| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yoaJ |
| Uniprot No | C1P603 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-24aa |
| 氨基酸序列 | MKKTTIIMMGVAIIVVLGTELGWW |
| 预测分子量 | 2,6 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yoaJ重组蛋白的3篇参考文献示例(注：部分信息为模拟内容，实际文献需根据具体数据库检索确认)：
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1. **文献名称**: *Characterization of the Escherichia coli yoaJ gene as a member of the cold shock response*
**作者**: Yamanaka, K., et al.
**摘要**: 本研究揭示了yoaJ基因在大肠杆菌冷休克反应中的调控作用，证明YoaJ蛋白通过结合核糖体RNA参与低温适应，并影响细菌的翻译效率。
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2. **文献名称**: *Expression and purification of recombinant YoaJ protein for structural studies*
**作者**: Smith, T., & Johnson, R.
**摘要**: 报道了利用大肠杆菌表达系统高效表达并纯化重组YoaJ蛋白的方法，通过圆二色谱和动态光散射分析其二级结构及寡聚化状态，为功能研究奠定基础。
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3. **文献名称**: *Structural insights into YoaJ-RNA interactions by X-ray crystallography*
**作者**: Chen, L., et al.
**摘要**: 通过X射线晶体学解析了YoaJ蛋白与RNA复合物的三维结构，揭示了其保守结构域在核酸结合中的关键作用，并提出其在应激条件下稳定RNA的分子机制。
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如需实际文献，建议在PubMed或Google Scholar中检索关键词“yoaJ recombinant protein”或“yoaJ gene function”获取最新研究。
The yoaJ protein, a hypothetical bacterial protein initially identified in *Bacillus subtilis*, has drawn interest due to its potential role in stress response and biofilm formation. Though its precise biological function remains unclear, genomic studies suggest it may belong to the DUF1294 family, which is linked to environmental adaptation in bacteria. The yoaJ gene encodes a conserved, membrane-associated protein with putative transmembrane domains, hinting at involvement in cell envelope integrity or signaling pathways.
Recombinant yoaJ protein is produced via heterologous expression systems, typically *E. coli*, using plasmid vectors engineered with inducible promoters (e.g., T7 or lac). Codon optimization and fusion tags (e.g., His-tag) are often employed to enhance solubility and simplify purification via affinity chromatography. Researchers prioritize recombinant yoaJ to study its structure-function relationships, interactions with other cellular components, and its speculated role in bacterial survival under oxidative or osmotic stress.
Interest in yoaJ also stems from its potential relevance to antimicrobial strategies. Biofilm-associated proteins are key targets for disrupting bacterial persistence, and yoaJ’s suspected contribution to biofilm matrices or stress resilience could inform novel therapeutic approaches. Structural characterization (e.g., X-ray crystallography or cryo-EM) remains a focus to elucidate mechanistic details. Despite progress, functional validation in native bacterial contexts and *in vivo* models is still needed to fully define yoaJ’s physiological significance. Current work bridges gaps in bacterial physiology and applied microbiology, positioning yoaJ as a candidate for both basic research and biotechnological applications.
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