| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ddl |
| Uniprot No | P63891 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-356aa |
| 氨基酸序列 | MTKENICIVFGGKSAEHEVSILTAQNVLNAIDKDKYHVDIIYITNDGDWRKQNNITAEIKSTDELHLENGEALEISQLLKESSSGQPYDAVFPLLHGPNGEDGTIQGLFEVLDVPYVGNGVLSAASSMDKLVMKQLFEHRGLPQLPYISFLRSEYEKYEHNILKLVNDKLNYPVFVKPANLGSSVGISKCNNEAELKEGIKEAFQFDRKLVIEQGVNAREIEVAVLGNDYPEATWPGEVVKDVAFYDYKSKYKDGKVQLQIPADLDEDVQLTLRNMALEAFKATDCSGLVRADFFVTEDNQIYINETNAMPGFTAFSMYPKLWENMGLSYPELITKLIELAKERHQDKQKNKYKID |
| 预测分子量 | 47.7 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. |
1. **《Heterologous Expression and Characterization of D-Alanine-D-Alanine Ligase from Mycobacterium tuberculosis》**
作者：Smith, J. et al.
摘要：研究利用大肠杆菌系统重组表达结核分枝杆菌Ddl酶，分析其酶活性和抗生素(如环丝氨酸)抑制机制，为抗结核药物开发提供依据。
2. **《Structural Insights into Ddl-Mediated Bacterial Cell Wall Biosynthesis》**
作者：Zhang, L. et al.
摘要：通过X射线晶体学解析革兰氏阳性菌Ddl的三维结构，揭示其底物结合域和催化机制，指导新型抗菌剂的合理化设计。
3. **《Engineering Thermostable D-Alanine-D-Alanine Ligase for Industrial Biocatalysis》**
作者：Wang, Y. et al.
摘要：采用定向进化技术改造Ddl酶的热稳定性，提升其在β-内酰胺类抗生素合成中的催化效率，推动绿色制药工艺发展。
4. **《Functional Analysis of Ddl Mutants in Vancomycin Resistance》**
作者：Kim, S. et al.
摘要：探究耐万古霉素肠球菌中Ddl基因突变对酶功能的影响，阐明耐药性产生的分子基础，为克服耐药性问题提供新思路。
(注：以上文献为虚拟示例，实际引用需根据具体研究检索PubMed、SciHub等数据库。)
**Background of Recombinant Proteins**
Recombinant proteins are genetically engineered molecules produced by inserting a target protein’s DNA sequence into a host organism, such as bacteria, yeast, or mammalian cells, enabling large-scale protein expression. This technology emerged in the 1970s with advancements in molecular cloning and gene editing, revolutionizing biomedical research and therapeutic development. Traditional protein extraction from natural sources faced limitations like low yield, contamination risks, and ethical concerns. Recombinant systems overcame these challenges, offering precise control over protein structure and function.
The process involves isolating the gene of interest, cloning it into an expression vector, and transferring it into a host for protein synthesis. Post-translational modifications in eukaryotic hosts (e.g., mammalian or insect cells) ensure proper folding and activity, critical for complex proteins like antibodies or hormones. Bacterial systems (e.g., *E. coli*) are preferred for simpler proteins due to cost-effectiveness and rapid production.
Recombinant proteins have transformed medicine, enabling therapies such as insulin for diabetes, monoclonal antibodies for cancer, and vaccines (e.g., hepatitis B). They also serve as research tools for studying protein interactions, signaling pathways, and drug discovery. Recent innovations, including cell-free systems and CRISPR-enhanced expression, further optimize yield and customization.
Despite successes, challenges remain, including achieving correct post-translational modifications in prokaryotic systems and scaling up production for high-demand applications. Ongoing research focuses on improving host systems, purification techniques, and computational design to expand therapeutic and industrial applications. Recombinant protein technology continues to bridge gaps between basic science and real-world solutions, underpinning modern biotechnology and personalized medicine.
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