| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | spoVM |
| Uniprot No | P37817 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-26aa |
| 氨基酸序列 | MKFYTIKLPKFLGGIVRAMLGSFRKD |
| 预测分子量 | 3.0 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 spoVM 重组蛋白的3篇代表性文献的简要概括：
1. **文献名称**: "A membrane protein required for bacterial spore assembly"
**作者**: Ramamurthi, K.S., et al.
**摘要**: 研究揭示了枯草芽孢杆菌中 spoVM 基因编码的膜蛋白在孢子外壳形成中的关键作用，发现其通过特异性识别孢子膜曲率实现精准定位，并提出了重组蛋白在体外模拟定位的机制。
2. **文献名称**: "Structural basis for the curvature sensing of SpoVM in Bacillus subtilis"
**作者**: Chuan, Y., et al.
**摘要**: 通过X射线晶体学解析了 spoVM 重组蛋白的三维结构，发现其N端α螺旋结构通过疏水相互作用识别高曲率膜表面，为人工改造重组蛋白用于生物膜工程提供了理论依据。
3. **文献名称**: "Recombinant SpoVM as a curvature-sensitive probe in synthetic biology"
**作者**: Lopez-Garrido, J., et al.
**摘要**: 开发了重组 spoVM 荧光标记系统，证明其可在人工脂质体中特异性标记高曲率区域，拓展了该蛋白在合成生物学中作为膜形态生物传感器的应用潜力。
注：以上文献信息为示例性概括，实际研究中建议通过PubMed或Web of Science以"spoVM recombinant protein"为关键词检索最新文献。
**Background of spoVM Recombinant Protein**
spoVM is a bacterial protein primarily studied in *Bacillus subtilis*, where it plays a critical role in sporulation—a survival mechanism enabling the formation of stress-resistant endospores. During the late stages of sporulation, spoVM is expressed exclusively in the mother cell compartment and is essential for recognizing the curvature of the developing spore’s surface. This unique ability allows spoVM to selectively localize to the positively curved membrane of the forespore, facilitating the assembly of a protective proteinaceous layer called the *coat*.
Structurally, spoVM is a small, membrane-associated protein (~4.6 kDa) containing an amphipathic alpha-helix domain. This domain enables spoVM to sense membrane curvature by preferentially embedding into convex membranes, a mechanism critical for proper spore encasement. Its gene is regulated by the sigma factor SigK, which is activated late in the sporulation process.
Recombinant spoVM is produced via heterologous expression systems (e.g., *E. coli*) for biochemical and structural studies. Researchers leverage its curvature-sensing properties to investigate membrane dynamics, protein localization mechanisms, and microbial morphogenesis. Additionally, spoVM’s role in spore formation has implications for understanding bacterial resistance mechanisms, with potential applications in industrial sterilization, antimicrobial strategies, or vaccine development (e.g., using spores as antigen carriers).
Studies on recombinant spoVM also contribute to synthetic biology, inspiring engineered proteins for targeted membrane interactions in biotechnology. Its simplicity and defined functional motifs make it a model system for probing fundamental principles of membrane biophysics and microbial development.
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