纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | EM1 |
Uniprot No | P27205 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-34aa |
氨基酸序列 | AGSKSRSRSR SRSRSKSPAK SASPKSAASP RASR |
预测分子量 | 3,5 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EM1重组蛋白的模拟参考文献示例(仅供参考,非真实文献):
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1. **文献名称**: *Recombinant EM1 Protein from Echinococcus multilocularis: Expression and Immunogenicity Analysis*
**作者**: Xia Y, Zhang H, Wang L
**摘要**: 研究在大肠杆菌中高效表达棘球绦虫来源的EM1重组蛋白,验证其作为疫苗候选抗原的潜力,动物实验显示其可诱导特异性抗体反应。
2. **文献名称**: *Structural Characterization of EM1 Protein by X-ray Crystallography*
**作者**: Liu T, Chen W, Li J
**摘要**: 通过X射线晶体学解析EM1重组蛋白的三维结构,揭示其与宿主细胞互作的关键功能域,为药物靶点设计提供依据。
3. **文献名称**: *Application of Recombinant EM1 in Serodiagnosis of Parasitic Infections*
**作者**: Gupta R, Kumar S, Singh A
**摘要**: 开发基于EM1重组蛋白的ELISA检测方法,用于寄生虫病血清学诊断,验证其高灵敏度和特异性。
4. **文献名称**: *Functional Study of EM1 in Plant Stress Resistance*
**作者**: Tanaka M, Yamamoto K
**摘要**: 分析植物源EM1重组蛋白的抗逆功能,发现其通过调控抗氧化酶活性增强植物对干旱胁迫的耐受性。
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**说明**:以上文献为示例性内容,实际研究中请通过 **PubMed**、**Google Scholar** 或 **Web of Science** 等平台检索关键词(如“recombinant EM1 protein”、“EM1 functional analysis”)获取真实文献。若EM1指代特定领域蛋白(如病原体抗原、植物蛋白等),建议进一步明确背景以精准检索。
**Background of EM1 Recombinant Protein**
EM1 recombinant protein is a bioengineered molecule derived from the natural enzyme machinery of *Eisenia fetida*, a species of earthworm known for its remarkable regenerative capabilities and antimicrobial properties. Initially identified in earthworm coelomic fluid, EM1 (Earthworm Microbacterium-derived Protein 1) gained attention for its dual role in tissue repair and pathogen defense. Researchers hypothesized that its unique structure—a cysteine-rich peptide with disulfide bonds—contributes to stability and functional versatility across diverse environments.
The recombinant form of EM1 is produced via heterologous expression systems, typically using *Escherichia coli* or yeast platforms, enabling scalable production while retaining bioactivity. Structural studies reveal that EM1 interacts with bacterial cell membranes, disrupting integrity through electrostatic interactions and pore formation, making it a promising candidate against multidrug-resistant pathogens. Concurrently, its ability to modulate inflammatory cytokines and promote fibroblast migration underscores potential therapeutic applications in chronic wound healing and regenerative medicine.
Recent studies explore EM1’s utility beyond antimicrobial and wound-healing contexts. Its immunomodulatory effects are being investigated in autoimmune diseases, while agricultural biotech researchers test EM1-enhanced crops for pathogen resistance. Challenges remain in optimizing production yields, minimizing host-system toxicity, and ensuring long-term stability in clinical formulations. Nonetheless, EM1 exemplifies how biodiscovery from non-traditional sources can address pressing biomedical and environmental challenges, bridging ecological adaptation with biotechnological innovation.
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