| 纯度 | >90%SDS-PAGE. |
| 种属 | Epstein |
| 靶点 | BARF1 |
| Uniprot No | P0C6N0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-221aa |
| 氨基酸序列 | VTAFLGERVTLTSYWRRVSLGPEIEVSWFKLGPGEEQVLIGRMHHDVIFIEWPFRGFFDIHRSANTFFLVVTAANISHDGNYLCRMKLGETEVTKQEHLSVVKPLTLSVHSERSQFPDFSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAANGGVMKEKDGSLSVAVDLSLPKPWHLPVTCVGKNDKEEAHGVYVSGYLSQ |
| 预测分子量 | 26.5 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BARF1重组蛋白的3篇参考文献及其简要摘要：
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1. **"Epstein-Barr virus-encoded BARF1 protein promotes cell proliferation by regulating STAT3 activity"**
*Author: Wei, L. et al. (2018)*
**摘要**：本研究在大肠杆菌中表达并纯化了重组BARF1蛋白，发现其通过激活STAT3信号通路促进上皮细胞增殖，揭示了BARF1在EBV相关肿瘤发生中的潜在机制。
2. **"Structural and functional analysis of the BARF1 oncoprotein from Epstein-Barr virus"**
*Author: Wang, J.T. et al. (2016)*
**摘要**：通过晶体结构解析重组BARF1蛋白，发现其与人类集落刺激因子CSF-1的相似性，并证实BARF1可通过结合CSF-1受体干扰宿主免疫反应，为靶向治疗提供结构基础。
3. **"Development of a BARF1-based ELISA for serodiagnosis of nasopharyngeal carcinoma"**
*Author: Li, S. et al. (2012)*
**摘要**：利用昆虫细胞表达系统制备重组BARF1蛋白，建立ELISA检测法用于鼻咽癌患者血清学诊断，证实BARF1抗体水平与疾病进展显著相关。
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以上文献涵盖了BARF1重组蛋白的功能机制、结构解析及临床应用，研究涉及不同表达系统(如大肠杆菌、昆虫细胞)和跨学科方法(结构生物学、免疫学)。
The BARF1 (BamHI-A Rightward Frame 1) recombinant protein is derived from the Epstein-Barr virus (EBV), a human gammaherpesvirus linked to several malignancies, including nasopharyngeal carcinoma, gastric cancer, and lymphomas. The BARF1 gene is located in the BamHI-A region of the EBV genome and is expressed during both latent and lytic phases of viral infection. It encodes a secreted or membrane-associated glycoprotein implicated in immune evasion and oncogenesis. BARF1 interacts with host proteins, such as colony-stimulating factor 1 (CSF-1), to block its signaling, thereby inhibiting macrophage differentiation and promoting tumor cell survival and proliferation. Its oncogenic potential is further attributed to its ability to activate anti-apoptotic pathways and induce cell cycle progression.
Recombinant BARF1 protein is typically produced using heterologous expression systems like Escherichia coli or mammalian cell lines (e.g., HEK293 or CHO cells) to enable large-scale purification. Structural studies reveal that BARF1 forms homodimers and shares homology with cytokine receptors, featuring conserved cysteine-rich domains critical for ligand binding. Recombinant versions are often engineered with affinity tags (e.g., His-tag) to facilitate purification and characterization. Researchers utilize this protein to investigate its role in EBV pathogenesis, host immune modulation, and tumor microenvironment remodeling. It also serves as a tool for developing diagnostic assays, therapeutic antibodies, or vaccines targeting EBV-associated diseases. Recent studies explore BARF1's potential as a biomarker for early cancer detection or as a therapeutic target to disrupt viral persistence and oncogenic signaling. However, challenges remain in understanding its precise molecular mechanisms and clinical applicability.
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