| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NMS |
| Uniprot No | Q5H8A3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 109-141aa |
| 氨基酸序列 | IL QRGSGTAAVD FTKKDHTATW GRPFFLFRPR N |
| 预测分子量 | 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NMS重组蛋白的参考文献示例(注：文献为虚构示例，供参考)：
1. **文献名称**：Efficient Expression and Purification of Recombinant NMS Protein in *E. coli*
**作者**：Zhang W, et al.
**摘要**：本研究建立了一种基于大肠杆菌表达系统的重组NMS蛋白高效生产方法，通过优化诱导条件和纯化工艺(如His标签亲和层析)，获得高纯度蛋白，为功能研究奠定基础。
2. **文献名称**：NMS Recombinant Protein as a Biomarker for Neuroendocrine Tumors
**作者**：Smith J, et al.
**摘要**：验证了重组NMS蛋白在神经内分泌肿瘤血清检测中的特异性，其与患者样本的抗体反应表现出高灵敏度和诊断价值，具有临床应用潜力。
3. **文献名称**：Structural Insights into NMS Recombinant Protein via X-ray Crystallography
**作者**：Li H, et al.
**摘要**：通过晶体学解析了NMS蛋白的三维结构，揭示了其活性位点与细胞受体的结合模式，为靶向药物开发提供结构生物学依据。
4. **文献名称**：NMS-based Nanoparticle Delivery System Enhances Anticancer Efficacy
**作者**：Wang Y, et al.
**摘要**：开发了以NMS重组蛋白修饰的纳米载体，实验证明其能靶向递送化疗药物至肿瘤组织，显著提高小鼠模型中的抑瘤效果并降低毒性。
**说明**：以上内容为模拟文献，实际研究中请替换为真实发表的论文。若需检索真实文献，建议在PubMed或Web of Science等平台以关键词“NMS recombinant protein”或结合具体蛋白全称进行查询。
Non-native modular scaffold (NMS) recombinant proteins are engineered biomolecules designed to address challenges in protein stability, functionality, and adaptability for biomedical applications. Traditional recombinant protein production relies on host systems (e.g., *E. coli*, yeast, mammalian cells*) to express natural protein sequences. However, limitations such as poor solubility, aggregation, or loss of activity in non-native environments often hinder their utility. NMS technology introduces synthetic or hybrid scaffolds to refold or stabilize protein domains, enabling the assembly of functional chimeric proteins that may not exist in nature. This approach combines modular design principles with computational modeling to optimize structural conformations, enhancing thermostability, protease resistance, and binding specificity.
The development of NMS proteins is driven by demands in targeted drug delivery, biosensing, and synthetic biology. For instance, they are explored as customizable carriers for cancer therapeutics, where fusion proteins can simultaneously target tumor-specific receptors and deliver payloads. Additionally, NMS platforms facilitate the creation of multi-enzyme cascades for industrial biocatalysis or engineered antibodies with improved pharmacokinetics. Challenges include balancing flexibility and rigidity in scaffold design, minimizing immunogenicity, and ensuring cost-effective scale-up. Advances in AI-driven protein folding prediction and high-throughput screening have accelerated iterative optimization of these systems. As a bridge between natural protein engineering and fully synthetic nanomachines, NMS recombinant proteins represent a versatile toolkit for next-generation biotherapeutics and biomanufacturing.
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