| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EE |
| Uniprot No | O95571 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 8-254aa |
| 氨基酸序列 | VARRQLSQRGGSGAPILLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA |
| 预测分子量 | 43.1 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篇与EE重组蛋白相关的文献示例(信息为模拟创作，仅供参考)：
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1. **文献名称**: *Optimized Expression and Purification of EE-tagged Recombinant Proteins in E. coli*
**作者**: Zhang, L., et al.
**摘要**: 研究通过优化大肠杆菌表达系统(诱导温度、培养基等)，显著提高了带有EE标签(6xHis标签)重组蛋白的产量和可溶性，为工业化生产提供参考。
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2. **文献名称**: *EE Fusion Proteins in Mammalian Systems: Applications for Vaccine Development*
**作者**: Gupta, R., & Lee, S.
**摘要**: 利用哺乳动物细胞表达系统(如HEK293)生产EE标记的重组抗原蛋白，验证其在动物模型中诱导高效免疫应答的能力，为疫苗设计提供新策略。
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3. **文献名称**: *Structural Analysis of EE-tagged Viral Envelope Proteins via Cryo-EM*
**作者**: Martinez, D., et al.
**摘要**: 通过昆虫细胞表达系统生产EE标签的病毒包膜蛋白，结合冷冻电镜技术解析其三维结构，揭示关键受体结合域构象变化机制。
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4. **文献名称**: *A Novel Affinity Chromatography Method for EE-tagged Protein Purification*
**作者**: Chen, X., & Wang, H.
**摘要**: 开发基于镍柱与新型缓冲液配方的EE标签蛋白纯化工艺，在保持蛋白活性的同时将纯化效率提升40%，适用于高纯度科研级蛋白制备。
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注：以上文献为示例性内容，实际文献需通过PubMed、Web of Science等平台检索关键词(如"His-tagged recombinant protein"、"affinity purification")。
EE recombinant proteins are engineered fusion proteins widely utilized in biomedical research and diagnostic applications, particularly for antibody detection and quality control. The term "EE" originates from their design, which combines two tandem exon-encoded epitopes derived from the Fc region of human IgG. These proteins are typically produced in prokaryotic systems (e.g., E. coli) using recombinant DNA technology, incorporating tags such as 6xHis for purification and identification.
Structurally, EE proteins retain high-affinity binding sites for Protein A, Protein G, and anti-Fc antibodies due to preserved conformational epitopes. This feature enables their use as universal detection reagents in immunoassays like ELISA, western blotting, and biosensor platforms. They serve as critical positive controls for validating antibody functionality and assessing assay performance across species (human, mouse, rabbit, etc.), overcoming limitations of full-length antibodies in stability and batch consistency.
In therapeutic antibody development, EE proteins facilitate Fc-mediated function studies and cross-species reactivity testing. Their small size (~20 kDa) enhances solubility and thermal stability compared to intact antibodies, while eliminating variability from light chain interactions. Recent applications extend to vaccine research, where they help evaluate antibody responses to Fc-dependent effector functions.
Commercial variants may include additional modifications like biotinylation or fluorescent labeling for multiplex detection systems. As standardized reagents, EE recombinant proteins address growing needs for reproducibility in biomedical research, particularly in pharmaceutical quality control and diagnostic kit manufacturing. Their design exemplifies rational protein engineering strategies to create multifunctional tools bridging basic research and industrial applications.
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