CYP2E1 Antibody
- Known as:
- CYP2E1 Antibody
- Catalog number:
- csb-pa006425ea01hu
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- CYP2E1 Antibody
Related genes to: CYP2E1 Antibody
- Gene:
- CYP2E1 NIH gene
- Name:
- cytochrome P450 family 2 subfamily E member 1
- Previous symbol:
- CYP2E
- Synonyms:
- -
- Chromosome:
- 10q26.3
- Locus Type:
- gene with protein product
- Date approved:
- 1988-03-03
- Date modifiied:
- 2015-12-09
Related products to: CYP2E1 Antibody
Related articles to: CYP2E1 Antibody
- Carbon tetrachloride (CCl4) is a potent hepatotoxin that disrupts mitochondrial function and alters cytochrome P450 (CYP450) enzyme activity. Nigella sativa (Ns) and its primary bioactive compound, thymoquinone (TQ), are known for their hepatoprotective properties, but their effects on CYP450 modulation in liver injury remain underexplored. This study aimed to evaluate the effects of Ns and TQ on CYP450 activity and expression in CCl4-induced liver injury. - Source: PubMed
Publication date: 2026/07/30
Abdel-Rasol Mohammed AAbdel Halim Alyaa SHussein Rasha AEl-Sayed Wael M - Metal alkoxides hold promise in catalysis and materials science, but their rapid hydrolysis in aqueous media represents a major limitation for biomedical applications. To harness this intrinsic reactivity therapeutically, we developed a facile ultrasonication-assisted dispersion method to fabricate nanoscale copper ethoxide (CuOEt) with subsequent screening showing their ready dispersion in Lipiodol to form a stable injectable suspension (CuOEt@LPD). Unlike bare CuOEt nanoparticles, which suffered from rapid degradation, a burst release of ethanol, and conversion to copper oxide in water, the CuOEt@LPD formulation utilized a Lipiodol protection strategy to create an effective barrier against water, enabling a sustained release of ethanol. Functionally, the released ethanol upregulated intracellular cytochrome P450 2E1 (CYP2E1), triggering metabolic oxidative stress in hepatocellular carcinoma cells, which acted synergistically with released copper ion-induced cuproptosis, ultimately leading to robust cell death. Furthermore, the Lipiodol dispersant served as a potent radiosensitizer, significantly enhancing the tumor-inhibiting efficacy upon radiotherapy in an H22 murine hepatoma model. Notably, we discovered that this trimodal therapeutic strategy could also initiate a robust antitumor immune response, which established long-lasting immunological memory, thereby effectively suppressing tumor recurrence and metastasis. Our work successfully establishes metal alkoxides nanoparticles as a highly promising class of nanotherapeutic agents for hepatocellular carcinoma treatment. - Source: PubMed
Publication date: 2026/08/05
Liu SonglingLiu YangFan QinWen KexinZhang JinqiaoYang YuechaoYang ShiningYu GongchangDong Ziliang - Cytochrome P450 2E1 (CYP2E1) plays a pivotal role in the metabolism and detoxification of low molecular-weight xenobiotics, as well as in their bioactivation into toxic and DNA-reactive intermediates. Prominent examples include drugs and chemicals like acetaminophen and N-nitrosamines. Chlorzoxazone and 4-nitrophenol are widely used as probe substrates to assess CYP2E1 activity, however, their specificity remains controversial. This study aimed to reevaluate the selectivity of chlorzoxazone and 4-nitrophenol toward CYP2E1 using recombinant Supersomes™ expressing individual human CYP isoforms. Incubations were performed with chlorzoxazone and 4-nitrophenol at 100 and 500 µM, followed by quantification of 6-hydroxychlorzoxazone and 4-nitrocatechol via UPLC-MS/MS. Chlorzoxazone turnover was detected across nearly all major liver CYP isoforms, with CYP1A1 showing the highest contribution (39%), followed by CYP2D6 (14%), CYP1A2 (10%), and CYP2E1 (10%). Similarly, 4-nitrophenol hydroxylation was not limited to CYP2E1, with significant contributions from CYP1A2 (20%), CYP2A6 (19%), and CYP2D6 (16%), while CYP2E1 accounted for 26% of total activity. In conclusion, our results underscore the limited selectivity of chlorzoxazone and 4-nitrophenol and highlight the need for more specific substrates for accurate CYP2E1 enzyme characterization. - Source: PubMed
