| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CFP |
| Uniprot No | P27918 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 213-334aa |
| 氨基酸序列 | PHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGP WGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPC PVDGEWDSWGEWSPCIRRNMKS |
| 预测分子量 | 39 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CFP(如CFP-10等)重组蛋白的3篇代表性文献示例(部分信息基于常见研究主题模拟，供参考)：
1. **文献名称**：*Expression and Purification of Recombinant Mycobacterium tuberculosis CFP-10 in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究成功构建了CFP-10重组蛋白的大肠杆菌表达系统，优化了诱导条件与纯化方法，获得高纯度蛋白，并通过Western blot验证其抗原特异性，为结核病血清学诊断试剂开发提供基础。
2. **文献名称**：*Immunogenicity of Recombinant CFP-10/ESAT-6 Fusion Protein in Tuberculosis Vaccine Development*
**作者**：Li X, et al.
**摘要**：研究将重组CFP-10与ESAT-6融合表达，评估其在小鼠模型中诱导的Th1型免疫反应，结果显示融合蛋白显著增强IFN-γ分泌，提示其作为结核亚单位疫苗的潜力。
3. **文献名称**：*Structural Analysis of CFP-10 Recombinant Protein by Circular Dichroism Spectroscopy*
**作者**：Wang Y, et al.
**摘要**：通过圆二色光谱分析重组CFP-10的二级结构，证实其在溶液中的α-螺旋构象稳定性，并探讨pH变化对蛋白折叠的影响，为结核分枝杆菌宿主互作机制研究提供结构依据。
---
**注**：若需真实文献，建议通过PubMed或Google Scholar搜索关键词“recombinant CFP-10 protein”或“CFP-10 expression”获取最新研究。
**Background of CFP Recombinant Protein**
Cyan Fluorescent Protein (CFP) is a genetically engineered variant derived from the original Green Fluorescent Protein (GFP), a naturally occurring protein first isolated from the jellyfish *Aequorea victoria*. GFP gained prominence as a revolutionary molecular tool due to its ability to fluoresce without requiring exogenous cofactors. Building on this discovery, researchers developed color-shifted mutants, including CFP, through targeted amino acid substitutions to alter spectral properties.
CFP was engineered by introducing specific mutations (e.g., Y66W, Y145F) into the GFP structure, shifting its emission spectrum to the cyan range (∼470–500 nm). This modification enabled its use in fluorescence resonance energy transfer (FRET)-based assays, where it serves as a donor fluorophore paired with yellow or orange acceptors (e.g., YFP, mCherry) to study protein-protein interactions, conformational changes, or intracellular signaling dynamics.
The development of recombinant DNA technology further enhanced CFP’s utility. By fusing the CFP gene to genes encoding proteins of interest, scientists could visualize subcellular localization, track protein movements in real time, and monitor gene expression in living cells or organisms. CFP-based reporters have been widely applied in cell biology, neuroscience, and drug discovery.
Despite its advantages, CFP has limitations, including lower brightness and photostability compared to newer fluorescent proteins like mTurquoise2. Nonetheless, ongoing protein engineering efforts aim to optimize its performance, balancing spectral properties, stability, and compatibility with imaging systems. CFP remains a foundational tool in the fluorescent protein toolkit, contributing to advances in live-cell imaging and molecular biosensing.
×
