PSMC2 Antibody
- Known as:
- PSMC2 Antibody
- Catalog number:
- XW-7935
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- PSMC2 Antibody
Related genes to: PSMC2 Antibody
- Gene:
- PSMC2 NIH gene
- Name:
- proteasome 26S subunit, ATPase 2
- Previous symbol:
- -
- Synonyms:
- MSS1, S7, Nbla10058
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-12-22
- Date modifiied:
- 2016-10-05
Related products to: PSMC2 Antibody
Related articles to: PSMC2 Antibody
- Nasopharyngeal carcinoma (NPC) mortality is driven primarily by malignant proliferation and metastasis. Although PSMC2 contributes to tumor progression, its mechanistic role in NPC pathogenesis remains undefined. - Source: PubMed
Publication date: 2026/06/03
Su JinDing ShipingHu ShousenYu JingZheng LinglingWang XinjieFeng Kun - Growing evidence highlights the critical involvement of the ubiquitin-proteasome system in cancer development. As an essential component of the 26 S proteasome, Proteasome 26 S Subunit ATPase 2 (PSMC2) has been implicated in various malignancies, but its role in hepatocellular carcinoma (HCC) progression remains poorly understood. We analyzed PSMC2 expression using The Cancer Genome Atlas database (TCGA) database, and validated findings in clinical HCC specimens and cell lines through immunohistochemistry (IHC) and Western blot. Functional assays (CCK-8, colony formation, Scratch test and transwell invasion assay) were performed to assess the oncogenic properties of PSMC2 in the progression of HCC. Mechanistic studies employed co-immunoprecipitation, Western blot, immunofluorescence and in vivo xenograft models to investigate PSMC2-EGFR interactions and downstream signaling. PSMC2 was significantly overexpressed in HCC tissues and correlated with poor patient prognosis. Genetic knockdown of PSMC2 inhibited HCC cell proliferation, migration, and invasion in vitro, while suppressing tumor growth in vivo. Conversely, PSMC2 overexpression enhanced malignant phenotypes. Mechanistically, PSMC2 physically interacted with EGFR, stabilizing EGFR protein levels and enhancing phosphorylation of downstream AKT and ERK1/2 pathways. Our study identifies PSMC2 as a novel regulator of HCC progression through EGFR-AKT/ERK1/2 signaling axis activation. These findings position PSMC2 as both a prognostic biomarker and a potential therapeutic target for HCC intervention. - Source: PubMed
Publication date: 2026/05/24
Li YechengSu QunxueFeng ZhenyuXu HuiHe Tengfei - Proteasome 26 S Subunit, ATPase 2 (PSMC2) was initially thought to be associated with the removal of misfolded or damaged proteins and the removal of excess proteins that are no longer necessary. However, recent studies have found that PSMC2 acts as an oncogene in the human body. In our research, PSMC2 serves as a tumor-initiating factor in glioma. Bioinformatics analysis of public databases, along with an examination of PSMC2 expression in glioma patients, revealed its high expression at both the mRNA and protein levels in this type of tumor. The expression of PSMC2 exhibits a negative correlation with glioma patient prognosis. Modulating PSMC2 levels through inhibition or overexpression alters glioma cell morphology and suppresses both proliferation and motility. Silencing PSMC2 impedes epithelial-mesenchymal transition (EMT), concurrently altering cellular polarity and cytoskeletal architecture. Mechanistically, proteomics analysis, corroborated by co-immunoprecipitation (CO-IP) and fluorescence co-localization assays, identified a interaction between PSMC2 and Enhancer of Zeste Homolog 2 (EZH2). Our research findings indicate that PSMC2 can promote the occurrence and development of glioma, and this process is closely related to EZH2. Targeting the PSMC2-EZH2 axis may become a promising option for glioma treatment. - Source: PubMed
Publication date: 2026/04/16
Zhu YufengLi XinlongFeng PengDai JunQiangWang JunchengYuan GuoqiangPan Yawen - The transcriptomic effects of hybridization and triploidization were investigated in diploid and triploid rainbow trout, diploid brook trout, as well as triploid hybrids of rainbow trout and brook trout. The examined fish were reared under identical conditions for about two and a half years after hatching. Expression of ten genes involved in cellular respiration (, ), mitochondrial functioning (, ), ribosome biogenesis (, ), proteasome-mediated protein turnover (, ), and protein chaperoning (, ) was studied in liver and muscle tissues. Most of the analyzed genes (, , , , , , and ) displayed comparable expression levels in the liver tissue across the examined triploid hybrids and diploid parental species, with stabilization of genes that were both positively and negatively compensated in the triploid rainbow trout. In turn, significant upregulation of , , and genes, together with downregulation of gene, was observed in the triploid rainbow trout liver and muscle, respectively. On the other hand, triploid hybrids showed marked transcriptional upregulation of genes primarily associated with energy metabolism and protein synthesis (, , , and ) relative to all the fish groups examined. Although protein-synthesis- and energy-related genes were upregulated in the muscles of triploid hybrids, the recorded growth performance data did not indicate clear evidence of growth heterosis (MPH = -14.3% for body weight; MPH = -0.4% for body length), suggesting that potential benefits of increased heterozygosity in this cross may not be fully reflected in enhanced growth. Three- to four-fold downregulation of the heat shock protein () gene was also observed in both tissues of triploid hybrids compared with purebred diploid and triploid trout, which may reflect potential maladaptive genomic effects commonly observed in distant salmonid crosses, suggesting altered stress-response regulation in the examined triploid hybrids. - Source: PubMed
Publication date: 2026/03/17
Kuciński MarcinRożyński RafałOcalewicz Konrad - In this exploratory pilot study, we profiled human periodontal ligament (PDL) transcriptomes during early orthodontic tooth movement (OTM). Early-stage (0-10 days) transcriptional dynamics under tension and compression remain insufficiently understood, and no dedicated user-friendly resource has been available for exploring large-scale human data. - Source: PubMed
Publication date: 2026/02/18
Zhang XiaoqiXing LuAi-Gumaei WaseemZhang XiaoqianWang QingxuanLi MinqiLong HuLai Wenli