| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NES |
| Uniprot No | P48681 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1321-1569aa |
| 氨基酸序列 | PPPQGETGKEGWDPAVLASEGLEAPPSEKEEGEEGEEECGRDSDLSEEFEDLGTEAPFLPGVPGEVAEPLGQVPQLLLDPAAWDRDGESDGFADEEESGEEGEEDQEEGREPGAGRWGPGSSVGSLQALSSSQRGEFLESDSVSVSVPWDDSLRGAVAGAPKTALETESQDSAEPSGSEEESDPVSLEREDKVPGPLEIPSGMEDAGPGADIIGVNGQGPNLEGKSQHVNGGVMNGLEQSEEVGQGMPL |
| 预测分子量 | 27.8kDa |
| 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条关于核输出信号(NES)重组蛋白研究的示例参考文献(内容为虚构示例，仅作格式参考)：
1. **《Structural analysis of CRM1-NES interactions through recombinant protein engineering》**
- Author: Zhang L, et al.
- 摘要：通过重组表达携带不同NES序列的融合蛋白，结合X射线晶体学解析了CRM1受体与NES的结合模式，揭示了关键疏水残基对核输出效率的影响。
2. **《Development of a fluorescent NES-reporter system for monitoring nuclear export dynamics》**
- Author: Müller S, et al.
- 摘要：构建了基于EGFP-NES重组蛋白的实时监测系统，证明其在活细胞中可量化表征化疗药物对核输出通路的抑制作用。
3. **《Recombinant NES-modified antigens enhance antitumor immune response》**
- Author: Chen H, et al.
- 摘要：设计了一种将病毒NES序列重组至肿瘤抗原中的新型疫苗，实验显示其通过促进抗原胞质递送显著提高了T细胞活化水平。
注：以上文献为模拟案例，实际研究请参考PubMed或Web of Science数据库(可搜索关键词：NES recombinant protein, CRM1. nuclear export signal engineering)。
**Background of NES Recombinant Proteins**
Recombinant proteins engineered with nuclear export signals (NESs) are pivotal tools in molecular and cellular biology for studying nucleocytoplasmic transport, protein localization, and disease mechanisms. NESs are short peptide sequences (typically 10-15 amino acids) that direct proteins out of the nucleus via the CRM1-dependent export pathway. By fusing NES motifs to target proteins, researchers can manipulate their subcellular distribution, enabling functional studies of nuclear-cytoplasmic shuttling or sequestering specific molecules in the cytoplasm.
The development of NES recombinant proteins emerged alongside advances in genetic engineering and protein trafficking research in the 1990s. Early studies on viral proteins, such as HIV-1 Rev and protein kinase A inhibitor (PKI), identified leucine-rich NES motifs critical for their export activity. These discoveries facilitated the design of synthetic or modified NES sequences for experimental use. Today, NES-tagged recombinant proteins are produced using expression systems (e.g., *E. coli*, mammalian cells) and purified via affinity chromatography.
Applications span basic research—such as dissecting signaling pathways (e.g., NF-κB, p53) or creating cytoplasmic relocalization models—to therapeutic exploration, including cancer (e.g., blocking oncogenic transcription factors) and antiviral strategies. For instance, NES-conjugated inhibitors can restrict viral replication by preventing nuclear entry of viral components. Challenges remain in optimizing NES efficiency and specificity, particularly in avoiding unintended interactions with endogenous transport machinery. Recent innovations, such as CRISPR-based tagging and optogenetic NES systems, further enhance spatiotemporal control.
Overall, NES recombinant proteins exemplify the intersection of protein engineering and cell biology, offering versatile solutions for both mechanistic inquiry and translational drug development.
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