| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | atpD |
| Uniprot No | P30049 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-168aa |
| 氨基酸序列 | AEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANEALVKALE |
| 预测分子量 | 31.0kDa |
| 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. |
以下是关于atpD重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*Cloning, expression, and characterization of the Brucella abortus ATP synthase β subunit (atpD) for use as a vaccine antigen*
**作者**：Luo D, et al.
**摘要**：该研究克隆并表达了布鲁氏菌的atpD基因，重组蛋白在大肠杆菌中高效表达并纯化。实验表明，atpD蛋白可诱导小鼠产生强烈的Th1免疫反应，并作为潜在疫苗候选抗原对抗布鲁氏菌感染。
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2. **文献名称**：*Functional analysis of recombinant atpD from Mycobacterium tuberculosis: ATPase activity and role in oxidative stress response*
**作者**：Gupta S, et al.
**摘要**：作者通过原核表达系统获得结核分枝杆菌atpD重组蛋白，证实其具有ATP水解酶活性。进一步研究发现，atpD缺失突变体对氧化应激敏感，提示该蛋白在细菌抗氧化防御中的关键作用。
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3. **文献名称**：*Structural insights into the ATP synthase β subunit (atpD) of Helicobacter pylori through X-ray crystallography*
**作者**：Kim J, et al.
**摘要**：本研究解析了幽门螺杆菌atpD重组蛋白的晶体结构(分辨率2.1Å)，揭示了其与ATP结合的活性位点及构象变化机制，为开发针对该病原体的ATP合酶抑制剂提供了结构基础。
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*注：以上文献信息为示例，实际引用需根据具体研究查阅真实文献。建议通过PubMed或Web of Science以“atpD recombinant protein”为关键词检索最新论文。*
ATP-D, commonly referred to as the beta subunit of ATP synthase, is a critical component of the ATP synthase complex, an enzyme responsible for ATP synthesis across cellular membranes in mitochondria, chloroplasts, and bacteria. This subunit plays a central role in the catalytic mechanism of ATP synthesis or hydrolysis, depending on cellular energy demands. Structurally, ATP-D forms part of the F1 catalytic core, where it facilitates conformational changes necessary for converting ADP and inorganic phosphate into ATP via rotational catalysis. Its function is tightly coupled to proton translocation across membranes, linking electrochemical gradients to biochemical energy production.
Recombinant ATP-D protein is produced using genetic engineering techniques, typically expressed in bacterial systems like *E. coli* for large-scale purification. This approach allows researchers to study the subunit's structure-function relationships, enzymatic kinetics, and interactions with other synthase components or inhibitors. Recombinant ATP-D retains the biological activity of its native counterpart, making it invaluable for biochemical assays, structural studies (e.g., X-ray crystallography, cryo-EM), and drug discovery efforts targeting ATP synthase.
Interest in ATP-D extends to biomedical applications, as ATP synthase dysregulation is implicated in metabolic disorders, neurodegenerative diseases, and microbial pathogenesis. In pathogenic bacteria, ATP-D serves as a potential antimicrobial target due to its essential role in energy metabolism. Additionally, autoantibodies against ATP synthase subunits, including ATP-D, have been identified in certain autoimmune conditions, highlighting its relevance in diagnostic research. The development of recombinant ATP-D thus supports both basic science and therapeutic innovation, bridging mechanistic enzymology with translational medicine.
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