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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FG |
| Uniprot No | Q969R8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-447aa |
| 氨基酸序列 | MRSVSYVQRVALEFSGSLFPHAICLGDVDNDTLNELVVGDTSGKVSVYKNDDSRPWLTCSCQGMLTCVGVGDVCNKGKNLLVAVSAEGWFHLFDLTPAKVLDASGHHETLIGEEQRPVFKQHIPANTKVMLISDIDGDGCRELVVGYTDRVVRAFRWEELGEGPEHLTGQLVSLKKWMLEGQVDSLSVTLGPLGLPELMVSQPGCAYAILLCTWKKDTGSPPASEGPTDGSRETPAARDVVLHQTSGRIHNKNVSTHLIGNIKQGHGTESSGSGLFALCTLDGTLKLMEEMEEADKLLWSVQVDHQLFALEKLDVTGNGHEEVVACAWDGQTYIIDHNRTVVRFQVDENIRAFCAGLYACKEGRNSPCLVYVTFNQKIYVYWEVQLERMESTNLVKLLETKPEYHSLLQELGVDPDDLPVTRALLHQTLYHPDQPPQCAPSSLQDPT |
| 预测分子量 | 49,3 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FG重组蛋白的3篇代表性文献的模拟示例(注：文献信息为示例，非真实存在)：
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1. **文献名称**：*Expression and functional characterization of recombinant FG-nucleoporins in vitro*
**作者**：Limbach, H.J. et al.
**摘要**：研究报道了在大肠杆菌系统中高效表达含有FG重复序列的核孔蛋白(如Nup153、Nup62)，通过体外实验验证了其与核转运受体Importin-β的结合能力，证实FG结构域在选择性物质运输中的关键作用。
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2. **文献名称**：*Dynamic structural analysis of FG-repeat proteins by NMR spectroscopy*
**作者**：Yamada, K. & Rosenblum, G.
**摘要**：利用核磁共振技术解析了重组FG蛋白(如Nsp1)的构象动态变化，发现其无序区域在结合转运受体时形成短暂α螺旋，揭示了FG重复序列通过构象灵活性实现快速可逆相互作用的机制。
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3. **文献名称**：*Self-assembly of recombinant FG domains into hydrogel for biomimetic nuclear pore modeling*
**作者**：Wei, Q. et al.
**摘要**：通过重组表达纯化的FG结构域蛋白(如Nup98)，构建了模拟核孔选择性屏障的水凝胶模型，证明其孔径可调性和分子筛分功能，为人工核膜设计提供了实验基础。
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**注**：如需真实文献，建议通过PubMed/Google Scholar检索关键词："FG repeat protein recombinant" 或 "FG-nucleoporin expression"。
FG recombinant proteins are engineered biomolecules derived from phenylalanine-glycine (FG)-repeat domains found in nucleoporins, key components of the nuclear pore complex (NPC). These intrinsically disordered proteins feature repetitive FG dipeptide motifs interspersed with hydrophilic spacers, creating dynamic, phase-separated hydrogels that regulate selective nucleocytoplasmic transport. The NPC's permeability barrier allows passive diffusion of small molecules while enabling receptor-mediated translocation of large cargoes (e.g., mRNA, proteins) through transient interactions between FG repeats and nuclear transport receptors.
Researchers produce FG recombinant proteins using heterologous expression systems (e.g., E. coli, yeast) to study their biophysical properties and transport mechanisms. These proteins retain the ability to form dense, selective matrices despite lacking the full NPC architecture. Their unique phase behavior—existing in a fuzzy polymer brush configuration—has inspired applications beyond basic research. Biomedical engineers exploit FG proteins' tunable permeability for drug delivery systems, biosensors, and artificial nuclear membrane prototypes. Nanotechnologists incorporate them into biomimetic nanopores for selective filtration or single-molecule sensing platforms.
Recent studies focus on modulating FG repeat composition and spatial arrangement to control mesh size and interaction kinetics. Challenges persist in replicating the NPC's exquisite transport efficiency, driving innovations in protein engineering and computational modeling. FG recombinant proteins also serve as simplified models for investigating phase separation phenomena in cellular organization and neurodegenerative diseases associated with nucleocytoplasmic transport defects. Their versatility continues to bridge structural biology, soft matter physics, and synthetic biology applications.
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