SUMO1 Monoclonal Antibody
- Known as:
- SUMO1 Monoclonal Antibody
- Catalog number:
- AM1200a
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SUMO1 Monoclonal Antibody
Related genes to: SUMO1 Monoclonal Antibody
- 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 Monoclonal Antibody
Related articles to: SUMO1 Monoclonal Antibody
- Immune thrombocytopenic purpura (ITP) is the most common autoimmune bleeding disorder in children and poses a serious threat to pediatric health and survival. An imbalance in Th17 and Treg cell differentiation leads to uncontrolled inflammation. - Source: PubMed
Publication date: 2026/07/17
Ge JiaoLiu Yan - Chronic tissue inflammation causes progressive tissue damage, organ dysfunction, and increased susceptibility to inflammatory diseases. Viral infections are major drivers of this process, but the molecular mechanisms linking antiviral immune responses to persistent inflammation and tissue pathology remain poorly understood. - Source: PubMed
Publication date: 2026/07/15
Lu WentingXing JunjiWang JunyingMinze Laurie JLi Xian CZhang Zhiqiang - Cellular metabolism dynamically adapts to nutrient fluctuations, yet the regulatory mechanisms underlying this plasticity remain incompletely understood. In particular, the adaptive activation mechanism of enoyl-CoA hydratase short-chain 1 (ECHS1), a key mitochondrial enzyme for fatty acid and amino acid catabolism, is poorly characterized. Herein, we identify SUMO1 modification at lysine 128 of ECHS1 as an essential activation switch that drives mitochondrial catabolism and restricts growth of lung cancer cells. Nutrients generating crotonyl-CoA (fatty acids, lysine, tryptophan) stimulate this modification, accelerating crotonyl-CoA oxidation to acetyl-CoA. This metabolic adaptation decreases crotonyl-CoA pools, thereby reducing histone crotonylation (e.g., H2BK20cr and H3K27cr). Conversely, SUMOylation deficiency impairs formation of the catalytic ECHS1 homohexamer, increasing crotonyl-CoA accumulation and histone crotonylation. This epigenetically suppresses oxidative phosphorylation and associated ROS generation while activating PI3K-Akt signaling, promoting lung cancer growth in vitro and in vivo. In lung adenocarcinoma patients, H2BK20cr and H3K27cr levels are elevated in tumor tissues and predict poor survival, highlighting their clinical prognostic significance. Collectively, these findings establish ECHS1 SUMOylation as a nutrient-sensitive activation mechanism for adaptive catabolism and reveal mitochondrial SUMOylation as a critical regulator of nuclear epigenetic reprogramming, defining a metabolite-driven paradigm in cancer epigenetics. - Source: PubMed
Publication date: 2026/07/09
Chen YalanMao HuiCai LiliLi QianyuSong JuanZhang MingmingChen ShanshanAi ZiqiXiong QiangqiangLiu KexinLin XinTan HongshengWang TianshiFan QiujuZuo YongHe JianliCheng JinkeTu Jun - SUMO1 (small ubiquitin-like modifier 1) is a central feature of post-translational SUMOylation, modifying a broad range of substrate proteins. SUMO1 itself is prone to succination, i.e., a post-translational Michael addition of cysteine onto fumarate, which results in the formation of succinated SUMO1 with modified properties. The present study assesses the structural and gas-phase stability modifications in SUMO1 induced by diethyl fumarate succination using advanced ion mobility spectrometry-mass spectrometry (IMS-MS) techniques. Among them, collision-induced unfolding (CIU) and slice-CIU highlight a modified unfolding process resulting from the creation of specific charge-dipole interactions involving the appended dicarbonyl moiety. The experimental results are further supported by molecular dynamics simulations to understand, at the atomistic level, the mechanisms underlying the CIU of gaseous (derivatized) SUMO1 ions. - Source: PubMed
Publication date: 2026/07/07
Groignet LouisRobert ThomasDuez QuentinClaessens JehanBrocorens PatrickGerbaux PascalDe Winter Julien - SUMOylation is a post-translational modification in which a Small Ubiquitin-like Modifier (SUMO) protein is reversibly attached to a lysine residue on a target protein in an ATP-dependent process. This modification can affect the function of target proteins by enhancing their stability or changing cellular translocation, thereby making SUMOylation a critical regulator in the pathogenesis of multiple diseases. The functional consequences of SUMOylation, however, are highly context dependent. In Alzheimer's disease, SUMOylation stabilizes proteins that drive disease progression and enhances neurotoxicity, thereby exacerbating these conditions. Similarly, in Progressive Supranuclear Palsy, SUMO-1 conjugation stabilizes truncated tau and blocks its ubiquitination, whereas SUMO-2/3 conjugation promotes Tau clearance and recovery from neuroinflammation, illustrating how distinct SUMO paralogues can exert opposing effects within the same disease. Conversely, increased SUMOylation can be neuroprotective in cerebral ischemia and Parkinson's disease by promoting autophagic clearance of pathogenic proteins. Beyond alterations in protein stability, aberrant SUMOylation can also lead to mis-localization of target proteins, which has been identified as a pathogenic mechanism in disorders such as Huntington's disease and Amyotrophic Lateral Sclerosis that results in impaired clearance and pathogenic buildup, which results in neuronal death. From a therapeutic standpoint, the SUMO inhibitor TAK-981 has shown promise in both Multiple Sclerosis and in pre-clinical glioblastoma models, underscoring the translational potential of targeting of this pathway. This review examines the multifaceted role of SUMOylation across diverse neurological conditions, evaluates the therapeutic potential of SUMO inhibitors and activators, and highlights the opportunities and challenges of modulating this pathway in currently incurable neurological disorders. - Source: PubMed
Publication date: 2026/06/26
Sidharth AdityaShin Daesung