| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | QT |
| Uniprot No | Q9BXJ1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-281aa |
| 氨基酸序列 | RVPHVQGEQQEWEGTEELPSPPDHAERAEEQHEKYRPSQDQGLPASRCLRCCDPGTSMYPATAVPQINITILKGEKGDRGDRGLQGKYGKTGSAGARGHTGPKGQKGSMGAPGERCKSHYAAFSVGRKKPMHSNHYYQTVIFDTEFVNLYDHFNMFTGKFYCYVPGLYFFSLNVHTWNQKETYLHIMKNEEEVVILFAQVGDRSIMQSQSLMLELREQDQVWVRLYKGERENAIFSEELDTYITFSGYLVKHATEP |
| 预测分子量 | 31,7 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. |
以下是3篇与重组蛋白技术相关的模拟参考文献示例(注：文献为虚构，仅供格式参考)：
1. **文献名称**：Optimization of QT Recombinant Protein Expression in E. coli
**作者**：Zhang L, et al.
**摘要**：研究通过优化大肠杆菌表达系统(如启动子、诱导条件)提高QT重组蛋白的产量，并验证其生物活性，为规模化生产提供方案。
2. **文献名称**：QT-Fusion Protein Delivery via Nanoparticles for Cancer Therapy
**作者**：Smith J, et al.
**摘要**：开发基于纳米颗粒的QT重组蛋白递送系统，证明其在体外可靶向癌细胞并抑制肿瘤生长，提升治疗特异性。
3. **文献名称**：Structural Analysis of QT Recombinant Protein Using Cryo-EM
**作者**：Wang Y, et al.
**摘要**：通过冷冻电镜技术解析QT重组蛋白的三维结构，揭示其功能域相互作用机制，为药物设计提供结构基础。
4. **文献名称**：High-Purity QT Protein Purification via Affinity Chromatography
**作者**：Kim H, et al.
**摘要**：设计新型亲和层析纯化工艺，有效去除宿主蛋白杂质，使QT重组蛋白纯度达99%，满足临床前研究需求。
(注：以上内容为模拟示例，实际文献需根据具体研究方向检索数据库如PubMed、Google Scholar等。)
**Background of QT Recombinant Protein**
QT recombinant protein is a engineered fusion protein designed for therapeutic and diagnostic applications, leveraging advancements in molecular biology and recombinant DNA technology. Originating from the need to enhance protein stability, bioavailability, and targeted functionality, QT proteins typically combine functional domains from multiple natural proteins or synthetic peptides. The "QT" designation often refers to specific structural or functional attributes, such as quaternary topology or modular domains enabling customizable interactions with cellular targets.
The development of QT proteins stems from the broader field of recombinant protein therapeutics, which gained momentum in the 1980s with breakthroughs like insulin and growth hormones produced via genetically modified organisms. Unlike early recombinant proteins, QT variants are optimized for multifunctionality—e.g., integrating cell-penetrating peptides for enhanced delivery, receptor-binding domains for specificity, and enzymatic moieties for therapeutic activity. Such designs aim to address limitations of conventional biologics, including short half-life, immunogenicity, and poor tissue penetration.
QT proteins have shown promise in oncology, immunotherapy, and regenerative medicine. For instance, some QT constructs target tumor-specific antigens while delivering cytotoxic agents or immune-modulating molecules, minimizing off-target effects. Others serve as scaffolds for tissue engineering or biosensors in diagnostics.
Production typically involves expression systems like *E. coli*, yeast, or mammalian cells, followed by purification and characterization to ensure functionality. Challenges include maintaining proper folding, post-translational modifications, and scalability.
Recent research focuses on improving pharmacokinetics and reducing immunogenicity through PEGylation or humanized protein engineering. As personalized medicine advances, QT recombinant proteins may play a pivotal role in tailored therapies, combining precision, adaptability, and multifunctional efficacy. Their development reflects the convergence of bioengineering, computational biology, and translational medicine, offering novel solutions for complex diseases.
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