| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Phe |
| Uniprot No | P00439 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-452aa |
| 氨基酸序列 | MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK |
| 预测分子量 | 51,8 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3-4条关于Phe重组蛋白的参考文献示例(注：内容为模拟生成，非真实文献)：
1. **文献名称**：**《重组苯丙氨酸解氨酶的高效表达及其在苯丙酮尿症治疗中的应用》**
**作者**：Zhang et al. (2018)
**摘要**：研究通过大肠杆菌表达系统高效生产重组苯丙氨酸解氨酶(PAL)，优化酶活性和热稳定性，验证其在体外降解苯丙氨酸的效果，为苯丙酮尿症(PKU)的酶替代疗法提供新策略。
2. **文献名称**：**《基于重组Phe降解酶的食品工程应用研究》**
**作者**：Li et al. (2020)
**摘要**：开发了一种重组Phe降解酶，通过基因编辑技术提高酶对苯丙氨酸的特异性催化效率，应用于低苯丙氨酸食品生产，为苯丙酮尿症患者提供安全的膳食解决方案。
3. **文献名称**：**《代谢工程改造酵母合成苯丙氨酸衍生物的重组蛋白技术》**
**作者**：Wang et al. (2017)
**摘要**：利用重组蛋白技术改造酵母代谢途径，高效合成苯丙氨酸衍生化合物(如植物多酚)，研究聚焦于关键酶的表达优化和产物纯化工艺。
4. **文献名称**：**《固定化重组Phe裂解酶在工业生物催化中的应用》**
**作者**：Chen et al. (2019)
**摘要**：将重组苯丙氨酸裂解酶固定在纳米载体上，显著提高酶的重复利用率和酸碱耐受性，应用于工业级L-苯丙氨酸的规模化生产。
(注：以上文献为示例，实际研究中需根据具体主题检索真实数据库如PubMed、ScienceDirect等。)
**Background of Recombinant Proteins**
Recombinant proteins are artificially engineered proteins produced through genetic modification, enabling the expression of specific genes in host organisms such as bacteria, yeast, or mammalian cells. This technology emerged in the 1970s with advancements in molecular cloning and DNA manipulation, revolutionizing biomedical research, therapeutics, and industrial applications.
The production process involves inserting a target gene into a plasmid vector, which is then introduced into a host cell. The host’s machinery translates the gene into the desired protein, which is subsequently purified. Common hosts include *E. coli* for simplicity and cost-effectiveness, yeast for eukaryotic post-translational modifications, and mammalian cells (e.g., CHO cells) for complex human proteins requiring precise folding or glycosylation.
Recombinant proteins have transformed medicine, enabling therapies like insulin for diabetes, monoclonal antibodies for cancer, and vaccines (e.g., hepatitis B). They also serve as critical tools in research, such as enzymes (e.g., Taq polymerase) and diagnostic reagents. In industry, they are used in biocatalysis, biofuels, and food processing.
Challenges include optimizing expression yields, ensuring proper protein folding, and minimizing host-related contaminants. Advances in synthetic biology, CRISPR, and AI-driven protein design continue to enhance production efficiency and expand applications.
Overall, recombinant protein technology bridges genetic information and functional biomolecules, driving innovation across healthcare, biotechnology, and beyond. Its evolution remains central to addressing global health challenges and sustainable industrial solutions.
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