| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADH1A |
| Uniprot No | P07327 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-375aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSTAGKVIKCKAAVLWELKKPFSIEEVEVA PPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEG VTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSR FTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKF AKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASL LCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVP KLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF |
| 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. |
以下是关于ADH1A重组蛋白的3篇文献概览(注：文献为示例性内容，实际引用需核实)：
1. **文献名称**：*Expression and characterization of recombinant human ADH1A in Escherichia coli*
**作者**：Smith J, et al.
**摘要**：研究通过大肠杆菌系统高效表达人源ADH1A重组蛋白，优化诱导条件后获得可溶性蛋白，经亲和层析纯化并验证其催化乙醇氧化活性，为酶动力学研究提供材料。
2. **文献名称**：*Crystal structure of ADH1A from Saccharomyces cerevisiae: Insights into substrate specificity*
**作者**：Lee H, et al.
**摘要**：首次解析酵母ADH1A重组蛋白的晶体结构，揭示其活性中心关键氨基酸残基与NAD+辅因子的结合模式，解释了其对短链醇类的底物选择性机制。
3. **文献名称**：*Functional analysis of ADH1A mutants in alcohol metabolism*
**作者**：Wang Y, et al.
**摘要**：通过定点突变技术构建ADH1A重组蛋白突变体，比较其与野生型的酶动力学参数(Km/Vmax)，发现第48位组氨酸突变显著降低催化效率，提示其在底物结合中的关键作用。
建议通过PubMed或Web of Science以“ADH1A recombinant protein expression”为关键词检索最新文献以获取具体研究数据。
**Background of ADH1A Recombinant Protein**
Alcohol dehydrogenase 1A (ADH1A), a member of the alcohol dehydrogenase (ADH) family, is an enzyme critical in the metabolism of alcohols, including ethanol. ADH1A is encoded by the *ADH1A* gene in humans and is primarily expressed in the liver, where it catalyzes the oxidation of ethanol to acetaldehyde using nicotinamide adenine dinucleotide (NAD+) as a cofactor. This reaction represents the first step in ethanol detoxification, linking ADH1A to alcohol metabolism and associated physiological or pathological processes, such as alcohol dependence and liver disease.
The ADH family comprises multiple isoforms (ADH1-7) with distinct tissue distributions and substrate specificities. ADH1A, along with ADH1B and ADH1C, forms the classical class I ADH subgroup, which exhibits high affinity for ethanol. However, ADH1A is less studied compared to ADH1B and ADH1C, partly due to its lower abundance in human tissues. Despite this, ADH1A’s role in metabolizing endogenous substrates (e.g., retinol) and xenobiotics highlights its broader biological significance beyond ethanol processing.
Recombinant ADH1A protein is produced via heterologous expression systems, such as *E. coli* or mammalian cell cultures, enabling large-scale purification for research and industrial applications. Its recombinant form retains enzymatic activity and structural stability, making it valuable for *in vitro* studies on enzyme kinetics, inhibitor screening, and structural biology. Additionally, ADH1A recombinant protein is utilized in biocatalysis for synthesizing chiral alcohols or pharmaceuticals, leveraging its substrate versatility.
Research on ADH1A also extends to understanding genetic polymorphisms and their implications in disease susceptibility or drug metabolism variability. As a tool in biomedical studies, recombinant ADH1A aids in elucidating alcohol-related pathologies and developing therapeutic strategies targeting metabolic pathways.
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