| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | U51 |
| Uniprot No | P52542 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-301aa |
| 氨基酸序列 | MEKETKSLAWPATAEFYGWVFIFSSIQLCTVVFLTVRFNGFKVGREYAVFTFAGMSFNCFLLPIKMGLLSGHWTLPRDFCAILLYIDDFSAYFSSWSLVFMAIERINYFCYSTPLLNENSKALAKVCFPIVWVVSGVQALQMLNNYKATALQNETGQCFLAFLRSGHDMWLMLVYSVVIPVMLVFFYLYSKNFMLLKDELSSVTTYLCIYLLLGTIAHLPKAALSEIESDKIFYGLRDIFMALPVLKVYYISAMAYCMACDDHTVPVRLCSIWLVNLCKKCFSCTRREKGSDLEVGIKMLK |
| 预测分子量 | 37.3 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U51重组蛋白的3篇代表性文献摘要信息(注：文献标题与作者为模拟示例，具体文献需通过学术数据库核实)：
1. **文献名称**：Functional characterization of the HHV-8-encoded chemokine receptor U51
**作者**：Smith A, et al.
**摘要**：该研究通过重组表达HHV-8病毒U51蛋白，证实其作为趋化因子受体的功能，可激活G蛋白信号通路并调控宿主细胞炎症反应，为病毒免疫逃逸机制提供依据。
2. **文献名称**：Structural analysis of recombinant U51 protein from human herpesvirus 6B
**作者**：Li X, et al.
**摘要**：利用昆虫细胞系统表达并纯化重组U51蛋白，通过冷冻电镜解析其三维结构，揭示其跨膜结构域与趋化因子结合的分子基础，为抗病毒药物设计提供结构模型。
3. **文献名称**：U51 recombinant protein modulates calcium signaling in transfected cells
**作者**：Garcia-Ruiz C, et al.
**摘要**：研究显示，重组表达的U51蛋白可诱导宿主细胞内钙离子浓度升高，并通过MAPK通路促进细胞迁移，提示其在病毒致病过程中的潜在作用。
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**提示**：实际文献需通过PubMed、Web of Science等平台以关键词“U51 recombinant protein”或“HHV U51”检索获取，并优先选择近5年发表的高影响力期刊论文。
U51 recombinant protein is a genetically engineered protein derived from the U51 gene encoded by human herpesvirus 6 (HHV-6) or its homologs in related herpesviruses. As a member of the G protein-coupled receptor (GPCR) family, U51 plays a critical role in viral pathogenesis and immune modulation. It is implicated in immune evasion by interacting with host chemokines, disrupting normal chemotactic signaling, and promoting viral latency or reactivation. The recombinant form is typically expressed in heterologous systems like *E. coli* or mammalian cells, enabling structural and functional studies.
Research on U51 focuses on its dual role as a viral virulence factor and a potential therapeutic target. Structurally, it features seven transmembrane domains characteristic of GPCRs, with extracellular loops mediating ligand binding. Studies reveal its ability to bind chemokines such as CCL2 and CCL5. interfering with immune cell recruitment. This interaction may contribute to HHV-6-associated diseases, including encephalitis and chronic fatigue syndrome. Additionally, U51 modulates intracellular signaling pathways, including MAPK and NF-κB, influencing both viral replication and host inflammatory responses.
The development of U51 recombinant protein has facilitated drug discovery efforts, particularly in screening inhibitors that block its chemokine-binding sites. Its unique mechanism of immune interference also provides insights into broader GPCR biology and viral-host coevolution. However, challenges remain in fully elucidating its in vivo conformational dynamics and tissue-specific effects. Current applications extend to diagnostic tools for detecting HHV-6 antibodies and experimental models studying neurotropic viral infections. Ongoing research aims to clarify its role in viral latency cycles and explore its potential as a biomarker for herpesvirus-associated pathologies.
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