| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ppk |
| Uniprot No | P0A7B1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-688aa |
| 氨基酸序列 | GQEKLYIEKELSWLSFNERVLQEAADKSNPLIERMRFLGIYSNNLDEFYKVRFAELKRRIIISEEQGSNSHSRHLLGKIQSRVLKADQEFDGLYNELLLEMARNQIFLINERQLSVNQQNWLRHYFKQYLRQHITPILINPDTDLVQFLKDDYTYLAVEIIRGDTIRYALLEIPSDKVPRFVNLPPEAPRRRKPMILLDNILRYCLDDIFKGFFDYDALNAYSMKMTRDAEYDLVHEMEASLMELMSSSLKQRLTAEPVRFVYQRDMPNALVEVLREKLTISRYDSIVPGGRYHNFKDFINFPNVGKANLVNKPLPRLRHIWFDKAQFRNGFDAIRERDVLLYYPYHTFEHVLELLRQASFDPSVLAIKINIYRVAKDSRIIDSMIHAAHNGKKVTVVVELQARFDEEANIHWAKRLTEAGVHVIFSAPGLKIHAKLFLISRKENGEVVRYAHIGTGNFNEKTARLYTDYSLLTADARITNEVRRVFNFIENPYRPVTFDYLMVSPQNSRRLLYEMVDREIANAQQGLPSGITLKLNNLVDKGLVDRLYAASSSGVPVNLLVRGMCSLIPNLEGISDNIRAISIVDRYLEHDRVYIFENGGDKKVYLSSADWMTRNIDYRIEVATPLLDPRLKQRVLDIIDILFSDTVKARYIDKELSNRYVPRGNRRKVRAQLAIYDYIKSLEQPE |
| 预测分子量 | 87.7 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PPK(聚磷酸激酶)重组蛋白的参考文献示例(内容为模拟生成，非真实文献)：
1. **文献名称**：*Heterologous Expression and Characterization of Recombinant Polyphosphate Kinase from Escherichia coli*
**作者**：Zhang, L. et al.
**摘要**：本研究报道了在大肠杆菌中异源表达重组PPK的优化策略，通过质粒构建和诱导条件优化，成功获得高纯度PPK蛋白，并验证其催化合成多聚磷酸盐的活性，为工业酶应用提供基础。
2. **文献名称**：*Structural and Functional Analysis of Recombinant PPK for Bioremediation Applications*
**作者**：Smith, J.R. & Patel, K.
**摘要**：文章解析了重组PPK的晶体结构，并探讨其结合多聚磷酸盐的分子机制。实验表明，重组PPK在重金属吸附中表现出潜力，为环境污染修复提供新思路。
3. ****文献名称**：*Enzymatic Synthesis of Polyphosphate Using Recombinant PPK from Pseudomonas aeruginosa*
**作者**：Wang, Y. et al.
**摘要**：研究从铜绿假单胞菌中克隆ppk基因，并在枯草芽孢杆菌中实现分泌表达。重组PPK在体外合成纳米级多聚磷酸盐，展示其在生物材料制备中的应用价值。
4. **文献名称**：*Enhancement of ATP Regeneration by Co-expression of Recombinant PPK in Metabolic Engineering*
**作者**：Kim, S. et al.
**摘要**：通过共表达重组PPK与目标代谢途径酶，显著提高了细胞内的ATP再生效率，为高能耗生物合成反应(如抗生素生产)提供了能量优化策略。
注：以上文献及作者名为示例性虚构内容，如需真实文献，建议通过PubMed、Web of Science等学术平台检索关键词"recombinant polyphosphate kinase"或"PPK heterologous expression"。
PPK (Polyphosphate Kinase) recombinant protein is a genetically engineered enzyme derived from various microbial sources, primarily bacteria like *Escherichia coli* or *Pseudomonas aeruginosa*. PPK catalyzes the reversible synthesis of inorganic polyphosphate (polyP), a linear polymer of orthophosphate residues linked by high-energy phosphoanhydride bonds. PolyP plays critical roles in microbial physiology, including energy storage, stress response, biofilm formation, and virulence regulation. The ability to produce recombinant PPK has enabled researchers to study these processes in detail and harness polyP for biotechnological applications.
Originally discovered in the 1960s, PPK gained renewed interest due to its involvement in bacterial persistence and antibiotic tolerance. Recombinant PPK is typically produced by cloning the *ppk* gene into expression vectors (e.g., pET systems) followed by overexpression in bacterial hosts. Advanced purification techniques like affinity chromatography yield high-purity, active enzyme preparations. This recombinant form retains catalytic efficiency while offering scalability for industrial use.
Applications of recombinant PPK span multiple fields. In biotechnology, it facilitates polyP synthesis for phosphate-rich fertilizers or heavy metal sequestration. In biomedicine, PPK inhibitors are explored as novel antimicrobial agents targeting bacterial stress adaptation mechanisms. Additionally, polyP generated by recombinant PPK shows promise in wound healing and bone regeneration due to its signaling properties. Recent studies also investigate PPK's role in eukaryotic systems, potentially linking polyP metabolism to aging and neurodegenerative diseases.
The development of thermostable or mutant PPK variants further expands its utility in industrial processes. Ongoing research focuses on optimizing expression systems and engineering PPK for tailored polyP chain lengths, highlighting its versatility as both a biological tool and a therapeutic target.
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