| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRS |
| Uniprot No | Q16548 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-152aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMTDCEF GYIYRLAQDY LQYVLQIPQP GSGPSKTSRV LQKVAFSVQK EVEKNLKSCL DNVNVVSVDT ARTLFNQVME KEFEDDIINW GRIVTIFAFE GILIKKLLRQ QIAPDVDTYK EISYFVAEFI MNNTGEWIRQ NGGWENGFVK KFEPKS |
| 预测分子量 | 20 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. |
以下是模拟生成的关于GRS(假设为谷氨酰胺-tRNA合成酶)重组蛋白的参考文献示例，供参考：
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1. **文献名称**：*Expression and Purification of Recombinant Glutamyl-tRNA Synthetase in E. coli*
**作者**：Zhang, L.; Wang, H. et al.
**摘要**：本研究成功在大肠杆菌系统中表达了具有活性的重组GRS蛋白，通过优化密码子和纯化条件，获得高纯度蛋白，并验证了其酶活性，为后续功能研究奠定基础。
2. **文献名称**：*Structural Insights into GRS in Mitochondrial Dysfunction*
**作者**：Smith, J.; Patel, R. et al.
**摘要**：通过X射线晶体学解析了重组GRS的三维结构，揭示了其与线粒体tRNA结合的机制，为治疗线粒体相关遗传疾病提供了潜在靶点。
3. **文献名称**：*GRS Recombinant Protein Attenuates Neuroinflammation in Alzheimer's Model*
**作者**：Kim, Y.; Lee, S. et al.
**摘要**：在阿尔茨海默病小鼠模型中，重组GRS蛋白通过调节神经炎症通路显著改善认知功能，表明其在神经退行性疾病治疗中的应用潜力。
4. **文献名称**：*Industrial-Scale Production of GRS for Enzymatic Synthesis*
**作者**：Müller, F.; Schmidt, D. et al.
**摘要**：开发了GRS重组蛋白的工业化发酵工艺，实现了低成本高产率生产，并证明其在酶催化反应中的高效性，适用于生物制造领域。
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**说明**：以上文献为模拟生成，实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体论文。若GRS指代其他特定蛋白(如某种病毒重组蛋白)，建议补充背景信息以便精准查找。
**Background of GRS Recombinant Proteins**
Recombinant proteins, including GRS (Glutamyl-tRNA Synthetase) recombinant variants, are engineered through genetic modification to enable large-scale production, functional studies, and therapeutic applications. GRS is a member of the aminoacyl-tRNA synthetase (aaRS) family, enzymes critical for protein synthesis. Specifically, GRS catalyzes the attachment of glutamine to its cognate tRNA, ensuring accurate translation of mRNA into proteins. Beyond its canonical role, GRS has been implicated in non-canonical functions, such as immune signaling and apoptosis regulation, highlighting its biological versatility.
The development of recombinant GRS proteins emerged from advancements in molecular cloning and expression systems. By isolating the GRS gene and inserting it into heterologous hosts (e.g., *E. coli*, yeast, or mammalian cells), researchers produce purified, functional GRS with high yield and consistency. This approach overcomes limitations of native protein extraction, such as low abundance or contamination.
GRS recombinant proteins are pivotal in structural and mechanistic studies. X-ray crystallography and cryo-EM analyses using recombinant GRS have revealed its domain architecture, active sites, and interactions with tRNA or small molecules. These insights aid in understanding mutations linked to neurodegenerative diseases (e.g., Charcot-Marie-Tooth neuropathy) and autoimmune disorders.
In therapeutics, recombinant GRS is explored as a target or tool. Autoantibodies against GRS are biomarkers in idiopathic inflammatory myopathies, driving diagnostic assay development. Additionally, GRS inhibitors are investigated for antimicrobial or anticancer therapies, leveraging its essential role in cell proliferation.
Recent innovations include engineered GRS variants with enhanced stability or altered substrate specificity, enabling applications in synthetic biology and enzyme engineering. Despite challenges in solubility and post-translational modification mimicry, GRS recombinant proteins remain indispensable for both basic research and translational medicine, bridging gaps between molecular biology and clinical innovation.
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