| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CFTR |
| Uniprot No | P13569 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1381-1480aa |
| 氨基酸序列 | YQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKL LNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL |
| 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CFTR重组蛋白的3-4篇参考文献及其摘要概括：
1. **《Structure of the human CFTR anion channel by cryo-electron microscopy》**
- **作者**：Zhang, Z., Chen, J.
- **摘要**：通过冷冻电镜技术解析了人类CFTR蛋白的高分辨率三维结构，揭示了其离子通道的构象特征，为理解囊性纤维化致病机制及药物设计提供结构基础。
2. **《Production of the human CFTR protein in insect cells for structural studies》**
- **作者**：Hegedüs, T., et al.
- **摘要**：利用昆虫细胞表达系统成功制备功能性重组CFTR蛋白，优化了纯化流程，支持后续结构生物学和功能研究。
3. **《CFTR function and prospects for therapy》**
- **作者**：Riordan, J.R.
- **摘要**：综述CFTR蛋白的生理功能及其基因突变导致的囊性纤维化病理机制，并探讨重组蛋白技术在基因治疗和药物开发中的应用潜力。
4. **《Recombinant CFTR protein delivery restores chloride transport in cystic fibrosis epithelial cells》**
- **作者**：Liu, F., et al.
- **摘要**：通过脂质体递送重组CFTR蛋白至囊性纤维化患者的上皮细胞，成功恢复氯离子通道功能，验证了蛋白替代疗法的可行性。
这些文献涵盖了CFTR重组蛋白的结构解析、表达系统开发、功能研究及治疗应用等方向。
The cystic fibrosis transmembrane conductance regulator (CFTR) protein is a chloride channel critical for maintaining fluid and electrolyte balance across epithelial surfaces. Dysfunctional CFTR causes cystic fibrosis (CF), a life-limiting genetic disorder affecting multiple organs, particularly the lungs and pancreas. The CFTR gene, identified in 1989. encodes a 1.480-amino-acid protein with two membrane-spanning domains, two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Over 2.000 CFTR mutations have been documented, with F508del (a deletion of phenylalanine at position 508) being the most common, causing misfolding and impaired trafficking to the cell membrane.
Recombinant CFTR protein production emerged as a key strategy for studying CF pathophysiology and developing therapies. Using heterologous expression systems (e.g., mammalian cells, insect cells, or yeast), researchers produce purified CFTR to analyze its structure, function, and interactions with modulators. Structural studies, notably cryo-EM advancements since 2017. have revealed atomic-level details of CFTR gating mechanisms and drug-binding sites, informing precision drug design.
Therapeutics like CFTR modulators (e.g., ivacaftor, lumacaftor, elexacaftor) aim to rescue mutant CFTR function. These drugs were developed using recombinant protein platforms to screen compounds that enhance folding, trafficking, or channel activity. The 2019 FDA-approved Triple Therapy (Trikafta®), combining three modulators, marked a breakthrough, improving lung function in ~90% of CF patients with F508del or similar mutations.
Current research focuses on expanding modulator efficacy to rare mutations, optimizing protein correction strategies, and addressing limitations like high costs and variable patient responses. Recombinant CFTR technology remains central to personalized medicine approaches and gene-editing therapies (e.g., CRISPR-Cas9), aiming for durable CFTR restoration.
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