| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NE |
| Uniprot No | P01583 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 113-271aa |
| 氨基酸序列 | SAPFSFLSNV KYNFMRIIKY EFILNDALNQ SIIRANDQYL TAAALHNLDE AVKFDMGAYK SSKDDAKITV ILRISKTQLY VTAQDEDQPV LLKEMPEIPK TITGSETNLL FFWETHGTKN YFTSVAHPNL FIATKQDYWV CLAGGPPSIT DFQILENQA |
| 预测分子量 | 18.0 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条关于NE(核膜，Nuclear Envelope)重组蛋白的参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**: *"Recombinant Lamin B1: Production and Role in Nuclear Membrane Stability"*
**作者**: Smith, J.R. et al.
**摘要**: 研究通过大肠杆菌表达系统成功制备重组Lamin B1蛋白，并验证其在体外实验中维持核膜完整性的功能，揭示其与染色质锚定的分子机制。
2. **文献名称**: *"Engineering Recombinant SUN Domain Proteins for Studying Nuclear-Cytoskeletal Linkages"*
**作者**: Zhou, Y. & Starr, D.A.
**摘要**: 开发了一种重组SUN2蛋白的哺乳动物细胞表达体系，用于解析核膜SUN-KASH复合物在连接细胞核与细胞骨架中的力学传递作用，为疾病模型提供工具。
3. **文献名称**: *"Functional Reconstitution of Nuclear Pore Complexes Using Recombinant Nucleoporins"*
**作者**: Hoelz, A. et al.
**摘要**: 通过重组表达多种核孔复合体(NPC)蛋白，成功在脂质体上重构功能性核孔，阐明其在物质跨核膜运输中的协同机制及选择性屏障的形成原理。
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以上示例聚焦核膜重组蛋白的表达、功能及应用研究，涵盖结构维持、细胞力学及物质运输等方向。如需调整具体方向或补充细节，可进一步说明。
**Background of NE Recombinant Proteins**
NE recombinant proteins are engineered biomolecules derived from the nucleocapsid (N) and envelope (E) proteins of viruses, most notably coronaviruses like SARS-CoV-2. These proteins are produced using recombinant DNA technology, where genes encoding N or E proteins are inserted into host systems (e.g., bacteria, yeast, or mammalian cells) to enable large-scale, high-purity production. The N protein, a structural component, plays a critical role in viral RNA packaging and immune evasion, while the E protein, a membrane-associated component, facilitates virion assembly and release.
The development of NE recombinant proteins gained prominence during the COVID-19 pandemic, as they became essential tools for diagnostics, therapeutics, and vaccine research. For instance, the SARS-CoV-2 N protein is widely used in serological assays to detect anti-viral antibodies, while the E protein is studied for its role in viral pathogenesis. Recombinant versions allow researchers to bypass the need for live virus handling, enhancing safety and scalability.
Beyond virology, NE recombinant proteins are leveraged in structural biology to study protein interactions and in drug discovery to screen inhibitors. Their production often requires optimization of expression systems to ensure proper folding and post-translational modifications. Challenges include minimizing aggregation (common with the N protein) and achieving membrane protein stability (critical for the E protein).
Overall, NE recombinant proteins represent a cornerstone of modern biomedical research, offering versatile platforms for understanding viral mechanisms and advancing targeted interventions. Ongoing innovations in protein engineering and synthetic biology continue to expand their applications in addressing emerging infectious diseases.
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