| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLS |
| Uniprot No | O94925 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 616-669aa |
| 氨基酸序列 | KDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL |
| 预测分子量 | 54.1 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GLS(谷氨酰胺酶)重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*"Expression and purification of recombinant human glutaminase (GLS) in E. coli for structural studies"*
**作者**：Smith J. et al.
**摘要**：报道了人源GLS蛋白在大肠杆菌中的高效表达及纯化方法，利用X射线晶体学解析了其三维结构，为靶向GLS的抑制剂设计提供了结构基础。
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2. **文献名称**：*"Functional characterization of a novel GLS isoform in cancer cell metabolism"*
**作者**：Lee H. et al.
**摘要**：通过重组GLS-KGA和GAC亚型的体外酶活实验，揭示了GAC亚型在肿瘤细胞异常代谢中的关键作用，并验证了其作为癌症治疗靶点的潜力。
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3. **文献名称**：*"Development of a high-throughput assay for screening GLS inhibitors using recombinant enzyme"*
**作者**：Wang Y. et al.
**摘要**：建立了基于重组GLS蛋白的高通量药物筛选平台，成功筛选出多个小分子抑制剂，为抗肿瘤药物开发提供了新策略。
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注：以上为示例文献，实际引用需根据具体研究主题检索真实发表的论文(可通过PubMed/Google Scholar搜索关键词如“recombinant GLS protein”或“glutaminase expression”获取)。
**Background of GLS Recombinant Proteins**
Glutaminase (GLS) is a critical enzyme involved in cellular metabolism, catalyzing the hydrolysis of glutamine to glutamate and ammonia. This reaction is essential for maintaining the tricarboxylic acid (TCA) cycle, amino acid biosynthesis, and redox balance, particularly in rapidly proliferating cells like cancer cells. GLS exists in two isoforms: kidney-type (GLS1) and liver-type (GLS2), with GLS1 being widely studied for its role in supporting tumor growth and metabolic reprogramming.
Recombinant GLS proteins are produced using genetic engineering techniques, where the GLS gene is cloned into expression vectors (e.g., bacterial, insect, or mammalian systems) to enable large-scale protein synthesis. These recombinant proteins retain enzymatic activity and structural integrity, allowing researchers to study their biochemical properties, substrate interactions, and regulatory mechanisms in vitro.
The development of GLS recombinant proteins has significant implications in both basic research and therapeutic development. In cancer biology, GLS1 is a promising therapeutic target, as many tumors exhibit "glutamine addiction," relying on glutaminolysis for energy and biomass production. Inhibitors targeting GLS1. such as CB-839. are under clinical investigation, highlighting the need for reliable recombinant proteins for drug screening and mechanistic studies. Additionally, GLS recombinant proteins are used to explore metabolic disorders, neurodegenerative diseases, and immune regulation, where glutamine metabolism plays a key role.
Overall, GLS recombinant proteins serve as vital tools for unraveling the enzyme's role in health and disease, bridging the gap between molecular insights and translational applications. Their production and characterization continue to advance precision medicine and biomarker discovery in glutamine-dependent pathologies.
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