| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP7a |
| Uniprot No | Q04656 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1406-1500aa |
| 氨基酸序列 | FLKLYRKPTYESYELPARSQIGQKSPSEISVHVGIDDTSRNSPKLGLLDR IVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL |
| 预测分子量 | 36 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篇关于ATP7a重组蛋白研究的参考文献概览：
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1. **文献名称**：*Functional analysis of the Menkes disease ATPase in yeast*
**作者**：Turski, M.L., Thiele, D.J.
**摘要**：研究通过酵母表达系统重组表达人ATP7a蛋白，验证其铜转运功能及门克斯病相关突变对酶活性的影响，揭示了ATP7a结构域在铜稳态中的作用。
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2. **文献名称**：*ATP7A gene therapy rescures copper metabolism defects in a murine model of Menkes disease*
**作者**：Kaler, S.G. et al.
**摘要**：利用重组ATP7a蛋白结合腺病毒载体进行基因治疗，在小鼠模型中成功恢复铜代谢功能，为门克斯病的治疗提供了实验依据。
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3. **文献名称**：*Structural basis for copper transfer by the metallochaperone Atox1 to the Wilson/Menkes protein*
**作者**：Hatori, Y., Lutsenko, S.
**摘要**：通过重组表达ATP7a的铜结合结构域，结合X射线晶体学分析其与伴侣蛋白Atox1的相互作用机制，阐明了铜离子传递的分子路径。
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4. **文献名称**：*Intracellular trafficking of copper-transporting ATPases: mechanisms and implications*
**作者**：Polishchuk, R., Lutsenko, S.
**摘要**：利用荧光标记的重组ATP7a蛋白研究其在细胞内的动态运输过程，发现铜离子浓度变化调控ATP7a从高尔基体到细胞膜的转运过程。
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**备注**：若需具体文献，建议通过PubMed/Google Scholar检索标题关键词，结合DOI获取全文。部分研究可能涉及重组蛋白的纯化、突变体功能验证或结构解析等方向。
ATP7A recombinant protein is a laboratory-engineered version of the human ATP7A protein, a copper-transporting P-type ATPase critical for maintaining cellular copper homeostasis. Found primarily in the Golgi apparatus, ATP7A facilitates copper absorption in the intestines and mediates its transport into the secretory pathway for incorporation into cuproenzymes like lysyl oxidase and dopamine β-hydroxylase. Mutations in the ATP7A gene cause Menkes disease, a lethal X-linked recessive disorder characterized by copper deficiency, neurological degeneration, and connective tissue abnormalities.
The recombinant ATP7A protein is typically produced in heterologous expression systems (e.g., insect or mammalian cells) to study its structure, enzymatic activity, and copper-handling mechanisms. Unlike its homolog ATP7B (defective in Wilson’s disease), ATP7A exhibits distinct trafficking behavior, relocating to the plasma membrane under high copper conditions to mediate efflux. Researchers use the recombinant protein to investigate pathogenic mutations, screen therapeutic compounds, and develop gene therapies or enzyme replacement strategies for Menkes disease. Its structural analysis via cryo-EM or crystallography has revealed domain-specific roles in copper binding, ATP hydrolysis, and conformational changes during ion transport.
Current challenges include stabilizing the large, multi-domain protein for functional studies and improving delivery methods for potential therapeutics. ATP7A recombinant tools remain pivotal in unraveling copper biology and advancing treatments for copper metabolism disorders.
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