| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGA5 |
| Uniprot No | P0DJD9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 63-388aa |
| 氨基酸序列 | VDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDKSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGETIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA |
| 预测分子量 | 41.6 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PGA5重组蛋白的模拟参考文献示例(注：以下内容为模拟生成，非真实文献，仅供格式参考)：
1. **文献名称**: *Cloning and enzymatic characterization of recombinant PGA5 from Aspergillus niger*
**作者**: Zhang, L., et al.
**摘要**: 本研究成功克隆了黑曲霉来源的PGA5基因，并在大肠杆菌中实现重组表达。纯化后的蛋白表现出聚半乳糖醛酸酶活性，最适pH为5.0.在食品工业果胶降解中具有应用潜力。
2. **文献名称**: *Structural insights into PGA5’s substrate binding mechanism*
**作者**: Wang, Y., et al.
**摘要**: 通过X射线晶体学解析了重组PGA5的三维结构，揭示了其催化活性位点及与果胶底物结合的关键氨基酸残基，为设计高效酶抑制剂提供了理论依据。
3. **文献名称**: *Heterologous expression of PGA5 in Pichia pastoris and its role in plant-pathogen interaction*
**作者**: Kim, H., et al.
**摘要**: 在毕赤酵母中高效表达重组PGA5.证实其在植物病原真菌侵染过程中通过降解细胞壁果胶层增强致病性，为抗病基因工程研究奠定基础。
4. **文献名称**: *Biotechnological application of recombinant PGA5 in biofuel production*
**作者**: Silva, R., et al.
**摘要**: 评估重组PGA5在木质纤维素预处理中的效率，证明其与纤维素酶协同作用可提升生物质糖化率，优化后酶活较天然提取物提高3倍。
建议通过 **PubMed** 或 **Web of Science** 检索真实文献，关键词可组合：*"recombinant PGA5" + "expression" / "enzymatic characterization" / "application"*。
**Background of PGA5 Recombinant Protein**
PGA5 (Poly-γ-glutamic acid synthase 5) is a key enzyme involved in the biosynthesis of poly-γ-glutamic acid (γ-PGA), a natural biopolymer composed of glutamic acid monomers linked by γ-amide bonds. γ-PGA is renowned for its biodegradability, water solubility, and non-toxic properties, making it valuable in biomedical, agricultural, and industrial applications. PGA5. as a critical component of the γ-PGA synthetase complex, catalyzes the polymerization of glutamate substrates into γ-PGA.
Recombinant PGA5 protein is produced through genetic engineering, typically by cloning the *pga5* gene into expression vectors (e.g., *E. coli* or *Bacillus* systems) to enable large-scale production. The recombinant form retains the enzymatic activity of native PGA5. allowing for controlled synthesis of γ-PGA with tailored molecular weights and properties. Structural studies reveal that PGA5 operates as part of a multi-enzyme complex, requiring ATP and metal ions (e.g., Mg²⁺) for optimal activity.
Research on PGA5 focuses on optimizing γ-PGA production for applications such as drug delivery (e.g., biocompatible carriers), environmental remediation (e.g., heavy metal absorbents), and agriculture (e.g., hydrogels for water retention). Additionally, its role in microbial biofilm formation and stress resistance has spurred interest in microbial physiology and industrial fermentation.
The development of recombinant PGA5 underscores advancements in synthetic biology and enzyme engineering, offering sustainable alternatives to synthetic polymers. Its versatility and eco-friendly profile position it as a promising candidate for addressing challenges in healthcare, agriculture, and environmental sustainability.
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