| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ppc |
| Uniprot No | P00864 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 5-883aa |
| 氨基酸序列 | YSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANRQELLTTLQNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEVIARTLRKLKNQPELSEDTIKKAVESLSLELVLTAHPTEITRRTLIHKMVEVNACLKQLDNKDIADYEHNQLMRRLRQLIAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEFVPVRFTSWMGGDRDGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELLALVGEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELWEPLYACYQSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHTEALGELTRYLGIGDYESWSEADKQAFLIRELNSKRPLLPRNWQPSAETREVLDTCQVIAEAPQGSIAAYVISMAKTPSDVLAVHLLLKEAGIGFAMPVAPLFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIGYSDSAKDAGVMAASWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQPPGSLKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESWRRIMDELSVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAKRRPTGGVESLRAIPWIFAWTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFFSTRLGMLEMVFAKADLWLAEYYDQRLVDKALWPLGKELRNLQEEDIKVVLAIANDSHLMADLPWIAESIQLRNIYTDPLNVLQAELLHRSRQAEKEGQEPDPRVEQALMVTIAGIAAGMRNTG |
| 预测分子量 | 102.6 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. |
以下是假设性参考文献示例，基于可能的PPC重组蛋白研究方向(注：实际文献需通过学术数据库验证)：
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1. **"Expression and kinetic analysis of recombinant phosphoenolpyruvate carboxylase (PPC) in Escherichia coli"**
*Author: Smith A, et al.*
**摘要**: 研究高粱来源的PPC酶在大肠杆菌中的重组表达，优化诱导条件提高可溶性蛋白产量，并分析其羧化酶活性及动力学参数。
2. **"Prokaryotic expression and purification of polyphosphate kinase (PPK) as a recombinant PPC fusion protein for industrial applications"**
*Author: Zhang L, et al.*
**摘要**: 开发聚磷酸盐激酶(PPK)的重组融合蛋白表达系统，利用His标签纯化技术，验证其在体外合成聚磷酸盐的生物催化潜力。
3. **"Recombinant PPC as a vaccine candidate: Production and immunogenicity against bacterial pathogens"**
*Author: Lee J, et al.*
**摘要**: 评估重组表达的PPC蛋白作为疫苗的可行性，通过动物实验证明其可诱导特异性抗体反应，增强对病原菌的免疫保护。
4. **"Structural and functional insights into recombinant PPC enzyme via cryo-EM analysis"**
*Author: Chen X, et al.*
**摘要**: 利用冷冻电镜技术解析重组PPC的三维结构，结合突变实验揭示其活性位点及底物结合机制。
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**建议**：若PPC指特定蛋白(如磷酸烯醇丙酮酸羧化酶、聚磷酸盐相关酶等)，建议在PubMed或Web of Science中检索全称或相关关键词(如“recombinant phosphoenolpyruvate carboxylase”)以获取准确文献。
**Background of PPC Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine since their emergence in the 1970s. These proteins are produced by inserting target DNA into host organisms (e.g., *E. coli*, yeast, mammalian cells), enabling large-scale synthesis of therapeutic, diagnostic, or industrial proteins. However, traditional production systems face challenges, including low yields, improper folding, or lack of post-translational modifications critical for functionality, particularly in eukaryotic proteins.
PPC (Plant-Produced Cell) recombinant proteins represent an innovative approach leveraging plant-based expression systems. Plants offer unique advantages: they are cost-effective, scalable, and capable of complex protein modifications (e.g., glycosylation) while minimizing risks of mammalian pathogen contamination. Pioneered in the 1980s, plant-based platforms gained momentum with advancements in transient expression technologies (e.g., *Agrobacterium*-mediated delivery) and viral vectors, enabling rapid protein production.
The development of PPC recombinant proteins accelerated with the success of plant-derived vaccines and antibodies. For instance, ZMapp, a plant-made monoclonal antibody for Ebola, demonstrated the feasibility of this platform during the 2014 outbreak. Additionally, plant systems have been utilized to produce enzymes, growth factors, and even SARS-CoV-2 antigens, highlighting their versatility.
Challenges remain, such as optimizing expression levels, standardizing regulatory frameworks, and addressing public skepticism about genetically modified crops. However, ongoing research in plant synthetic biology, CRISPR-based genome editing, and glycoengineering continues to enhance the precision and efficiency of PPC systems. As demand for sustainable biomanufacturing grows, plant-produced recombinant proteins are poised to play a pivotal role in global health and industrial biotechnology.
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