| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ppk2 |
| Uniprot No | O68984 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 140-343aa |
| 氨基酸序列 | EQQQLLQHYFRKEVFPVLTPLAFDTGHPFPFMSNLSLNLAIELEDEESGAIKFARVKVPGILSRIIRLDQIEGLGFDDGRIRLLWLEDLVEHNLDQLFPKMRILQCHPFRIIRDADIEIEEDEAGDLLESIEQGVRSRRYGKVVRLDINPDMPHSIRSLLVKNLETYERNVYEIGGVLGMSALMELLKIDRPDLKDELFVPNNP |
| 预测分子量 | 34.4 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篇与PPK2重组蛋白相关的模拟参考文献示例(仅供参考，建议通过学术数据库核实具体文献)：
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1. **文献名称**: "Cloning, Expression, and Characterization of Recombinant Polyphosphate Kinase 2 from *Escherichia coli*"
**作者**: Smith A, et al.
**摘要**: 该研究报道了通过克隆*E. coli*的*ppk2*基因，在大肠杆菌表达系统中成功表达并纯化重组PPK2蛋白。酶活性分析表明，该重组蛋白具有催化ADP依赖的多聚磷酸盐合成能力，为后续代谢工程研究提供了工具。
2. **文献名称**: "Structural Insights into the Catalytic Mechanism of PPK2 through Recombinant Protein Crystallography"
**作者**: Zhang L, et al.
**摘要**: 作者利用重组表达的人源PPK2蛋白进行结晶和结构解析，揭示了其底物结合口袋的三维构象及ATP/ADP结合的关键残基，阐明了PPK2在调控细胞内多聚磷酸盐动态平衡中的分子机制。
3. **文献名称**: "Application of Recombinant PPK2 in Biotechnological Phosphate Recycling Systems"
**作者**: Tanaka K, et al.
**摘要**: 研究开发了一种基于重组PPK2酶的体外磷酸盐回收系统，证明该酶可将ADP转化为ATP并耦合多聚磷酸盐合成，为降低生物制造过程中的高能磷酸化合物成本提供了新策略。
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**注意**：以上文献为示例，实际研究中请通过PubMed、Web of Science等平台检索关键词(如“PPK2 recombinant”“polyphosphate kinase heterologous expression”)获取真实文献。
**Background of PPK2 Recombinant Protein**
The **polyphosphate kinase 2 (PPK2)** family comprises enzymes critical for polyphosphate (polyP) metabolism, primarily found in bacteria and archaea. Unlike PPK1. which synthesizes polyP from ATP, PPK2 enzymes predominantly catalyze the reverse reaction, generating ATP from polyP and ADP. This ATP-replenishing function is vital for bacterial survival under stress conditions, such as nutrient limitation or oxidative stress, making PPK2 a potential target for antimicrobial strategies.
PPK2 recombinant proteins are engineered via heterologous expression systems (e.g., *E. coli*) to study their structural and functional properties. Recombinant production enables large-scale purification and characterization, facilitating insights into enzymatic mechanisms, substrate specificity, and interactions with polyP. Structural studies using X-ray crystallography or cryo-EM have revealed conserved domains responsible for binding polyP and nucleotides, aiding in the design of inhibitors.
Biotechnologically, PPK2 recombinant proteins hold promise for ATP regeneration in cell-free systems, enhancing yields in enzymatic synthesis or biosensing applications. Their ability to recycle polyP—a low-cost phosphate polymer—into ATP also aligns with sustainable industrial processes. Additionally, PPK2’s role in bacterial virulence and stress adaptation has spurred interest in developing PPK2 inhibitors as novel antibiotics, particularly against multidrug-resistant pathogens.
Despite progress, challenges remain in optimizing PPK2 stability and activity *in vitro* and understanding species-specific functional variations. Ongoing research focuses on enzyme engineering for improved catalytic efficiency and exploring PPK2’s interplay with other metabolic pathways. Overall, PPK2 recombinant proteins serve as versatile tools for both fundamental microbiology and applied biotechnology.
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