ABHD10 (Human) Recombinant Protein (P01)
- Known as:
- ABHD10 (Human) Recombinant Protein (P01)
- Catalog number:
- H00055347-P01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- ABHD10 (Human) Recombinant Protein (P01)
Related genes to: ABHD10 (Human) Recombinant Protein (P01)
- Gene:
- ABHD10 NIH gene
- Name:
- abhydrolase domain containing 10
- Previous symbol:
- -
- Synonyms:
- FLJ11342
- Chromosome:
- 3q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-24
- Date modifiied:
- 2012-03-26
- Gene:
- BZW2 NIH gene
- Name:
- basic leucine zipper and W2 domains 2
- Previous symbol:
- -
- Synonyms:
- HSPC028, MST017, MSTP017
- Chromosome:
- 7p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-05
- Date modifiied:
- 2016-10-05
- Gene:
- C2CD3 NIH gene
- Name:
- C2 calcium dependent domain containing 3
- Previous symbol:
- -
- Synonyms:
- DKFZP586P0123
- Chromosome:
- 11q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2007-10-17
- Date modifiied:
- 2016-06-08
- Gene:
- MBTD1 NIH gene
- Name:
- mbt domain containing 1
- Previous symbol:
- -
- Synonyms:
- SA49P01, FLJ20055
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-15
- Date modifiied:
- 2015-04-21
- Gene:
- TMEM63C NIH gene
- Name:
- transmembrane protein 63C
- Previous symbol:
- C14orf171
- Synonyms:
- DKFZp434P0111, CSC1, hsCSC1
- Chromosome:
- 14q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-10
- Date modifiied:
- 2017-10-17
Related products to: ABHD10 (Human) Recombinant Protein (P01)
Related articles to: ABHD10 (Human) Recombinant Protein (P01)
- Purines are essential bioactive molecules that interact with a large fraction of the human proteome. Despite their importance, the scope of actionable purine-binding pockets for ligand discovery remains limited. Here, we develop a quantitative chemoproteomics platform using sulfonyl-purine (SuPUR) chemistry to produce a massive and functional map of the human purine interactome. The SuPUR platform captures 31,000+ targetable tyrosine and lysine sites, representing the most comprehensive beyond cysteine chemoproteomics database for enabling protein ligand discovery. SuPUR ligands that bind through a regioselective fashion serve as enabling starting points for developing potent (nanomolar) and proteome-wide-selective modulators of enzymatic and protein-protein interaction function. Phenotypic screening identifies a site-specific (Y237) and regioselective SuPUR ligand of ACAT2 to reveal an unexpected metabolic dependency in cancer cells. A crystal structure of SuPUR ligand-bound ACAT2 reveals the purine group binds deep in the CoA pocket forming key interactions with catalytic residues via a water bridge to guide future structure-based ligand design. - Source: PubMed
Publication date: 2026/06/05
Li ZhihongTsai Hsiao-KueiLibby Adam HFounds Michael WMurtagh Olivia LWare Madeleine LLeace David MWolfe Wesley JGingrich Phillip WAl-Lazikani BissanChang Chin-YuanHsu Ku-Lung - Presbycusis is caused by multiple factors, the mechanisms of which are not fully understood. This study investigated mitochondria-related genes in presbycusis, a condition with multifactorial and incompletely understood mechanisms, by combining Mendelian randomization analysis and functional validation. Genetically predicted higher ABHD10 expression was identified as a protective factor against presbycusis and was regulated by methylation sites such as cg15684481, whereas methylation at other sites inhibited ABHD10 expression and alleviated the condition. In contrast, ABHD10 was upregulated in d-galactose-induced HEI-OC1 cells and aged mouse cochlear hair cells, where it promoted senescence. Silencing ABHD10 in senescent cells reduced P21 and P16 protein levels, decreased reactive oxygen species levels, improved mitochondrial membrane potential, and lowered lipid droplet formation along with triglycerides and fatty acids. Co-immunoprecipitation experiments showed that ABHD10 interacts with KCMF1, indicating that the complex may regulate cellular metabolism and stress responses through signaling pathways. This was supported by GO and KEGG analyses linking ABHD10 to aging-related processes such as energy metabolism and oxidative stress. Overall, ABHD10 functions as a context-dependent mitochondrial regulator, with the ABHD10-KCMF1 axis integrating mitochondrial quality control, lipid homeostasis, and redox balance, thereby offering a potential druggable target for presbycusis. - Source: PubMed
