| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLIP1 |
| Uniprot No | A9UHW6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222 |
| 氨基酸序列 | MGEPSREEYK IQSFDAETQQ LLKTALKDPG AVDLEKVANV IVDHSLQDCV FSKEAGRMCY AIIQAESKQA GQSVFRRGLL NRLQQEYQAR EQLRARSLQG WVCYVTFICN IFDYLRVNNM PMMALVNPVY DCLFRLAQPD SLSKEEEVDC LVLQLHRVGE QLEKMNGQRM DELFVLIRDG FLLPTGLSSL AQLLLLEIIE FRAAGWKTTP AAHKYYYSEV SD |
| 预测分子量 | 25.5kDa |
| 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gD重组蛋白的3篇代表性文献示例(内容为模拟生成，仅供参考)：
1. **文献名称**: "Recombinant glycoprotein D vaccine for the prevention of genital HSV-2 infection"
**作者**: Corey L. et al.
**摘要**: 该研究报道了一种基于HSV-2 gD重组蛋白的疫苗临床试验，证明其在预防生殖器疱疹感染中的有效性。实验显示，疫苗可诱导高水平中和抗体，并显著降低HSV-2血清阴性人群的发病率。
2. **文献名称**: "Expression and purification of functional herpes simplex virus glycoprotein D in insect cells"
**作者**: Kuo T. et al.
**摘要**: 本文开发了一种利用杆状病毒-昆虫细胞系统高效表达HSV-1 gD重组蛋白的方法，并通过亲和层析纯化获得高纯度蛋白。功能实验证实该重组蛋白保留与受体nectin-1结合的能力，适用于疫苗开发。
3. **文献名称**: "Structural analysis of glycoprotein D-herpesvirus entry mediator complex by X-ray crystallography"
**作者**: Carfí A. et al.
**摘要**: 通过X射线晶体学解析了HSV gD重组蛋白与其宿主受体HVEM的复合物结构，揭示了gD的受体结合域构象变化，为设计阻断病毒进入的小分子药物提供了结构基础。
*注：以上文献信息为示例性内容，实际引用需以正式出版物为准。建议通过PubMed或Web of Science检索最新研究。*
**Background of gD Recombinant Protein**
The glycoprotein D (gD) is a critical envelope component of herpes simplex viruses (HSVs), primarily HSV-1 and HSV-2. which are associated with oral and genital herpes infections. As a viral surface protein, gD plays an essential role in viral entry by mediating attachment and fusion to host cells. It interacts with specific cell receptors, such as nectin-1. HVEM (herpesvirus entry mediator), and 3-O-sulfated heparan sulfate, initiating conformational changes that facilitate viral membrane fusion and cytoplasmic entry. This receptor-binding function makes gD a key target for neutralizing antibodies and antiviral strategies.
Recombinant gD protein, produced via genetic engineering in heterologous systems (e.g., bacterial, insect, or mammalian cells), retains the antigenic properties of native gD while eliminating infectious risks. Its production often involves cloning the *gD gene* into expression vectors, followed by purification using chromatographic techniques. The recombinant protein has been extensively studied for its immunogenicity, demonstrating the ability to elicit potent humoral and cellular immune responses in preclinical and clinical settings.
Clinically, recombinant gD has been a cornerstone in HSV vaccine development. For example, the HSV-2 glycoprotein D2 subunit vaccine, combined with adjuvants like AS04. showed partial efficacy in reducing symptomatic genital herpes in clinical trials. Beyond vaccines, gD recombinant protein serves as a diagnostic tool in serological assays to detect HSV-specific antibodies. Additionally, it is utilized in basic research to dissect viral entry mechanisms and host-pathogen interactions.
Despite advancements, challenges remain, such as optimizing gD-based vaccines for broader protection and overcoming viral immune evasion strategies. Nonetheless, gD recombinant protein remains a vital molecule in virology, bridging therapeutic innovation and fundamental research in herpesvirus biology.
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