| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FLAG |
| Uniprot No | Q9H4M3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-255aa |
| 氨基酸序列 | MAVGNINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL IDLVTLWKRK CLREGFITED WDQPVADWKI FYFLRSLHRN LLHNPCAEEG FEFWSLDVNG GDEWKVEDLS RDQRKEFPND QVKKYFVTSY YTCLKSQVVD LKAEGYWEEL MDTTRPDIEV KDWFAARPDC GSKYQLCVQL LSSAHAPLGT FQPDPATIQQ KSDAKWREVS HTFSNYPPGV RYIWFQHGGV DTHYWAGWYG PRVTNSSITI GPPLP |
| 预测分子量 | 29,7 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3篇关于FLAG重组蛋白的经典文献概览：
---
1. **文献名称**: "A short polypeptide marker sequence useful for recombinant protein identification and purification"
**作者**: Hopp, T.P. et al. (1988)
**摘要**: 首次提出FLAG标签的设计，证明其作为重组蛋白亲和纯化和免疫检测的通用短肽标记，适用于哺乳动物表达系统。
2. **文献名称**: "The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins"
**作者**: Einhauer, A., & Jungbauer, A. (2001)
**摘要**: 系统比较FLAG与其他标签(如His、HA)的优缺点，重点讨论其在抗体亲和层析中的应用及高纯度蛋白获取策略。
3. **文献名称**: "Affinity purification of FLAG-tagged protein complexes using a synthetic peptide"
**作者**: Cristea, I.M. et al. (2010)
**摘要**: 开发基于FLAG标签的温和洗脱纯化方案，结合质谱技术解析蛋白质相互作用网络，应用于核蛋白复合物功能研究。
---
这些文献覆盖了FLAG标签的开发、优化及多场景应用，建议通过PubMed或Web of Science输入标题/作者获取全文。
**Background of FLAG-Tagged Recombinant Proteins**
The FLAG epitope tag is a widely utilized tool in molecular biology for the detection, purification, and characterization of recombinant proteins. Developed in the 1980s by researchers at the Harvard Medical School and commercialized by Sigma-Aldrich, the FLAG system employs a short, hydrophilic peptide sequence (DYKDDDDK) engineered onto target proteins. Its small size (8 amino acids) minimizes interference with protein folding or function, making it ideal for studying structurally sensitive proteins.
A key advantage of FLAG lies in its high-affinity interaction with monoclonal antibodies (e.g., M1. M2. and M5 clones), enabling precise immunoprecipitation, Western blotting, or immunofluorescence. Unlike larger tags (e.g., GST or GFP), FLAG’s compact design supports seamless integration into multi-tag systems, often combined with His-tags or HA-tags for orthogonal purification or detection.
FLAG-tagged proteins are commonly purified via affinity chromatography using antibody-conjugated resins. Notably, the FLAG sequence includes an enterokinase cleavage site (DDDDK), allowing tag removal post-purification to restore native protein structure. This feature is critical for functional assays or therapeutic applications requiring untagged proteins.
The system’s versatility extends to diverse applications: tracking protein expression in cell cultures, mapping protein-protein interactions, and facilitating structural studies (e.g., crystallography). Its commercial availability in plasmid vectors and optimized kits has cemented FLAG as a staple in both academic and industrial research.
Despite its benefits, challenges include potential non-specific antibody binding and costs associated with proprietary reagents. Nonetheless, ongoing innovations in epitope tag engineering continue to enhance FLAG’s utility, ensuring its prominence in recombinant protein workflows.
×
