| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADH1C |
| Uniprot No | P00326 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-375aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSTAGK VIKCKAAVLW ELKKPFSIEE VEVAPPKAHE VRIKMVAAGI CRSDEHVVSG NLVTPLPVIL GHEAAGIVES VGEGVTTVKP GDKVIPLFTP QCGKCRICKN PESNYCLKND LGNPRGTLQD GTRRFTCSGK PIHHFVGVST FSQYTVVDEN AVAKIDAASP LEKVCLIGCG FSTGYGSAVK VAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIAVDIN KDKFAKAKEL GATECINPQD YKKPIQEVLK EMTDGGVDFS FEVIGRLDTM MASLLCCHEA CGTSVIVGVP PDSQNLSINP MLLLTGRTWK GAIFGGFKSK ESVPKLVADF MAKKFSLDAL ITNILPFEKI NEGFDLLRSG KSIRTVLTF |
| 预测分子量 | 42 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3篇关于ADH1C重组蛋白的参考文献信息(基于虚拟示例，建议通过学术数据库核实具体文献)：
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1. **文献名称**: "Expression and Characterization of Recombinant Human ADH1C in *Escherichia coli*"
**作者**: Smith J. et al.
**摘要**: 本研究成功构建了人源ADH1C基因的原核表达系统，利用大肠杆菌表达并纯化重组蛋白。酶动力学实验表明，重组ADH1C对乙醇和视黄醇的催化效率存在组织特异性差异，为研究其代谢功能提供实验基础。
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2. **文献名称**: "Structural Insights into ADH1C Polymorphism: Role of Arg272Gln Mutation"
**作者**: Lee H. et al.
**摘要**: 通过X射线晶体学解析ADH1C Arg272Gln突变体重组蛋白的三维结构，发现该突变导致底物结合口袋构象变化，影响酶对长链醇类的催化活性，解释了人群酒精代谢差异的分子机制。
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3. **文献名称**: "Functional Analysis of ADH1C in Retinoic Acid Biosynthesis"
**作者**: Garcia-Ruiz C. et al.
**摘要**: 利用昆虫细胞表达系统制备高纯度ADH1C重组蛋白，证实其参与视黄酸合成的双功能催化特性，并发现其表达水平与肝癌细胞分化相关，提示潜在病理生理学作用。
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**注意**：以上为模拟示例，实际文献需通过PubMed、Web of Science等平台检索关键词(如“ADH1C recombinant protein”或“ADH1C expression”)获取。如需具体文章，可提供更多研究背景以便精准推荐。
**Background of ADH1C Recombinant Protein**
Alcohol dehydrogenase 1C (ADH1C), a member of the alcohol dehydrogenase (ADH) family, is a critical enzyme involved in the metabolism of ethanol and other alcohols. It catalyzes the oxidation of ethanol to acetaldehyde, a key step in alcohol detoxification. ADH1C is primarily expressed in the liver and gastrointestinal tract, where it contributes to first-pass metabolism of ingested alcohols. The enzyme also plays roles in retinol metabolism and steroidogenesis, linking it to broader physiological processes.
Genetic polymorphisms in the *ADH1C* gene influence enzyme activity, with specific variants (e.g., ADH1C*1 and ADH1C*2) associated with varying catalytic efficiencies. These polymorphisms have been studied in the context of alcohol-related diseases, cancer susceptibility, and population genetics. For instance, certain alleles correlate with altered risks for alcoholism, liver cirrhosis, or oral cancers, highlighting its clinical relevance.
Recombinant ADH1C protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional and structural studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, inhibition kinetics, and interactions with cofactors like NAD⁺. Structural analyses using recombinant ADH1C have elucidated its zinc-dependent catalytic mechanism and dimeric quaternary architecture, providing insights into substrate binding and enzyme regulation.
Beyond basic research, ADH1C recombinant protein is utilized in drug discovery, toxicology screens, and diagnostic assays. It serves as a tool to study metabolic pathways, evaluate ethanol-drug interactions, or develop inhibitors targeting alcohol metabolism. Additionally, its role in metabolizing xenobiotics and endogenous compounds underscores its importance in pharmacogenomics and personalized medicine.
In summary, ADH1C recombinant protein bridges molecular biology, clinical research, and biotechnological applications, offering a versatile platform to explore alcohol metabolism, disease mechanisms, and therapeutic strategies.
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