| 纯度 | >90%SDS-PAGE. |
| 种属 | E.col |
| 靶点 | BLLF3 |
| Uniprot No | K9US42 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-278aa |
| 氨基酸序列 | MEACPHIRYAFQNDKLLLQQASVGRLTLVNKTTILLRPMKTTTVDLGLYARPPEGHGLMLWGSTSRPVTSHVGIIDPGYTGELRLILQNQRRYNSTLRPSELKIHLAAFRYATPQMEEDKGPINHPQYPGDVGLDVSLPKDLALFPHQTVSVTLTVPPPSIPHHRPTIFGRSGLAMQGILVKPCRWRRGGVDVSLTNFSDQTVFLNKYRRFCQLVYLHKHHLTSFYSPHSDAGVLGPRSLFRWASCAFEEVPSLAMGDSGLSEALEGRQGRGFGSSGQ |
| 预测分子量 | 46.9 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BLLF3重组蛋白的假设性参考文献示例(仅供参考，具体文献需通过学术数据库验证)：
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1. **文献名称**：*Epstein-Barr Virus BLLF3 Protein Interacts with Human USP47 to Modulate Immune Evasion*
**作者**：Horst D, et al.
**摘要**：研究通过重组表达EBV BLLF3蛋白，发现其与宿主去泛素化酶USP47结合，抑制MHC II类分子抗原递呈，揭示其在病毒免疫逃逸中的机制。
2. **文献名称**：*Structural Characterization of Recombinant BLLF3 Glycoprotein in EBV Entry*
**作者**：Ressing ME, et al.
**摘要**：利用哺乳动物系统表达重组BLLF3蛋白，解析其结构并证明其与宿主细胞表面受体相互作用，促进EBV侵入宿主细胞的分子机制。
3. **文献名称**：*Recombinant BLLF3 as a Target for Neutralizing Antibodies Against EBV*
**作者**：Wang X, et al.
**摘要**：通过重组BLLF3蛋白免疫动物模型，筛选出中和抗体，验证其在体外抑制EBV感染的作用，为疫苗开发提供潜在靶点。
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**提示**：以上文献为示例性质，实际研究中请通过**PubMed/Google Scholar**以关键词“BLLF3 recombinant”、“EBV BLLF3”检索最新文献，并优先选择近5年发表的高影响力期刊论文。
The BLLF3 recombinant protein is derived from the Epstein-Barr virus (EBV), a γ-herpesvirus linked to infectious mononucleosis and malignancies such as Burkitt’s lymphoma and nasopharyngeal carcinoma. BLLF3. a glycoprotein encoded by the BLLF3 gene, is implicated in viral entry and immune evasion. It interacts with host cell receptors, potentially facilitating viral attachment and entry. Studies suggest its role in modulating immune responses, including binding to MHC class II molecules on immune cells, which may help EBV evade immune detection.
Recombinant BLLF3 is engineered using expression systems like Escherichia coli or mammalian cells to produce purified protein for research. Its production enables structural and functional studies, particularly in understanding EBV pathogenesis. Researchers utilize it to map antigenic epitopes, investigate host-virus interactions, and explore immune evasion mechanisms. Additionally, recombinant BLLF3 serves as a tool in diagnostic assays, vaccine development, and therapeutic targeting. Structural analyses via X-ray crystallography or cryo-EM aim to clarify its molecular architecture, guiding antiviral drug design.
Interest in BLLF3 also extends to immunotherapy, as it may contribute to EBV-associated oncogenesis. By studying its interactions with immune checkpoints or signaling pathways, scientists seek strategies to block viral persistence or tumor progression. Despite progress, challenges remain in fully elucidating its biological roles and therapeutic potential, underscoring the need for continued interdisciplinary research in virology, immunology, and molecular engineering.
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