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
- Protein -sulfinylation is a reversible oxidative cysteine modification, but its contribution to acute liver injury such as those induced by acetaminophen (APAP) overdose has not been reported. Sulfiredoxin-1 (SRXN1) is the only oxidoreductase known to reduce the sulfinylated proteins, yet the substrates and mechanisms through which it protects against acute liver injury are unclear. Here, we show that hepatic protein -sulfinylation was markedly upregulated in APAP-overdose patients and mice. Hepatocyte-specific knockout or pharmacological inhibition of sensitized mice to APAP-induced acute liver injury. In contrast, overexpression of SRXN1, but not its oxidoreductase-dead C99S mutant, protected mice from APAP-induced liver injury. Mechanistically, we identified the deubiquitinase ubiquitin-specific protease 7 (USP7) as an SRXN1 substrate required for hepatoprotection. USP7 inhibition worsened APAP-induced liver injury, whereas its overexpression alleviated injury by stabilizing its deubiquitinase substrate heme oxygenase-1 (HO-1). Loss of SRXN1 enhanced -sulfinylation of USP7 at Cys315, promoting its ubiquitination and degradation. SRXN1 expression correlated with USP7 levels in human liver samples. Delayed lipid nanoparticle (LNP) delivery of SRXN1 messenger RNA (mRNA) mitigated established APAP-induced liver injury beyond the therapeutic window of -acetylcysteine. These findings define an SRXN1-USP7-HO-1 axis as a promising therapeutic target for oxidative liver injury and highlight LNP-mediated SRXN1 mRNA delivery as a potential treatment approach. - Source: PubMed
Publication date: 2026/09/29
Ke MengyunKim Jong-WonXu MeishuWang JingyuanLiu LingyiN P SyamprasadYang BinWang XiaofeiLi HuatianRen SongrongCarroll Kate SLi SongXie Wen - Ubiquitination is a crucial post-translational modification of proteins in eukaryotic cells. Deubiquitinating enzymes (DUBs) remove ubiquitin molecules from substrate proteins, thereby reversing ubiquitination and maintaining intracellular ubiquitin homeostasis. Dysregulation or dysfunction of DUBs is closely associated with various diseases. Among them, the ubiquitin-specific protease (USP) family, the largest subfamily of DUBs, plays a key regulatory role in tumor initiation and progression. This article systematically reviews the research progress on five representative USP family members closely linked to tumors, including USP7, USP22, USP10, USP35, and USP4, with a focus on their functional mechanisms in regulating major tumor-related signaling molecules and pathways, including p53, PTEN, c-Myc, and PD-L1. It also highlights their dual regulatory roles in tumor proliferation, resistance to apoptosis, metastasis, and immune evasion. Furthermore, this review summarizes the structural basis of USP catalysis and selectivity, the determinants of context-dependent USP functions, and the emerging roles of DUBs in tumor microenvironment remodeling and therapy resistance. We also discuss the latest advances in the development of selective inhibitors and new therapeutic modalities targeting these USPs, including PROTAC-mediated degradation, DUBTAC-mediated tumor suppressor stabilization, and molecular glue strategies. Although targeting DUBs for cancer therapy faces challenges such as substrate diversity, context-dependent functions, and functional redundancy within the family, it remains a promising strategy for tumor treatment. This review provides a theoretical foundation and research directions for further understanding the roles and mechanisms of the USP family in cancer and for developing targeted DUB-based anti-tumor therapies. - Source: PubMed
Publication date: 2026/09/10
Wang YananShi Jing - Precise and rapid control over cellular protein levels is essential to dissect complex biological systems. Chemical genetic approaches such as dTAG, in which a target is fused to a degron tag (FKBP12) and degraded upon small molecule-mediated recruitment of E3 ligases, have enabled rapid and tunable control over protein abundance. However, no analogous tool exists to precisely increase protein levels and actively reverse dTAG-mediated degradation. Here, we developed heterobifunctional small molecules (dubTAGs) that stabilize FKBP12-tagged proteins by recruiting endogenous deubiquitinases. Utilizing stem cell-derived cranial neural crest cells (CNCCs) in which the transcription factors SOX9 or TWIST1 are endogenously tagged with FKBP12, we