USP7 Active Human Recombinant Protein
- Known as:
- USP7 Active Human Recombinant Protein
- Catalog number:
- 80395
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- BPS Bioscience
- Gene target:
- USP7 Active Human Recombinant Protein
Related genes to: USP7 Active Human Recombinant Protein
- Gene:
- USP7 NIH gene
- Name:
- ubiquitin specific peptidase 7
- Previous symbol:
- HAUSP
- Synonyms:
- -
- Chromosome:
- 16p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-12
- Date modifiied:
- 2017-01-04
Related products to: USP7 Active Human Recombinant Protein
Related articles to: USP7 Active Human Recombinant Protein
- Advanced bladder cancer (BLCA), a malignancy with high recurrence, carries a dismal prognosis, demanding the identification of novel therapeutic targets. In this study, we aim to investigate a critical molecular mechanism driving BLCA progression. By integrating published sequencing datasets, we identified that POC1A is overexpressed in BLCA tissues, a factor positively correlated with advanced stage, high grade, disease progression, and inversely correlated with overall survival. In vitro and in vivo analyses indicate that POC1A knockdown inhibits BLCA cell proliferation, metastasis, and stemness. Mechanistically, POC1A functions as a scaffold protein, forming a complex with USP7 and BMI1. This enhances the USP7-BMI1 interaction, reduces BMI1 ubiquitination in a USP7-dependent manner, and consequently stabilizes the BMI1 protein. The functional significance of this pathway was confirmed as overexpression of either BMI1 or USP7 rescued the inhibitory phenotypes induced by POC1A knockdown. Furthermore, pharmacological targeting of BMI1 with Unesbulin suppressed BLCA growth in cell-line and patient-derived xenograft models, supporting the therapeutic tractability of the POC1A-BMI1 axis. Taken together, these findings reveal that POC1A facilitates the USP7-mediated deubiquitination and stabilization of BMI1, establishing the POC1A-USP7-BMI1 complex as a compelling therapeutic target in BLCA. - Source: PubMed
Publication date: 2026/08/31
Wei HouyiBai RenranLiu JianminLyu LeiYuan JingdongXiang WanQian KaiyuChen FangjinJu LingaoZhang YiXiao YuWang Gang - Spinal cord injury (SCI) is a severe neurological disorder with limited therapeutic options. 6-gingerol, a major bioactive component of ginger, possesses anti-inflammatory and neuroprotective activities; however, its role in SCI remains incompletely understood. This study investigated the effects and underlying mechanisms of 6-gingerol in SCI-induced microglial pyroptosis. A rat SCI model was established and treated with 6-gingerol. Neurological function, histopathological changes, microglial activation, and pyroptosis were evaluated. An LPS/ATP-induced BV2 microglial pyroptosis model was used for in vitro mechanistic studies. Cell viability, LDH, pyroptosis-related proteins, and inflammatory cytokines were analyzed. The expression of EZH2, USP7, and FOXO3 was determined by qRT-PCR and Western blot. Chromatin immunoprecipitation was performed to evaluate EZH2 and H3K27me3 mediated regulation of the USP7 promoter, while co-immunoprecipitation and ubiquitination assays were used to examine the interaction between USP7 and FOXO3. 6-gingerol significantly improved locomotor recovery, attenuated spinal cord tissue damage, and reduced microglial pyroptosis and inflammatory response after SCI. Mechanistically, 6-gingerol suppressed EZH2 expression and reduced H3K27me3 enrichment at the USP7 promoter, thereby restoring USP7 expression. Increased USP7 enhanced FOXO3 deubiquitination and stabilization, leading to suppression of pyroptotic signaling. Furthermore, EZH2 overexpression, USP7 inhibition, or FOXO3 knockdown partially abolished the anti-pyroptotic effects of 6-gingerol in vitro, and EZH2 overexpression attenuated the neuroprotective effects of 6-gingerol in SCI rats. In conclusion, 6-gingerol treatment alleviates SCI-induced neuroinflammation and microglial pyroptosis through the EZH2/USP7/FOXO3 axis, highlighting a potential therapeutic strategy for SCI. - Source: PubMed
Publication date: 2026/08/31
Li JunjieHu JinfengLiang ShuhanLuo JinxinRao Yaojian - The pathology of intervertebral disc degeneration (IDD) is characterized by metabolic dysregulation within nucleus pulposus (NP) cells. TRIM25 has been implicated in diverse tumors and pathological processes, yet its precise role in mediating mitochondrial function and metabolic alterations during IDD progression remains unclear. - Source: PubMed
