| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLA2G2E |
| Uniprot No | Q9NZK7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDWCCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNLGTYNRKYAHYPNKLCTGPTPPC |
| 预测分子量 | 16.1kDa |
| 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gE重组蛋白的模拟参考文献示例(仅供参考，建议通过学术数据库获取真实文献)：
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1. **文献名称**：*Expression and Immunogenicity of a Recombinant gE Protein of Varicella-Zoster Virus in a Mammalian Cell System*
**作者**：Smith A, et al.
**摘要**：本研究通过哺乳动物细胞系统表达并纯化了VZV的gE重组蛋白，证实其具有高免疫原性，可诱导小鼠模型产生中和抗体，为亚单位疫苗开发提供实验基础。
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2. **文献名称**：*Development of a gE-Specific ELISA Using Recombinant Protein for Serodiagnosis of Herpes Simplex Virus Infection*
**作者**：Chen L, et al.
**摘要**：利用大肠杆菌表达系统制备HSV-1的gE重组蛋白，并建立ELISA检测方法，验证其在临床血清样本中特异性识别HSV抗体的能力，提高诊断准确性。
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3. **文献名称**：*Structural Analysis of gE/gI Complex in Pseudorabies Virus: Implications for Viral Cell-to-Cell Spread*
**作者**：Zhao Y, et al.
**摘要**：通过重组gE与gI蛋白共表达，解析了伪狂犬病毒中gE/gI复合体的晶体结构，揭示了其介导病毒细胞间传播的分子机制，为抗病毒药物设计提供靶点。
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4. **文献名称**：*Recombinant gE Protein of Cytomegalovirus Induces Protective T-Cell Responses in a Murine Model*
**作者**：Patel R, et al.
**摘要**：构建并纯化HCMV的gE重组蛋白，联合佐剂免疫小鼠，结果显示其可激活CD4+和CD8+ T细胞应答，为巨细胞病毒疫苗的细胞免疫策略提供依据。
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**注**：以上为模拟示例，实际文献需通过PubMed、Google Scholar等平台检索关键词(如“recombinant gE protein”“glycoprotein E vaccine”)获取。
**Background of gE Recombinant Protein**
Glycoprotein E (gE) is a structural protein encoded by herpesviruses, notably herpes simplex virus (HSV), varicella-zoster virus (VZV), and pseudorabies virus (PRV). It plays critical roles in viral pathogenesis, immune evasion, and cell-to-cell spread. As a type I transmembrane protein, gE typically forms heterodimers with glycoprotein I (gI), facilitating viral entry into host cells, modulation of host immune responses, and intracellular trafficking.
The development of recombinant gE (rgE) leverages genetic engineering to express purified gE in vitro, often using mammalian, insect, or bacterial expression systems. Recombinant technology allows for the production of gE with high specificity and consistency, avoiding risks associated with live-virus handling. This approach has been pivotal in studying gE’s functional domains, receptor interactions, and its role in immune evasion mechanisms, such as binding to Fc regions of antibodies to inhibit complement activation.
Clinically, rgE has significant applications. In diagnostics, it serves as a target antigen in serological assays to detect past infections or vaccine-induced immunity. For example, the VZV gE-based ELISA is widely used to assess immunity against chickenpox and shingles. In vaccinology, rgE is a key component of subunit vaccines. The FDA-approved Shingrix® vaccine against shingles contains recombinant VZV gE combined with an adjuvant, demonstrating over 90% efficacy in preventing herpes zoster.
Research on rgE also extends to antiviral therapies. Studies explore its potential as a target for monoclonal antibodies or small-molecule inhibitors to block viral entry or spread. Additionally, rgE is utilized in basic virology to dissect viral assembly pathways and host-pathogen interactions.
Overall, gE recombinant protein represents a convergence of virology, immunology, and biotechnology, driving advancements in diagnostics, vaccine development, and therapeutic strategies against herpesvirus infections.
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