| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBe1 |
| Uniprot No | P02100 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-147aa |
| 氨基酸序列 | VHFTAEEKA AVTSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDSFGNLS SPSAILGNPK VKAHGKKVLT SFGDAIKNMD NLKPAFAKLS ELHCDKLHVD PENFKLLGNV MVIILATHFG KEFTPEVQAA WQKLVSAVAI ALAHKYH |
| 预测分子量 | 16,2 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HBe1重组蛋白的3篇代表性文献示例(注：文献为模拟概括，具体内容建议通过PubMed或Google Scholar检索验证)：
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1. **文献名称**: *Expression and purification of recombinant HBe1 protein in E. coli for serological diagnosis*
**作者**: Smith A, et al.
**摘要**: 研究利用大肠杆菌系统高效表达HBe1重组蛋白，优化纯化工艺后证实其与乙肝患者血清抗体特异性结合，可作为低成本诊断抗原。
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2. **文献名称**: *HBe1-based virus-like particles as a vaccine carrier for epitope presentation*
**作者**: Zhang L, et al.
**摘要**: 构建以HBe1重组蛋白为骨架的病毒样颗粒(VLPs)，展示HIV抗原表位，动物实验显示其可诱导强烈的Th1型免疫应答，证明其作为疫苗载体的潜力。
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3. **文献名称**: *Structural analysis of HBe1 core protein and its role in immune modulation*
**作者**: Kim T, et al.
**摘要**: 通过冷冻电镜解析HBe1重组蛋白的三维结构，发现其C端柔性区与TLR2受体互作，可能解释HBeAg在慢性乙肝免疫逃逸中的作用机制。
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**提示**：实际文献请通过关键词“HBe1 recombinant protein”“HBV core antigen”或“hepatitis B e antigen”在学术数据库中检索，重点关注蛋白表达、结构研究或免疫应用方向。
**Background of HBe1 Recombinant Protein**
Hepatitis B e antigen (HBeAg), a secretory protein derived from the precore/core gene of the hepatitis B virus (HBV), plays a critical role in viral persistence and immune modulation during HBV infection. The HBe1 recombinant protein is a truncated, non-particulate form of HBeAg, typically lacking the C-terminal domain required for viral capsid assembly. This modification enhances its solubility and simplifies production in heterologous expression systems, such as *Escherichia coli* or yeast, while retaining key antigenic and immunomodulatory properties.
HBeAg is structurally related to the hepatitis B core antigen (HBcAg) but differs in its N-terminal precore region, which directs secretion and allows interaction with host immune cells. HBe1 often preserves this region, enabling studies on its role in immune tolerance, particularly in chronic HBV infections. Researchers leverage HBe1 to investigate mechanisms of viral immune evasion, such as suppression of Toll-like receptor signaling or modulation of T-cell responses.
In vaccine development, HBe1 serves as a versatile carrier for heterologous epitopes due to its high immunogenicity and ability to induce T-helper cell responses. Its lack of viral particle formation reduces safety concerns, making it suitable for antigen display platforms targeting pathogens like HIV or malaria. Additionally, HBe1-based assays are employed in diagnostic research to detect anti-HBe antibodies, aiding in staging HBV infections or monitoring treatment efficacy.
Despite its utility, HBe1's strong immunogenicity can complicate studies requiring precise immune targeting, necessitating careful experimental design. Ongoing research continues to explore its dual role as both an immune modulator and a vaccine scaffold, bridging insights into HBV pathogenesis and therapeutic innovation.
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