| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LDP |
| Uniprot No | Q9BVJ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-150aa |
| 氨基酸序列 | MGVQPPNFSWVLPGRLAGLALPRLPAHYQFLLDLGVRHLVSLTERGPPHSDSCPGLTLHRLRIPDFCPPAPDQIDRFVQIVDEANARGEAVGVHCALGFGRTGTMLACYLVKERGLAAGDAIAEIRRLRPGSIETYEQEKAVFQFYQRTK |
| 预测分子量 | 16,5 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LDP(光敏剂相关)重组蛋白的参考文献示例。需要说明的是，这些文献信息为模拟示例，实际引用前请通过学术数据库核实准确性：
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1. **标题**：LDP重组蛋白介导的光动力疗法靶向治疗宫颈癌的实验研究
**作者**：G. Li, Y. Chen, X. Wang
**摘要**：本研究构建了LDP重组蛋白与光敏剂Ce6的复合物(LDP-Ce6)，通过体外和荷瘤小鼠模型验证其对宫颈癌细胞的靶向杀伤作用，证实其通过激活凋亡通路抑制肿瘤生长，为靶向光动力疗法提供新策略。
2. **标题**：重组LDP蛋白在肺癌光敏药物递送中的优化与应用
**作者**：M. Zhang, et al.
**摘要**：利用基因工程技术优化LDP重组蛋白的表达与纯化，将其与光敏剂ZnPc结合，显著提高了药物在肺癌细胞内的富集效率，并通过降低正常组织毒性证明了其临床转化潜力。
3. **标题**：LDP-AE重组蛋白增强肿瘤血管靶向性的机制研究
**作者**：R. Kumar, S. Patel
**摘要**：通过融合LDP重组蛋白与血管内皮生长因子受体(VEGFR)配体AE，开发出LDP-AE重组蛋白。实验表明该蛋白可特异性结合肿瘤血管，提高光敏剂传递效率，并抑制肿瘤转移相关通路。
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**注意事项**：
- LDP在光动力疗法中常作为药物载体，但不同文献中具体定义可能不同，建议结合研究背景筛选文献。
- 实际研究中可检索关键词如 **"LDP recombinant protein"、"photodynamic therapy"、"drug delivery"** 等扩大结果范围。
- 推荐使用PubMed、Web of Science或Google Scholar验证文献，优先选择近五年内发表于 **《Journal of Controlled Release》《Biomaterials》** 等期刊的研究。
**Background of LDP Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine. LDP (Ligand-Directed Prodrug-activating protein) recombinant proteins represent a specialized class designed for targeted therapeutic applications. These proteins are typically engineered by fusing a ligand-binding domain (e.g., antibodies or peptides) with a prodrug-activating enzyme, enabling precise delivery of therapeutic agents to specific cells or tissues.
The concept stems from advancements in recombinant DNA technology in the late 20th century, which allowed precise manipulation of protein structures. LDPs leverage this to minimize systemic toxicity in treatments like cancer therapy. By directing prodrug-converting enzymes to tumor sites, inactive prodrugs are locally activated, enhancing efficacy while sparing healthy tissues.
Production involves cloning target gene sequences into expression vectors (e.g., *E. coli*, yeast, or mammalian cells), followed by purification and functional validation. Challenges include maintaining protein stability, ensuring correct folding, and achieving high yield. Innovations in protein engineering, such as directed evolution or fusion tags, have addressed some limitations.
LDP-based therapies are under active research, particularly in oncology. For example, antibody-directed enzyme prodrug therapy (ADEPT) utilizes LDP principles. Beyond cancer, applications extend to autoimmune diseases and infectious diseases, where targeted delivery is critical.
Despite promise, hurdles remain: immunogenicity, enzyme efficiency, and tissue penetration. Ongoing studies focus on optimizing ligand specificity and enzyme kinetics. With advancements in personalized medicine and bioconjugation techniques, LDP recombinant proteins hold potential as next-generation precision therapeutics, bridging the gap between molecular biology and clinical application.
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