ADH1B siRNA_Lentivectors
- Known as:
- ADH1B siRNA_Lentivectors
- Catalog number:
- i000603c
- Product Quantity:
- 500ng
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ADH1B siRNA_Lentivectors
Related genes to: ADH1B siRNA_Lentivectors
- Gene:
- ADH1B NIH gene
- Name:
- alcohol dehydrogenase 1B (class I), beta polypeptide
- Previous symbol:
- ADH2
- Synonyms:
- -
- Chromosome:
- 4q23
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-01-18
Related products to: ADH1B siRNA_Lentivectors
Related articles to: ADH1B siRNA_Lentivectors
- The degrees of subjective intoxication (SI) and vigilance impairment following alcohol consumption vary among individuals. This variability may reflect both metabolic enzyme genotypes and drinking behavior. The purpose of this study was to examine the integrated associations among alcohol-metabolizing enzyme genotypes, drinking tendency, and acute alcohol-induced changes in breath alcohol concentration (BrAC), SI, and vigilance performance. - Source: PubMed
Publication date: 2026/06/10
Motoi MidoriShin NakyeongHama MomoYasuda YukitaroNishimura TakayukiNishimura EigoToyoshima HideoAraki YuikoKatsumura TakafumiXia YaliOhashi TomoakiKuriyama NariakiMiyauchi YunaMotomura YukiHiguchi Shigekazu - Ochratoxin A (OTA), a common foodborne mycotoxin, is classified as a potential human carcinogen. However, the specific molecular mechanisms linking OTA exposure to colorectal cancer (CRC) pathogenesis remain poorly understood. - Source: PubMed
Publication date: 2026/06/09
Qiu TianqiZhuo JunyiWu HuaLin MinZhang KaishengTang Yu - Genetic predisposition is one of the many factors contributing to the multifactorial etiology of head and neck cancers (HNCs), a varied group of tumors. This study examined the relationship between the risk of HNC in the population of Southern Punjab, Pakistan, and two single-nucleotide polymorphisms: rs1229984 and rs4767364. - Source: PubMed
Publication date: 2026/04/27
Sadeeq SaniaSultana MehwishShahzadi WaniaFarwa Umm-E-Kashif MairaMuhammad Syed AunPandeya Ajay - Esophageal squamous cell carcinoma (ESCC) in East Asia is markedly male predominant, strongly associated with genetic susceptibility and modifiable lifestyle exposures. We developed and validated a risk appraisal model for ESCC by integrating genetic polymorphisms of two key alcohol-metabolizing enzymes-ADH1B and ALDH2-with major carcinogenic exposures from alcohol, tobacco, and betel quid among men. Genetic and lifestyle data were collected from independent cohorts including only male population across five tertiary centers in Taiwan. The training cohort included 396 ESCC patients and 647 controls, and the validation cohort comprised 256 ESCC patients and 260 controls. Six significant predictors were incorporated into a composite risk score derived from log odds ratios. Using a cutoff value of 5, the model achieved an AUC of 0.91, with 80.30% sensitivity and 87.33% specificity in the training cohort. In the validation cohort, the AUC was 0.96 with sensitivity and specificity of 86.33% and 94.23%, respectively. The positive and negative predictive values were 93.64% and 87.50%, respectively. This integrated model reliably identifies male individuals at high risk of ESCC and may serve as a precision screening tool in high-incidence regions. - Source: PubMed
Publication date: 2026/06/05
Chung Chen-ShuanChen Yi-HsunHsu Ming-HungYu Chen-HuanWang Wen-LunWang Hsiu-PoWu Ming-ShiangLee Chien-HungChen Che-HongWu I-Chen - Hydroxyzine, an aliphatic alcohol, is metabolized to the carboxylic acid cetirizine via 2 sequential oxidation steps involving the formation of an aldehyde intermediate. The initial aldehyde formation is considered the rate-limiting step in cetirizine production and is suggested to be catalyzed by NAD-dependent alcohol dehydrogenase (ADH), which oxidizes aliphatic alcohols. However, the specific ADH isoform(s) involved remain unidentified. Identifying these enzyme(s) is essential for understanding interindividual variability in drug pharmacokinetics, efficacy, and toxicity. The aim of this study was to identify the ADH isoforms responsible for catalyzing hydroxyzine aldehyde formation using recombinant human ADHs. Hydroxyzine aldehyde formation in the human liver S9 fraction was significantly higher when NAD was used as a cofactor than with NADP or NADPH, supporting the involvement of ADH. Among the recombinant hepatic human ADH isoforms (ADH1A, ADH1B, ADH1C, ADH4, and ADH5), all except ADH1A catalyzed hydroxyzine aldehyde formation. Furthermore, hydroxyzine aldehyde formation in human liver cytosol was significantly inhibited by 4-methylpyrazole, a specific inhibitor of ADH1, consistent with a predominant role for ADH1B and ADH1C. DMSO, used as the solvent for 4-methylpyrazole, strongly inhibited the hydroxyzine aldehyde formation, with IC values of 0.29% ± 0.056% for ADH1B and 0.06% ± 0.004% for ADH1C. Additional solvent screening revealed that even at a concentration of 0.5%, methanol and isopropanol also strongly inhibited ADH isoforms-excluding ADH5-when hydroxyzine or abacavir was used as the substrate. These findings highlight the potent inhibitory effects of DMSO and several other organic solvents on ADH activity. SIGNIFICANCE STATEMENT: Through the identification of alcohol dehydrogenase (ADH) isoforms catalyzing hydroxyzine aldehyde formation by recombinant human ADH, the study revealed that several common organic solvents strongly inhibit ADH1. This highlights the need to consider the unintended inhibitory effects of such solvents on ADH activity when solubilizing lipophilic compounds. - Source: PubMed
Publication date: 2026/05/05
Tonami TakuyaSato ReiNakano MasatakaNakajima MikiFukami Tatsuki