| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP7b |
| Uniprot No | P35670 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1372-1465aa |
| 氨基酸序列 | QLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQ VSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI |
| 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. |
以下是关于ATP7B重组蛋白的3篇代表性文献摘要(虚构示例，供参考)：
1. **文献名称**：Expression and functional characterization of recombinant ATP7B in Saccharomyces cerevisiae
**作者**：Smith J, et al.
**摘要**：研究利用酿酒酵母系统表达人源ATP7B重组蛋白，证实其铜转运功能，并分析常见致病突变体(如H1069Q)的功能缺失机制。
2. **文献名称**：Crystallographic analysis of the N-terminal domain of ATP7B reveals copper-binding sites
**作者**：Chen L, et al.
**摘要**：通过大肠杆菌表达并纯化ATP7B的N端金属结合结构域，利用X射线晶体学解析其三维结构，揭示6个铜离子结合位点的空间排列特征。
3. **文献名称**：ATP7B reconstitution in human hepatocytes rescues Wilson disease phenotypes in vitro
**作者**：Wang Y, et al.
**摘要**：构建重组ATP7B慢病毒载体，在威尔逊病患者来源的肝细胞中实现蛋白表达，成功恢复细胞铜外排能力，为基因治疗提供实验依据。
(注：以上文献信息为模拟生成，实际引用请查询PubMed等数据库获取真实文献)
ATP7b recombinant protein is derived from the ATP7b gene, which encodes a copper-transporting P-type ATPase critical for maintaining copper homeostasis in humans. Primarily expressed in the liver, ATP7b facilitates the excretion of excess copper into bile and incorporates copper into ceruloplasmin, a key copper-carrier protein. Mutations in ATP7b disrupt copper regulation, leading to Wilson disease (WD), a rare autosomal recessive disorder characterized by toxic copper accumulation in the liver, brain, and other organs.
Recombinant ATP7b protein is engineered using biotechnological approaches, often expressed in mammalian cell systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications and functional folding. Researchers utilize this protein to study copper-binding domains, enzymatic activity, and trafficking mechanisms under physiological and pathological conditions. It serves as a tool to investigate WD pathogenesis, screen potential therapeutics, and develop enzyme replacement therapies.
The production of ATP7b recombinant protein faces challenges due to its large size (~1.500 amino acids), transmembrane domains, and susceptibility to aggregation. Optimizing expression systems and purification protocols remains a focus to enhance yield and stability. Recent advances in structural biology, such as cryo-EM, have provided insights into ATP7b’s conformational changes during copper transport, aiding drug design.
Additionally, recombinant ATP7b holds promise for gene therapy vectors or copper-chelation adjuvants. However, therapeutic applications require addressing delivery efficiency, immunogenicity, and long-term efficacy. Ongoing research aims to bridge these gaps, leveraging recombinant protein technology to translate mechanistic insights into clinical solutions for Wilson disease and related copper-metabolism disorders.
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