| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | U27 |
| Uniprot No | P52439 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-393aa |
| 氨基酸序列 | MCWSFHLFFKAHKARVGARTSFLTEMERGSRDHHRDHRDHREHRETREPPTLAFHMKSWKTINKSLKAFAKLLKENTTVTFTPQPSIIIQSAKNHLVQKLTIQAECLFLSDTDRFLTKTINNHIPLFESFMNIISNPEVTKMYIQHDSDLYTRVLVTASDTCTQASVPCVHGQEVVRDTGRSPLRIDLDHSTVSDVLKWLSPVTKTKRSGKSDALMAHIIVQVNPPTIKFVTEMNELEFSNSNKVIFYDVKNMRFNLSAKNLQQALSMCAVIKTSCSLRTVAAKDCKLILTSKSTLLTVEAFLTQEQLKEESRFERMGKQDDGKGDRSHKNDDGSALASKQEMQYKITNYMVPAKNGTAGSSLFNEKEDSESDDSMHFDYSSNPNPKRQRCVV |
| 预测分子量 | 46.8 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U27重组蛋白的参考文献示例(注：部分信息为示例性概括，建议通过学术数据库核实具体文献)：
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1. **文献名称**：*"Cloning and Expression of Recombinant U27 Protein from Human Herpesvirus 6B in Escherichia coli"*
**作者**：Smith J, et al.
**摘要**：本研究成功克隆并表达了HHV-6B U27基因的重组蛋白，通过大肠杆菌系统实现高效可溶性表达，并验证其ATP酶活性，为后续功能研究奠定基础。
2. **文献名称**：*"Functional Role of U27 Helicase in HHV-6 Viral Genome Replication"*
**作者**：Zhang L, et al.
**摘要**：通过体外重组U27蛋白实验，证实其具有DNA解旋酶活性，并参与病毒基因组复制过程，提示其作为抗病毒药物开发靶点的潜力。
3. **文献名称**：*"Structural Insights into U27 Recombinant Protein from HHV-6A Using Cryo-EM"*
**作者**：Wang Y, et al.
**摘要**：利用冷冻电镜技术解析了HHV-6A U27重组蛋白的三维结构，揭示了其ATP结合域的关键构象，为基于结构的药物设计提供依据。
4. **文献名称**：*"Immunogenicity Evaluation of Recombinant U27 Protein as a Vaccine Candidate Against HHV-6 Infection"*
**作者**：Kim S, et al.
**摘要**：在小鼠模型中评估重组U27蛋白的免疫原性，结果显示其可诱导特异性抗体和T细胞反应，提示其作为候选疫苗组分的可行性。
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**注意事项**：
- 上述文献信息为基于领域常见研究方向的模拟概括，实际文献需通过PubMed、Web of Science等平台以关键词“U27 recombinant protein”或“HHV-6 U27”检索确认。
- 若U27蛋白涉及其他物种或病毒(如疱疹病毒不同亚型)，建议明确具体研究对象以精准查询。
**Background of U27 Recombinant Protein**
The U27 recombinant protein is a genetically engineered molecule derived from the U27 gene, which is commonly associated with viral genomes, particularly in certain herpesviruses such as Human Herpesvirus 6 (HHV-6) and HHV-7. The U27 gene encodes a structural protein implicated in viral capsid assembly and maturation. In HHV-6. U27 is classified as a tegument protein, playing a role in mediating interactions between the viral capsid and envelope during virion morphogenesis. Its homologs in other herpesviruses, such as UL47 in HSV-1. share functional similarities, underscoring its conserved role in viral replication.
Recombinant U27 is produced using expression systems like *E. coli* or mammalian cell cultures, enabling large-scale purification for research applications. The protein’s recombinant form retains key antigenic epitopes, making it valuable for immunological studies, diagnostic assay development, and vaccine research. Studies leveraging U27 have focused on elucidating its interactions with host proteins, its role in immune evasion, and its potential as a therapeutic target. For instance, antibodies against U27 have been explored for neutralizing viral infectivity or diagnosing HHV-6-associated diseases like roseola and encephalitis.
Structural characterization of U27. aided by techniques like X-ray crystallography or cryo-EM, has provided insights into its conformational dynamics and binding interfaces. Additionally, U27’s involvement in viral latency and reactivation mechanisms highlights its significance in understanding herpesvirus persistence. Ongoing research aims to exploit U27’s immunogenic properties for novel antiviral strategies while addressing challenges related to cross-reactivity with other herpesvirus proteins. Overall, U27 recombinant protein serves as a critical tool in virology, bridging fundamental research and translational applications.
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