USP47 antibody Host rabbit
- Known as:
- USP47 (anti-) Host host: rabbit
- Catalog number:
- 'ARP59333_P050
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- ACR
- Gene target:
- USP47 antibody Host rabbit
Related genes to: USP47 antibody Host rabbit
- Gene:
- USP47 NIH gene
- Name:
- ubiquitin specific peptidase 47
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 11p15.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-04
- Date modifiied:
- 2016-10-05
Related products to: USP47 antibody Host rabbit
Related articles to: USP47 antibody Host rabbit
- The complex pathophysiological mechanism of end-stage renal disease (ESRD) has not been fully understood. Cuproptosis is a newly discovered type of programmed cell death. Therefore, this study attempts to clarify the relationship between cuproptosis-related genes (CRGs) and the phenotype of ESRD. - Source: PubMed
Publication date: 2026/07/01
Ma DeJianWei YiHu XiaoJingGao YanRongHou BoZheng ShuTingWang ShaoHui - Osteosarcoma (OS) is the most prevalent primary malignant bone tumor in children. We previously showed that rotenone suppressed OS cell metastasis. However, its effects on OS cell growth and the underlying mechanisms remain unclear. The purpose of this study was to investigate the role of rotenone in OS and identify its direct target. - Source: PubMed
Publication date: 2026/05/04
Li ZhenMa XiangMa HengweiChen BaoJiang KunZhu ZiqiangWang JianqiangWang BaoqingWang YunqingDong Suwei - Metabolic-associated fatty liver disease (MAFLD) is a common chronic liver disease caused by lipid accumulation in hepatocytes, and multiple deubiquitinating enzymes (DUBs) have been reported to play roles in the pathogenesis of MAFLD. However, the role of ubiquitin-specific protease 47 (USP47) in MAFLD remains unclear. - Source: PubMed
Publication date: 2026/04/01
Cao YaWen ZhengrongChen JiachuanZhang HuangyanLi QiaoyangHu Zongqiang - Liver fibrosis is a pathological process caused by excessive deposition of extracellular matrix (ECM) in the liver stimulated by chronic injury or inflammation. Nuclear pore protein 85 (NUP85) has been implicated in the development of various liver diseases. However, its involvement in liver fibrosis remains unclear. The present study aimed to explore the role of NUP85 in liver fibrosis. The expression level of NUP85 was found to be elevated in the liver tissues of liver fibrosis patients and mice. Knockdown of NUP85 not only ameliorated liver injury and collagen deposition, but also suppressed endoplasmic reticulum stress (ERS). Conversely, the opposite pathological and biochemical changes are observed with NUP85 overexpression. Mechanistically, NUP85 competitively binds ubiquitin-specific peptidase 47 (USP47) to apoptosis signal-regulating kinase 1 (ASK1), deubiquitinates lysine residue 805 of ASK1, and regulates the activation of ASK1, thereby exacerbating collagen deposition and ERS. Furthermore, we developed a CREKA-coupled liposome as a targeted delivery system to deliver Mogroside V (MV), a pharmacological inhibitor of NUP85, to activated HSCs and attenuate liver fibrosis. Taken together, the present study demonstrated that NUP85 is a novel regulator of liver fibrosis and that the NUP85-USP47-ASK1 signaling pathway might be a strategy for therapeutic intervention. - Source: PubMed
Publication date: 2026/03/28
Yang DashuaiYang HaoranPan LinxinTian ChangZuo FuchengHuang ShileiLi XianruiChen MingQian ChengWang JieChen ZhaolinXu Tao - Diabetic cataract has become the second-largest blind causing disease among the complications of diabetes mellitus in eyes. Ferroptosis is responsible for many complications associated with diabetes mellitus, but the role of ferroptosis in diabetic cataract has not yet been studied. Here, we first ascertained that ferroptosis was triggered during diabetic cataract, as identified by elevated levels of transferrin receptor protein 1 (CD71) and solute carrier family 7 member 11 (SLC7A11), lipid peroxidation , total iron and Fe under conditions of excessive glucose. Moreover, voltage-dependent anion channel 3 (VDAC3) was found to decrease under high levels of glucose both in vivo and in vitro. VDAC3 knockdown resulted in increased reactive oxygen species (ROS) levels and reduced nicotinamide adenine dinucleotide (NADH) levels, indicating that decreased VDAC3 modulates ferroptosis in diabetic cataract via ROS-induced lipid peroxidation. Furthermore, we verified that the level of ubiquitin-specific peptidase 47 (USP47) was decreased in high glucose-treated lens epithelial cells. We found that USP47 bound to and modulated the deubiquitination of VDAC3. This binding between USP47 and VDAC3 was weakened and VDAC3 was subsequently ubiquitinated and degraded under high glucose conditions, which ultimately resulted in ferroptosis and diabetic cataract. Overall, we verified that the USP47-VDAC3-ROS/NADH axis regulates ferroptosis in high glucose-treated lens epithelial cells (LECs) and in an animal model of diabetic cataract. Our findings increase the understanding of human diabetic cataract and provide important mechanistic insight into potential ferroptosis treatments in medicine and technology for treating diabetic cataract. - Source: PubMed
Publication date: 2026/03/05
Xu HaoranWang WenjingLi JianqiaoZhao XiaofeiZhang Han