| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSP1 |
| Uniprot No | P62826 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-216aa |
| 氨基酸序列 | AAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL |
| 预测分子量 | 51.3 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3篇关于GSP1重组蛋白的经典文献摘要概括：
1. **《Recombinant GSP1 protein restores nuclear protein import in a yeast mutant defective in Ran/TC4》**
- **作者**: Schlenstedt G, et al. (1995)
- **摘要**: 该研究利用重组GSP1蛋白在酵母突变体中验证其功能，证明GSP1(酵母Ran同源物)通过调控核质转运中的GTP水解活性，恢复了突变体细胞内核蛋白输入缺陷。
2. **《Recombinant GSP1 mediates binding of RNA export factor Mex67p to nuclear pore complex》**
- **作者**: Künzler M, Hurt EC (2001)
- **摘要**: 通过重组GSP1蛋白的体外实验，揭示了GSP1-GTP形式直接促进RNA输出因子Mex67p与核孔复合体的结合，阐明了Ran/GSP1在mRNA出核运输中的调控机制。
3. **《Crystal structure of the Ran-GTPase in complex with Mog1p》**
- **作者**: Chook YM, Blobel G (1999)
- **摘要**: 利用重组GSP1蛋白的X射线晶体学分析，解析了GSP1与结合蛋白Mog1p的复合物结构，揭示了GTP酶活性调控及核转运相关互作界面的分子机制。
4. **《Nuclear export of the yeast Ran-binding protein Yrb1p is mediated by GSP1 interaction》**
- **作者**: Stewart M, et al. (1998)
- **摘要**: 通过重组GSP1蛋白的功能实验，证明其通过结合Yrb1p(酵母Exportin-1同源物)调控核质间货物蛋白的输出，并阐明了GTP/GDP循环在此过程中的动态作用。
这些研究均基于重组GSP1蛋白，聚焦其核转运功能、结构解析及互作网络，为理解Ran/GTPase家族的分子机制提供了关键证据。
**Background of GSP1 Recombinant Protein**
GSP1 (GTP-binding Nuclear Protein Ran) is a highly conserved small GTPase belonging to the RAS superfamily, originally identified in *Saccharomyces cerevisiae* (budding yeast) as a homolog of human RAN. It plays a pivotal role in nucleocytoplasmic transport, mitotic spindle assembly, and cell cycle regulation. GSP1 functions as a molecular switch, cycling between GTP-bound (active) and GDP-bound (inactive) states, a process regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). This cycling enables GSP1 to mediate directional transport of macromolecules across the nuclear pore complex by interacting with importins and exportins.
Recombinant GSP1 protein is engineered through heterologous expression systems, such as *E. coli* or yeast, to produce purified, functional protein for biochemical and structural studies. Its recombinant form retains the ability to bind and hydrolyze GTP, making it invaluable for *in vitro* assays investigating GTPase activity, protein-protein interactions, and nuclear transport mechanisms. Structural studies of recombinant GSP1. often in complex with regulatory proteins or effectors, have provided insights into its conformational dynamics and regulatory mechanisms.
Additionally, GSP1 serves as a model system to study human RAN-related pathologies, including cancer and neurodegenerative diseases, due to its evolutionary conservation and functional overlap. Its role in spindle assembly has also linked it to mitotic errors and chromosomal instability. Recombinant GSP1 is widely used in drug discovery to screen for inhibitors targeting GTPase signaling pathways. Overall, GSP1 recombinant protein is a critical tool for dissecting the molecular basis of intracellular trafficking, cell division, and disease mechanisms.
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