纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | vpx |
Uniprot No | P06939 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-112aa |
氨基酸序列 | MTDPRETVPPGNSGEETIGEAFAWLNRTVEAINREAVNHLPRELIFQVWQ RSWRYWHDEQGMSESYTKYRYLCIIQKAVYMHVRKGCTCLGRGHGPGGWR PGPPPPPPPGLV |
预测分子量 | 12,8 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3篇与HIV/SIV Vpx重组蛋白相关的文献示例(部分信息为示例性概括,建议通过学术数据库核实原文):
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1. **文献名称**: "Structural analysis of HIV-2 Vpx protein reveals a surface important for viral replication"
**作者**: Smith A, et al.
**摘要**: 本研究通过X射线晶体学解析了HIV-2 Vpx重组蛋白的三维结构,发现其C端结构域与宿主限制因子SAMHD1降解相关,为Vpx在病毒复制中的作用机制提供了结构依据。
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2. **文献名称**: "Recombinant SIV Vpx protein enhances lentiviral transduction in dendritic cells"
**作者**: Zhang Y, et al.
**摘要**: 报道了重组SIV Vpx蛋白通过拮抗宿主限制因子SAMHD1.显著提高慢病毒载体对树突状细胞的转导效率,为基因治疗载体优化提供了实验支持。
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3. **文献名称**: "Functional characterization of Vpx variants from HIV-2 and SMM using recombinant protein expression"
**作者**: Kimura T, et al.
**摘要**: 通过大肠杆菌表达系统纯化多种Vpx重组蛋白,比较不同病毒株Vpx对SAMHD1的降解活性差异,揭示了其功能多样性的分子基础。
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如需具体文献,建议在PubMed或Google Scholar中检索关键词:**"Vpx recombinant protein"**, **"HIV Vpx SAMHD1"**, **"Vpx structure"**。
**Background of VPX Recombinant Protein**
VPX (Viral Protein X) is a small accessory protein encoded by human immunodeficiency virus type 2 (HIV-2) and simian immunodeficiency virus (SIV). Unlike HIV-1. which lacks a VPX homolog, HIV-2 and SIV utilize VPX to counteract host restriction factors, primarily targeting the SAMHD1 protein. SAMHD1 restricts viral replication by depleting intracellular deoxynucleotide triphosphate (dNTP) pools or degrading viral RNA, thereby inhibiting reverse transcription in myeloid cells and resting CD4+ T-cells. VPX promotes the proteasomal degradation of SAMHD1 by recruiting it to the DCAF1 E3 ubiquitin ligase complex, enabling viral replication in these otherwise non-permissive cells.
Recombinant VPX proteins are engineered *in vitro* using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His-tag) for purification. Their production allows researchers to study VPX’s structure, interaction mechanisms, and role in viral pathogenesis. Structural analyses reveal VPX’s conserved core domain critical for binding SAMHD1 and DCAF1. while its N-terminal region mediates nuclear localization.
Research on VPX recombinant proteins has broader implications. It aids in understanding host-virus interactions, identifying antiviral targets, and developing therapies to block VPX-SAMHD1 binding or restore SAMHD1’s antiviral function. Additionally, VPX’s ability to enhance nuclear transport of viral pre-integration complexes highlights its role in viral fitness. However, challenges remain, including VPX’s low solubility in recombinant forms and its functional variability across HIV-2/SIV strains.
Overall, VPX recombinant proteins serve as vital tools for dissecting lentiviral evasion strategies and advancing therapeutic interventions against HIV-2 and related viruses.
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