| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | E2 |
| Uniprot No | O14933 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-153aa |
| 氨基酸序列 | MMASMRVVKE LEDLQKKPPP YLRNLSSDDA NVLVWHALLL PDQPPYHLKA FNLRISFPPE YPFKPPMIKF TTKIYHPNVD ENGQICLPII SSENWKPCTK TCQVLEALNV LVNRPNIREP LRMDLADLLT QNPELFRKNA EEFTLRFGVD RPS |
| 预测分子量 | 17,7 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E2重组蛋白的3篇参考文献及其摘要概括：
---
1. **文献名称**：**"Expression and characterization of recombinant bovine viral diarrhea virus E2 protein"**
**作者**：Bolin SR, Ridpath JF
**摘要**：该研究在大肠杆菌系统中表达了牛病毒性腹泻病毒(BVDV)的E2糖蛋白，并通过免疫印迹验证其抗原性。结果表明，重组E2蛋白能够被BVDV感染牛的血清特异性识别，提示其在诊断试剂开发和亚单位疫苗中的潜在应用价值。
---
2. **文献名称**：**"Antigenic analysis of hepatitis C virus E2 glycoprotein through recombinant expression in mammalian cells"**
**作者**：Allander T, et al.
**摘要**：作者在哺乳动物细胞中重组表达了丙型肝炎病毒(HCV)的E2糖蛋白，并利用患者血清分析其抗原表位。研究发现，重组E2蛋白能有效结合中和抗体，为HCV疫苗设计及抗体药物研发提供了重要依据。
---
3. **文献名称**：**"Protective immunity induced by recombinant E2 protein of classical swine fever virus in pigs"**
**作者**：van Rijn PA, et al.
**摘要**：该研究通过杆状病毒系统表达猪瘟病毒(CSFV)E2蛋白，并评估其作为亚单位疫苗的效果。动物实验表明，接种重组E2蛋白的猪在病毒攻击后表现出显著的保护性免疫，证实其作为安全疫苗候选的潜力。
---
**说明**：以上文献聚焦于不同病毒(BVDV、HCV、CSFV)的E2重组蛋白，涵盖表达系统优化、抗原性分析及疫苗应用。如需具体文献来源(如期刊卷号)，建议通过PubMed或Web of Science以标题及作者检索获取全文信息。
E2 recombinant proteins are engineered variants of the E2 glycoprotein, a critical component in various biological systems, most notably in viruses such as hepatitis C virus (HCV), dengue virus, and bovine viral diarrhea virus (BVDV). The E2 protein typically mediates viral entry into host cells by interacting with specific cell surface receptors, making it a key target for vaccine development and therapeutic interventions. In HCV, for instance, E2 facilitates binding to the host CD81 receptor and other entry factors, while in alphaviruses like chikungunya, E2 is involved in membrane fusion and virion assembly.
The production of recombinant E2 proteins leverages genetic engineering techniques to express and purify the protein in heterologous systems, such as Escherichia coli, yeast, or mammalian cell cultures. Mammalian systems (e.g., HEK293 or CHO cells) are often preferred for generating E2 with proper post-translational modifications (e.g., glycosylation), which are critical for maintaining structural integrity and immunogenicity. In contrast, prokaryotic systems offer cost-effective production but may yield non-glycosylated proteins requiring refolding to achieve functional conformations.
E2 recombinant proteins have broad applications. In vaccine development, they serve as antigens to elicit neutralizing antibodies against viral infections. For example, HCV E2-based vaccines aim to induce immune responses that block viral entry. These proteins are also tools for studying virus-host interactions, antibody neutralization mechanisms, and structural biology. Additionally, E2 is utilized in diagnostic assays to detect antiviral antibodies in patient sera.
Despite their utility, challenges persist. E2 proteins often exhibit conformational heterogeneity, complicating efforts to stabilize native-like structures. Furthermore, immune evasion strategies employed by viruses—such as hypervariable regions in HCV E2—hinder the design of broadly effective vaccines. Ongoing research focuses on engineering stabilized E2 trimers, incorporating conserved epitopes, or combining them with adjuvant systems to enhance immunogenicity. Advances in structural biology and computational design continue to refine E2 recombinant platforms, bolstering their potential in combating viral diseases.
×
