CYP2E1 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- CYP2E1 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100476
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- CYP2E1 antibody Polyclonal Antibodies Primary antibodies
Related genes to: CYP2E1 antibody Polyclonal Antibodies Primary antibodies
- 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 Polyclonal Antibodies Primary antibodies
Related articles to: CYP2E1 antibody Polyclonal Antibodies Primary antibodies
- There are currently no FDA-approved drugs for the treatment of alcohol-related liver diseases (ALD) due to their lack of effectiveness. Selenium-modified Lycium barbarum polysaccharides (SeLBP), as a promising agent for ALD, has not been studied before. In this study, with LBP and sodium selenite (NaSeO) as controls, and silymarin capsules, a clinical therapeutic agent, as a positive control, the therapeutic effects and mechanisms of SeLBP on ALD were systematically evaluated in an acute ALD mouse model. The results demonstrated that SeLBP, at the same dose, showed superior therapeutic effects on ALD compared to the use of LBP or NaSeO alone, exhibiting a significant dose-response effect and significantly reversing alcohol-induced liver cell damage and inflammation (p < 0.05). Furthermore, 5.7 mg/kg BW of SeLBP demonstrated comparable efficacy to 50 mg/kg BW of silymarin (p > 0.05), highlighting a low-dose advantage. Mechanistic studies revealed that SeLBP significantly enhanced the activities of ADH and ALDH (p < 0.05) and significantly inhibited the activity and expression levels of cytochrome P450 2E1 (CYP2E1) and NADPH oxidase (NOX) that produce reactive oxygen species (ROS) (p < 0.05), thereby reducing ROS generation and restoring redox homeostasis (p < 0.05). Additionally, SeLBP significantly decreased the elevated levels of TG, TC, MDA, AST, and ALT caused by alcohol, while enhancing the activities of GSH-Px and SOD (p < 0.05), highlighting SeLBP's significant functions in promoting the normal metabolism of ethanol and preventing lipid peroxidation and oxidative damage. This study provides new insights and evidence for the potential use of SeLBP in ALD treatment. - Source: PubMed
Publication date: 2026/06/04
Mao ShuangzheZhang XinWei LuluZhang HanLi AboSun MengmengFeng JiaoRen TingHuang YitingLiu XiaoyingZhang ZhifengZhao ZhihuiDong JianfangWu KangningMa YouliMi HongbinHu Zhongqiu - Maternal per- and polyfluoroalkyl substances (PFAS) exposure has been linked to adverse health effects on offspring, but the mechanisms remain unclear. The present study investigates the relationship between maternal PFAS exposure and the expression of placental cytochrome P450 enzymes (CYP19A1, CYP2J2, and CYP2E1), and explores the potential role of these enzymes in linking maternal PFAS exposure to offspring development. - Source: PubMed
Publication date: 2026/06/02
Song XiuxiaZhang ZhaofengZhou XiaoyuLiang HongChen YaoZhu WeiqiangYuan WeiDu JingWang ZiliangMiao Maohua - Bicyclo[1.1.1]pentane (BCP) is widely used as a bioisostere of 1,4-disubstituted benzene to prevent oxidative metabolism of the benzene ring by cytochrome P450s (P450s). In this study, we investigated its effectiveness in reducing metabolism-dependent toxicity using acetaminophen (APAP) as a model compound, which causes hepatotoxicity by forming the reactive metabolite N-acetyl-p-benzoquinone imine (NAPQI). In cultured rat hepatocytes, APAP markedly reduced intracellular glutathione levels, whereas N-{3-hydroxybicyclo[1.1.1]pentan-1-yl}acetamide (BCP-APAP), in which the benzene ring of APAP is replaced with BCP, had only a minor effect, suggesting that BCP-APAP does not form NAPQI-like reactive metabolites. We then investigated the interactions of these compounds with human CYP1A2, CYP2E1, and CYP3A4, the major P450s involved in NAPQI formation, using inhibition assays. While both compounds similarly inhibited CYP1A2 and CYP3A4, only APAP inhibited CYP2E1, suggesting that BCP-APAP does not bind to CYP2E1. Docking simulations with 3D crystal structures of these P450s revealed that both compounds can bind to CYP1A2 and CYP3A4 in a similar orientation for heme-mediated metabolism, whereas BCP-APAP did not adopt an APAP-like docking pose in CYP2E1. These findings indicate that replacing the benzene ring in APAP with BCP prevents the formation of reactive metabolites and may subtly alter P450 binding properties in an isoform-dependent manner. - Source: PubMed
