PARK7 Antibody
- Known as:
- PARK7 Antibody
- Catalog number:
- 32112
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- PARK7 Antibody
Related genes to: PARK7 Antibody
- Gene:
- PARK7 NIH gene
- Name:
- Parkinsonism associated deglycase
- Previous symbol:
- -
- Synonyms:
- DJ-1, DJ1, GATD2
- Chromosome:
- 1p36.23
- Locus Type:
- gene with protein product
- Date approved:
- 2001-08-07
- Date modifiied:
- 2018-07-11
Related products to: PARK7 Antibody
Related articles to: PARK7 Antibody
- DJ-1, also known as PARK7 (Parkinson's disease protein 7), is an oncoprotein and a causative factor for hereditary recessive Parkinson's disease. DJ-1 contains three cysteines Cys46 (C46), Cys53 (C53), and Cys106 (C106) undergoing oxidation modifications under oxidative stress and affecting the anti-oxidative role of DJ-1. While C106 is known as a key catalytic active site for the enzymatic activity of DJ-1, the roles of C46 and C53 in the enzymatic activity regulation, along with the underlying mechanisms, remain poorly understood. Here, we revealed that mutations of the two cysteines resulted in decrease of both the glyoxalase and esterase activities of DJ-1. Structural analyses manifested that C46 and C53 mutations caused allosteric effects on the conformations of the catalytic active sites, which subsequently altered the interactions with the substrates. Furthermore, through modulating the reducing agent in the DJ-1 solution, we obtained the samples with varying degrees of oxidation at C46 and C53, and evidenced the influence of the oxidation states of C46 and C53 on the enzymatic activity of DJ-1. Importantly, an enhanced enzymatic activity associated with the increased oxidation of C46 in a C53-mutated background compared to wild-type DJ-1 was found. These results provide insights into the role and underlying mechanism of the mutation and oxidation modification of C46 and C53 in the glyoxalase and esterase activity of DJ-1, and offer informative clues for developing allosteric drugs potentially improving the enzymatic activity of DJ-1, which may facilitate the treatment of Parkinson's disease. - Source: PubMed
Publication date: 2026/08/17
Xia YupiaoHe XiaolingZhang YuanyuanWang ZiHu RuiLi YingZhu JiangYang YunhuangLiu Maili - Parkinson's disease (PD) is a neurodegenerative disease characterized by progressive loss of dopaminergic neurons. Studies have shown that mesenchymal stem cells (MSCs) have prominent neuroprotective potential to improve PD. Previous study found that dental pulp‑derived MSCs, including stem cells from human exfoliated deciduous teeth (SHED), significantly ameliorated PD-related pathology, but the underlying molecular mechanism remains unclear. In this study, HSPB1 and PARK7 were initially identified through transcriptomic analyses of mouse and clinical samples, immunoprecipitation‑mass spectrometry (IP‑pulldown), and protein‑protein interaction (PPI) network analysis. Using an MPTP-induced SH-SY5Y cell model of PD, we found that SHED treatment alleviated oxidative stress, restored mitochondrial membrane potential, and inhibited apoptosis, accompanied by significant upregulation of HSPB1 and PARK7. Using siRNA interference, we confirmed that both HSPB1 and PARK7 are involved in the improvement of PD by SHED. Rescue experiments showed that HSPB1 overexpression partially restored the neuroprotective effects impaired by PARK7 knockdown, whereas PARK7 overexpression failed to compensate for HSPB1 deficiency, suggesting a functional dependence between PARK7 and HSPB1 in SHED-mediated neuroprotection. This study demonstrates that SHED improves PD pathological progression through the PARK7/HSPB1-related mechanism and indicates that HSPB1 may serve as a potential therapeutic target for PD. - Source: PubMed
Publication date: 2026/08/14
Yu YiqiChen HongyuZheng JingleiLiu ShutingWang XiaoXing CencanDu Hongwu - Ulcerative colitis (UC) and psoriasis (PS) are both chronic inflammatory disorders that frequently occur together in clinical settings. Nevertheless, the common genetic basis and biological mechanisms underlying this comorbidity remain insufficiently understood. - Source: PubMed
Publication date: 2026/08/11
Liu GuoWu NaLuo QinghuaHu Siyao - [This retracts the article DOI: 10.1016/j.omto.2021.01.013.]. - Source: PubMed
Publication date: 2026/07/24
He XiangyiSun YunweiFan RongSun JingZou DouwuYuan Yaozong - Triple-negative breast cancer (TNBC) has a poor prognosis due to the lack of targeted treatment. Previous studies have shown that the deubiquitinase UCHL1 is significantly upregulated in TNBC tissues and positively correlated with shorter overall survival in patients, suggesting that UCHL1 may drive TNBC progression. The latest research suggests that ferroptosis deficiency can promote tumor metastasis, but it is still unclear whether UCHL1 affects TNBC by regulating ferroptosis. Based on the potential role of UCHL1 in ferroptosis, we propose the hypothesis that UCHL1 enhances the survival and invasion ability of TNBC cells by inhibiting ferroptosis. We downloaded the single-cell RNA sequencing dataset for breast cancer (GSE176078) from the Gene Expression Omnibus database and integrated it with The Cancer Genome Atlas data to conduct bioinformatics analysis, focusing on identifying key genes related to TNBC. We performed gene set enrichment analysis (GSEA) to explore the pathways associated with UCHL1. After that, we validated the expression of UCHL1 in TNBC tissues and cell lines and examined its influence on cell proliferation, migration, and invasion through functional experiments. Finally, we explored the downstream targets of UCHL1, utilizing co-immunoprecipitation, western blot, immunofluorescence colocalization, and establishing TNBC xenograft models in nude mice to elucidate its mechanisms in TNBC progression. Public database analysis revealed high levels of UCHL1 in TNBC. Additional research confirmed its overexpression in TNBC tissues and cells, along with significantly increased TNBC cell proliferation, migration, and invasion associated with high UCHL1 expression. GSEA further identified UCHL1 as being predominantly enriched in pathways related to ferroptosis. UCHL1 interacted with Parkinson's disease-related glycosylation enzyme PARK7 and reduced the degradation of PARK7 protein, which was mediated through the ubiquitin-proteasome pathway. Lastly, both in vitro and in vivo studies revealed that the UCHL1-PARK7 axis fostered tumor progression in TNBC by inhibiting ferroptosis. UCHL1 deubiquitinates and stabilizes PARK7, thereby inhibiting ferroptosis and boosting tumor progression in TNBC, indicating the potential of UCHL1 and PARK7 as therapeutic targets for TNBC patients. - Source: PubMed
Publication date: 2026/07/31
Chen ShaojunLiang NaZhang YimingLi ZhuoyingHou HaiqinLi HuanZhang Wenxia