PSMB7 Antibody
- Known as:
- PSMB7 Antibody
- Catalog number:
- csb-pa01345a0rb
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- PSMB7 Antibody
Related genes to: PSMB7 Antibody
- Gene:
- PSMB7 NIH gene
- Name:
- proteasome subunit beta 7
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 9q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-11-22
- Date modifiied:
- 2016-10-05
Related products to: PSMB7 Antibody
Related articles to: PSMB7 Antibody
- Psoriasis is a chronic inflammatory skin disease. Narrow-band ultraviolet B (NB-UVB) phototherapy is an effective, cost-efficient, and safe treatment for plaque psoriasis; however, predictors of treatment response remain limited. - Source: PubMed
Publication date: 2026/05/25
Yu YingyuanLi BingjieWang YuQu ZhengkaiWang XinJiang YuxiongZhong XiaoyuanChen YoudongHuang DaweiBi XinlingLu JiajingDing YangfengGong YuGu JunZhang XilinShi Yuling - Dysregulated immunometabolism is central to the pathogenesis of metabolic dysfunction-associated steatotic liver disease (MASLD). Although polyamines contribute to cellular stress responses and immune-cell function, their cell-type-specific transcriptional associations within the hepatic immune microenvironment remain incompletely understood. - Source: PubMed
Publication date: 2026/04/29
Zou PengSun LinLin Zhibin - Lung adenocarcinoma (LUAD) leads to death primarily due to its high metastatic potential. Risk assessment methodologies currently predicated on histopathological and imaging features possess a limited capacity to predict metastatic potential. Therefore, integrating single-cell transcriptomics and CT radiomics to identify key molecular drivers of metastasis and establishing a noninvasive imaging prediction model for LUAD is important. - Source: PubMed
Publication date: 2026/03/16
Wu ShengqianHu TaoCao ZhikaiLin ChengbinHuang ShuoLi YingxiZhu KeyunTian YaoHe Jinxian - This study investigated mitochondrial permeability transition-driven necrosis-related genes (MPTDNRGs) and its association with lung adenocarcinoma (LUAD). We systematically investigated their genetic variation, expression patterns, and prognostic value. A risk prediction model for MPTDNRGs was contrasted using Cox regression and least absolute shrinkage and selection operator regression analyses. MPTDNRG scores were used to quantify LUAD subtypes. We evaluated their value in the tumor microenvironment (TME), tumor mutational burden (TMB), prognostic prediction, and drug sensitivity in LUAD. The expression level, copy number variation, methylation, and microRNA (miRNA) status of PSMB7 were analyzed. We also analyzed the expression and knockdown efficiency of PSMB7 in LUAD by immunohistochemical staining, real-time fluorescence quantitative polymerase chain reaction, and western blotting. PSMB7 function in LUAD cells and in vivo was assayed using Cell Counting Kit 8, colony formation, wound healing, Transwell assays, flow cytometry, and mouse models. Seven MPTDNRG features were successfully constructed to predict LUAD prognosis and validated in an external cohort. Patients were categorized into high- and low-risk groups based on risk scores. The high-risk group exhibited shorter survival times, lower TME scores, weaker TME cell infiltration, and higher TMB scores than the low-risk group. Cancer stem cell index, mutation frequency, and drug sensitivity significantly differed between the two groups. MPTDNRG score could independently predict LUAD. PSMB7 was highly expressed in various tumors, and copy number variation, methylation, and miRNA expression significantly differed among different cancers. PSMB7 was highly expressed in LUAD tissues and cell lines. PSMB7 knockdown inhibited cancer cell proliferation, migration, invasion, and epithelial - mesenchymal transition, and promoted apoptosis. PSMB7 exerted tumorigenic effects in mice. In conclusion, we comprehensively demonstrated the characterization of MPTDNRGs in LUAD and constructed a new risk prediction model. Meanwhile, PSMB7 was shown to be a possible new target for LUAD treatment. - Source: PubMed
Publication date: 2025/12/28
Liu LinGao MingjunHe WenboWang MengmengZhou SidingWang XiaolinShu Yusheng - Tau protein aggregates exhibit distinct conformations across tauopathies, but their disease-specific protein interactions remain poorly understood. Here, we demonstrate that disease-specific tau conformations determine unique protein interaction landscapes across Alzheimer's disease (AD), progressive supranuclear palsy (PSP), and dementia with Lewy bodies (DLB). Through comprehensive interactome profiling of misfolded tau aggregates from PBS- and sarkosyl-soluble fractions. We identified 493 high-confidence proteins with remarkable disease specificity-notably, no common interactors overlapping across all three tauopathies. Machine learning classification achieved compelling discrimination between diseases using as few as 4-6 proteins features, demonstrating robust molecular signatures underlying clinical heterogeneity. AD derived tau aggregates uniquely engaged cellular metabolism machinery, including key glycolytic enzymes and TCA cycle proteins, alongside glutamate/GABA neurotransmitter cycling components, with the astrocytic glutamate transporter SLC1A2 showing 27-fold enrichment over other tauopathies. In contrast, PSP tau displayed the most distinctive profile, with extensive protein depletion (52/57 significant proteins) and selective enrichment of proteasome components, particularly PSMB7 showing >3000-fold abundance. DLB tau is associated with neurogenesis modulators while depleting neuroinflammatory mediators. These interaction patterns were validated through proximity ligation assays and correlated with distinct post-translational modification profiles, with PSP tau exhibiting globally elevated ubiquitination, AD showing mixed modification patterns, and DLB displaying minimal ubiquitination. Critically, sarkosyl-soluble fractions revealed reduced interactome complexity across diseases, except for PSP tau which maintained robust interactions with GPCR-ERK signaling and kinetochore proteins, suggesting unique aggregation mechanisms. Our findings establish that conformationally distinct tau strains dictate disease-specific protein interaction networks, providing molecular insight into tauopathy diversity and identifying novel therapeutic targets for precision medicine approaches in neurodegeneration. - Source: PubMed
Publication date: 2025/09/15
Puangmalai NichaBhatt NemilSuthprasertporn NopparatMiranda-Morales Ernesto GShchankin NikitaSamples MadisonBalci Ahmet ELiew Jia YiMontalbano MauroZhao YingxinKayed Rakez