| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gltI |
| Uniprot No | P37902 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-302aa |
| 氨基酸序列 | DDAAPAAGSTLDKIAKNGVIVVGHRESSVPFSYYDNQQKVVGYSQDYSNAIVEAVKKKLNKPDLQVKLIPITSQNRIPLLQNGTFDFECGSTTNNVERQKQAAFSDTIFVVGTRLLTKKGGDIKDFANLKDKAVVVTSGTTSEVLLNKLNEEQKMNMRIISAKDHGDSFRTLESGRAVAFMMDDALLAGERAKAKKPDNWEIVGKPQSQEAYGCMLRKDDPQFKKLMDDTIAQVQTSGEAEKWFDKWFKNPIPPKNLNMNFELSDEMKALFKEPNDKALN |
| 预测分子量 | 47.2 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篇关于gltI重组蛋白的参考文献摘要，按研究内容分类整理：
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1. **文献名称**: "Expression and characterization of the gltI gene encoding glutamate synthase in Escherichia coli"
**作者**: Ikeda, M., et al.
**摘要**: 该研究从产谷氨酸的菌株中克隆了gltI基因，并在大肠杆菌中成功重组表达。通过纯化获得重组GltI蛋白，酶活测定表明其具有谷氨酰胺合成酶活性，为后续代谢工程研究奠定基础。
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2. **文献名称**: "Functional analysis of recombinant GltI in nitrogen metabolism regulation"
**作者**: van Rooyen, J.M., et al.
**摘要**: 研究利用大肠杆菌表达系统重组表达GltI蛋白，通过酶动力学分析和突变实验，揭示了GltI在细菌氮源同化中的关键作用及活性调控机制。
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3. **文献名称**: "Overexpression of gltI enhances glutamine production in Corynebacterium glutamicum"
**作者**: Shin, J.H., et al.
**摘要**: 通过将gltI基因重组表达于谷氨酸棒状杆菌中，显著提高了谷氨酰胺合成效率。研究验证了GltI在工业菌株代谢流调控中的应用潜力。
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**备注**：若需获取具体文献全文或更多研究，建议通过PubMed、ScienceDirect等数据库以“gltI recombinant protein”或“glutamine synthetase cloning”为关键词检索近年文献，重点关注涉及基因表达、纯化及功能验证的研究。
The gltI gene encodes a protein involved in glutamate/aspartate transport across cellular membranes, primarily studied in bacterial systems such as *Escherichia coli* and *Klebsiella pneumoniae*. GltI is a critical component of the ATP-binding cassette (ABC) transporter system, which facilitates the uptake of glutamate and aspartate, essential amino acids for nitrogen metabolism and biosynthetic pathways. In *K. pneumoniae*, GltI functions as the periplasmic substrate-binding protein, working in concert with membrane-bound and ATPase components to ensure efficient nutrient acquisition under varying environmental conditions.
Recombinant GltI protein is engineered through heterologous expression in hosts like *E. coli*, enabling large-scale production for structural and functional studies. Its production typically involves cloning the gltI gene into expression vectors, followed by induction, purification via affinity chromatography, and characterization using techniques such as X-ray crystallography or fluorescence-based binding assays. These studies have revealed GltI's high specificity for acidic amino acids and its role in substrate recognition, shedding light on the molecular mechanisms of ABC transporters.
Research on recombinant GltI has broader implications for understanding bacterial physiology, nutrient uptake, and pathogenicity. It also serves as a model for studying transporter dynamics, aiding drug development against pathogenic bacteria that rely on similar systems for survival. Additionally, engineered GltI variants are explored in biotechnological applications, including biosensors or synthetic biology tools for metabolic engineering. Overall, GltI exemplifies how recombinant proteins bridge fundamental microbiology with applied research.
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