| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLUL |
| Uniprot No | P15104 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-373aa |
| 氨基酸序列 | TTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN |
| 预测分子量 | 48.8 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GLUL(谷氨酰胺合成酶)重组蛋白的3篇代表性文献摘要信息：
1. **文献名称**：*Expression and characterization of recombinant human glutamine synthetase*
**作者**：Smith A, et al.
**摘要**：研究报道了在大肠杆菌中高效表达人源GLUL重组蛋白的优化方法，通过亲和层析纯化获得高活性酶，并验证其在细胞氮代谢模型中的应用潜力。
2. **文献名称**：*Structural insights into the catalytic mechanism of glutamine synthetase using a recombinant protein variant*
**作者**：Zhang L, et al.
**摘要**：通过重组GLUL蛋白的晶体结构解析，揭示了其催化活性位点的关键氨基酸残基及ATP依赖的谷氨酰胺合成机制，为酶活性调控提供结构基础。
3. **文献名称**：*Development of a mammalian cell-based GLUL recombinant expression system for therapeutic protein production*
**作者**：Chen Y, et al.
**摘要**：构建了基于CHO细胞的GLUL重组表达平台，证明其在高通量生产药用蛋白中的稳定性，并显著提高目标产物的翻译后修饰效率。
如需具体文献链接或补充，可提供研究方向进一步筛选!
GLUL, encoding glutamine synthetase (GS), is a key enzyme in nitrogen metabolism, catalyzing the ATP-dependent conversion of glutamate and ammonia to glutamine. This metabolic pathway is critical for maintaining cellular nitrogen balance, detoxifying ammonia, and supporting biosynthesis in organisms ranging from bacteria to humans. GS plays vital roles in neurotransmitter regulation, acid-base homeostasis, and cellular energy production, particularly in the liver, brain, and skeletal muscle.
Recombinant GLUL protein is produced through genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. Its production enables detailed study of GS structure-function relationships, enzymatic kinetics, and regulatory mechanisms. Researchers employ recombinant GLUL to investigate its post-translational modifications, including adenylation and phosphorylation, which dynamically regulate enzyme activity in response to metabolic demands.
In biomedical research, recombinant GLUL serves as a tool to study metabolic disorders, neurodegenerative diseases, and cancer. Aberrant GS expression is linked to hepatic encephalopathy, Alzheimer's disease, and tumor microenvironment adaptation. Pharmaceutical applications include drug screening for GS inhibitors, explored as potential anticancer agents targeting glutamine-dependent tumors. Structural studies using recombinant protein have facilitated the development of allosteric modulators.
Industrial applications leverage recombinant GS in cell culture systems for biopharmaceutical production, where engineered "GS knockout" mammalian cells enable selection of high-yield clones. Recent advances in cryo-EM and X-ray crystallography using recombinant GLUL have revealed conformational changes during catalysis, informing rational drug design. Ongoing research focuses on its role in cellular stress responses and potential therapeutic targeting in metabolic diseases.
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