| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COPT1 |
| Uniprot No | O15431 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-190aa |
| 氨基酸序列 | MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFG FKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVS IRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLM LIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH |
| 预测分子量 | 37 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COPT1重组蛋白的参考文献示例(注：文献信息为示例性概括，具体内容需根据实际研究调整)：
1. **"Molecular characterization of the copper transporter COPT1 in Arabidopsis thaliana"**
- **作者**: Sancenón, V., et al. (2004)
- **摘要**: 研究通过克隆拟南芥COPT1基因并在酵母铜转运缺陷突变体中表达，证实COPT1重组蛋白具有铜离子转运功能，并参与植物体内铜稳态调控。
2. **"Functional analysis of rice COPT1 in copper uptake and redistribution"**
- **作者**: Zhou, H., et al. (2010)
- **摘要**: 利用大肠杆菌表达系统纯化水稻COPT1重组蛋白，结合异源酵母实验，发现COPT1在低铜条件下特异性介导铜吸收，且其表达受铜缺乏诱导。
3. **"Structural insights into the metal selectivity of COPT1 transporter"**
- **作者**: García, O., et al. (2016)
- **摘要**: 通过体外重组表达COPT1蛋白并进行晶体结构解析，揭示了其铜结合域的关键氨基酸残基及对铜离子的高选择性机制。
4. **"COPT1 localization and function in tomato under copper stress"**
- **作者**: Chen, L., et al. (2019)
- **摘要**: 在昆虫细胞中表达番茄COPT1重组蛋白，结合荧光标记技术，证明其定位于质膜，并在铜胁迫下调节细胞内的铜离子平衡。
(注：以上为模拟文献，实际引用时需以真实发表论文为准。)
COPT1 (Copper Transporter 1) is a member of the COPT/CTR family of copper transport proteins, which play critical roles in cellular copper uptake and homeostasis. Copper is an essential micronutrient acting as a cofactor for numerous enzymes involved in vital processes such as respiration (e.g., cytochrome c oxidase), antioxidant defense (e.g., superoxide dismutase), and iron metabolism. However, excess copper is toxic, necessitating tight regulation of its intracellular levels. COPT1. initially identified in plants like *Arabidopsis thaliana*, functions as a high-affinity copper transporter localized primarily in plasma membranes, facilitating copper influx under copper-deficient conditions.
Recombinant COPT1 proteins are engineered to study its structure-function relationships, regulatory mechanisms, and interactions. These proteins are typically expressed in heterologous systems (e.g., yeast, *E. coli*, or mammalian cells) to overcome challenges in isolating native COPT1 due to low abundance or membrane-associated complexity. Purification often involves affinity tags (e.g., His-tag) and detergent solubilization to maintain functionality. Structural studies suggest COPT1 forms homodimers or oligomers, with conserved methionine-rich motifs in transmembrane domains critical for copper binding and transport.
Research on recombinant COPT1 has elucidated its role in copper homeostasis, including its regulation by post-translational modifications (e.g., phosphorylation) and interactions with chaperones. In plants, COPT1 expression is tissue-specific (e.g., roots) and responsive to copper availability, impacting growth and stress responses. Dysregulation of COPT homologs in humans is linked to disorders like Wilson’s disease and cancer, highlighting evolutionary conservation in copper metabolism pathways.
Applications of recombinant COPT1 extend to biotechnology and agriculture, such as engineering copper-efficient crops or bioremediation strategies. Its study also provides insights into designing therapeutics targeting copper dysregulation in diseases. Overall, COPT1 recombinant proteins serve as vital tools for dissecting copper biology and developing translational solutions.
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