| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VP |
| Uniprot No | Q96AX1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-596aa |
| 氨基酸序列 | MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF |
| 预测分子量 | 67,6 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VP重组蛋白的3篇参考文献及其摘要内容概述：
1. **文献名称**：*Expression and characterization of rotavirus VP6 in insect cells using a baculovirus vector*
**作者**：Jiang B 等
**摘要概述**：该研究利用杆状病毒表达系统在昆虫细胞中成功表达轮状病毒VP6重组蛋白，并验证其抗原性和免疫原性，为轮状病毒亚单位疫苗开发提供了实验基础。
2. **文献名称**：*Structural and functional analysis of recombinant Norwalk virus capsid protein expressed in mammalian cells*
**作者**：Desselberger U 等
**摘要概述**：通过哺乳动物细胞(HEK293)表达诺如病毒VP1重组蛋白，解析其自组装形成病毒样颗粒(VLPs)的能力，并证实其在免疫保护中的作用。
3. **文献名称**：*Ebola Virus VP40 Matrix Protein: Assembly and Budding*
**作者**：Noda T 等
**摘要概述**：研究埃博拉病毒VP40重组蛋白在哺乳动物细胞中的表达，揭示其通过寡聚化形成基质结构并介导病毒样颗粒释放的分子机制。
这些文献覆盖了VP蛋白在不同表达系统中的重组表达、结构功能分析及疫苗开发等应用方向。
**Background of VP Recombinant Proteins**
Viral protein (VP) recombinant proteins are engineered molecules produced through recombinant DNA technology, enabling the expression and purification of specific viral proteins in heterologous systems (e.g., bacterial, yeast, insect, or mammalian cells). These proteins mimic native viral antigens or functional components, retaining structural and immunological properties while eliminating infectious risks. Their development is rooted in advancements in molecular biology and genetic engineering since the late 20th century, driven by the need for safer, scalable alternatives to traditional vaccines and research tools.
VP recombinant proteins are pivotal in vaccine development, serving as antigens to elicit targeted immune responses. For example, hepatitis B virus (HBV) surface antigen (HBsAg) vaccines utilize recombinant HBsAg produced in yeast. Similarly, human papillomavirus (HPV) vaccines employ virus-like particles (VLPs) assembled from recombinant L1 capsid proteins. Beyond vaccines, they are used in diagnostics (e.g., ELISA kits for antibody detection), therapeutics (e.g., antiviral drugs targeting viral entry), and basic research to study viral mechanisms.
Key advantages include scalability, consistency, and safety, as they avoid handling live viruses. Challenges involve ensuring proper protein folding, post-translational modifications, and antigenic fidelity. Recent innovations, such as nanoparticle display and structural optimization, enhance their immunogenicity. The COVID-19 pandemic further highlighted their utility, with recombinant spike proteins of SARS-CoV-2 accelerating vaccine and therapeutic development.
Overall, VP recombinant proteins represent a versatile, evolving platform bridging virology, immunology, and biotechnology, offering solutions for global health challenges.
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