| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADH2 |
| Uniprot No | P08319 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-380aa |
| 氨基酸序列 | MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTD ATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCR KCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTS TFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGST CAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPR DLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV AAGSKGLTVFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDA LVTHTLPFDKISEAFDLMNQGKSIRTILIF |
| 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. |
以下是关于ADH2重组蛋白的示例参考文献(内容为模拟虚构，仅供参考)：
1. **《Expression and characterization of recombinant ADH2 from Saccharomyces cerevisiae in E. coli》**
- 作者：Zhang, L. et al.
- 摘要：研究通过大肠杆菌表达系统成功克隆并表达了酿酒酵母ADH2基因，纯化后测定其酶动力学参数，证明重组蛋白具有高效的乙醇脱氢酶活性，适用于生物催化反应。
2. **《Enhancing thermostability of ADH2 through directed evolution for industrial applications》**
- 作者：Wang, Y. et al.
- 摘要：通过定向进化技术改造ADH2重组蛋白，提高了其热稳定性，在60℃下仍保留80%活性，为高温环境中的生物乙醇生产提供了潜在工具。
3. **《Immobilization of recombinant ADH2 on magnetic nanoparticles for efficient biocatalysis》**
- 作者：Kim, S. et al.
- 摘要：将重组ADH2固定在磁性纳米颗粒上，优化固定化条件后，酶重复使用5次仍保持90%活性，显著降低了生物催化过程的成本。
4. **《Functional analysis of ADH2 in ethanol tolerance of engineered yeast strains》**
- 作者：Garcia-Ramos, C. et al.
- 摘要：通过过表达重组ADH2提高工程酵母的乙醇耐受性，发现其代谢通量变化与细胞内NAD+/NADH平衡相关，为生物燃料生产提供新策略。
注：以上文献为示例，实际研究需通过PubMed、Web of Science或Google Scholar等平台检索关键词“recombinant ADH2”、“alcohol dehydrogenase expression”等获取。
**Background of ADH2 Recombinant Protein**
Alcohol dehydrogenase 2 (ADH2), a member of the alcohol dehydrogenase (ADH) enzyme family, plays a critical role in the oxidation of alcohols to aldehydes or ketones, utilizing NAD⁺ or NADP⁺ as cofactors. This enzyme is particularly notable for its involvement in ethanol metabolism, where it catalyzes the conversion of ethanol to acetaldehyde. ADH2 is found across various organisms, including yeast, plants, and mammals, with functional and structural variations reflecting species-specific adaptations. In humans, ADH2 exists as multiple isoforms, with polymorphisms influencing enzymatic activity and individual susceptibility to alcohol-related conditions.
The recombinant form of ADH2 is engineered through heterologous expression systems, such as *E. coli* or yeast, to enable large-scale production for research and industrial applications. Cloning the *ADH2* gene into expression vectors allows precise control over protein yield and purity, bypassing challenges associated with native protein extraction. Recombinant ADH2 retains the catalytic properties of its native counterpart, making it invaluable for studies on enzyme kinetics, substrate specificity, and inhibitor screening.
In biotechnology, ADH2 recombinant protein is leveraged for biofuel production, where it facilitates the conversion of renewable substrates into alcohols or other value-added chemicals. It also serves as a model enzyme for metabolic engineering and synthetic biology projects aimed at optimizing alcohol metabolism pathways. Additionally, its role in detoxification pathways has sparked interest in pharmaceutical research, particularly in developing therapies for alcohol metabolism disorders or alcohol dependence.
Overall, ADH2 recombinant protein bridges fundamental biochemistry with practical applications, offering insights into enzyme mechanisms while supporting advancements in industrial and medical fields.
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