| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RRAS2 |
| Uniprot No | P62070 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-204aa |
| 氨基酸序列 | MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMREQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKIRMNVDQAFHELVRVIRKFQEQECPPSPEPTRKEKDKKGCHCVIF |
| 预测分子量 | 50.1kDa |
| 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RRAS2重组蛋白的模拟参考文献示例(注：部分内容为虚构，仅作格式参考)：
1. **标题**: "Expression and Functional Characterization of Recombinant RRAS2 GTPase in Mammalian Cells"
**作者**: Smith A, et al.
**摘要**: 研究利用哺乳动物表达系统成功表达并纯化RRAS2重组蛋白，验证其GTP水解活性及对MAPK信号通路的调控作用，为体外功能研究提供工具。
2. **标题**: "Crystal Structure Analysis of RRAS2 Reveals Conformational Changes upon GTP Binding"
**作者**: Chen L, et al.
**摘要**: 通过重组RRAS2蛋白的结晶和结构解析，揭示了其GTP结合状态下的构象变化，为靶向RRAS2的癌症药物设计提供结构基础。
3. **标题**: "Role of Oncogenic RRAS2 Mutants in Tumorigenesis: Insights from Recombinant Protein Assays"
**作者**: Gonzalez R, et al.
**摘要**: 利用重组RRAS2突变体蛋白进行体外实验，证明特定突变(如Q72L)导致GTP酶活性丧失，持续激活下游信号通路，促进癌细胞增殖。
4. **标题**: "Development of a High-Yield E. coli System for Recombinant RRAS2 Production"
**作者**: Tanaka K, et al.
**摘要**: 优化大肠杆菌表达体系，实现RRAS2重组蛋白的高效可溶性表达，并通过镍柱亲和层析获得高纯度蛋白，适用于大规模生化研究。
(注：以上文献为示例性质，实际引用请通过学术数据库核实。)
The RRAS2 recombinant protein is derived from the RRAS2 gene, which encodes a member of the RAS GTPase superfamily. This small GTP-binding protein plays critical roles in regulating cellular processes such as proliferation, differentiation, and survival by cycling between active GTP-bound and inactive GDP-bound states. RRAS2 shares structural and functional similarities with classical RAS proteins (HRAS, KRAS, NRAS) but exhibits distinct signaling preferences, particularly influencing pathways like PI3K/AKT and MAPK/ERK. Its dysregulation has been implicated in various cancers, cardiovascular diseases, and RASopathies—developmental disorders caused by RAS pathway mutations.
Recombinant RRAS2 protein is typically produced using bacterial or mammalian expression systems, enabling controlled studies of its biochemical properties and interactions. Purification methods often involve affinity chromatography with tags like GST or His for isolation. Researchers utilize this protein to investigate GTP/GDP binding kinetics, effector interactions, and post-translational modifications (e.g., prenylation) critical for membrane localization and function.
In therapeutic contexts, RRAS2 recombinant proteins serve as tools for drug screening, particularly for cancers driven by RRAS2 mutations or overexpression. Its oncogenic variants (e.g., Q72L) are studied to understand constitutive activation mechanisms. Additionally, engineered mutants help dissect signaling specificity within the RAS family. Current challenges include resolving its structural nuances and developing isoform-specific inhibitors, given the high conservation among RAS proteins. As a less studied RAS member, RRAS2 continues to attract attention for its unique regulatory roles and potential as a biomarker or therapeutic target.
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