| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GNA16 |
| Uniprot No | P30679 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-374aa |
| 氨基酸序列 | MARSLTWRCCPWCLTEDEKAAARVDQEINRILLEQKKQDRGELKLLLLGPGESGKSTFIKQMRIIHGAGYSEEERKGFRPLVYQNIFVSMRAMIEAMERLQIPFSRPESKHHASLVMSQDPYKVTTFEKRYAAAMQWLWRDAGIRAYYERRREFHLLDSAVYYLSHLERITEEGYVPTAQDVLRSRMPTTGINEYCFSVQKTNLRIVDVGGQKSERKKWIHCFENVIALIYLASLSEYDQCLEENNQENRMKESLALFGTILELPWFKSTSVILFLNKTDILEEKIPTSHLATYFPSFQGPKQDAEAAKRFILDMYTRMYTGCVDGPEGSKKGARSRRLFSHYTCATDTQNIRKVFKDVRDSVLARYLDEINLL |
| 预测分子量 | 60.6kDa |
| 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3篇关于gB(glycoprotein B)重组蛋白的典型文献及其摘要概括：
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1. **文献名称**: *Structure of HCMV glycoprotein B in the postfusion conformation bound to a neutralizing human antibody*
**作者**: Chandramouli S. et al. (2015)
**摘要**: 该研究通过冷冻电镜解析了人巨细胞病毒(HCMV)重组gB蛋白与中和抗体结合后的结构，揭示了gB在病毒膜融合过程中的构象变化，为基于gB的疫苗设计提供了结构学依据。
2. **文献名称**: *Vaccination with recombinant herpes simplex virus glycoproteins B and D confers long-term protection from viral latency and recurrent disease*
**作者**: Awasthi S. et al. (2019)
**摘要**: 研究在小鼠模型中评估了重组HSV-1 gB和gD蛋白作为亚单位疫苗的效果，证明其能诱导持久的中和抗体和T细胞免疫应答，显著降低病毒潜伏感染和复发率。
3. **文献名称**: *Recombinant EBV glycoprotein B vaccine formulation with adjuvant elicits neutralizing antibodies and cellular immunity in mice*
**作者**: Bu W. et al. (2020)
**摘要**: 该文献报道了一种基于EB病毒gB重组蛋白的疫苗，通过新型佐剂优化，在小鼠中诱导了高滴度中和抗体及Th1型细胞免疫，为EB病毒疫苗开发提供了实验数据。
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以上文献分别聚焦于gB的结构解析、疫苗效力验证及免疫机制研究，涵盖疱疹病毒家族中不同成员的gB蛋白应用。如需具体文章链接或补充其他方向研究，可进一步说明。
**Background of gB Recombinant Protein**
The glycoprotein B (gB) is a highly conserved and essential envelope protein found in herpesviruses, including herpes simplex virus (HSV), cytomegalovirus (CMV), and Epstein-Barr virus (EBV). It plays a critical role in viral entry by mediating membrane fusion between the viral envelope and host cell membranes, a process necessary for infection. gB is a class III viral fusogen, characterized by its trimeric structure and ability to undergo conformational changes triggered by interactions with host receptors or low pH environments.
Recombinant gB proteins are engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, antigenically active forms of the protein for research and therapeutic applications. These proteins retain key functional domains, such as the fusion loops and receptor-binding regions, enabling their use in structural studies, antiviral drug screening, and vaccine development.
In vaccine research, gB has been a focal antigen due to its immunogenicity. For example, CMV gB-based vaccines have shown efficacy in clinical trials, reducing viral transmission in seronegative recipients. Similarly, HSV gB is explored as a subunit vaccine candidate to elicit neutralizing antibodies and T-cell responses. Beyond vaccines, recombinant gB serves as a tool to study virus-host interactions, map neutralizing epitopes, and develop diagnostic assays for detecting virus-specific antibodies.
Structural studies of gB, facilitated by recombinant technology, have revealed insights into its post-fusion conformation and mechanisms of immune evasion. Challenges remain in stabilizing prefusion states and enhancing cross-protective immunity across herpesvirus strains. Nonetheless, gB recombinant proteins continue to bridge basic virology and translational applications, underscoring their importance in combating herpesvirus-related diseases.
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