| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pvdA |
| Uniprot No | Q51548 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-443aa |
| 氨基酸序列 | MTQATATAVVHDLIGVGFGPSNIALAIALQERAQAQGALEVLFLDKQGDYRWHGNTLVSQSELQISFLKDLVSLRNPTSPYSFVNYLHKHDRLVDFINLGTFYPCRMEFNDYLRWVASHFQEQSRYGEEVLRIEPMLSAGQVEALRVISRNADGEELVRTTRALVVSPGGTPRIPQVFRALKGDGRVFHHSQYLEHMAKQPCSSGKPMKIAIIGGGQSAAEAFIDLNDSYPSVQADMILRASALKPADDSPFVNEVFAPKFTDLIYSREHAERERLLREYHNTNYSVVDTDLIERIYGVFYRQKVSGIPRHAFRCMTTVERATATAQGIELALRDAGSGELSVETYDAVILATGYERQLHRQLLEPLAEYLGDHEIGRDYRLQTDERCKVAIYAQGFSQASHGLSDTLLSVLPVRAEEISGSLYQHLKPGTAARALHEHALAS |
| 预测分子量 | 65.5 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条关于PvdA(假单胞菌铁载体合成相关蛋白)重组蛋白的虚构参考文献示例(实际文献需通过学术数据库查询)：
1. **文献名称**: "Heterologous Expression and Purification of Pseudomonas aeruginosa PvdA in Escherichia coli"
**作者**: Müller, J. et al.
**摘要**: 本研究成功将绿脓杆菌PvdA基因克隆至大肠杆菌表达系统，通过His标签亲和层析纯化获得高纯度重组蛋白，并验证其参与铁载体前体合成的酶活性，为后续结构研究奠定基础。
2. **文献名称**: "Structural Insights into PvdA Function in Pyoverdine Biosynthesis"
**作者**: Zhang, L. & Visca, P.
**摘要**: 通过X射线晶体学解析重组PvdA蛋白的三维结构，揭示其底物结合位点及催化机制，突变实验证实特定氨基酸残基对铁载体生物合成的关键作用。
3. **文献名称**: "Recombinant PvdA as a Novel Vaccine Candidate Against Pseudomonas Infections"
**作者**: Rossi, G. et al.
**摘要**: 评估重组PvdA蛋白在小鼠模型中的免疫保护效果，显示其能诱导特异性抗体产生并提高宿主对绿脓杆菌肺部感染的清除率，提示其疫苗开发潜力。
(注：以上为模拟示例，实际研究需参考PubMed/Web of Science等平台的真实文献)
The pvdA gene encodes a key enzyme involved in the biosynthesis of pyoverdine, a high-affinity iron-chelating siderophore produced by Pseudomonas species, notably Pseudomonas aeruginosa. Pyoverdine plays a critical role in bacterial iron acquisition under iron-limited conditions, a common challenge in host environments or during infections. The pvdA gene is part of the pyoverdine synthesis gene cluster and encodes a non-ribosomal peptide synthetase (NRPS) responsible for assembling the peptide backbone of pyoverdine. This molecule not only scavenges iron but also contributes to bacterial virulence, biofilm formation, and pathogenicity.
Recombinant PvdA protein is engineered for structural and functional studies to elucidate its role in pyoverdine production and iron metabolism. Researchers express pvdA in heterologous systems like Escherichia coli or yeast to overcome challenges in purifying the native protein from Pseudomonas, which often produces pyoverdine in low quantities or with regulatory complexity. Recombinant technology enables scalable production, facilitating biochemical assays, crystallography, and inhibitor screening for potential antimicrobial therapies targeting iron uptake pathways.
Interest in PvdA also stems from its potential applications in biotechnology and medicine. Inhibiting pyoverdine biosynthesis could disrupt bacterial iron homeostasis, offering a strategy to combat antibiotic-resistant Pseudomonas infections. Additionally, understanding PvdA's enzymatic mechanisms may inspire synthetic biology approaches for designing novel iron-scavenging molecules or optimizing industrial microbial strains for metal bioremediation. However, challenges persist in recombinant expression due to PvdA's large size, multi-domain structure, and post-translational modification requirements. Recent advances in codon optimization, fusion tags, and chaperone co-expression have improved yields, aiding both basic research and translational applications.
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