| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPC |
| Uniprot No | O15118 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-261aa |
| 氨基酸序列 | QSCVWYGECGIAYGDKRYNCEYSGPPKPLPKDGYDLVQELCPGFFFGNVSLCCDVRQLQTLKDNLQLPLQFLSRCPSCFYNLLNLFCELTCSPRQSQFLNVTATEDYVDPVTNQTKTNVKELQYYVGQSFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQAPFTITPVFSDFPVHGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPKPQPPPPPAPWT |
| 预测分子量 | 30.2 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. |
以下是关于核孔复合体(NPC)重组蛋白研究的参考文献示例，涵盖结构、功能及疾病相关研究：
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1. **标题**: *Architecture of the symmetric core of the nuclear pore complex*
**作者**: Hoelz A, et al.
**摘要**: 本研究通过X射线晶体学和冷冻电镜技术解析了核孔复合体对称核心的高分辨率结构。利用重组表达的酵母核孔蛋白(Nup145c、Nup120等)，揭示了关键结构域如何介导复合体的组装及运输机制。
2. **标题**: *In vitro reconstitution of the cytoplasmic face of the human nuclear pore complex*
**作者**: Maimon T, et al.
**摘要**: 作者通过重组表达人源核孔蛋白(如Nup358、Nup214)，在体外重构了NPC胞质面的纤维状结构，并证明其与运输因子(如Importin-β)的动态相互作用，阐明了核质运输的分子基础。
3. **标题**: *Disease-associated mutations in nuclear pore complexes exhibit defective trimerization of scaffold nucleoporins*
**作者**: Mendoza S, et al.
**摘要**: 研究分析了遗传性疾病相关的NPC支架蛋白(如Nup133、Nup160)突变体，发现重组蛋白的三聚化缺陷导致复合体组装异常，揭示了部分先天性疾病与NPC结构破坏的关联。
4. **标题**: *Selective degradation of nuclear pore complexes in cancer cells via engineered proteolysis-targeting chimeras*
**作者**: Zhang Y, et al.
**摘要**: 利用重组核孔蛋白设计靶向降解分子(PROTACs)，在癌细胞中特异性诱导NPC降解，抑制增殖并增强化疗敏感性，为癌症治疗提供新策略。
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**备注**：上述文献标题与摘要为示例性质，实际文献需通过学术数据库检索。建议使用关键词“NPC recombinant protein”或“nucleoporin reconstitution”在PubMed/Google Scholar查找最新研究。
Nuclear pore complexes (NPCs) are massive protein assemblies embedded in the nuclear envelope, serving as selective gatekeepers for nucleocytoplasmic transport. Composed of ~30 distinct proteins (nucleoporins), NPCs regulate the passage of macromolecules, including RNAs and proteins, while maintaining cellular compartmentalization. Dysfunctional NPCs are linked to diseases such as cancer, neurodegenerative disorders, and rare genetic conditions like Hutchinson-Gilford progeria syndrome.
Recombinant NPC proteins are engineered using molecular cloning to express specific nucleoporins in heterologous systems (e.g., bacteria, yeast, or mammalian cells). This approach enables large-scale production of purified proteins for structural and functional studies. For instance, recombinant Nup153 or Nup62 helps dissect their roles in binding transport receptors or forming the NPC's permeability barrier.
The structural complexity and low cellular abundance of native NPCs make recombinant versions invaluable. Techniques like cryo-EM and X-ray crystallography rely on recombinant nucleoporins to resolve atomic details of NPC architecture. Additionally, disease-associated mutations can be introduced into recombinant proteins to study mechanistic defects. Recent advances in AI-driven protein modeling further leverage recombinant NPC components to predict interaction networks and drug-binding sites.
Despite progress, challenges persist. Many nucleoporins contain intrinsically disordered regions, complicating recombinant expression and crystallization. Innovations in fusion tags, solubilization strategies, and cell-free systems aim to overcome these hurdles. Recombinant NPC proteins remain pivotal in developing therapies targeting nuclear transport, offering insights into both basic biology and translational applications.
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