| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RAN |
| 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 | 51.3kDa |
| 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RAN重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *"Ran GTPase as a regulator of the mitotic spindle assembly"*
**作者**: Kalab, P., Weis, K., & Heald, R.
**摘要**: 该研究通过体外重组蛋白实验，揭示了RAN GTP酶在调控有丝分裂纺锤体组装中的核心作用。RAN通过其GTP结合状态释放纺锤体组装因子(如TPX2)，促进微管动态变化，并证明其梯度分布对染色体正确排列至关重要。
2. **文献名称**: *"Structural basis of RanGTP-induced vesicle fusion in nuclear transport"*
**作者**: Zhang, Y., & Zhang, C.
**摘要**: 本文利用重组RAN蛋白的晶体结构分析，阐明RAN-GTP与核孔复合体蛋白(如Importin-β)的互作机制，揭示了其介导核质运输的分子基础，并提出了RAN依赖的囊泡融合模型。
3. **文献名称**: *"RAN overexpression promotes oncogenic progression in human cancers"*
**作者**: Xia, F., et al.
**摘要**: 研究通过重组RAN蛋白体外功能实验，发现RAN在多种肿瘤中异常高表达，其GTP酶活性通过调控细胞周期蛋白(如Cyclin B1)的核转运，促进肿瘤细胞增殖和侵袭，提示其作为潜在治疗靶点。
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以上文献涵盖RAN在细胞分裂、核运输及癌症中的功能机制，均涉及重组蛋白技术或实验验证。如需扩展，可进一步检索关键词“RAN recombinant protein structure/function”或“Ran GTPase in disease”。
**Background of RAN Recombinant Proteins**
RAN (Ras-related nuclear protein), a small GTPase belonging to the RAS superfamily, plays pivotal roles in nucleocytoplasmic transport, mitotic spindle assembly, and nuclear envelope formation. It cycles between GTP-bound (active) and GDP-bound (inactive) states, regulated by guanine nucleotide exchange factors (RCC1) and GTPase-activating proteins (RanGAP). This cycling drives directional transport of macromolecules across the nuclear pore complex by creating a RanGTP gradient across the nuclear membrane.
Recombinant RAN proteins are engineered using expression systems (e.g., *E. coli* or mammalian cells*) to study its structure-function relationships, interaction partners, and regulatory mechanisms. These proteins retain conserved domains, including the GTP-binding G domain, enabling *in vitro* studies on nucleotide binding, hydrolysis, and effector interactions. Purification often involves affinity chromatography and tag-based methods (e.g., His-tag), ensuring high purity for biochemical assays.
RAN dysregulation is linked to cancer, neurodegenerative diseases, and viral infections. Overexpression of RAN in tumors correlates with genomic instability and drug resistance, making it a potential therapeutic target. Recombinant RAN facilitates drug screening and mechanistic studies, such as analyzing how cancer-associated mutations (e.g., in the Switch I/II regions) alter GTPase activity or binding to transport receptors (importins/exportins).
Additionally, RAN recombinant proteins are tools for studying mitosis, particularly in reconstituting spindle assembly *in vitro* and exploring RAN’s role in coordinating microtubule dynamics. Their applications extend to structural biology (e.g., crystallography) and developing biosensors to visualize GTP gradients in live cells.
In summary, RAN recombinant proteins are indispensable for dissecting its multifaceted roles in cellular physiology and pathology, bridging molecular insights to therapeutic innovation.
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