| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | kcsA |
| Uniprot No | P0A333 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MPPMLSGLLARLVKLLLGRHGSALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWSVETATTVGYGDLYPVTLWGRLVAVVVMVAGITSFGLVTAALATWFVGREQERRGHFVRHSEKAAEEAYTRTTRALHERFDRLERMLDDNRR |
| 预测分子量 | 23.7 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3条关于KcsA重组蛋白的经典文献及其摘要概括：
1. **文献名称**：*The Structure of the Potassium Channel: Molecular Basis of K⁺ Conduction and Selectivity*
**作者**：Doyle, D.A., et al.
**摘要**：该研究首次通过X射线晶体学解析了重组KcsA蛋白的高分辨率三维结构，揭示了钾离子通道的选择性过滤机制及跨膜螺旋排列，为理解离子通道的门控和导电机制提供了结构基础。
2. **文献名称**：*pH-Dependent Gating in the Streptomyces lividans K⁺ Channel*
**作者**：Heginbotham, L., et al.
**摘要**：文章研究了重组KcsA通道蛋白在脂质双层中的电生理特性，发现其门控行为受pH调控，阐明了胞内结构域在通道激活中的作用，为后续功能研究奠定基础。
3. **文献名称**：*Expression and Purification of the Functional Tetrameric KcsA Potassium Channel in Escherichia coli*
**作者**：Valiyaveetil, F.I., et al.
**摘要**：报道了在大肠杆菌中高效表达和纯化重组KcsA四聚体蛋白的方法，通过优化膜蛋白表达条件及亲和层析步骤，获得了具有天然构象的活性蛋白，适用于生物物理和结构研究。
(注：以上文献信息为示例，具体年份和作者需根据实际引用文献核对。)
**Background of KcsA Recombinant Protein**
KcsA is a prokaryotic potassium (K⁺) channel protein originally identified in *Streptomyces lividans*. It serves as a foundational model for studying the structure and function of potassium channels due to its simplicity, stability, and homology to eukaryotic counterparts. As a tetrameric protein, each subunit of KcsA consists of two transmembrane helices connected by a pore-forming region, which includes a highly conserved selectivity filter responsible for precise K⁺ ion discrimination over smaller Na⁺ ions.
The recombinant KcsA protein is typically expressed in *Escherichia coli* using genetic engineering techniques, enabling large-scale production for biochemical and biophysical studies. Its overexpression and purification have facilitated breakthroughs in understanding ion permeation mechanisms, gating dynamics, and channel regulation. Unlike eukaryotic voltage-gated or ligand-gated channels, KcsA is pH-dependent, undergoing conformational changes in response to cytoplasmic acidification, making it a valuable tool for probing gating mechanisms.
KcsA’s crystal structure, first resolved in 1998. revolutionized membrane protein structural biology, providing atomic-level insights into ion selectivity and conduction. These findings have broader implications for designing therapeutics targeting potassium channels involved in neurological, cardiac, and metabolic disorders. Additionally, recombinant KcsA is utilized in drug screening, synthetic biology, and nanotechnology due to its stability and modular architecture.
Research on KcsA continues to bridge gaps between prokaryotic and eukaryotic channel biology, offering a simplified yet powerful system to explore fundamental principles of membrane transport and allosteric regulation. Its recombinant form remains indispensable for advancing both basic science and biomedical applications.
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