| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP |
| Uniprot No | P53396 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1101aa |
| 氨基酸序列 | MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWL LSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATG FLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQ KLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYL EINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEE AYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNV AATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGI PIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAP SRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAI VWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILI PVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASK LYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDH VLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCAT MFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSV YEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQ ELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAF DSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPA TPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADE YIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMS M |
| 预测分子量 | 147 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3-4条关于ATP重组蛋白的参考文献示例(虚拟文献，仅供格式参考)：
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1. **文献名称**: "Structural insights into ATP-dependent protein assembly by AAA+ proteases"
**作者**: Smith J. et al.
**摘要**: 研究利用冷冻电镜解析ATP依赖性重组蛋白复合物AAA+蛋白酶的结构，阐明其通过ATP水解驱动底物蛋白折叠与组装的分子机制。
2. **文献名称**: "Engineered ATP-binding proteins for biosensing applications"
**作者**: Lee S. & Zhang F.
**摘要**: 开发了一种基于ATP结合结构域的重组荧光蛋白探针，可通过ATP浓度变化实时监测细胞内能量代谢状态。
3. **文献名称**: "ATP-driven chaperone function in recombinant protein production"
**作者**: Wang Y. et al.
**摘要**: 探讨ATP依赖性分子伴侣(如Hsp70)在大肠杆菌重组蛋白表达系统中的作用，证明其通过ATP循环提高难溶性蛋白的折叠效率。
4. **文献名称**: "CRISPR-Cas9-mediated ATP synthase engineering for enhanced metabolic flux"
**作者**: Tanaka K. et al.
**摘要**: 利用CRISPR技术对ATP合酶亚基进行重组改造，优化微生物细胞工厂中ATP供应，显著提升目标代谢产物的合成速率。
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*注：以上文献为示例，实际引用需查询真实数据库(如PubMed、Nature、Science)。如需真实文献，可补充具体研究方向进一步筛选。*
**Background of ATP Recombinant Proteins**
Adenosine triphosphate (ATP), the primary energy currency of cells, plays a central role in metabolism, signaling, and cellular processes. Recombinant ATP-related proteins, engineered through genetic modification, are pivotal tools in biochemistry and biotechnology. These proteins include ATPases, kinases, ATP-binding transporters, and synthases, which are produced in heterologous systems like *E. coli*, yeast, or mammalian cells to study their structure-function relationships or therapeutic potential.
The development of ATP recombinant proteins stems from advances in molecular cloning and protein engineering. By isolating genes encoding ATP-interacting proteins and expressing them in controlled systems, researchers obtain purified, functional proteins for mechanistic studies. For instance, ATP-dependent enzymes (e.g., ATP synthase) are reconstituted to dissect energy transduction mechanisms, while ATP-binding cassette (ABC) transporters are studied for drug resistance or substrate specificity. Structural insights from X-ray crystallography or cryo-EM often rely on recombinant proteins to resolve ATP-driven conformational changes.
Applications span biomedicine and industry. Recombinant ATPases are used in bioenergy research to optimize ATP synthesis or hydrolysis. Kinases, critical in signaling pathways, are drug targets, and their recombinant forms aid in high-throughput inhibitor screening. In synthetic biology, ATP-dependent biosensors or engineered ATP-consuming systems enable real-time monitoring of metabolic fluxes.
Challenges include maintaining protein stability, proper folding, and post-translational modifications (e.g., phosphorylation), which often necessitate tailored expression systems. Innovations like fusion tags (e.g., His-tags) and chaperone co-expression enhance yields and functionality.
Overall, ATP recombinant proteins bridge fundamental research and applied sciences, offering insights into cellular energetics and enabling innovations in therapeutics, bioenergy, and biocatalysis. Their continued optimization aligns with growing demands for sustainable biotechnologies and precision medicine.
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