| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPB |
| Uniprot No | Q8NG41 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-53aa |
| 氨基酸序列 | WYKPAAGHSSYSVGRAAGLLSGLRRSPYA |
| 预测分子量 | 3.1 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NPB(Neuroblastoma Breakpoint Family)重组蛋白的3篇参考文献示例(文献信息为虚构，仅供格式参考)：
1. **文献名称**：*Efficient expression and purification of NPB recombinant protein in E. coli for structural analysis*
**作者**：Zhang L, et al.
**摘要**：本研究优化了NPB基因在大肠杆菌中的表达条件，采用His标签亲和层析技术纯化获得高纯度重组蛋白，并通过X射线晶体学解析其三维结构，为功能研究奠定基础。
2. **文献名称**：*Functional characterization of NPB recombinant protein in cancer cell signaling pathways*
**作者**：Tanaka K, et al.
**摘要**：通过哺乳动物细胞表达系统制备NPB重组蛋白，发现其通过调控MAPK/ERK通路抑制神经母细胞瘤细胞增殖，提示其作为潜在治疗靶点的可能性。
3. **文献名称**：*Development of a high-yield NPB fusion protein production system using Pichia pastoris*
**作者**：Müller S, et al.
**摘要**：利用毕赤酵母表达系统实现NPB重组蛋白的高效分泌表达，优化发酵条件后产量提升5倍，并验证其在体外诊断试剂中的稳定性与应用潜力。
(注：以上文献为模拟内容，实际研究中请通过PubMed或Google Scholar检索真实文献。)
**Background of NPB Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and biomedical research. NPB (Non-Pathogen-Based) recombinant proteins represent a specialized class produced using non-pathogenic host systems, such as *E. coli*, yeast, or insect cells, to ensure safety and scalability. These proteins are synthesized by inserting target gene sequences into expression vectors, which are then introduced into host organisms for controlled protein production.
The development of NPB recombinant proteins emerged to address challenges in traditional protein production, including contamination risks from pathogenic hosts, low yields, and complex purification processes. By leveraging non-pathogenic systems, NPB technology minimizes biosafety concerns while enhancing reproducibility—a critical factor for therapeutic and diagnostic applications. For instance, *E. coli*-derived NPB proteins are widely used due to their cost-effectiveness and rapid growth, whereas yeast and insect cell systems enable proper post-translational modifications for complex proteins.
Applications of NPB recombinant proteins span therapeutics (e.g., insulin, monoclonal antibodies), vaccines (e.g., HPV vaccines), and research tools (e.g., enzymes, cytokines). They are indispensable in drug discovery, structural biology, and diagnostics, where purity and functionality are paramount. Recent advancements, such as CRISPR-assisted gene editing and AI-driven protein design, further optimize their expression and stability.
Despite progress, challenges remain, including achieving proper protein folding in prokaryotic systems and scaling up eukaryotic production cost-effectively. Nonetheless, NPB recombinant proteins continue to drive innovation in precision medicine and biomanufacturing, underscoring their role as a cornerstone of biotechnological advancement. Their integration with sustainable practices and novel delivery systems promises to expand their impact across global healthcare and industrial sectors.
×
