| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UL132 |
| Uniprot No | P69339 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 157-270aa |
| 氨基酸序列 | SPYQRLETRDWDEEEEASAARERMKHDPENVIYFRKDGNLDTSFVNPNYGRGSPLTIESHLSDNEEDPIRYYVSVYDELTASEMEEPSNSTSWQIPKLMKVAMQPVSLRDPEYD |
| 预测分子量 | 61.1 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HCMV UL132重组蛋白的3篇参考文献示例(注：部分文献信息为模拟概括，实际引用时请核实原文)：
1. **"Characterization of Human Cytomegalovirus UL132 Recombinant Protein and Its Role in Viral Tropism"**
*作者：Smith A, et al. (2018)*
摘要：研究利用重组UL132蛋白分析其与宿主细胞表面受体相互作用，证实其在病毒内皮细胞嗜性中的关键作用，并揭示其与整合素αVβ3的结合能力。
2. **"Structural and Functional Analysis of HCMV UL132-Encoded Glycoprotein Expressed in Mammalian Cells"**
*作者：Zhang Y, et al. (2020)*
摘要：通过哺乳动物系统表达重组UL132蛋白并进行结构解析，发现其C端结构域对病毒粒子组装至关重要，并证明其可诱导中和抗体反应。
3. **"Recombinant UL132 Protein of Human Cytomegalovirus Modulates Innate Immune Response in Dendritic Cells"**
*作者：Lee J, et al. (2021)*
摘要：研究重组UL132蛋白对树突状细胞TLR信号通路的影响，发现其通过抑制IRF3磷酸化削弱I型干扰素产生，提示其在免疫逃逸中的作用。
**备注**：上述文献为领域典型研究方向模拟，实际文献需通过PubMed或Google Scholar以关键词“HCMV UL132 recombinant”检索。近期研究可能侧重其与病毒潜伏感染、疫苗开发或宿主互作机制的关联。
UL132 recombinant protein is derived from the UL132 gene of human cytomegalovirus (HCMV), a betaherpesvirus with widespread global prevalence. HCMV establishes lifelong latent infections and poses significant risks to immunocompromised individuals, transplant recipients, and neonates. The UL132 gene encodes a glycoprotein that is part of the virion envelope and plays a role in viral entry, cell tropism, and immune evasion. While its exact mechanistic functions remain under investigation, UL132 is implicated in interactions with host cell receptors, facilitating viral attachment and entry, particularly in endothelial and epithelial cells.
Recombinant UL132 protein is typically produced using expression systems like mammalian cells or bacteria, followed by purification to retain its antigenic and structural properties. It serves as a critical tool for studying HCMV pathogenesis, host-virus interactions, and neutralizing antibody responses. Researchers utilize UL132 recombinant protein to dissect its role in viral entry, map antibody-binding epitopes, and evaluate its potential as a diagnostic marker or vaccine component. Studies suggest that UL132 may contribute to immune evasion by modulating host cell signaling pathways or interfering with antigen presentation.
Additionally, UL132 is part of the HCMV pentameric complex (gH/gL/UL128-UL130-UL131A), essential for infecting non-fibroblast cells. This complex is a major target for neutralizing antibodies, making UL132 recombinant protein valuable in vaccine development. Its inclusion in subunit vaccines aims to elicit robust immune responses to block viral entry into diverse cell types. However, challenges remain in maintaining the native conformation of recombinant UL132. as its antigenicity is highly dependent on proper folding and post-translational modifications. Ongoing research continues to explore its structural and functional nuances to advance therapeutic strategies against HCMV.
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