| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | egfp |
| Uniprot No | C5MKY7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-239aa |
| 氨基酸序列 | MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK |
| 预测分子量 | 28.4 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3篇关于EGFP重组蛋白的模拟参考文献(内容基于常见研究方向虚构，仅供参考)：
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1. **文献名称**：Construction and Application of EGFP-Tagged Recombinant Protein for Live-Cell Imaging
**作者**：Zhang L, et al.
**摘要**：研究团队构建了EGFP融合的重组表达载体，通过转染哺乳动物细胞验证其荧光标记效果，并成功用于实时追踪目标蛋白在细胞内的动态分布。
2. **文献名称**：Optimization of EGFP Fusion Protein Expression in Escherichia coli
**作者**：Kim S, et al.
**摘要**：通过优化启动子、诱导条件及宿主菌株，显著提高了EGFP重组蛋白在大肠杆菌中的可溶性表达，为大规模生产荧光标记蛋白提供技术方案。
3. **文献名称**：EGFP as a Reporter for Protein-Protein Interaction Studies
**作者**：Müller J, et al.
**摘要**：利用EGFP重组蛋白的双分子荧光互补技术(BiFC)，开发了一种可视化检测细胞内蛋白质相互作用的方法，并验证其在信号通路研究中的可靠性。
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*注：以上文献为示例性内容，实际引用需查询真实数据库(如PubMed)并核对原文。*
Enhanced green fluorescent protein (EGFP) is a genetically engineered variant of the original green fluorescent protein (GFP) derived from the jellyfish *Aequorea victoria*. Since its discovery in the 1960s, GFP revolutionized molecular and cellular biology by enabling real-time visualization of biological processes in living systems. However, wild-type GFP has limitations, including low brightness and suboptimal folding in mammalian cells. To address these, EGFP was developed in the 1990s through targeted mutagenesis, enhancing its fluorescence intensity, photostability, and expression efficiency in eukaryotic systems.
EGFP retains the core β-barrel structure of GFP, which encapsulates a chromophore formed by cyclization and oxidation of three internal amino acids (Ser65. Tyr66. Gly67). Key modifications in EGFP include the S65T mutation, which shifts the excitation peak to 488 nm (aligning with standard fluorescein filters) and improves fluorescence quantum yield. Additional codon optimization for mammalian expression further boosts its utility in research. As a recombinant protein, EGFP is widely used as a reporter gene to track gene expression, protein localization, and intracellular dynamics. It also serves as a fusion tag to visualize target proteins in live cells, enabling studies on cellular trafficking, protein interactions, and organelle dynamics. Its non-invasive nature, lack of cofactor requirements, and compatibility with high-resolution microscopy make it indispensable in fields like developmental biology, neuroscience, and drug screening. EGFP’s versatility continues to drive innovations in bioimaging and synthetic biology applications.
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