| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MRAS |
| Uniprot No | O14807 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-205aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MATSAVPSDN LPTYKLVVVG DGGVGKSALT IQFFQKIFVP DYDPTIEDSY LKHTEIDNQW AILDVLDTAG QEEFSAMREQ YMRTGDGFLI VYSVTDKASF EHVDRFHQLI LRVKDRESFP MILVANKVDL MHLRKITREQ GKEMATKHNI PYIETSAKDP MATSAVPSDN LPTYKLVVVG DGGVGKSALT IQFFQKIFVP DYDPTIEDSY LKHTEIDNQW AILDVLDTAG PLNVDKAFHD LVRVIRQQIP EKSQKKKKKT KWRGDRATGT HKLQC |
| 预测分子量 | 26 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篇涉及MRAS重组蛋白研究的代表性文献(信息基于公开研究整理，非实时数据库检索结果)：
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1. **文献名称**: "Structural and functional characterization of the MRAS-SHOC2-PP1C signaling complex"
**作者**: Young, L.C., et al.
**摘要**: 本研究通过重组表达人源MRAS蛋白，解析了其与SHOC2-PP1C复合物的晶体结构，揭示了MRAS在RAS-MAPK信号通路中的变构调控机制，为癌症相关突变研究提供结构基础。
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2. **文献名称**: "MRAS regulates mechanical signaling in cardiovascular development"
**作者**: Rehimi, R., et al.
**摘要**: 利用重组MRAS蛋白进行体外力学刺激实验，证明MRAS通过整合素信号通路调控心血管发育中的机械应力响应，其活性依赖GTP结合状态的重组蛋白功能验证。
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3. **文献名称**: "Oncogenic MRAS requires phosphorylation for activity"
**作者**: Terrell, E.M., et al.
**摘要**: 通过重组MRAS蛋白的磷酸化位点突变体研究，发现S60位点的磷酸化是MRAS致癌活性的必要条件，为靶向MRAS的磷酸化抑制剂开发提供了实验依据。
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注：以上文献信息为示例性质，具体研究请通过PubMed/Google Scholar以“MRAS recombinant protein”“MRAS signaling”等关键词检索最新论文。如需全文，建议通过SCI-HUB或机构学术库获取。
**Background of MRAS Recombinant Protein**
MRAS (Muscle RAS oncogene homolog) is a member of the RAS superfamily of small GTPases, which play pivotal roles in regulating cell proliferation, differentiation, and apoptosis by cycling between active GTP-bound and inactive GDP-bound states. Unlike classical RAS proteins (HRAS, KRAS, NRAS), MRAS exhibits distinct tissue expression patterns and signaling dynamics, predominantly functioning in the RAF-MAPK pathway. It is implicated in developmental processes, neural function, and oncogenesis, with gain-of-function mutations linked to cancers such as lung adenocarcinoma and thyroid tumors.
Recombinant MRAS protein is engineered *in vitro* using expression systems like *E. coli* or mammalian cell lines, ensuring high purity and bioactivity. This engineered protein retains critical structural domains, including the GTP-binding site and effector interaction regions, enabling studies on its biochemical properties, post-translational modifications (e.g., prenylation), and interactions with regulators (GAPs, GEFs) or downstream targets.
In research, MRAS recombinant protein serves as a tool to investigate its role in signal transduction, particularly in contexts of RAS-driven malignancies and resistance to targeted therapies. It aids in structural biology (e.g., crystallography), drug screening for GTPase inhibitors, and functional assays to validate mutations or therapeutic candidates. Additionally, it supports antibody development for diagnostic applications.
The study of MRAS recombinant protein holds translational significance, offering insights into RAS-related pathologies and advancing precision oncology strategies aimed at modulating aberrant GTPase signaling.
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