| 纯度 | >90%SDS-PAGE. |
| 种属 | Epstein-Barr |
| 靶点 | BDLF3 |
| Uniprot No | P03224 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-186aa |
| 氨基酸序列 | SSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTFTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVPDERQPSLSYGLPLWT |
| 预测分子量 | 22.7 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BDLF3重组蛋白的3篇参考文献及其摘要内容的简要概括：
1. **文献名称**：*Structural and functional analysis of Epstein-Barr virus BDLF3 protein in viral capsid assembly*
**作者**：Smith A, et al.
**摘要**：该研究通过重组BDLF3蛋白的体外表达，揭示了其在EB病毒衣壳组装中的关键作用，证明了BDLF3与BORF1蛋白的相互作用对病毒颗粒形态形成的必要性。
2. **文献名称**：*Development of a recombinant BDLF2-BDLF3 fusion protein-based serological assay for EBV detection*
**作者**：Chen L, et al.
**摘要**：作者构建了BDLF3与BDLF2的重组融合蛋白，并评估其作为诊断抗原的潜力，结果显示其在ELISA检测中能高效识别EBV感染者血清中的特异性抗体。
3. **文献名称**：*Immunogenicity of recombinant BDLF3 protein in a murine model of EBV infection*
**作者**：Wang Y, et al.
**摘要**：研究通过表达纯化的重组BDLF3蛋白进行小鼠免疫实验，发现其能诱导强烈的T细胞应答和中和抗体，提示其在EBV疫苗开发中的潜在应用价值。
注：以上文献信息为示例性质，实际文献需通过学术数据库核实。若需具体文章，建议在PubMed或Web of Science中以关键词“BDLF3 recombinant protein”或“EBV BDLF3”检索。
The BDLF3 recombinant protein is derived from the BDLF3 gene encoded by Epstein-Barr virus (EBV), a gammaherpesvirus associated with malignancies such as nasopharyngeal carcinoma, Burkitt's lymphoma, and lymphoproliferative disorders. BDLF3. also referred to as EBV deubiquitinase (DUB), is a late lytic cycle protein implicated in immune evasion and viral maturation. It exhibits deubiquitinating activity, targeting both host and viral proteins to modulate cellular pathways. Specifically, BDLF3 interacts with the ubiquitin-proteasome system, counteracting host antiviral responses by destabilizing immune signaling molecules like MHC class I complexes, thereby aiding viral persistence.
Recombinant BDLF3 is typically expressed in bacterial or eukaryotic systems (e.g., E. coli or HEK293 cells) using plasmid vectors, followed by purification via affinity chromatography. Its production enables functional studies to elucidate mechanisms underlying EBV pathogenesis, particularly its role in immune modulation and viral replication. Researchers employ the protein to investigate structural features, enzymatic kinetics, and interactions with host proteins using techniques like X-ray crystallography, enzymatic assays, and co-immunoprecipitation. Additionally, BDLF3 serves as a tool for screening small-molecule inhibitors targeting its DUB activity, offering potential therapeutic avenues for EBV-associated diseases. Its recombinant form is also utilized in diagnostic assays to detect EBV-specific antibodies in patient sera, aiding clinical diagnosis. Despite progress, challenges remain in fully characterizing its in vivo functions and regulatory networks, necessitating further interdisciplinary research to exploit BDLF3 as a biomarker or therapeutic target.
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