| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | epiA |
| Uniprot No | P08136 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-52aa |
| 氨基酸序列 | IASKFICTPGCAKTGSFNSYCC |
| 预测分子量 | 17.7 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. |
以下是关于epiA(假设为某特定重组蛋白)的3篇示例文献摘要(注：epiA名称可能为虚构或需进一步确认，以下为模拟内容)：
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1. **《Recombinant epiA protein promotes neuronal regeneration in vitro》**
- **作者**: Smith J, et al.
- **摘要**: 研究通过大肠杆菌系统表达并纯化epiA重组蛋白，发现其能显著增强神经元轴突生长，机制可能与激活PI3K/Akt信号通路相关，提示其在神经修复中的潜在应用价值。
2. **《Structural and functional characterization of epiA as a bacterial adhesin》**
- **作者**: Lee H, et al.
- **摘要**: 解析了epiA重组蛋白的晶体结构，揭示其通过特定结构域介导病原体与宿主细胞的黏附，为开发靶向抗菌疗法提供了理论基础。
3. **《EpiA recombinant protein enhances vaccine efficacy against viral infection》**
- **作者**: Zhang R, et al.
- **摘要**: 利用哺乳动物细胞表达的epiA重组蛋白作为疫苗佐剂，显著提升了小鼠模型中对流感病毒的免疫应答，表明其在疫苗开发中的辅助作用。
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**注意**：若"epiA"为特定领域术语(如细菌毒素或细胞因子)，请确认名称准确性后调整检索关键词(例如：是否应为EphA受体、EpiA毒素等)。实际文献需通过PubMed/Google Scholar等平台查询。
**Background of EpiA Recombinant Protein**
EpiA, a recombinant protein engineered through genetic modification, is typically derived from a specific gene of interest cloned into an expression vector and produced in heterologous systems like *E. coli*, yeast, or mammalian cells. The "EpiA" designation often refers to its functional association with epithelial tissues or signaling pathways, though its exact biological role may vary depending on the target molecule. For instance, EpiA could be linked to epidermal growth factor (EGF)-like domains, cell adhesion, or immune modulation, making it relevant in studies of tissue repair, cancer biology, or inflammatory diseases.
Recombinant production enables scalable, high-purity yields of EpiA, free from contaminants found in native sources. Techniques such as affinity chromatography (e.g., His-tag purification) ensure precise isolation. Post-translational modifications (e.g., glycosylation) may be incorporated via mammalian expression systems to enhance functionality.
EpiA’s applications span *in vitro* and *in vivo* research, including ligand-receptor interaction assays, cell proliferation studies, and therapeutic development. In oncology, it might regulate tumor microenvironment signaling; in regenerative medicine, it could promote epithelial cell migration. Its recombinant form allows for standardized experimentation, overcoming batch variability inherent in natural extracts.
Current research focuses on optimizing EpiA’s stability, bioactivity, and delivery mechanisms. Challenges include maintaining conformational integrity during production and ensuring compatibility with physiological systems. As a tool, EpiA exemplifies the intersection of biotechnology and translational medicine, offering insights into disease mechanisms and potential therapeutic avenues.
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