| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | G6PD |
| Uniprot No | P11413 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-515aa |
| 氨基酸序列 | AEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL |
| 预测分子量 | 60.1 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3篇关于G6PD重组蛋白研究的示例文献(内容基于真实研究主题概括，具体文献需根据实际检索结果调整)：
---
1. **文献名称**: *Expression and characterization of recombinant human glucose-6-phosphate dehydrogenase in E. coli*
**作者**: Zhang Y, et al.
**摘要**: 研究报道了利用大肠杆菌表达系统高效表达人源G6PD重组蛋白，通过优化诱导条件和纯化步骤获得高活性酶，并验证其在体外催化葡萄糖-6-磷酸生成NADPH的功能。
2. **文献名称**: *Structural insights into the functional dynamics of G6PD through recombinant protein crystallography*
**作者**: Chen L, et al.
**摘要**: 通过重组G6PD蛋白的晶体结构解析，揭示了其底物结合域和NADP+结合位点的构象变化，为理解G6PD缺乏症相关突变对酶活性的影响提供结构基础。
3. **文献名称**: *Functional analysis of G6PD variants using recombinant enzyme systems*
**作者**: Gómez-Manzo S, et al.
**摘要**: 构建了多种G6PD突变体重组蛋白，比较其酶动力学参数和热稳定性，发现某些临床突变导致酶活性显著下降，为遗传性G6PD缺乏症的分子机制提供实验依据。
---
如需具体文献，建议通过PubMed或Web of Science检索关键词：**"G6PD recombinant protein"** 或 **"glucose-6-phosphate dehydrogenase expression"**，并筛选近年高影响力论文。
Glucose-6-phosphate dehydrogenase (G6PD) recombinant protein is a biologically engineered form of the human G6PD enzyme, produced using recombinant DNA technology. G6PD is a critical metabolic enzyme encoded by the G6PD gene located on the X chromosome. It catalyzes the first step in the pentose phosphate pathway, converting glucose-6-phosphate to 6-phosphogluconolactone while generating NADPH, a key reducing agent essential for maintaining cellular redox balance and protecting against oxidative stress. G6PD deficiency, an X-linked hereditary condition affecting over 400 million people globally, underscores the enzyme's biological significance and drives research interest.
Recombinant G6PD production typically involves cloning the human G6PD gene into expression vectors, followed by protein synthesis in heterologous systems like E. coli, yeast, or mammalian cell cultures. This approach enables large-scale production of high-purity, soluble enzyme variants for research and therapeutic applications. The recombinant protein retains catalytic activity comparable to native G6PD while offering advantages such as batch consistency and reduced contamination risks.
Pharmaceutical research utilizes recombinant G6PD to study drug-induced hemolysis mechanisms, particularly for antimalarials like primaquine. It serves as a critical reagent in diagnostic kits for G6PD deficiency screening and in biochemical assays measuring NADPH production. Structural studies using recombinant variants have advanced understanding of enzyme kinetics, substrate binding, and mutation impacts (e.g., Class I-III deficiency variants). Recent developments include thermostable engineered versions and fusion proteins for enhanced analytical applications.
Ongoing research focuses on optimizing expression systems, improving protein stability, and characterizing rare mutations. Recombinant G6PD also shows potential in industrial biocatalysis and as a therapeutic protein for enzyme replacement strategies. Its production and characterization remain vital for advancing hematology research, personalized medicine approaches for G6PD-deficient populations, and drug safety assessments.
×
