纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ADH1 |
Uniprot No | P07327 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-375aa |
氨基酸序列 | STAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMF |
预测分子量 | 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ADH1重组蛋白的参考文献示例(内容为模拟概括,非真实文献):
1. **文献名称**:*Cloning, Expression, and Characterization of Recombinant ADH1 from Saccharomyces cerevisiae in E. coli*
**作者**:Smith J, Brown KL
**摘要**:该研究报道了酿酒酵母ADH1基因在大肠杆菌中的重组表达与纯化,分析了重组蛋白的酶动力学参数(如Km和Vmax),并验证其在乙醇氧化反应中的催化活性。
2. **文献名称**:*High-Yield Production of ADH1 in Pichia pastoris for Industrial Biocatalysis*
**作者**:Zhang R, Wang Y, et al.
**摘要**:通过优化毕赤酵母表达系统,实现了ADH1重组蛋白的高效分泌表达,其产量较传统系统提升5倍,并成功应用于手性醇的不对称合成。
3. **文献名称**:*Crystal Structure Analysis of Recombinant Human ADH1: Insights into Substrate Specificity*
**作者**:Lee S, Johnson M
**摘要**:解析了人源ADH1重组蛋白的X射线晶体结构,揭示了其底物结合口袋的关键氨基酸残基,为设计定向突变体以拓展底物范围提供了结构基础。
4. **文献名称**:*Thermostability Engineering of ADH1 via Directed Evolution for Enhanced Industrial Performance*
**作者**:Chen X, Müller TE
**摘要**:采用定向进化技术改造ADH1重组蛋白,获得耐高温突变体(Tm提高12℃),显著提升了其在生物催化反应中的操作稳定性。
(注:以上文献为示例模板,实际引用需以真实出版物为准。)
**Background of ADH1 Recombinant Protein**
Alcohol dehydrogenase 1 (ADH1) is a member of the alcohol dehydrogenase enzyme family, which plays a central role in the metabolism of ethanol and other alcohols. These enzymes catalyze the oxidation of alcohols to aldehydes or ketones, coupled with the reduction of nicotinamide adenine dinucleotide (NAD⁺) to NADH. ADH1. specifically, is primarily expressed in the liver and gastrointestinal tract, where it contributes to the first-pass metabolism of ingested ethanol. Human ADH1 exists as multiple isoforms (e.g., ADH1A, ADH1B, ADH1C) encoded by distinct genes, exhibiting variations in substrate specificity and catalytic efficiency.
Recombinant ADH1 proteins are engineered through heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to enable large-scale production for research and industrial applications. These proteins retain the enzymatic activity of native ADH1 but are optimized for stability, solubility, and ease of purification via affinity tags (e.g., His-tag). Recombinant ADH1 is widely used in biochemical studies to investigate enzyme kinetics, substrate interactions, and structural properties via X-ray crystallography or cryo-EM.
In biotechnology, ADH1 recombinant proteins are employed in biofuel production (converting alcohols to aldehydes), pharmaceutical synthesis (chiral compound resolution), and biosensor development for ethanol detection. Additionally, they serve as tools in metabolic engineering to design pathways for chemical synthesis. Research on ADH1 variants also explores their roles in alcohol-related diseases, such as liver cirrhosis, and genetic polymorphisms affecting alcohol tolerance.
Overall, ADH1 recombinant proteins bridge fundamental enzymology with practical applications, underscoring their importance in both academic and industrial settings.
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