| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UL32 |
| Uniprot No | P08318 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-285aa |
| 氨基酸序列 | MSLQFIGLQRRDVVALVNFLRHLTQKPDVDLEAHPKILKKCGEKRLHRRTVLFNELMLWLGYYRELRFHNPDLSSVLEEFEVRCVAVARRGYTYPFGDRGKARDHLAVLDRTEFDTDVRHDAEIVERALVSAVILAKMSVRETLVTAIGQTEPIAFVHLKDTEVQRIEENLEGVRRNMFCVKPLDLNLDRHANTALVNAVNKLVYTGRLIMNVRRSWEELERKCLARIQERCKLLVKELRMCLSFDSNYCRNILKHAVENGDSADTLLELLIEDFDIYVDSFPQS |
| 预测分子量 | 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UL32重组蛋白的3篇示例性参考文献(注：文献为示例性质，非真实存在)：
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1. **文献名称**：*Recombinant UL32 Protein of Human Cytomegalovirus Facilitates Viral Assembly*
**作者**：A. Smith et al.
**摘要**：研究通过大肠杆菌表达系统获得重组UL32蛋白，证实其在体外促进病毒衣壳与内膜蛋白的相互作用，揭示了UL32在病毒颗粒组装中的关键支架功能。
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2. **文献名称**：*Immunogenicity of UL32 Recombinant Protein in Murine Models*
**作者**：B. Lee & C. Wang
**摘要**：评估重组UL32蛋白作为疫苗候选的潜力，实验表明其可诱导小鼠产生中和抗体，并增强T细胞免疫应答，提示其在抗巨细胞病毒疫苗开发中的应用前景。
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3. **文献名称**：*Structural Characterization of UL32 Recombinant Protein by X-ray Crystallography*
**作者**：M. Garcia et al.
**摘要**：通过晶体学解析UL32重组蛋白的N端结构域，发现其具有独特的α螺旋构象，为设计靶向UL32的抗病毒药物提供了分子基础。
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**备注**：实际研究中建议通过PubMed、Google Scholar等平台，以关键词“UL32 recombinant protein”“HCMV pp150”或“cytomegalovirus UL32”检索最新文献。真实研究多聚焦于UL32(pp150)在病毒复制、宿主相互作用及疫苗/诊断试剂开发中的角色。
**Background on UL32 Recomcombinant Protein**
The UL32 protein, encoded by human cytomegalovirus (HCMV), is a critical structural component of the viral tegument, a layer between the capsid and envelope that facilitates viral assembly, egress, and host-cell interactions. UL32. also known as pp150. is unique to betaherpesviruses and is essential for virion maturation. It interacts with capsid components, stabilizing the nucleocapsid during cytoplasmic envelopment, and aids in tegumentation by scaffolding other viral proteins.
Recombinant UL32 is produced using expression systems (e.g., *E. coli*, baculovirus, or mammalian cells*) to study its structural and functional roles. Its modular architecture includes conserved acidic and proline-rich domains, which mediate protein-protein interactions critical for viral replication. Research on recombinant UL32 has advanced understanding of HCMV’s life cycle, particularly in tegument assembly and secondary envelopment.
Studies using UL32 recombinant proteins have also explored its immunogenicity, revealing potential as a diagnostic antigen or vaccine candidate. UL32-specific antibodies and T-cell responses are detected in HCMV-infected individuals, highlighting its relevance in immune surveillance. Additionally, UL32’s interactions with host factors, such as components of the nuclear egress complex, underscore its role in subverting cellular defenses.
Despite progress, challenges remain in resolving UL32’s full 3D structure and its dynamic interactions during infection. Recombinant UL32 tools continue to support antiviral drug discovery, aiming to disrupt tegument formation—a promising therapeutic target. Overall, UL32 remains a focal point in HCMV research, bridging virology, immunology, and drug development.
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