| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADH |
| Uniprot No | P41181 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-271aa |
| 氨基酸序列 | MWELRSIAFSRAVFAEFLATLLFVFFGLGSALNWPQALPSVLQIAMAFGLGIGTLVQALGHISGAHINPAVTVACLVGCHVSVLRAAFYVAAQLLGAVAGAALLHEITPADIRGDLAVNALSNSTTAGQAVTVELFLTLQLVLCIFASTDERRGENPGTPALSIGFSVALGHLLGIHYTGCSMNPARSLAPAVVTGKFDDHWVFWIGPLVGAILGSLLYNYVLFPPAKSLSERLAVLKGLEPDTDWEEREVRRRQSVELHSPQSLPRGTKA |
| 预测分子量 | 30.3 kDa |
| 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ADH(酒精脱氢酶)重组蛋白的3篇代表性文献概览(注：文献信息为模拟示例，仅供参考)：
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1. **文献名称**：*Heterologous Expression and Characterization of Recombinant Alcohol Dehydrogenase from Saccharomyces cerevisiae in E. coli*
**作者**：Zhang, L., et al.
**摘要**：研究报道了将酿酒酵母ADH基因克隆至大肠杆菌表达系统，通过优化诱导条件(如IPTG浓度、温度)实现高效可溶性表达。纯化的重组ADH在体外表现出对乙醇和NAD+的高催化活性，为工业生物催化提供了候选酶。
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2. **文献名称**：*Immobilization of Recombinant ADH from Thermotoga maritima for Enhanced Stability in Organic Solvents*
**作者**：Müller, J., & Schmidt, H.
**摘要**：通过将嗜热菌来源的重组ADH固定化到磁性纳米颗粒上，显著提高了酶在高温和有机溶剂中的稳定性。固定化酶在连续批次反应中催化酮类还原，转化率保持在80%以上，展现了工业化生产的潜力。
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3. **文献名称**：*Functional Expression of Human ADH1B in Pichia pastoris: Role in Drug Metabolism Studies*
**作者**：Chen, Y., et al.
**摘要**：利用毕赤酵母系统表达人源ADH1B，通过糖基化修饰获得高活性酶。该重组蛋白在体外模型中成功模拟了肝脏药物代谢途径，为抗病毒药物(如齐多夫定)的代谢机制研究提供了工具。
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**提示**：实际研究中建议通过PubMed、Google Scholar等平台，以关键词“recombinant ADH expression”“alcohol dehydrogenase cloning”等检索最新文献，优先选择近五年内发表于*Protein Expression and Purification*、*Enzyme and Microbial Technology*等期刊的文章。
**Background of Recombinant ADH (Alcohol Dehydrogenase)**
Alcohol dehydrogenase (ADH) is a critical enzyme involved in the metabolism of ethanol and other alcohols, catalyzing the oxidation of alcohols to aldehydes or ketones while reducing nicotinamide adenine dinucleotide (NAD⁺) to NADH. Naturally found in organisms ranging from bacteria to humans, ADHs play essential roles in detoxification, energy production, and biosynthesis. However, extracting native ADHs from their original sources often faces challenges such as low yield, purity issues, and variability in enzymatic activity.
Recombinant ADH technology emerged to address these limitations. By cloning the ADH gene into heterologous expression systems (e.g., *E. coli*, yeast, or insect cells*), scientists can produce ADH proteins with high consistency, scalability, and tailored properties. Recombinant production allows for genetic modifications, such as introducing point mutations or fusion tags, to enhance enzyme stability, substrate specificity, or catalytic efficiency. For example, thermostable ADH variants derived from extremophiles have been engineered for industrial processes requiring high-temperature tolerance.
The applications of recombinant ADHs span multiple fields. In biotechnology, they serve as biocatalysts for synthesizing chiral alcohols, pharmaceuticals, and fine chemicals. In biofuel production, ADHs are utilized to convert renewable substrates into ethanol or butanol. Additionally, recombinant ADHs are valuable tools in diagnostic kits (e.g., alcohol detection) and academic research for studying enzyme mechanisms or metabolic pathways.
Advantages over native ADHs include cost-effectiveness, reduced batch-to-batch variability, and the ability to customize enzymes for specific industrial needs. As sustainable practices gain momentum, recombinant ADHs align with green chemistry principles by enabling efficient, eco-friendly manufacturing processes. Ongoing advancements in protein engineering and synthetic biology continue to expand their potential, positioning recombinant ADHs as versatile catalysts in both existing and emerging biotechnological applications.
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