| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MTL |
| Uniprot No | Q9Y4I5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-508aa |
| 氨基酸序列 | EEGPLPGGLPSPEDAMVTELLSPEGPFASENIGLKAPVKYEEDEFHVFKEAYLGPADPKEPVLHAFNPALGADCKGQVKAKLAGGDSDGGELLGEYPGIPELSALEDVALLQAPQPPACNVHFLSSLLPAHRSPAVLPLGAWVLEGASHPGVRMIPVEIKEAGGTTTSNNPEEATLQNLLAQESCCKFPSSQELEDASCCSLKKDSNPMVICQLKGGTQMLCIDNSRTRELKALHLVPQYQDQNNYLQSDVPKPMTALVGRFLPASTKLNLITQQLEGALPSVVNGSAFPSGSTLPGPPKITLAGYCDCFASGDFCNNCNCNNCCNNLHHDIERFKAIKACLGRNPEAFQPKIGKGQLGNVKPQHNKGCNCRRSGCLKNYCECYEAQIMCSSICKCIGCKNYEESPERKTLMSMPNYMQTGGLEGSHYLPPTKFSGLPRFSHDRRPSSCISWEVVEATCACLLAQGEEAEKEHCSKCLAEQMILEEFGRCLSQILHTEFKSKGLKME |
| 预测分子量 | 55 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MTL(假设为金属硫蛋白样蛋白)重组蛋白研究的模拟参考文献示例，供参考：
1. **文献名称**：*Expression and Purification of Recombinant MTL Protein in E. coli for Heavy Metal Binding Studies*
**作者**：Zhang Y., et al.
**摘要**：本研究成功在大肠杆菌中表达了重组MTL蛋白，并通过亲和层析技术实现高效纯化。实验表明，纯化的MTL蛋白对镉(Cd²⁺)和锌(Zn²⁺)具有高亲和力，为重金属污染修复提供了潜在工具。
2. **文献名称**：*Structural Characterization of MTL Recombinant Protein by X-ray Crystallography*
**作者**：Smith J.R., et al.
**摘要**：通过X射线晶体学解析了重组MTL蛋白的三维结构，揭示了其独特的金属结合结构域。研究阐明了MTL与多种二价金属离子的结合模式，为设计新型金属螯合剂奠定基础。
3. **文献名称**：*Functional Analysis of MTL in Oxidative Stress Resistance Using Transgenic Arabidopsis*
**作者**：Lee H., et al.
**摘要**：将重组MTL基因导入拟南芥中，发现转基因植株对铜诱导的氧化胁迫耐受性显著增强。结果表明MTL通过调节活性氧(ROS)代谢发挥保护作用。
4. **文献名称**：*Development of an MTL-based Biosensor for Real-time Detection of Environmental Heavy Metals*
**作者**：Patel S., et al.
**摘要**：利用重组MTL蛋白构建了荧光生物传感器，可特异性检测水体中痕量铅(Pb²⁺)和汞(Hg²⁺)。该传感器灵敏度达nM级，具有快速、环保的应用潜力。
**注**：以上文献为示例性内容，实际研究中请通过PubMed、Web of Science等平台检索真实文献，并核实作者及摘要信息。
**Background of MTL Recombinant Proteins**
Recombinant protein technology, developed in the 1970s, revolutionized biotechnology by enabling the production of proteins through genetic engineering. MTL (Modified Thermostable Lysozyme) recombinant proteins represent a specialized class of engineered proteins derived from this technology. These proteins are designed by modifying the native lysozyme structure—a naturally occurring enzyme with antimicrobial properties—to enhance thermal stability, catalytic efficiency, or substrate specificity.
The production of MTL recombinant proteins typically involves cloning the modified lysozyme gene into expression vectors, followed by transfection into host systems like *E. coli*, yeast, or mammalian cells. Advanced techniques, such as site-directed mutagenesis or fusion tagging, are employed to introduce desired traits. For instance, thermostability is often achieved by stabilizing protein folds through amino acid substitutions.
MTL recombinant proteins hold significant promise in industrial and biomedical applications. Their enhanced stability allows them to function under harsh conditions, making them ideal for food preservation, biocatalysis, or antimicrobial treatments. In healthcare, they are explored as alternatives to traditional antibiotics, particularly against drug-resistant pathogens.
Challenges persist in optimizing expression yields, ensuring proper folding, and minimizing host-induced post-translational modifications. Innovations in synthetic biology, such as cell-free systems or AI-driven protein design, are addressing these hurdles. Additionally, regulatory frameworks and scalability for commercial production remain critical considerations.
Overall, MTL recombinant proteins exemplify the synergy between protein engineering and practical applications, underscoring their potential to address global challenges in healthcare, agriculture, and sustainable industry.
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