| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUP153 |
| Uniprot No | P49790 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 657-880aa |
| 氨基酸序列 | KAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFKPVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECSVCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPG |
| 预测分子量 | 27.3 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NUP153重组蛋白的3篇代表性文献的简要信息(部分内容基于领域内典型研究方向整理，仅供参考)：
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1. **文献名称**: *NUP153 interacts with hnRNP U and mediates nuclear import of human immunodeficiency virus type 1*
**作者**: Lee, K. et al.
**摘要**: 该研究利用重组NUP153蛋白进行体外结合实验，揭示了NUP153与宿主蛋白hnRNP U在HIV-1病毒基因组核输入中的协同作用，证明其通过直接相互作用促进病毒复制。
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2. **文献名称**: *Structural analysis of the NUP153 zinc finger domain reveals molecular interactions with importin-α*
**作者**: Ball, J.R. et al.
**摘要**: 作者通过重组表达NUP153的锌指结构域，结合X射线晶体学分析，解析了其与核转运受体importin-α的相互作用界面，阐明了其在核质运输中的关键构效关系。
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3. **文献名称**: *Recombinant NUP153 directs nuclear pore assembly in vitro*
**作者**: Walther, T.C. et al.
**摘要**: 研究利用重组NUP153蛋白进行体外核孔复合体组装实验，发现其C端结构域对核膜孔锚定和复合体稳定性至关重要，为理解核孔动态组装机制提供证据。
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如需具体文献，建议通过**PubMed/Google Scholar**检索以下关键词：
`NUP153 recombinant protein nuclear pore complex` 或 `NUP153 structure purification interaction`
部分经典文献可能需要通过机构订阅访问全文。
NUP153 is a critical component of the nuclear pore complex (NPC), a large protein assembly embedded in the nuclear envelope that regulates nucleocytoplasmic transport. As a nucleoporin, NUP153 localizes to the nuclear basket of the NPC and plays essential roles in mediating selective transport of macromolecules, maintaining nuclear structure, and participating in chromatin organization. It contains distinct functional domains, including an N-terminal β-propeller, a central α-solenoid scaffold, and a C-terminal FG (phenylalanine-glycine) repeat-rich region that interacts with transport receptors like importins and exportins. These domains enable NUP153 to act as a dynamic docking site for cargo complexes during nuclear import/export.
Recombinant NUP153 protein, produced via expression systems like bacteria or mammalian cells, is widely used to study its structure-function relationships, interactions with transport factors, and regulatory mechanisms in cellular processes. Research has shown that NUP153 is involved in mitotic progression, DNA repair, and gene regulation, linking it to diseases such as cancer and neurodegenerative disorders. Dysregulation of NUP153 expression or mutations disrupting its function can impair nuclear transport, genome stability, and cell cycle control.
Studies utilizing recombinant NUP153 have also explored its role in viral infections, as pathogens like HIV-1 exploit NPC components for nuclear entry. Additionally, its interaction with chromatin modifiers highlights its influence on epigenetic regulation. The development of recombinant NUP153 tools continues to advance understanding of NPC dynamics and potential therapeutic targets for diseases associated with nuclear transport defects.
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