identified OTUB1- or USP7-recruiting heterobifunctional molecules that demonstrated effective target stabilization and ternary complex formation. We demonstrate that dubTAG-mediated protein stabilization is dependent on deubiquitinase recruitment, target-specific, and can tunably and rapidly reverse dTAG-mediated degradation. We applied dubTAGs to assess how stabilizing endogenous SOX9 impacts chromatin accessibility in CNCCs, finding both monotonic and non-monotonic regulatory element responses that are driven by distinct sequence features. dubTAGs are readily applicable tools for investigating the effects of elevated protein levels and tunably reversing targeted degradation, enabling new approaches to study protein dosage effects in development, disease, and therapeutic discovery. - Source: PubMed
Publication date: 2026/09/18
Guharajan SunilSong XiangyangSengupta SachiWu QiongWei WenyiXiong YanJin JianNaqvi Sahin - Metabolic reprogramming, particularly dysregulated lipid metabolism, is a hallmark of clear cell renal cell carcinoma (ccRCC) progression. However, the upstream regulators responsible for lipid metabolic rewiring remain largely unknown. Here, we integrated single-cell RNA sequencing, spatial transcriptomics, and functional validation to identify MCM10 as a critical regulator of lipid metabolism in ccRCC. Single-cell and spatial analyses revealed that MCM10 was predominantly expressed in malignant epithelial cells and positively associated with lipid metabolic activity and poor clinical outcomes. Functional studies demonstrated that MCM10 promoted ccRCC cell proliferation, migration, and lipid accumulation in vitro and enhanced tumor growth and metastasis in vivo. Mechanistically, MCM10 interacted with c-Myc and increased its protein stability by facilitating USP7-mediated deubiquitination and suppressing FBW7-dependent ubiquitination. Stabilized c-Myc directly bound to the promoter region of fatty acid synthase (FASN) and transcriptionally activated FASN expression, thereby promoting de novo fatty acid synthesis and lipid metabolic reprogramming. Collectively, our study reveals a previously unrecognized role of MCM10 in regulating lipid metabolic remodeling through the USP7/c-Myc/FASN axis and provides new insights into the molecular mechanisms underlying ccRCC progression. These findings suggest that targeting the MCM10-mediated metabolic pathway may represent a potential therapeutic strategy for ccRCC. - Source: PubMed
Publication date: 2026/09/23
Du AshuaiJiang KehuaLi KaiDeng XinpeiYuan DongboLuo YuanyuanTan SongsongDai XuchaoYu BoYan BoHuang HuichaoXu JunjieWang YanjunZhu Jianguo - Multiple myeloma (MM) is the second most common hematological malignancy. Ferroptosis, a distinct form of programmed cell death, has attracted the interest of researchers because of its unique role and biological significance across various diseases. As a first-line clinical treatment drug for MM, lenalidomide (LEN) has shown remarkable therapeutic efficacy. Accumulating evidence has highlighted the significant role of LEN in MM treatment; however, to date, no studies have investigated its potential efficacy in the ferroptosis pathway of MM and the underlying mechanisms. To investigate the therapeutic effects of LEN on MM, several in vitro and in vivo experiments were performed. Our data confirmed that LEN exerts antitumor activity in a dose-dependent manner by inducing ferroptosis, which is characterized by an abnormal increase in ROS and MDA levels, a decrease in GSH levels and mitochondrial membrane potential, and iron overload. Mechanistically, in vitro experiments have revealed that LEN directly targets the c-Maf protein and subsequently suppresses USP7 transcription, thereby inducing FTH1 degradation via the ubiquitin-proteasome pathway, triggering ferroptosis in MM cells. Finally, in vivo experiments demonstrated that LEN (10 mg/kg) significantly suppresses the c-Maf/USP7/FTH1 signaling pathway, further inhibiting MM growth by triggering ferroptosis. In conclusion, this study is the first to demonstrate that LEN suppresses MM by inducing ferroptosis via FTH1-dependent iron homeostasis, suggesting that the ferroptosis induced by the c-Maf/USP7/FTH1 signaling pathway during LEN treatment is a novel mechanism underlying its antitumor activity. - Source: PubMed
Publication date: 2026/09/19
Zhang ErhaoZhang TingtingXu JinjinZhang YufeiCui JiananLi XiaominXu JintaoZhang TenglongJia HuiLin ZenghuaXu LiqinGuo DanHuang Hongming