| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gltS |
| Uniprot No | P55038 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-435aa |
| 氨基酸序列 | MSFQYPLLAPMTNSSVATNSNQPFLGQPWLVEERDACGVGFIANLRGKPDHTLVEQALKALGCMEHRGGCSADNDSGDGAGVMTAIPRELLAQWFNTRNLPMPDGDRLGVGMVFLPQEPSAREVARAYVEEVVRLEKLTVLGWREVPVNSDVLGIQAKNNQPHIEQILVTCPEGCAGDELDRRLYIARSIIGKKLAEDFYVCSFSCRTIVYKGMVRSIILGEFYLDLKNPGYTSNFAVYHRRFSTNTMPKWPLAQPMRLLGHNGEINTLLGNINWMAAREKELEVSGWTKAELEALTPIVNQANSDSYNLDSALELLVRTGRSPLEAAMILVPEAYKNQPALKDYPEISDFHDYYSGLQEPWDGPALLVFSDGKIVGAGLDRNGLRPARYCITKDDYIVLGSEAGVVDLPEVDIVEKGRLAPGQMIAVDLAEQKI |
| 预测分子量 | 55.5 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. |
以下是关于gltS重组蛋白的参考文献示例(注：文献为示例性质，具体文献请通过学术数据库核实)：
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1. **文献名称**：*"Cloning and Heterologous Expression of the gltS Gene from Bacillus subtilis"*
**作者**：Müller, R. et al.
**摘要**：研究通过克隆枯草芽孢杆菌gltS基因，在大肠杆菌中实现重组蛋白表达，并验证其谷氨酰胺合成酶活性，探讨其在氮代谢中的功能。
2. **文献名称**：*"Crystallographic Study of Recombinant GltS: Insights into Substrate Binding"*
**作者**：Tanaka, K. et al.
**摘要**：解析了重组GltS蛋白的晶体结构，揭示了其底物(谷氨酸和氨)结合位点的关键氨基酸残基，为酶催化机制提供结构依据。
3. **文献名称**：*"Optimization of GltS Recombinant Protein Production in E. coli Using Inducible Promoters"*
**作者**：Chen, L. & Wang, H.
**摘要**：比较不同诱导表达系统(如IPTG和温度诱导)对重组GltS产量的影响，优化培养条件以提高可溶性蛋白表达水平。
4. **文献名称**：*"Functional Complementation of gltS-Deficient E. coli with Recombinant GltS from Pseudomonas aeruginosa"*
**作者**：Gomez, J.E. et al.
**摘要**：通过异源表达铜绿假单胞菌来源的重组GltS蛋白，恢复大肠杆菌gltS缺陷株的谷氨酰胺合成能力，验证其跨物种功能保守性。
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**建议**：如需具体文献，可在PubMed、Web of Science等平台搜索关键词 **"gltS recombinant protein"** 或 **"gltS cloning expression"**，并筛选近年的研究以获取最新进展。
**Background of gltS Recombinant Protein**
The *gltS* gene encodes glutamate synthase, a key enzyme in nitrogen metabolism, primarily found in bacteria, plants, and some archaea. Glutamate synthase catalyzes the synthesis of glutamate from glutamine and α-ketoglutarate, playing a critical role in ammonia assimilation and maintaining cellular nitrogen balance. In microorganisms, this enzyme is vital for growth under nitrogen-limiting conditions, while in plants, it supports amino acid biosynthesis and photorespiration.
Recombinant gltS protein is produced via heterologous expression systems, such as *E. coli*, to enable large-scale purification and functional studies. Traditional purification of native gltS is challenging due to its instability and low abundance. Recombinant technology overcomes these limitations, allowing researchers to obtain high-purity, active enzyme variants for structural and biochemical analyses.
Studies on recombinant gltS have elucidated its bimodal structure, comprising a glutaminase domain (responsible for hydrolyzing glutamine) and a synthase domain (for α-ketoglutarate binding). These insights have advanced understanding of its catalytic mechanism, including electron transfer processes and allosteric regulation. Additionally, recombinant gltS is utilized in industrial applications, such as biofertilizer development and microbial cell factories for sustainable amino acid production.
Research on gltS also addresses its role in microbial pathogenesis, as glutamate synthesis is crucial for pathogen survival in host environments. Inhibitors targeting gltS are explored as potential antimicrobial agents. Overall, recombinant gltS serves as a versatile tool in both basic science and biotechnology, bridging gaps between metabolic enzymology and applied biotechnological innovations.
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