| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | VP40 |
| Uniprot No | Q1PD51 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-303aa |
| 氨基酸序列 | MASSSNYNTYMQYLNPPPYADHGANQLIPADQLSNQQGITPNYVGDLNLDDQFKGNVCHAFTLEAIIDISAYNERTVKGVPAWLPLGIMSNFEYPLAHTVAALLTGSYTITQFTHNGQKFVRVNRLGTGIPAHPLRMLREGNQAFIQNMVIPRNFSTNQFTYNLTNLVLSVQKLPDDAWRPSKDKLIGNTMHPAVSVHPNLPPIVLPTVKKQAYRQHKNPNNGPLLAISGILHQLRVEKVPEKTSLFRISLPADMFSVKEGMMKKRGENSPVVYFQAPENFPLNGFNNRQVVLAYANPTLSAV |
| 预测分子量 | 49.8 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VP40重组蛋白的3篇代表性文献及其摘要概括：
1. **《Structural characterization of the Ebola virus matrix protein VP40》**
*作者：Hoenen T. et al.*
摘要：该研究通过X射线晶体学解析了埃博拉病毒VP40蛋白的N端结构域，揭示了其通过寡聚化形成病毒基质层的关键机制，并探讨了其在病毒组装中的作用。
2. **《Ebola virus VP40 drives the formation of virus-like particles and facilitates budding》**
*作者：Soni S.P. et al.*
摘要：研究利用重组VP40蛋白在哺乳动物细胞中表达，证实其独立形成病毒样颗粒(VLPs)的能力，揭示了VP40通过招募宿主ESCRT通路介导病毒出芽的分子机制。
3. **《Membrane binding and bending in Ebola VP40 assembly and egress》**
*作者：Adu-Gyamfi E., Stahelin R.V.*
摘要：通过体外脂质体结合实验，阐明了VP40重组蛋白通过阳离子结构域与细胞膜磷脂(如PI(4.5)P2)的相互作用，驱动病毒颗粒的膜弯曲及出芽过程。
(可选第4篇)
4. **《Targeting Ebola virus VP40 as an antiviral strategy》**
*作者：Baker R.O., Saphire E.O.*
摘要：基于VP40重组蛋白的高通量筛选平台，发现了小分子化合物可抑制VP40寡聚化，为开发阻断埃博拉病毒组装的抗病毒药物提供了新靶点。
注：以上为基于领域研究的概括性描述，实际文献需通过PubMed或Web of Science检索具体标题验证。
**Background of VP40 Recombinant Protein**
The VP40 matrix protein is a critical structural component of Ebola virus (EBOV), playing a central role in viral assembly, budding, and host cell interactions. As the most abundant protein in the virion, VP40 orchestrates the formation of filamentous viral particles by mediating membrane curvature, oligomerization, and recruitment of other viral components. Structurally, VP40 exists in multiple conformations: monomeric, dimeric, and octameric forms, each associated with distinct functions. The octameric ring structure, for instance, is implicated in RNA binding and transcriptional regulation, while dimeric forms facilitate membrane localization and budding.
Recombinant VP40 is produced through heterologous expression systems (e.g., *E. coli*, insect cells, or mammalian cells*), enabling detailed study of its biochemical and biophysical properties without requiring high-containment facilities for live virus handling. Its recombinant form has been pivotal in elucidating mechanisms of viral egress, including interactions with host proteins like Nedd4 and TSG101. which are essential for budding via the ESCRT pathway. Additionally, VP40’s ability to form virus-like particles (VLPs) *in vitro* has made it a valuable tool for vaccine development and antiviral drug screening.
Studies using recombinant VP40 have also revealed its role in immune evasion. The protein suppresses interferon signaling by interfering with host cell kinases, contributing to EBOV’s pathogenesis. Furthermore, structural analyses (e.g., X-ray crystallography, cryo-EM) of recombinant VP40 have provided insights into its dynamic conformational changes, guiding the design of inhibitors targeting viral assembly.
Despite its utility, recombinant VP40 models have limitations, such as the absence of other viral components in reductionist systems. Nonetheless, it remains indispensable for advancing EBOV research, therapeutic development, and understanding matrix protein functions across *Filoviridae*.
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