Peng LuLiao XingweiLiu YingQiu ChunqinTang ZhenzhenHuang ZhanrongLiao HongxiangYin Shihua - Palmitoylation is the only fully reversible post-translational lipid modification that impacts 10-20% of the human proteome, but its role during spermatogenesis remains enigmatic. In this study, through generating HA-tagged Abhd10 knock-in mice, Abhd10-null mice, and combining super-resolution fluorescence imaging and electron microscopy, we identify that the S-depalmitoylase ABHD10 (abhydrolase domain containing 10) is a mitochondrial matrix protein, specifically expressed in testis and is essential for male fertility. Abhd10 knockout mice manifest severe sperm motility defects accompanied by malformed mitochondrial sheaths of sperm. Mitochondrial proteomic analysis reveals that ABHD10 deficiency downregulates respiratory chain complex proteins and mitochondrial sheath formation factors SPATA19 and GK2. Using mass spectrometry-based mitochondrial acyl-biotin exchange assays, we systematically identify that loss of ABHD10 leads to the hyper-palmitoylation of multiple functionally critical proteins, including mitochondrial sheath formation factors (SPATA19 and GK2) and aerobic respiration regulators (PDHX, NDUFV1 and SDHB). Co-immunoprecipitation and proximity labeling assays reveal the physical interactions between ABHD10 and its substrates (SPATA19, GK2, PDHX). Collectively, ABHD10 may bind to and mediate the S-depalmitoylation of SPATA19, GK2, and PDHX, thereby regulating the formation of the sperm mitochondrial sheath and mitochondrial function. This work not only identifies S-depalmitoylase ABHD10 as a key determinant of male fertility but also advances our understanding of post-translational regulation during spermatogenesis. - Source: PubMed
Publication date: 2025/11/24
Zhou ShuminZhou HaoXu HaoranXiong MengnengGan ShimingLiu DalinZhao YifanYu ZiqiLuo ChunhaiZhang YujunZhang BeibeiSun Fei - Cardiac conduction disorders predispose individuals to arrhythmias, currently but the exact mechanisms of cardiac conduction remain elusive. The study sought to identify the causal association between circulating plasma proteins and electrocardiogram (ECG) traits, offer valuable biological insights and clinical guidance into cardiac conduction. - Source: PubMed
Publication date: 2024/10/31
Zhao PengMeng LiHan FeiyuanYu ZhongzhiWang YidanWu YunfeiWang YanYu BoLiu XinxinTian Jinwei - Alcoholic liver disease (ALD) and other forms of chronic hepatotoxic injury can lead to transforming growth factor β1 (TGFβ1)-induced hepatic fibrosis and compromised liver function, underscoring the need to develop novel treatments for these conditions. Herein, our analyses of liver tissue samples from severe alcoholic hepatitis (SAH) patients and two murine models of ALD reveals that the ALD phenotype was associated with upregulation of the transcription factor ETS domain-containing protein (ELK-3) and ELK-3 signaling activity coupled with downregulation of α/β hydrolase domain containing 10 (ABHD10) and upregulation of deactivating S-palmitoylation of the antioxidant protein Peroxiredoxin 5 (PRDX5). In vitro, we further demonstrate that ELK-3 can directly bind to the ABHD10 promoter to inhibit its transactivation. TGFβ1 and epidermal growth factor (EGF) signaling induce ABHD10 downregulation and PRDX5 S-palmitoylation via ELK-3. This ELK-3-mediated ABHD10 downregulation drives oxidative stress and disrupts mature hepatocyte function via enhancing S-palmitoylation of PRDX5's Cys100 residue. In vivo, ectopic Abhd10 overexpression ameliorates liver damage in ALD model mice. Overall, these data suggest that the therapeutic targeting of the ABHD10-PRDX5 axis may represent a viable approach to treating ALD and other forms of hepatotoxicity. - Source: PubMed
Publication date: 2023/07/03
Li Tian-ZhuBai Chun-YingWu BaoZhang Cong-Ying Wang Wen-TaoShi Tie-WeiZhou Jing