| 纯度 | >85% (SDS-PAGE) |
| 种属 | Human |
| 靶点 | ATOX1 |
| Uniprot No | O00244 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-68aa |
| 氨基酸序列 | MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK TVSYLGLE |
| 预测分子量 | 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. |
以下是关于ATOX1重组蛋白的3-4篇参考文献及其简要摘要：
1. **"Crystal structure of the copper chaperone ATOX1 bound to the fourth metal-binding domain of the Wilson disease protein"**
- **作者**: Wernimont, A.K., Huffman, D.L., Lamb, A.L., et al.
- **摘要**: 通过X射线晶体学解析了人源ATOX1与Wilson病蛋白(ATP7B)第四金属结合结构域的复合物结构，揭示了铜离子传递的分子机制，并阐明ATOX1特异性识别靶蛋白的结构基础。
2. **"Functional analysis of ATOX1 in copper homeostasis using recombinant protein and knockout models"**
- **作者**: Hamza, I., Schaefer, M., Klomp, L.W., et al.
- **摘要**: 在大肠杆菌中重组表达并纯化ATOX1.验证其铜结合能力，结合基因敲除细胞模型，证明ATOX1在维持细胞内铜稳态中的关键作用，尤其是在铜转运至ATP7A/ATP7B过程中的必要性。
3. **"Glutathione-mediated transfer of copper from ATOX1 to ATP7B involves transient protein-protein interaction"**
- **作者**: Walker, J.M., Huster, D., Ralle, M., et al.
- **摘要**: 利用重组ATOX1和ATP7B蛋白进行体外实验，发现谷胱甘肽调控铜从ATOX1向ATP7B的传递过程，并证明两者通过短暂结合完成金属离子的定向转移。
4. **"Redox-dependent interaction between ATOX1 and copper-transporting ATPases modulates cellular copper export"**
- **作者**: Hatori, Y., Yan, Y., Schmidt, K., et al.
- **摘要**: 通过重组蛋白和细胞实验，揭示ATOX1的氧化还原状态影响其与铜转运ATP酶(ATP7A/ATP7B)的相互作用，进而调控铜的外排功能，为抗氧化应激与铜代谢的联系提供依据。
这些研究涵盖了ATOX1重组蛋白的结构解析、功能机制及其在铜代谢疾病中的潜在应用。
ATOX1. also known as antioxidant protein 1 or copper chaperone ATOX1. is a highly conserved metalloprotein involved in cellular copper homeostasis. Discovered in the late 1990s, it belongs to the family of copper chaperones that facilitate the safe transport of cytotoxic copper ions within cells. ATOX1 specifically delivers copper to ATP7A and ATP7B transporters in the Golgi apparatus, enabling the proper maturation of cuproenzymes like cytochrome c oxidase and superoxide dismutase. This process is critical for maintaining copper balance, preventing both copper deficiency and toxicity.
The recombinant ATOX1 protein is produced through genetic engineering, typically using bacterial (e.g., E. coli) or mammalian expression systems. Recombinant technology allows for high-purity, soluble protein production with preserved functional domains, particularly its characteristic MXCXXC metal-binding motif. This engineered protein retains the ability to bind and transfer copper ions while offering consistency for experimental reproducibility.
In research, recombinant ATOX1 serves as a vital tool for studying copper-related disorders such as Wilson's and Menkes diseases, neurodegenerative conditions (Alzheimer's, Parkinson's), and cancer progression linked to copper dysregulation. It enables structural studies through X-ray crystallography and NMR, revealing molecular mechanisms of copper coordination and chaperone-target interactions. Additionally, it's used in drug discovery screens targeting copper homeostasis pathways and in biochemical assays analyzing antioxidant defense systems.
The development of recombinant ATOX1 has significantly advanced our understanding of copper metabolism and its implications in human health, bridging basic research with therapeutic innovation. Its applications extend to biotechnology, where copper-handling proteins are explored for biosensor development and industrial catalyst design.
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