| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADH7 |
| Uniprot No | P40394 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-386aa |
| 氨基酸序列 | MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFELLNSGQSIRTVLTF |
| 预测分子量 | 43.5kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ADH7重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Expression, purification, and characterization of recombinant human alcohol dehydrogenase class VII (ADH7)"
**作者**: Parés X, et al.
**摘要**: 研究报道了人源ADH7在大肠杆菌中的重组表达与纯化，分析了其酶动力学特性，证明其对视黄醇和乙醇的催化活性，并探讨了其在视黄酸代谢中的作用。
2. **文献名称**: "Structural and functional insights into human alcohol dehydrogenase 7: Role in retinol metabolism and implications in cancer"
**作者**: Kedishvili NY, et al.
**摘要**: 通过晶体结构解析和功能实验，揭示了ADH7在视黄醇转化为视黄酸过程中的关键作用，并发现其重组蛋白在癌细胞中的异常表达可能与肿瘤发生相关。
3. **文献名称**: "Functional characterization of recombinant human ADH7: Substrate specificity and inhibition by flavonoids"
**作者**: Han CL, et al.
**摘要**: 研究利用重组ADH7蛋白系统评估了其对多种底物(如乙醇、视黄醇)的催化效率，并发现黄酮类化合物可显著抑制其活性，提示潜在药理调控机制。
(注：上述文献信息为示例，实际文献需通过PubMed或Web of Science等平台检索确认。)
ADH7 (Alcohol Dehydrogenase 7), also known as class IV alcohol dehydrogenase, is a member of the alcohol dehydrogenase enzyme family that plays a critical role in the metabolism of alcohols, retinoids, and other substrates. It is encoded by the ADH7 gene in humans and is primarily expressed in the gastrointestinal tract, including the stomach and esophagus, distinguishing it from other ADH isoforms that are predominantly liver-specific. ADH7 exhibits a unique substrate preference for medium- to long-chain alcohols and retinols, linking it to both ethanol detoxification and vitamin A metabolism. Its activity contributes to the oxidation of retinol to retinoic acid, a process essential for cellular differentiation and development.
Recombinant ADH7 protein is produced through genetic engineering techniques, often using expression systems like *E. coli* or yeast, to enable large-scale purification and functional studies. This engineered protein retains the catalytic properties of native ADH7. including NAD(H)-dependent redox reactions. Research on recombinant ADH7 has advanced understanding of its structural features, such as its zinc-binding catalytic domain and substrate-binding pocket, which influence enzyme kinetics and inhibitor interactions.
Biotechnologically, recombinant ADH7 is explored for applications in biocatalysis, particularly in synthesizing chiral alcohols for pharmaceuticals, and in metabolic engineering for biofuel production. Its thermostability and broad substrate tolerance make it attractive for industrial processes. Additionally, ADH7’s role in retinoic acid synthesis has implications for cancer research, as dysregulation of retinoid signaling is associated with tumorigenesis. Studies also investigate its potential involvement in alcohol-related pathologies, such as esophageal cancer, due to tissue-specific expression in alcohol-exposed mucosal tissues. Overall, recombinant ADH7 serves as a valuable tool for both basic research and applied biotechnology.
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