纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | PGLS |
Uniprot No | O95336 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-258aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL DEAAARLLTV PFEKHSTL |
预测分子量 | 30 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PGLS(磷酸葡萄糖酸内酯酶)重组蛋白研究的示例参考文献(注:文献为虚构示例,仅供格式参考):
1. **标题**:*Heterologous expression and characterization of 6-phosphogluconolactonase from Escherichia coli*
**作者**:Smith J. et al.
**摘要**:研究利用大肠杆菌表达系统成功表达并纯化重组PGLS酶,分析了其最适pH、温度及金属离子对酶活性的影响,为后续代谢工程应用提供基础数据。
2. **标题**:*Crystal structure of recombinant PGLS from Saccharomyces cerevisiae*
**作者**:Lee H. & Zhang W.
**摘要**:首次报道了酿酒酵母来源的PGLS重组蛋白的晶体结构,揭示了其催化活性中心的构象特征,并探讨了底物结合机制。
3. **标题**:*Functional analysis of PGLS in the oxidative phase of the pentose phosphate pathway*
**作者**:Garcia R. et al.
**摘要**:通过重组PGLS蛋白的体外酶活实验,验证了其在磷酸戊糖途径中防止6-磷酸葡萄糖酸内酯自发水解的关键作用,并量化了其对代谢通量的调控效应。
4. **标题**:*Optimization of PGLS recombinant protein production in Pichia pastoris*
**作者**:Chen L. et al.
**摘要**:比较了毕赤酵母系统中不同表达条件对PGLS重组蛋白产量及活性的影响,开发出高效可规模化的纯化工艺。
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建议通过 **PubMed**(https://pubmed.ncbi.nlm.nih.gov)或 **Google Scholar** 检索真实文献,关键词可尝试:
`"6-phosphogluconolactonase" recombinant expression` 或 `PGLS heterologous production`。
**Background of PGLS Recombinant Proteins**
Phosphogluconolactonase (PGLS) is a critical enzyme involved in the oxidative phase of the pentose phosphate pathway (PPP), a fundamental metabolic route that generates NADPH and pentoses for nucleotide synthesis. PGLS catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate, a step essential for maintaining metabolic flux and redox balance in cells. NADPH produced via this pathway supports antioxidant defense, lipid biosynthesis, and detoxification processes, highlighting PGLS's role in cellular homeostasis.
Recombinant PGLS proteins are engineered using biotechnological platforms (e.g., *E. coli*, yeast, or mammalian expression systems*) to produce purified, functional enzymes for research and industrial applications. The recombinant form enables precise study of PGLS's structure, kinetics, and regulatory mechanisms, bypassing challenges associated with isolating the enzyme from native tissues.
Research on PGLS recombinant proteins has gained traction due to their potential implications in diseases linked to metabolic dysregulation, such as cancer, diabetes, and neurodegenerative disorders. For instance, cancer cells often upregulate the PPP to meet heightened demands for NADPH and biosynthesis, making PGLS a potential therapeutic target. Additionally, genetic variants or dysfunctions in PGLS may contribute to rare metabolic disorders, driving interest in recombinant forms for diagnostic or therapeutic development.
In biotechnology, recombinant PGLS is explored for optimizing NADPH-dependent biosynthesis in microbial cell factories, enhancing yields of biofuels, pharmaceuticals, or specialty chemicals. Its stability and activity under varying conditions are also studied for industrial enzyme engineering.
Overall, PGLS recombinant proteins serve as vital tools for unraveling metabolic networks, disease mechanisms, and bioproduction strategies, bridging fundamental biochemistry with translational applications.
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