| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HVD3 |
| Uniprot No | P |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | aa |
| 氨基酸序列 | full |
| 预测分子量 | 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HVD3重组蛋白的3篇示例参考文献(注：HVD3相关研究较少，以下内容为假设性示例，建议通过学术数据库核实具体文献)：
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1. **文献名称**: "Structural and Functional Analysis of Herpesvirus Glycoprotein D HVD3 Domain"
**作者**: Smith J, et al.
**摘要**: 本研究解析了疱疹病毒糖蛋白D(gD)的第三高变区(HVD3)的晶体结构，揭示了其与细胞受体nectin-1的结合机制。通过重组蛋白表达和突变实验，证明HVD3在病毒入侵宿主细胞过程中起关键作用，为抗病毒药物设计提供结构基础。
2. **文献名称**: "Recombinant HVD3 Protein as a Vaccine Candidate for HSV-2 Infection"
**作者**: Lee S, et al.
**摘要**: 研究利用大肠杆菌表达系统制备了重组HVD3蛋白，并在小鼠模型中验证其免疫原性。结果显示，HVD3重组蛋白可诱导中和抗体，显著降低疱疹病毒2型(HSV-2)感染后的病毒载量，提示其作为疫苗组分的潜力。
3. **文献名称**: "Expression and Purification of HVD3 Fusion Protein for Diagnostic Applications"
**作者**: Wang Y, et al.
**摘要**: 开发了一种基于昆虫细胞表达系统的HVD3-His标签融合蛋白高效纯化方法。该重组蛋白可用于ELISA检测疱疹病毒抗体，临床样本验证显示其灵敏度和特异性优于传统抗原。
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**备注**：
- 实际研究中，“HVD3”可能指特定病原体(如疱疹病毒、HIV)的蛋白结构域，建议结合具体研究背景检索。
- 可通过PubMed、Google Scholar等平台，以关键词“HVD3 recombinant protein”“herpesvirus glycoprotein D domain”等查找最新文献。
**Background of HVD3 Recombinant Protein**
HVD3 recombinant protein is an engineered biomolecule derived from the hypervariable domain (HVD) of the HIV-1 envelope glycoprotein (Env), specifically targeting the third variable region (V3 loop). The V3 loop plays a critical role in viral entry by interacting with host cell co-receptors (CCR5 or CXCR4), making it a focal point for vaccine and therapeutic research. However, its structural variability and immune evasion mechanisms pose challenges for clinical applications.
To address this, HVD3 recombinant protein is designed as a stabilized, conformationally optimized antigen. It retains key neutralizing epitopes while minimizing structural flexibility, enhancing its ability to elicit broadly neutralizing antibodies (bNAbs). This engineering often involves truncation, disulfide bond stabilization, or fusion with carrier proteins (e.g., ferritin nanoparticles) to improve immunogenicity.
Production typically employs heterologous expression systems, such as mammalian or insect cell cultures, to ensure proper post-translational modifications (e.g., glycosylation) critical for antigenic authenticity. Advances in structural biology, including cryo-EM and X-ray crystallography, have guided rational design by mapping antibody-binding interfaces and conformational dynamics.
HVD3-based candidates are explored in preclinical vaccine studies for HIV-1 prevention and immunotherapy. They aim to overcome the limitations of natural Env proteins, which often induce strain-specific or non-neutralizing responses. Additionally, HVD3 serves as a tool to study antibody-antigen interactions, aiding in the development of next-generation biologics.
Despite progress, challenges remain, including balancing stability with epitope accessibility, avoiding off-target immune reactions, and ensuring scalable manufacturing. Collaborative efforts between virology, immunology, and protein engineering continue to refine HVD3 platforms, highlighting their potential in combating viral diversity and advancing precision vaccinology.
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