 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 - Small ubiquitin-related modifiers (SUMOs) are covalently conjugated onto the proteome and serve as signaling molecules in many aspects of eukaryotic cell biology, from and to . The conjugatable SUMO variants, SUMO1 and the almost identical SUMO2 and SUMO3 (designated SUMO2/3), are processed by an E1(SAE1:SAE2)-E2(UBC9)-E3 enzyme cascade to produce SUMO-modified proteins. The prerogative of the SUMO biology field is to identify and study the specific proteins undergoing SUMOylation, which grants us insights into the biological pathway of interest. This protocol was developed using the human osteosarcoma cell line U2OS to enable the investigation of SUMO conjugates in mitosis, the cell division phase of the cell cycle. We enrich the cell population for mitotic cells, which are isolated and subjected to stringent lysis conditions involving a high concentration of SDS and DTT in RIPA buffer, to promote complete protein denaturation. The lysates in high SDS RIPA buffer are diluted to reduce the overall SDS concentration and undergo conventional immunoprecipitation using SUMO1- or SUMO2/3-specific antibodies bound to protein A/G agarose beads. The samples are then compatible with downstream readouts such as western blots and mass spectrometry. This protocol detects endogenous SUMOylated proteins and avoids exogenous SUMO overexpression, which can alter SUMO conjugate formation. Furthermore, this denaturing protocol ensures only SUMOylated proteins are immunoprecipitated, and not their interactors. Key features • Purifies endogenous SUMO-modified proteins by building on Becker et al. [1]. • Enriches and isolates cells in mitosis using nocodazole and mitotic shake-off. • 1% SDS RIPA lysis promotes robust denaturation ahead of SUMO-specific immunoprecipitation. • Compatible with downstream readouts such as western blots and mass spectrometry. - Source: PubMed
Publication date: 2026/04/05
Walker Alexandra KLanz Alexander JMorris Joanna R - Dysfunction of SUMOylation is closely associated with various diseases, yet its role in lung ischemia-reperfusion injury (LIRI) remains poorly understood. This study used quantitative real-time PCR and Western blot to assess the expression levels of small ubiquitin-like modifier 3 (SUMO3) and heat shock protein 70 (HSP70). The stability of HSP70 and protein-protein interactions were also detected. Flow cytometry and terminal deoxynucleotidyl transferase-mediated dUTP nick-end labeling staining were performed to detect cell apoptosis. Immunofluorescence was applied to assess the expression levels of Bip, phosphorylated protein kinase r-like endoplasmic reticulum kinase, and phosphorylated inositol-requiring enzyme 1. Enzyme-linked immunosorbent assay kits were used to measure the content of cytokines. This study found that SUMO3 was down-regulated in both the hypoxia/reoxygenation-induced cell model and the in vivo ischemia-reperfusion injury-mediated lung injury model. SUMO3 up-regulation effectively promoted cell growth in vitro and attenuated lung injury in vivo. Mechanistically, SUMO3 interacts with HSP70 and promotes its SUMOylation, thereby stabilizing HSP70 protein and subsequently suppressing endoplasmic reticulum (ER) stress. Knockdown of HSP70 reversed the beneficial effects induced by SUMO3 up-regulation, such as inhibiting cell growth and activating ER stress in vitro and aggravating lung injury and enhancing inflammatory response in vivo. These findings demonstrate that SUMO3 exerts a protective role in LIRI progression by stabilizing HSP70 and inhibiting ER stress, providing a potential therapeutic strategy for LIRI treatment. - Source: PubMed
Publication date: 2026/03/23
Li AoLi ChunkeLi HuLiu YuweiDing ZhiTan Jing