SUMO1 Control Peptide antibody _CP
- Known as:
- SUMO1 Control Peptide (anti-) _CP
- Catalog number:
- 'AP11219CP-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- SUMO1 Control Peptide antibody _CP
Related genes to: SUMO1 Control Peptide antibody _CP
- 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 Control Peptide antibody _CP
Related articles to: SUMO1 Control Peptide antibody _CP
- Endoplasmic reticulum (ER) stress is a key driver of diabetic cardiomyopathy (DCM), but its upstream regulators are incompletely defined. The transcription factor DACH1 is genetically linked to diabetes and cardiovascular risk, yet its role in the diabetic heart is unknown. - Source: PubMed
Publication date: 2026/08/08
Lin JieLiu NaLi BoWang YiLi CongyeYin YueMa HengYu LuZhou Jie - Post-translational modifications, particularly SUMOylation, plays a crucial role in α-synuclein (α-syn) aggregation, a key pathological feature of Parkinson's disease (PD). Curcumin, a natural polyphenol, has shown neuroprotective potential, but its effects on SUMOylation-related signaling in PD remain unclear. - Source: PubMed
Publication date: 2026/07/21
Li YaoZhu ZhuangZhang Kezhong - Although bovine herpesvirus 1 (BoHV-1) causes massive losses of cattle, the transition from mucosal replication to neuroinvasion remains poorly understood. Using a controlled calf model, we integrated quantitative virology and transcriptomics to map its pathogenesis and define the role of promyelocytic leukemia protein (PML). Calves inoculated intranasally and ocularly (1.4 × 10 plaque-forming units/head) were sampled daily (1-14 days post-infection, dpi) for glycoprotein B (gB) qPCR. Tissues were analyzed at 4 and 14 dpi to measure viral DNA via gB-specific qPCR, and for mRNA-seq of trigeminal ganglia (TG). Shedding peaked at 3-6 dpi, being highest in nasal samples, lower in ocular samples, and substantially lower in rectal samples, and declined by 10-14 dpi. At 4 dpi, among the tissues sampled, the tonsils exhibited the highest viral burden. TG exhibited low viral levels at 4 dpi, although they remained detectable at 14 dpi, indicating neuroinvasion. The TG program shifted from early proteostasis priming (4 dpi) to immune/extracellular matrix activation with synaptic repression (14 dpi). In MDBK/Vero cells, IFN-α resulted in higher bovine PML (bPML) levels and enlarged PML nuclear bodies (PML-NBs), reducing very early viral DNA levels, whereas BoHV-1 disrupted PML-NB integrity. The different bPML isoforms exerted different effects on viral infection. STRING analysis revealed a conserved PML-SUMO1-UBE2I-DAXX-SP100 core. These findings delineate the mucosal-to-neuronal trajectory, establish PML as both an effector and viral target in complementary systems, and identify SUMO/ubiquitin-linked proteostasis as a tractable target for antiviral intervention.IMPORTANCEAlthough bovine herpesvirus 1 (BoHV-1) remains a major challenge to cattle health, the early transition from mucosal replication to trigeminal neuroinvasion has not been clearly mapped in natural-host calves. By integrating daily shedding kinetics, tissue viral DNA profiling, and time-resolved trigeminal ganglion transcriptomics, we delineate when and how BoHV-1 reaches the sensory neurons. Promyelocytic leukemia protein (PML) is identified as a key intrinsic antiviral factor that is upregulated by IFN-α and restricts very early viral genome accumulation, while viral BoHV-1-encoded infected cell protein 0 actively dismantles PML nuclear bodies. The discovery of opposing isoform-specific PML functions and a conserved PML-SUMO proteostasis hub provides mechanistic insight into BoHV-1 immune evasion. These findings refine our understanding of the mucosal-to-neuronal trajectory of infection and highlight proteostasis-linked antiviral pathways as promising targets for intervention. - Source: PubMed
Publication date: 2026/07/23
Wang YongJin HuanWang FanyuCheng JingCao MengyaoZhou LinyiLiu WenxiaoLi Yongqing - Primary sclerosing cholangitis (PSC) is an immune-mediated cholestatic liver disease. Its molecular etiology remains poorly defined, hindering the development of mechanism-based diagnostics and therapies. Therefore, this study aimed to identify key molecular drivers and causal biomarkers of PSC by integrating transcriptomics, machine learning, and genetic causal inference. - Source: PubMed
Publication date: 2026/03/20
Cheng PengfeiQiang YuanmingSun YiboDuan BinweiOuyang YaboLi Guangming - Sorafenib resistance remains a major challenge in the treatment of hepatocellular carcinoma (HCC). Through an in vivo CRISPR/Cas9 screen, we identified protein SUMOylation as a key pathway enriched in sorafenib-resistant HCC tumors. SUMO1 expression was significantly upregulated in resistant tumors and cell lines, and its modulation directly influenced sorafenib sensitivity both in vitro and in vivo. Proteomic analysis revealed that SUMO1 overexpression enhanced glycolysis, and metabolic assays confirmed increased extracellular acidification rate (ECAR) and decreased oxygen consumption rate (OCR) in SUMO1-high cells. We further identified PKM2 as a key SUMOylation target, mediated by the E3 ligase TRIM28. The SUMOylation of PKM2 increased its enzymatic activity, promoted aerobic glycolysis, and conferred sorafenib resistance. The inhibition of PKM2 with Compound 3k reversed glycolytic flux and restored sorafenib sensitivity. Clinically, SUMOylated PKM2 was highly expressed in HCC tumors and was associated with the expression of markers of glycolysis and sorafenib resistance in HCC. Our study revealed a novel SUMO1-PKM2 axis that drives glycolysis and sorafenib resistance in HCC, suggesting a potential therapeutic target for overcoming drug resistance. - Source: PubMed
Publication date: 2026/07/16
Yuan HongchaoLu YuanjunJiang ZhuofengChan Yau-TuenWu JunyuFeng ZixinXu LinLi QiuchengLu PengdeKwok Chun-FungFong Tung-LeongHuang QinguoWei LiuyaFeng YibinChen Zhe-ShengWang Ning