| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADH1B |
| Uniprot No | P00325 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-375aa |
| 氨基酸序列 | MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTD DHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGK CRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQY TVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFG LGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKP IQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQ NLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHV LPFEKINEGFDLLHSGKSIRTVLTF |
| 预测分子量 | 67 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ADH1B重组蛋白的参考文献及其摘要概括：
1. **文献名称**: "Expression and characterization of recombinant human ADH1B: Role in alcohol metabolism"
**作者**: Smith J, et al.
**摘要**: 该研究在大肠杆菌中成功表达并纯化了带有His标签的人源ADH1B重组蛋白。通过酶动力学分析，发现该蛋白对乙醇的催化效率(Km和Vmax)显著高于其他ADH亚型，揭示了其在酒精代谢中的关键作用。
2. **文献名称**: "Structural insights into ADH1B polymorphism via recombinant protein crystallography"
**作者**: Chen L, et al.
**摘要**: 利用X射线晶体学解析了ADH1B*2(Arg47His突变体)重组蛋白的三维结构，发现该突变导致活性中心构象变化，解释了其增强的乙醇脱氢酶活性，为人群酒精代谢差异提供分子机制依据。
3. **文献名称**: "Functional analysis of ADH1B recombinant protein in aldehyde detoxification"
**作者**: Tanaka K, et al.
**摘要**: 研究比较了ADH1B与其他亚型对乙醛的催化能力，发现重组ADH1B在低浓度底物下表现出更高的亲和力，提示其在解毒过程中可能具有独特生理意义，并验证了其在体外模型中的保护作用。
注：以上文献信息为示例性概括，实际文献需通过学术数据库检索获取。
**Background of ADH1B Recombinant Protein**
ADH1B (Alcohol Dehydrogenase 1B), a member of the alcohol dehydrogenase (ADH) enzyme family, plays a critical role in ethanol metabolism by catalyzing the oxidation of ethanol to acetaldehyde. This enzyme is encoded by the *ADH1B* gene, located on chromosome 4 in humans. ADH1B is particularly notable for its genetic polymorphisms, such as the His47Arg variant (rs1229984), which significantly enhances enzymatic activity and influences ethanol metabolism rates. Populations with this variant exhibit reduced risks of alcohol dependence, making *ADH1B* a key gene in studies of alcoholism and related disorders.
Recombinant ADH1B protein is produced using biotechnological methods, often through expression in bacterial (e.g., *E. coli*) or mammalian cell systems. This allows large-scale production of the purified enzyme for functional and structural studies. Recombinant ADH1B retains the catalytic properties of the native enzyme, enabling researchers to investigate its kinetic parameters, substrate specificity, and interactions with inhibitors or cofactors like NAD⁺.
Studies leveraging recombinant ADH1B have advanced our understanding of its role in alcohol-related diseases, pharmacogenetics, and metabolic disorders. For instance, its hyperactivity in certain variants correlates with faster acetaldehyde accumulation, causing adverse reactions (e.g., facial flushing) that deter excessive alcohol consumption. Beyond ethanol metabolism, ADH1B is implicated in metabolizing other substrates, including retinol and lipid peroxidation products, suggesting broader physiological roles in cellular detoxification and oxidative stress regulation.
The enzyme’s structure, resolved via X-ray crystallography using recombinant protein, reveals insights into active-site architecture and mechanisms underlying genetic variants. Additionally, recombinant ADH1B serves as a tool for drug screening, toxicology assessments, and enzyme replacement strategies. Its study remains vital for developing targeted therapies for alcohol use disorder, cancer (linked to acetaldehyde toxicity), and metabolic syndromes. Overall, ADH1B recombinant protein bridges genetic insights with biochemical applications, highlighting its importance in biomedical research.
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