| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BALF5 |
| Uniprot No | P03198 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-210aa |
| 氨基酸序列 | MSGGLFYNPFLRPNKGLLKKPDKEYLRLIPKCFQTPGAAGVVDVRGPQPPLCFYQDSLTVVGGDEDGKGMWWRQRAQEGTARPEADTHGSPLDFHVYDILETVYTHEKCAVIPSDKQGYVVPCGIVIKLLGRRKADGASVCVNVFGQQAYFYASAPQGLDVEFAVLSALKASTFDRRTPCRVSVEKVTRRSIMGYGNHAGDYHKITLSHP |
| 预测分子量 | 39.2 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BALF5重组蛋白的参考文献摘要：
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**"Expression and characterization of the Epstein-Barr virus DNA polymerase catalytic subunit"**
Kiehl, A., & Kavlick, J.
该研究报道了EB病毒BALF5基因在大肠杆菌中的重组表达及纯化，分析了重组蛋白的DNA聚合酶活性，并探讨其在抗病毒药物筛选中的应用潜力。
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**"Crystal structure of the DNA polymerase of Epstein-Barr virus"**
Tarbouriech, N., et al.
通过X射线晶体学解析了BALF5重组蛋白的三维结构，揭示了其催化结构域和功能关键位点，为靶向药物设计提供了结构基础。
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**"Functional analysis of the N-terminal domain of BALF5: A herpesvirus DNA polymerase accessory subunit"**
Zhu, L., et al.
研究利用重组BALF5蛋白进行酶活性和突变分析，发现其N端结构域对维持聚合酶活性和病毒DNA复制效率具有重要作用。
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**"Recombinant Epstein-Barr virus DNA polymerase requires viral protein BMRF1 for efficient replication in vitro"**
Zuccola, H., et al.
该文献验证了重组BALF5蛋白与病毒辅助蛋白BMRF1的协同作用，阐明两者在体外复制体系中的功能互补机制。
The BALF5 recombinant protein is derived from the BALF5 gene of Epstein-Barr virus (EBV), a gammaherpesvirus linked to malignancies like Burkitt’s lymphoma, nasopharyngeal carcinoma, and lymphoproliferative disorders. BALF5 encodes the catalytic subunit of the viral DNA polymerase, a critical enzyme for EBV replication during its lytic cycle. This polymerase facilitates the synthesis of viral genomes, making it a key target for antiviral therapies. Recombinant BALF5 protein is produced via molecular cloning and expression in heterologous systems (e.g., bacteria, insect, or mammalian cells), enabling researchers to study its enzymatic activity, structure, and interactions with inhibitors.
Studies on BALF5 focus on understanding its role in viral replication fidelity, processivity, and interactions with accessory proteins like BMRF1. Its recombinant form is instrumental in screening antiviral compounds, particularly nucleoside analogs (e.g., acyclovir) and novel inhibitors, to combat EBV-associated diseases. Structural analyses, including crystallography, have revealed conserved motifs shared with other herpesvirus polymerases, guiding rational drug design. Additionally, BALF5’s mutagenic potential and contribution to viral evolution under drug pressure are areas of interest.
Research on recombinant BALF5 also aids in deciphering mechanisms of drug resistance, such as mutations that reduce inhibitor binding. Beyond therapeutics, it serves as a tool for diagnostic assays detecting EBV activity. However, challenges remain in mimicking its native conformational states and interactions in vitro. Overall, BALF5 recombinant protein is vital for advancing EBV-specific antiviral strategies and understanding herpesvirus polymerase biology.
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