纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PGA4 |
Uniprot No | P0DJD7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 63-388aa |
氨基酸序列 | VDEQPLEN YLDMEYFGTI GIGTPAQDFT VVFDTGSSNL WVPSVYCSSL ACTNHNRFNP EDSSTYQSTS ETVSITYGTG SMTGILGYDT VQVGGISDTN QIFGLSETEP GSFLYYAPFD GILGLAYPSI SSSGATPVFD NIWNQGLVSQ DLFSVYLSAD DQSGSVVIFG GIDSSYYTGS LNWVPVTVEG YWQITVDSIT MNGEAIACAE GCQAIVDTGT SLLTGPTSPI ANIQSDIGAS ENSDGDMVVS CSAISSLPDI VFTINGVQYP VPPSAYILQS EGSCISGFQG MNLPTESGEL WILGDVFIRQ YFTVFDRANN QVGLAPVA |
预测分子量 | 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PGA4重组蛋白的3篇参考文献示例(注:以下内容为假设性示例,实际文献需根据具体研究领域核实):
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1. **文献名称**:*Heterologous Expression and Characterization of Recombinant PGA4 from Bacillus subtilis in E. coli*
**作者**:Zhang, Y. et al.
**摘要**:本研究在大肠杆菌中成功表达了枯草芽孢杆菌来源的PGA4基因,优化了诱导条件并纯化了重组蛋白。该蛋白展现出高效的聚γ-谷氨酸合成活性,为生物可降解材料开发提供了基础。
2. **文献名称**:*Structural Insights into PGA4: Crystallographic Analysis of a Novel Poly-γ-glutamic Acid Synthase*
**作者**:Chen, L. et al.
**摘要**:通过X射线晶体学解析了PGA4蛋白的三维结构,揭示了其催化位点及底物结合机制,为理性设计高活性酶变体提供了结构依据。
3. **文献名称**:*Application of Recombinant PGA4 in Drug Delivery: Enhancing Nanoparticle Stability*
**作者**:Wang, Q. et al.
**摘要**:评估了重组PGA4作为药物纳米载体的潜力,证明其能显著提高载药系统的稳定性和缓释性能,具有潜在的生物医学应用价值。
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**备注**:若需真实文献,建议通过学术数据库(如PubMed、Web of Science)以关键词“PGA4 recombinant protein”或“poly-γ-glutamic acid synthase 4”进一步检索,并核实具体研究背景(如微生物合成、结构或应用方向)。
**Background of PGA4 Recombinant Protein**
Penicillin G acylase (PGA) is a critical enzyme in the pharmaceutical industry, primarily known for its role in the production of β-lactam antibiotics. PGA4. a recombinant variant of this enzyme, is engineered to enhance catalytic efficiency, stability, and production yield compared to wild-type PGAs. Naturally produced by certain bacteria (e.g., *E. coli*), PGA catalyzes the hydrolysis of penicillin G to 6-aminopenicillanic acid (6-APA), a key intermediate for semisynthetic penicillins and cephalosporins. However, native PGAs often exhibit limitations such as low expression levels, substrate specificity constraints, or instability under industrial conditions.
Recombinant PGA4 addresses these challenges through genetic optimization. The *pga* gene is cloned into high-expression microbial systems (e.g., *E. coli* or *Bacillus* strains), enabling scalable production. Structural modifications, such as rational mutagenesis or directed evolution, improve its thermostability, pH tolerance, and activity toward diverse substrates. PGA4’s bifunctional active site, comprising distinct α and β subunits processed from a single precursor, is often engineered to reduce autocatalytic degradation and enhance operational lifespan.
Industrial applications of PGA4 extend beyond antibiotic synthesis. It is utilized in enzymatic cascades for chiral compound resolution, green chemistry processes, and the synthesis of non-β-lactam drugs. Its recombinant form also supports sustainable manufacturing by reducing reliance on harsh chemical methods. Ongoing research focuses on tailoring PGA4 for biocatalytic versatility, including immobilized enzyme systems for continuous production. As antibiotic resistance grows, PGA4’s role in developing next-generation therapeutics underscores its biotechnological significance.
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