Publication date: 2026/04/15
Shibata MinamiMizuno AyatoNakayoshi TomokiOda AkifumiNakajima MasayaUchiyama MasanobuHiratsuka MasahiroYamanishi YoshihiroYoshinari Kouichi - Muttony flavor is a species-specific characteristic of ovine meat and a critical determinant of consumer acceptance and market demand worldwide. The characteristic flavor primarily originates from two key classes of compounds: Branched-chain fatty acids (BCFAs), particularly 4-methyloctanoic acid (4-MOA), 4-ethyloctanoic acid (4-EOA), and 4-methylnonanoic acid (4-MNA); and skatole (3-methylindole), a ruminal microbial metabolite of tryptophan. Genetic analysis based on candidate genes is considered an effective approach to elucidate the physiological mechanisms regulating the expression of complex traits. This review systematically examines the biosynthetic pathways of these compounds, clarifying the roles of ruminal microorganisms, host genetic factors, and key regulatory genes including FASN, CYP2E1, CYP2A6, and MMUT, thereby providing genetic strategies and methods for the regulation of muttony flavor, while also supplementing nongenetic approaches for flavor control. The integration of these strategies indicates that the identification of candidate genes and the elucidation of their expression regulatory networks provide a theoretical basis for future marker-assisted selection programs, thereby potentially enhancing the precision and sustainability of ovine industry breeding strategies, while nongenetic regulation can further assist in fine-tuning flavor control. As a validation, this review also provides a systematic overview of analytical methods for muttony flavor evaluation, tracing the evolutionary trajectory from traditional sensory evaluation through instrumental analysis to intelligent sensory technologies, and clarifying the applicable scenarios and complementary relationships among various techniques. By integrating the current understanding of formation mechanisms, regulatory networks, and evaluation technologies, this review establishes a theoretical framework for developing market-oriented flavor control strategies. - Source: PubMed
Wang YushuanLiu Wangjing - CYP2E1 expression is often negatively correlated with hepatocellular carcinoma (HCC) progression, and its overexpression induces apoptosis in HCC cells. However, the underlying mechanism of CYP2E1 in apoptosis induction remains unclear. Given the crucial role of lysosomal dysfunction through lysosomal membrane permeabilization (LMP) in promoting apoptosis, this study aimed to investigate whether and how lysosomal dysfunction and LMP contribute to CYP2E1-induced apoptosis in HCC. Here, we demonstrated that CYP2E1 overexpression induced LMP, leading to the translocation of cathepsin D and subsequent apoptosis in HCC cells. Notably, cathepsin D inhibitor attenuated CYP2E1 overexpression-induced LMP and apoptosis. In addition, through sialidase Neuraminidase 4 (NEU4), CYP2E1 overexpression resulted in the deglycosylation and degradation of lysosome-associated membrane protein 1 and 2 (LAMP1/2), contributing to LMP and apoptosis both and . Clinically, decreased CYP2E1 expression in the tumor tissues of HCC patients is strongly associated with upregulated LAMP1/2 expression and glycosylation. Collectively, our findings elucidate the role of LMP in CYP2E1-induced cell apoptosis with the involvement of NEU4, providing novel insight for CYP2E1 function in apoptosis. - Source: PubMed
Publication date: 2026/05/16
Wang XuanWang AnHe HuanhuanQiao JiaqiWang ChengyiDu HaiyuanShu XijiSun BinlianChen XiaoqingChen QiongxiaHuang XuanHu ShaoboLiu YuchenFu Zhengqi