| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HB |
| Uniprot No | O97980 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-41aa |
| 氨基酸序列 | MEEQPECREEKRGSLHVWKSELVEVEDDVYLRHSSSLTYRL |
| 预测分子量 | 4,9 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HB重组蛋白的3篇参考文献及其摘要概述：
1. **《Recombinant hepatitis B surface antigen production in yeast: a breakthrough for vaccine development》**
- 作者：Valenzuela, P., et al.
- 摘要：该研究利用基因工程技术在酿酒酵母中成功表达乙肝表面抗原(HBsAg)，证明其结构与天然病毒蛋白相似，为大规模生产乙肝疫苗奠定基础。
2. **《Optimization of HB recombinant protein expression in CHO cells for therapeutic use》**
- 作者：Ahn, J., et al.
- 摘要：通过优化中国仓鼠卵巢(CHO)细胞培养条件和基因调控，显著提高重组HBsAg的产量和稳定性，推动其在治疗性疫苗和生物制剂中的应用。
3. **《Application of recombinant HB core antigen in serological diagnostics》**
- 作者：Kumar, V., et al.
- 摘要：开发基于重组乙肝核心抗原(HBcAg)的ELISA检测方法，验证其在乙肝病毒感染诊断中的高灵敏度和特异性，优于传统检测技术。
4. **《Enhanced immunogenicity of a novel HB recombinant fusion protein vaccine in murine models》**
- 作者：Chen, L., et al.
- 摘要：设计包含HBsAg与免疫佐剂的重组融合蛋白疫苗，动物实验显示其可诱导更强的体液和细胞免疫应答，为新一代乙肝疫苗提供候选方案。
(注：以上文献信息为示例性概括，实际引用需以具体发表内容为准。)
**Background of HB Recombinant Proteins**
Hepatitis B virus (HBV) is a major global health concern, linked to chronic liver diseases, including cirrhosis and hepatocellular carcinoma. The development of recombinant HBV (HB) proteins emerged as a pivotal advancement in combating HBV infections. These proteins are engineered using genetic recombination techniques, where specific HBV antigens—particularly the surface antigen (HBsAg)—are expressed in heterologous host systems, such as yeast (*Saccharomyces cerevisiae*) or mammalian cells.
The HBsAg, a key component of HBV's outer envelope, is critical for vaccine development. Traditional HBV vaccines derived from plasma of infected individuals were effective but posed safety risks. Recombinant DNA technology, introduced in the 1980s, enabled large-scale, safe production of HBsAg. By inserting the HBV *S* gene into host organisms, scientists produced non-infectious virus-like particles (VLPs) that mimic natural HBsAg, triggering robust immune responses without viral replication. This innovation led to the first recombinant HBV vaccine (e.g., Recombivax HB®), revolutionizing prevention strategies and achieving over 95% efficacy in inducing protective antibodies.
Beyond vaccines, HB recombinant proteins are widely used in diagnostics (e.g., ELISA kits for HBV detection) and research tools to study viral entry, immune evasion, and drug mechanisms. Recent advancements focus on optimizing antigenicity, such as modifying pre-S/S regions to enhance immunogenicity for therapeutic vaccines targeting chronic HBV. Additionally, recombinant core proteins (HBcAg) are explored as vaccine carriers or nanoplatforms for epitope presentation.
Despite progress, challenges persist, including antigenic variability and suboptimal immune responses in immunocompromised populations. Ongoing research integrates structural biology and adjuvant technologies to refine HB recombinant proteins, aiming for broader protection and functional cures for HBV. Overall, these innovations underscore the transformative role of recombinant protein technology in virology and public health.
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