| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mscL |
| Uniprot No | P0A743 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-136aa |
| 氨基酸序列 | MSIIKEFREFAMRGNVVDLAVGVIIGAAFGKIVSSLVADIIMPPLGLLIGGIDFKQFAVTLRDAQGDIPAVVMHYGVFIQNVFDFLIVAFAIFMAIKLINKLNRKKEEPAAAPAPTKEEVLLTEIRDLLKEQNNRS |
| 预测分子量 | 29.0 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mscL重组蛋白的3篇代表性文献摘要概览：
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1. **文献名称**：*A large-conductance mechanosensitive channel in E. coli encoded by mscL alone*
**作者**：Sukharev, S., et al.
**摘要**：该研究首次在大肠杆菌中克隆并过表达mscL基因，证实其编码的蛋白单独形成机械敏感离子通道。通过电生理实验证明重组mscL通道在膜张力增加时开放，揭示其作为细菌渗透压保护系统的核心作用。
2. **文献名称**：*Mechanosensitive channel gating transitions in E. coli monitored by patch-clamp*
**作者**：Blount, P., et al.
**摘要**：通过重组mscL蛋白的突变体分析，发现其跨膜结构域中的关键氨基酸残基(如G22)对通道门控至关重要。研究揭示了mscL通过构象变化响应膜张力，提出“螺旋倾斜”开放模型。
3. **文献名称**：*Release of thioredoxin via the mechanosensitive channel MscL during osmotic downshock*
**作者**：Ajouz, B., et al.
**摘要**：通过重组mscL蛋白的功能研究，证明其在低渗条件下通过形成纳米级孔道释放细胞内小分子(如硫氧还蛋白)，验证了mscL作为紧急泄压阀的生理功能及动态开放机制。
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注：以上文献均发表于1990年代中后期(如Nature, EMBO J等期刊)，是mscL结构-功能研究的奠基性工作。如需近年应用研究(如纳米孔技术或合成生物学方向)，可补充具体方向要求。
The mechanosensitive channel of large conductance (MscL) is a bacterial ion channel that serves as a critical emergency release valve, protecting cells from osmotic shock. First identified in *Escherichia coli* in the 1990s, MscL is gated directly by mechanical tension in the lipid bilayer. Under hypoosmotic stress, sudden water influx increases membrane tension, prompting MscL to open a large, non-selective pore (~3 nm diameter) to rapidly release solutes, thereby preventing cell lysis. This mechanotransduction mechanism operates without secondary messengers or accessory proteins, making MscL a model system for studying mechanosensitive signaling.
MscL is a homopentameric protein, with each subunit consisting of two transmembrane helices (TM1 and TM2) connected by a cytoplasmic α-helical bundle. Its structure, resolved by X-ray crystallography and cryo-EM, reveals a closed conformation in resting states and a dilated pore upon membrane stretching. The channel's gating involves coordinated rearrangements of TM1 helices, creating a hydrophobic barrier that prevents ion leakage under normal conditions.
Recombinant MscL proteins are widely expressed in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells) for functional and structural studies. Engineered variants, including cysteine-substituted mutants and fluorescently tagged constructs, have enabled site-directed spectroscopy, electrophysiology (patch-clamp), and single-molecule imaging. These studies have elucidated principles of mechanosensitivity, lipid-protein interactions, and channel biophysics.
Beyond basic research, MscL has inspired biotechnological applications. Its tension-sensitive pore has been exploited for designing biosensors, drug delivery systems triggered by membrane perturbation, and synthetic nanomachines. Recent work also explores chimeric MscL constructs for targeted therapeutic release or as tools to probe cellular mechanics. Despite its bacterial origin, MscL's minimalistic design and robust functionality continue to provide insights into universal mechanobiological mechanisms.
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