| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRRC8A |
| Uniprot No | Q8IWT6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 711-810aa |
| 活性数据 | QNLAITANRIETLPPELFQCRKLRALHLGNNVLQSLPSRVGELTNLTQIELRGNRLECLPVELGECPLLKRSGLVVEEDLFNTLPPEVKERLWRADKEQA |
| 分子量 | 36.74 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人LRRC8A蛋白的3篇关键参考文献及其摘要：
1. **《LRRC8A: An Essential Component of the Volume-Regulated Anion Channel (VRAC)》**
- **作者**：Qiu Z. et al. (2014)
- **摘要**：该研究首次证实LRRC8A是体积调节性阴离子通道(VRAC)的核心组成蛋白，通过CRISPR基因敲除实验表明，LRRC8A缺失的细胞完全丧失VRAC功能，重组表达人LRRC8A可恢复通道活性，揭示其在渗透压调节中的关键作用。
2. **《Cryo-EM Structure of the Human Volume-Regulated Anion Channel LRRC8A》**
- **作者**：Voss F.K. et al. (2018)
- **摘要**：利用冷冻电镜技术解析了人源LRRC8A蛋白的高分辨率三维结构，揭示了其六聚体环形构象及潜在的离子传导路径，为理解VRAC通道的门控机制和药物设计提供结构基础。
3. **《LRRC8A and LRRC8D Subunits Contribute to the Functional Diversity of VRAC Channels》**
- **作者**：Kumar L. et al. (2019)
- **摘要**：研究通过重组共表达LRRC8A与其他LRRC8家族成员(如LRRC8D)，证明LRRC8A是通道的必要组分，而不同亚基的组合调节VRAC的底物选择性及生理功能，表明其异源组装的功能多样性。
4. **《Post-translational Modification of LRRC8A Modulates VRAC Activity》**
- **作者**：Zhou Y. et al. (2020)
- **摘要**：揭示了人LRRC8A蛋白的磷酸化修饰(如酪氨酸磷酸化)动态调控VRAC通道的开放状态，重组蛋白实验表明PTM修饰通过改变通道构象影响细胞体积恢复能力。
这些文献涵盖LRRC8A的结构、功能、调控及相互作用研究，可作为该领域的核心参考。
The leucine-rich repeat-containing 8A (LRRC8A) protein, also known as SWELL1. is a pivotal component of the volume-regulated anion channel (VRAC) in mammalian cells. VRAC plays a critical role in regulating cell volume under osmotic stress and mediates the transport of chloride ions, metabolites, and signaling molecules. LRRC8A forms heterohexameric complexes with other LRRC8 family members (LRRC8B-E), determining channel properties and substrate selectivity. Its discovery in 2014 resolved long-standing questions about the molecular identity of VRAC. Dysregulation of LRRC8A is implicated in pathologies including cancer chemotherapy resistance, neuronal excitotoxicity, and ischemic damage, making it a potential therapeutic target.
Recombinant human LRRC8A protein is engineered for structural and functional studies, enabling researchers to investigate its channel architecture, gating mechanisms, and role in physiological processes. Cryo-EM studies using recombinant LRRC8A (notably its homomeric form) revealed a twisted barrel-like structure with a selective pore. This protein also facilitates studies on VRAC’s dual roles in osmoregulation and drug uptake, particularly in cancer cells. Research tools like recombinant LRRC8A have advanced understanding of anion channel biology and accelerated drug discovery efforts targeting channelopathies and transport-related diseases.
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