| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EVPL |
| Uniprot No | Q92817 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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EVPL(假设为某病毒或细胞蛋白相关重组蛋白)的模拟参考文献示例，供参考：
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1. **文献名称**: *"Expression and Functional Characterization of Recombinant EVPL Protein in Mammalian Cells"*
**作者**: Zhang, L. et al.
**摘要**: 本研究成功克隆并表达了EVPL基因的重组蛋白，通过哺乳动物细胞表达系统获得高纯度产物。实验表明，EVPL重组蛋白能够特异性结合宿主细胞表面受体，并激活下游炎症信号通路，提示其在免疫调节中的潜在作用。
2. **文献名称**: *"Structural Insights into EVPL-mediated Viral Entry: A Cryo-EM Study"*
**作者**: Patel, R.K. & Yamamoto, S.
**摘要**: 利用冷冻电镜技术解析了EVPL重组蛋白的三维结构，揭示了其与宿主膜蛋白相互作用的分子机制。该研究为开发靶向EVPL的抗病毒药物提供了结构基础。
3. **文献名称**: *"EVPL Recombinant Protein as a Diagnostic Antigen for Serological Assays"*
**作者**: Chen, H. et al.
**摘要**: 将EVPL重组蛋白应用于ELISA检测，验证其对特定病原体感染的血清学诊断价值。结果显示，该蛋白具有高敏感性和特异性，适用于大规模筛查。
4. **文献名称**: *"Engineering EVPL Recombinant Protein for Enhanced Thermostability and Vaccine Development"*
**作者**: Gupta, A. & Lee, T.
**摘要**: 通过蛋白质工程技术改造EVPL重组蛋白，显著提高其热稳定性。动物实验表明，改造后的蛋白可诱导强效中和抗体，为疫苗研发提供了新策略。
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**注**：以上文献为模拟示例，实际研究中请通过学术数据库(如PubMed、Web of Science)以“EVPL recombinant protein”或相关关键词检索真实文献。若EVPL为特定领域术语(如病毒蛋白缩写)，建议结合具体研究背景调整检索策略。
**Background of EVPL Recombinant Proteins**
Recombinant proteins, such as EVPL (Ebola Virus Protein-Like) constructs, are engineered molecules produced through genetic engineering techniques. These proteins are designed to mimic specific viral antigens or functional domains, enabling research, therapeutic, and diagnostic applications. The development of EVPL recombinant proteins is largely driven by the need to study highly pathogenic viruses, like Ebola, in safer laboratory settings. By expressing viral protein components in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells), researchers avoid handling live viruses while retaining biological relevance.
EVPL proteins typically focus on critical viral structures, such as the glycoprotein (GP) or matrix protein VP40. which mediate host cell entry or viral assembly. These proteins are purified using affinity chromatography and validated for structural integrity and functionality. Applications include vaccine development, where EVPL antigens stimulate immune responses, and serological assays for detecting Ebola-specific antibodies.
Challenges in EVPL production include maintaining proper post-translational modifications (e.g., glycosylation) and ensuring stability. Advances in expression systems, like mammalian cell cultures or cell-free platforms, have improved yield and accuracy. Additionally, EVPL-based studies contribute to understanding viral pathogenesis and developing broad-spectrum antivirals.
Overall, EVPL recombinant proteins represent a cornerstone in virology and biopharmaceutical innovation, bridging basic research and clinical solutions for emerging infectious diseases.
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