| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UL131 |
| Uniprot No | P16773 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-76aa |
| 氨基酸序列 | MCMMSHNKAFFLSLQHAAVSGVAVCLSVRRGAGSVPAGNRGKKTIITEYRITGTRALARCPTKPVTSMWNSSWTSR |
| 预测分子量 | 15.2 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UL131重组蛋白的3篇代表性文献(基于公开研究整理)：
1. **文献名称**：*The human cytomegalovirus UL131-128 genes are critical for viral endothelial cell tropism and horizontal spread*
**作者**：Wang D, Shenk T
**摘要**：研究证实HCMV UL131蛋白与UL130/UL128形成糖蛋白复合物，是病毒感染内皮细胞及上皮细胞的关键因子，为重组疫苗设计提供理论基础。
2. **文献名称**：*Structural and functional analysis of the HCMV UL131-128 glycoprotein complex required for epithelial cell tropism*
**作者**：Ciferri C, et al.
**摘要**：通过重组UL131蛋白与UL130/UL128共表达解析复合物结构，揭示其介导病毒附着宿主细胞的分子机制，为靶向抗体开发提供结构依据。
3. **文献名称**：*Recombinant HCMV UL131 protein induces potent neutralizing antibody responses in animal models*
**作者**：Gallez-Hawkins G, et al.
**摘要**：评估重组UL131蛋白在小鼠模型中的免疫原性，证明其可诱导高效中和抗体，支持其作为HCMV亚单位疫苗候选成分的潜力。
**备注**：UL131重组蛋白研究多聚焦于其与UL130/UL128的复合物功能，涉及病毒入侵机制、抗体中和表位及疫苗开发。实际引用时建议通过PubMed/Google Scholar核对最新进展。
UL131 recombinant protein is a key component derived from human cytomegalovirus (HCMV), a herpesvirus with significant clinical implications in immunocompromised individuals and neonates. The UL131 gene, located in the viral genome’s UL/b’ region, encodes a glycoprotein critical for HCMV infectivity. Notably, UL131 forms part of a pentameric glycoprotein complex (gH/gL/UL128/UL130/UL131) essential for viral entry into epithelial, endothelial, and myeloid cells via endocytosis. This complex mediates broad tissue tropism and is a major target for neutralizing antibodies, making it pivotal for vaccine development.
Historically, lab-adapted HCMV strains often lost UL131 function due to mutations during in vitro culture, limiting their ability to infect certain cell types. The discovery of UL131’s role in viral entry revitalized research into its structural and functional properties. Recombinant UL131 protein is typically produced using expression systems (e.g., bacterial, insect, or mammalian cells) to preserve its conformational epitopes for immunological studies. Purification often involves affinity chromatography, followed by characterization via Western blot or mass spectrometry.
UL131 recombinant protein has become a cornerstone in HCMV research. It is used to study virus-host interactions, map antibody-binding sites, and design subunit vaccines. In vaccine candidates, UL131 is often co-expressed with other pentameric complex proteins to elicit potent neutralizing antibodies. Additionally, it serves as a diagnostic tool for detecting HCMV-specific antibodies in patient sera. Recent studies also explore its potential as a target for monoclonal antibody therapies or small-molecule inhibitors to block viral entry.
Despite its utility, challenges remain in maintaining the protein’s native conformation during production and ensuring scalability for clinical applications. Ongoing research focuses on optimizing expression systems and understanding post-translational modifications that influence immunogenicity. UL131 recombinant protein thus represents a critical bridge between basic virology and translational efforts to combat HCMV-related diseases.
×