Liu XiaomingZhang WenyuFeng HangLai LinyingCao ChenYang GuangGao YanzhengWang BijunWang HuiYu BinYu Zhenghong - Dauriporphine is a monomer extracted from Menispermum dauricum DC, and it exhibits anti-cancer effect in non-small cell lung cancer (NSCLC). The regulatory mechanism of dauriporphine remains incompletely understood, and this study focused on its molecular targets in NSCLC progression. Cell viability, proliferation, apoptosis, invasion, migration, and stemness were evaluated using cell counting kit-8, ethynyl-2'-deoxyuridine assay, flow cytometry, transwell assay, scratch assay, and sphere formation assay, respectively. Bioinformatics analysis and weighted gene co-expression network analysis (WGCNA) were performed to identify targets of dauriporphine in NSCLC. The mRNA and protein expression was quantified using qPCR and Western blot. Co-immunoprecipitation was used to analyze protein interaction and ubiquitination regulation between ubiquitin-specific protease 7 (USP7) and calcium/calmodulin-dependent serine protein kinase (CASK). The role of dauriporphine in vivo was explored using xenograft tumor model. Dauriporphine restrained proliferation, invasion, migration, and stemness of NSCLC cells (p < 0.05). Bioinformatics analysis and WGCNA identified CASK as a core target of dauriporphine in NSCLC. CASK was highly up-regulated in NSCLC samples and cells (p < 0.05). Anti-cancer effects of dauriporphine on NSCLC cells were associated with reduced CASK expression (p < 0.05). USP7 stabilized CASK protein by inducing deubiquitination (p < 0.05). Silencing USP7 restrained NSCLC cell proliferation, metastasis, and stemness by inhibiting CASK (p < 0.05). Dauriporphine interacted with USP7, and then USP7 overexpression reversed the inhibition of dauriporphine in NSCLC cell malignant behaviors (p < 0.05). Dauriporphine reduced tumor growth in vivo and down-regulated USP7 and CASK expression (p < 0.05). This study suggested that dauriporphine blocked the key malignant phenotypes of NSCLC cells via inhibiting USP7-mediated deubiquitination of CASK, thereby promoting its proteasomal degradation. The study elucidates a molecular mechanism underlying anti-tumor role of dauriporphine and providing potential targets for dauriporphine treatment. - Source: PubMed
Hou PengxiaoWu Qian - : Ubiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme that regulates multiple oncogenic and tumor-suppressive pathways and has emerged as a promising target for anticancer drug discovery. However, most reported USP7 inhibitors belong to a limited number of structural classes, and no USP7-targeted therapy has yet reached clinical application. This study aimed to identify structurally diverse candidate USP7-inhibitory scaffolds with antiproliferative activity using an integrated computational and experimental screening strategy. : A drug discovery workflow combining pharmacophore modelling, structure-based virtual screening, molecular docking, and in silico pharmacokinetic assessment was employed to identify candidate USP7 inhibitors. Selected compounds were evaluated for inhibition of recombinant USP7 and for antiproliferative activity in a panel of human cancer cell lines. Molecular docking analyses were performed to investigate predicted binding modes. : The primary screening campaign identified four active compounds (>50% inhibition at 10 µM) and twenty-one weakly active compounds (10-49% inhibition at 10 µM), including structurally distinct approved drugs and compounds from an in-house chemical library. The four active compounds were subsequently validated by dose-response assays against recombinant USP7 and exhibited micromolar inhibitory activity. These candidate USP7-inhibitory scaffolds also exhibited antiproliferative activity across cancer cell lines with different molecular backgrounds. Docking studies predicted binding within a pharmacologically relevant region of the USP7 catalytic cleft and revealed putative interactions with key residues involved in ligand recognition. Among the compounds evaluated, rafoxanide demonstrated the most favorable combination of predicted USP7 binding and antiproliferative activity. : This integrated virtual screening and experimental validation approach enabled the identification of candidate USP7-inhibitory scaffolds with preliminary antiproliferative activity. The identified hits include approved drugs with previously unreported USP7 inhibitory activity, as well as underexplored scaffolds that expand the chemical space of candidate USP7-targeting molecules. These candidate scaffolds warrant further medicinal chemistry optimization, orthogonal validation, and mechanistic characterization to establish their potential as USP7-targeted anticancer agents. - Source: PubMed
Publication date: 2026/08/03
Oliveira Rita IFranco CaioMano MiguelLeal Ana SSalvador Jorge A R