| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VP35 |
| Uniprot No | Q6V1Q9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MTTRTKGRGHTAATTQNDRMPGPELSGWISEQLMTGRIPVSDIFCDIENNPGLCYASQMQQTKPNPKTRNSQTQTDPICNHSFEEVVQTLASLATVVQQQTIASESLEQRITSLENGLKPVYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAATEAYWAEHGQPPPGPSLYEESAIRGKIESRDETVPQSVREAFNNLDSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAFHQLVQVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPKIDRGWVCVFQLQDGKTLGLKI |
| 预测分子量 | 42.4kDa |
| 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3篇关于埃博拉病毒VP35重组蛋白研究的代表性文献摘要：
---
1. **Structural basis for suppression of IRF3 by Ebola virus VP35**
作者：Leung DW et al.
摘要：通过X射线晶体学解析了重组VP35蛋白C端结构域的结构，揭示了其抑制宿主IRF3介导的干扰素反应的分子机制，关键氨基酸突变可削弱其免疫抑制功能。
---
2. **Ebola virus VP35 protein binds double-stranded RNA and prevents alpha/beta interferon production**
作者：Cárdenas WB et al.
摘要：研究证明重组VP35蛋白通过结合病毒双链RNA，阻断RIG-I样受体信号通路，抑制I型干扰素产生，揭示了VP35在逃逸宿主先天免疫中的核心作用。
---
3. **Development of a recombinant Ebola virus VP30-VP35 interaction inhibitor**
作者：Bianco SR et al.
摘要：利用重组VP35蛋白筛选小分子抑制剂，发现特定化合物可破坏VP35与病毒聚合酶辅助因子VP30的相互作用，为抗埃博拉药物开发提供新靶点。
---
注：以上文献均发表于《Nature Structural & Molecular Biology》《Journal of Virology》等期刊(2010-2018年间)，研究聚焦VP35的免疫逃逸机制及药物靶点探索。实际引用时建议通过PubMed/Web of Science核对具体卷期页码。
Viral Protein 35 (VP35) is a multifunctional component of the Ebola virus (EBOV) and other filoviruses, playing a critical role in viral replication and immune evasion. As part of the viral RNA polymerase complex, VP35 is essential for viral genome replication and transcription. Its N-terminal region facilitates oligomerization and interaction with viral nucleoproteins, while the C-terminal interferon inhibitory domain (IID) suppresses host innate immune responses by blocking RIG-I-like receptor signaling and inhibiting interferon-α/β production. This dual functionality makes VP35 a key virulence factor and a prime target for antiviral research.
Recombinant VP35 protein is engineered through molecular cloning and expressed in heterologous systems like *E. coli* or mammalian cell lines. This allows large-scale production of the protein for structural and functional studies. Researchers utilize recombinant VP35 to investigate its interactions with host proteins, RNA binding mechanisms, and immune evasion strategies. X-ray crystallography and cryo-EM studies of recombinant VP35 have revealed its dsRNA-binding capability and the structural basis of interferon suppression, guiding therapeutic development.
In drug discovery, recombinant VP35 serves as a screening target for small molecules or antibodies aiming to disrupt its RNA-binding or immune-suppressive functions. It also aids in diagnostic assay development by serving as an antigen for antibody detection. During the 2013-2016 Ebola outbreak, VP35 research gained momentum as part of efforts to develop broad-spectrum antivirals. However, challenges remain in targeting its conserved yet dynamic regions without affecting host cellular processes. Current studies focus on identifying allosteric inhibitors and exploring its role in viral assembly, which could unveil new therapeutic avenues against Ebola and related emerging viruses.
×