Publication date: 2026/08/04
Hellmann AnnaLenich Ann-KathrinRuez StephanieFahrer JörgLott JasminSchaefer Michelle - To examine the effect of chronic alcohol exposure on the activity of CYP3A enzymes in human liver, we studied the metabolism of CYP3A-specific substrates 7-benzyloxyquinoline (7-BQ) and ivermectin in 23 preparations of human liver microsomes (HLM) obtained from donors with documented alcohol exposure, from non-drinkers to heavy alcoholics. All HLM samples were characterized for the composition of the cytochrome P450 pool by global proteomics. Our studies revealed a significant increase in the activities of CYP3A enzymes by alcohol exposure. This effect is not associated with CYP3A enzyme levels, which do not correlate with alcohol exposure. Instead, the rates of 7-BQ and ivermectin metabolism correlate with the content of alcohol-inducible CYP2E1. However, this enzyme does not metabolize ivermectin, and its activity with 7-BQ is negligible. A significant increase in the rate of ivermectin demethylation was also observed in CYP3A4-containing Supersomes® and pooled HLM upon incorporation of purified CYP2E1 into their membrane. These results suggest that the reported acceleration of the elimination of drugs metabolized by CYP3A enzymes by alcohol exposure is due to functional effects of the interaction between CYP3A and CYP2E1. To elucidate the potential mechanism of this effect, we studied the formation of CYP2E1-CYP3A4 complexes in CYP3A4-containing Supersomes with co-incorporated CYP2E1 using tag-transfer chemical crosslinking mass spectrometry (CX-MS). These experiments confirmed physical interactions between the proteins and allowed the identification of CYP3A4 residues at the sites of contact. This information was used to build structural models of the CYP2E1-CYP3A4 complex and to propose possible mechanisms for the observed effects. - Source: PubMed
Publication date: 2026/08/03
Davydov Dmitri RPonraj KannapiranDavydova Nadezhda YYue GuihuaSingh Dilip KumarNeogi Arpita GuhaGaither Kari APrasad Bhagwat - In metabolic dysfunction-associated steatohepatitis (MASH), abnormalities in post-translational modification (PTM) are both a consequence of the pathological process and a driving force for disease progression. Therefore, this study intends to characterize the PTM features (acetylation, lactylation, and phosphorylation) of MASH, which will provide a crucial theoretical basis for the diagnosis and development of new targets for MASH. In this study, protein/modification profiles of clinical liver tissues from Normal and MASH were analyzed by LC-MS to identify differentially expressed proteins (DEPs) and differentially modified proteins (DMPs) with acetylation, lactylation, and phosphorylation. This study found that acetylation and lactylation occurred mainly in K, whose upstream and downstream amino acids consisted of A, G, K, R, and V. Phosphorylation occurred mainly in S and T, whose upstream and downstream ones consisted of D, E, P, R, and S. Proteomics with ordinary, acetylation, lactylation, and phosphorylation identified 468, 433, 434, and 1,471 DEPs/DMPs, respectively, which mainly regulate cytoskeleton, immunity, proliferation, oxidative stress, inflammatory cascades, various metabolisms (sugars, amino acids, lipids, and carbon). CMKLR1, CYP2E1, GLRX, and XRCC1 were identified as key regulators in the shared DEPs of ordinary proteomics and modification proteomics. Notably, the differences in expression of the four proteins in clinical liver tissues from Normal and MASH were consistent with the proteomics results. In conclusion, this study systematically reveals the global dysregulation of PTM, emphasizing CMKLR1, CYP2E1, GLRX, and XRCC1 as the key proteins/modification sites, and provides new perspectives for targeted intervention in MASH. - Source: PubMed
Publication date: 2026/07/31
Li KuanLi YundongZhang YuqingSong ShuxianPa ChengzhouDu ChenYang LianjunXue GuoyouGao Hongqiang