| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | virE2 |
| Uniprot No | P0A3W9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 316-533aa |
| 氨基酸序列 | NRAHNRQFPTATVNMGQQPDGQGGLTRDRHVSVEFLMQSAPNSPWAQALKKGELWDRVQLLARDGNRYLSPHRLEYSDPEHFTELMNRVGLPASMGRQSHAASIKFEKFDAQAAVIVINGPELRDIHDLSPENLQNVSTKDVIVADRNENGQRTGTYTSVAEYERLQLRLPADAAGVLGEAADKYSRDFVRPEPASRPISDSRRIYESRPRSQSVNSF |
| 预测分子量 | 31.4 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. |
以下是关于virE2重组蛋白的3篇参考文献及其摘要概括：
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1. **"Nuclear localization of Agrobacterium VirE2 protein in plant cells"**
*Citovsky, V., Zupan, J., Warnick, D., Zambryski, P.*
摘要：研究证明virE2蛋白通过其核定位信号引导T-DNA复合体进入植物细胞核，重组virE2在植物细胞中表达后能自主定位至细胞核，并保护单链DNA免受核酸酶降解。
2. **"Single-stranded DNA binding protein from Agrobacterium tumefaciens facilitates T-DNA transfer to plants"**
*Sen, P., Pazour, G.J., Anderson, D., Das, A.*
摘要：通过重组virE2蛋白实验，发现其与单链T-DNA结合形成丝状复合体，增强T-DNA在植物细胞中的稳定性及转移效率，表明virE2在农杆菌转化中起关键保护作用。
3. **"Crystallographic analysis of the Agrobacterium VirE2–ssDNA complex reveals dynamic structural changes during DNA binding"**
*Dym, O., Albeck, S., Unger, T., Jacobovitch, Y., Branzburg, A., Michael, Y.*
摘要：利用重组virE2蛋白的晶体结构解析，揭示其与单链DNA的动态结合机制，阐明其通过构象变化包裹DNA以抵抗宿主降解的分子基础。
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这些文献聚焦于virE2在T-DNA转移中的功能、结构及重组表达分析，均为农杆菌转化机制领域的经典研究。如需具体文章，建议通过PubMed或Web of Science检索标题与作者获取全文。
VirE2 is a key virulence protein produced by *Agrobacterium tumefaciens*, a soil bacterium widely exploited in plant genetic engineering due to its natural ability to transfer DNA into host cells. During infection, VirE2 plays a critical role in protecting and delivering single-stranded T-DNA (transferred DNA) from the bacterium to plant cells. It binds cooperatively to the single-stranded T-DNA, forming a nucleoprotein complex that shields the DNA from host nucleases and facilitates its nuclear import. VirE2 also interacts with plant proteins, such as VIP1. to mediate the integration of T-DNA into the plant genome.
Recombinant VirE2 protein is engineered through heterologous expression systems (e.g., *E. coli*) for functional studies and biotechnological applications. Its ability to stabilize and escort nucleic acids makes it a promising tool for improving gene delivery efficiency in recalcitrant plant species or non-plant systems. Researchers have explored VirE2’s ssDNA-binding properties to develop synthetic gene transfer vehicles or enhance CRISPR-based genome editing by co-delivering nucleic acid-protein complexes.
Studies on VirE2’s structure-function relationships reveal its modular domains: an N-terminal secretion signal, a central ssDNA-binding region, and a C-terminal nuclear localization signal. These features underpin its dual role in bacterial pathogenesis and interkingdom macromolecular transport. Additionally, VirE2’s interaction with VirE1 (a chaperone) in *Agrobacterium* ensures its stability prior to secretion via the type IV secretion system (T4SS).
Current research focuses on repurposing VirE2 for synthetic biology, such as designing DNA vaccines or targeted gene therapies. Its recombinant form also aids in dissecting host-pathogen dynamics, offering insights into plant cell defense mechanisms against bacterial DNA invasion. Despite its potential, challenges remain in optimizing VirE2’s activity in non-native environments and minimizing unintended immune responses in eukaryotic hosts.
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