纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | EBNA1 |
Uniprot No | Q1HVF7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 458-641aa |
氨基酸序列 | RRKKGGWYGKHRGEGGSSQKFENIAEGLRLLLARCHVERTTEDGNWVAGVFVYGGSKTSLYNLRRGIGLAIPQCRLTPLSRLPFGMAPGPGPQPGPLRESIVCYFIVFLQTHIFAEGLKDAIKDLVLPKPAPTCNIKVTVCSFDDGVDLPPWFPPMVEGAAAEGDDGDDGDEGGDGDEGEEGQE |
预测分子量 | 26.7 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. |
以下是关于EBNA1重组蛋白的3篇参考文献及其简要摘要:
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1. **文献名称**:*Crystal structure of the DNA-binding domain of the Epstein-Barr virus nuclear antigen 1*
**作者**:Bochkarev, A., et al.
**摘要**:该研究通过X射线晶体学解析了EBNA1重组蛋白的DNA结合域结构,揭示了其与病毒基因组中特定序列(*oriP*)结合的分子机制,并阐明了二聚化对功能的重要性。
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2. **文献名称**:*Recombinant EBNA1 protein integrates and supports replication of Epstein-Barr virus origin-based plasmids in human cells*
**作者**:Leight, E.R., Sugden, B.
**摘要**:研究利用重组EBNA1蛋白证明其在宿主细胞中维持EB病毒复制起点(*oriP*)依赖性质粒的复制和持久性,揭示了EBNA1在病毒潜伏感染中的关键作用。
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3. **文献名称**:*Expression and purification of Epstein-Barr virus EBNA1 protein from Drosophila Schneider cells*
**作者**:Frappier, L., O'Donnell, M.
**摘要**:该文献描述了一种利用果蝇Schneider细胞系统高效表达重组EBNA1蛋白的方法,并验证了其与DNA结合及自我组装的功能活性,为后续生化研究提供了可靠工具。
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以上文献涵盖了EBNA1重组蛋白的结构解析、功能验证及表达方法,适用于病毒学或蛋白质工程领域的研究参考。
Epstein-Barr virus nuclear antigen 1 (EBNA1) is a critical latent-phase protein encoded by the Epstein-Barr virus (EBV), a herpesvirus linked to malignancies like Burkitt's lymphoma, nasopharyngeal carcinoma, and autoimmune conditions. EBNA1 plays essential roles in viral genome replication and persistence during latency by binding to the viral origin of replication (oriP) and tethering EBV episomes to host chromosomes. Its unique structure includes a DNA-binding domain and a Gly-Ala repeat region that limits proteasomal degradation, enabling immune evasion.
Recombinant EBNA1 proteins are engineered using expression systems (e.g., *E. coli*, insect, or mammalian cells) for functional and clinical studies. Purification often involves affinity tags (e.g., His-tag) followed by chromatography. Recombinant EBNA1 retains key biological activities, including sequence-specific DNA binding and dimerization, making it valuable for studying EBV replication mechanisms, host interactions, and oncogenic pathways. It is also used in diagnostic assays to detect EBV-specific antibodies and in vaccine development efforts, as EBNA1's conserved epitopes are potential targets for T-cell immunity.
Research on recombinant EBNA1 has advanced understanding of EBV-associated diseases and inspired therapeutic strategies, such as inhibitors disrupting its DNA-binding activity. However, challenges remain in addressing its structural complexity and minimizing cross-reactivity with host proteins in diagnostics. Ongoing studies aim to refine its applications in virology, oncology, and immunology.
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