PSMA4 antibody Host Mouse
- Known as:
- PSMA4 (anti-) Host Mouse
- Catalog number:
- 'H00005685-A01
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- ACR
- Gene target:
- PSMA4 antibody Host Mouse
Related genes to: PSMA4 antibody Host Mouse
- Gene:
- PSMA4 NIH gene
- Name:
- proteasome subunit alpha 4
- Previous symbol:
- -
- Synonyms:
- HC9, HsT17706
- Chromosome:
- 15q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-03
- Date modifiied:
- 2016-10-05
Related products to: PSMA4 antibody Host Mouse
Related articles to: PSMA4 antibody Host Mouse
- Lung adenocarcinoma (LUAD) remains a leading cause of cancer-related mortality worldwide, and although targeted therapy and immunotherapy have improved clinical outcomes, their long-term efficacy is frequently limited by therapeutic resistance, underscoring the need to identify additional biologically relevant and potentially actionable targets. In this study, we applied summary-data-based Mendelian randomization (SMR) by integrating lung cancer genome-wide association study (GWAS) summary statistics with cis-expression quantitative trait locus (cis-eQTL) and cis-methylation quantitative trait locus (cis-mQTL) datasets to prioritize candidate genes associated with LUAD risk. The robustness of SMR-significant signals was further evaluated using the heterogeneity in dependent instruments (HEIDI) test and Bayesian colocalization analysis. Independent transcriptomic datasets from the Gene Expression Omnibus (GEO), together with multiple public databases, were used for expression and prognostic validation, while protein-protein interaction (PPI) and functional enrichment analyses were performed to provide mechanistic context. Among 13 genes prioritized by integrative genetic analyses, PSMA4 (Proteasome 20S Subunit Alpha 4) emerged as the leading LUAD-relevant candidate on the basis of convergent multi-omics evidence, colocalization support, reproducible overexpression (OE) across independent cohorts, and adverse prognostic association. Functional experiments demonstrated that PSMA4 knockdown (KD) suppressed LUAD cell proliferation, migration, invasion, and xenograft tumor growth, whereas PSMA4 overexpression produced the opposite effects. Mechanistically, PSMA4 interacted with p53 and facilitated the proteasome-dependent turnover of ubiquitinated p53, as supported by co-immunoprecipitation, immunofluorescence, ubiquitination, proteasome inhibition, and cycloheximide chase assays, thereby attenuating p53 signaling. Collectively, these findings support PSMA4 as a biologically relevant and potentially actionable target in LUAD and provide a mechanistic rationale for further translational investigation. - Source: PubMed
Publication date: 2026/04/25
Lu HuiWang SaiMa YuhangShen ZhimingYao LongKang NingningSi PanpanZhang Renquan - Atherosclerosis (AS) is a leading cause of cardiovascular disease, and current treatments often fail to induce plaque regression. This study aims to identify novel, genetically supported therapeutic targets for AS to enable more effective drug development. - Source: PubMed
Publication date: 2026/04/24
Yu YongchaoZhu YuanTian QianShao LijuanZeng JiaoXu DandanMo Xiangang - To identify specific, sensitive, and non-invasive circulating protein biomarkers that could facilitate the diagnosis of brain metastasis (BrM) and improve risk prediction for BrM among patients with non-small cell lung cancer (NSCLC). We performed data-independent acquisition mass spectrometry (DIA-MS)-based proteomic profiling of 14 tissue specimens obtained from 7 patients, together with 89 serum samples from NSCLC and NSCLC-BrM cohorts, to identify candidate biomarkers associated with BrM. A total of 12,808 proteins were identified in the tissue proteome and 6041 proteins in the serum proteome, representing an extensive proteomic analysis of lung cancer with BrM reported to date. Using integrated analyses, we identified a four-protein classifier that served as biomarkers for predicting the risk of NSCLC metastasis to the brain. Notably, PSMA4, LAP3, and LZIC were consistently downregulated in both the sera and tissues of patients with NSCLC-BrM compared with those with NSCLC without BrM. These biomarkers were subsequently validated by ELISA in an additional cohort, demonstrating high concordance with the PRM results. Immunohistochemical analyses further supported the utility of these proteins in distinguishing BrM from primary brain tumors. The integrated analysis of tissue and serum proteomics across the cohorts supports the potential value of proteomics-guided, biomarker-assisted diagnosis and risk prediction in BrM and may help enable more accurate stratification and more targeted treatment strategies. - Source: PubMed
Publication date: 2026/04/13
Zheng YongtaoXiong YuetingMa YuxiaoQiu YijieBu QingfangWang ZhenxiSun QingfangSun YuhaoLiu XiaohuiYuan QuanLi YupingBian LiuguanWang Baofeng - https://bit.ly/435kxK0. - Source: PubMed
Publication date: 2026/04/07
Jin YangXu JiuyangHu QidanLi JingyaWang YemingCao Bin - Glycogen storage disease type Ia (GSD Ia) is a rare autosomal recessive inherited disorder of carbohydrate metabolism, caused by a deficiency in glucose 6-phosphatase-α (G6PC1). Patients primarily suffer from failure to thrive, hepatomegaly, and severe fasting intolerance, biochemically characterized by hypoketotic, hypoglycemia, and hyperlipidemia. Because of clinical and biochemical heterogeneity, identifying biomarkers is imperative for prognosis and monitoring. An untargeted proteomics workflow was employed for identifying protein changes in liver and plasma from hepatocyte-specific G6pc knockout mice under fed and fasted conditions. This links the effect of hepatic G6Pase/G6pc deficiency to circulating protein biomarkers and allows assessment of the relationship with different clinical circumstances and long-term complications. In the liver, the main differences between hepatic GSD Ia mice versus controls were observed in proteins related to carbohydrate and lipid metabolism, proteasome, ribosome, NAD metabolism, and mitochondria. In GSD Ia mouse plasma, proteins were mainly down-regulated in the complement and coagulation cascades. Effects in hepatic GSD Ia mice were in general more pronounced under fasting conditions. Several potential biomarkers that showed significant alterations in both liver and plasma were identified. These include proteins involved in carbohydrate and lipid metabolism (e.g., UGP2, ALDOB, and FASN), complement and coagulation cascades (SERPINA1E, C8b, and MBL2), 20S proteasome subunits (PSMA4, PSMA7, and PSMB5), and the electron transport chain (SDHA). Their consistent changes observed in both the liver and circulation indicate their potential as circulating biomarkers reflecting liver condition. Together with their reported associations with liver diseases, we hypothesize that they could monitor hepatic complications. - Source: PubMed
Xiao Ruiqide Vries Hilda IGross-Valle CandelasBleeker AychaDerks Terry G JBakker Barbara MOosterveer Maaike HWolters Justina C