| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vpr |
| Uniprot No | O12160 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-96aa |
| 氨基酸序列 | MEQAPEDQGPQREPYNEWTLELLEELKREAVRHFPRPWLHGLGQHIYETYGDTWTGVEAIIRILQRLLFVHFRIGCQHSRIGILRQRRARNGASRS |
| 预测分子量 | 18.9 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HIV-1 Vpr重组蛋白的3篇代表性文献及其摘要概括：
1. **"HIV-1 Vpr induces apoptosis through caspase-9-dependent mitochondrial pathway"**
*作者：Muthumani et al. (2002)*
摘要：研究利用重组Vpr蛋白在体外验证其诱导细胞凋亡的机制，发现Vpr通过激活caspase-9依赖性线粒体途径触发细胞凋亡，提示其在HIV感染中调控宿主细胞死亡的作用。
2. **"Structural and functional characterization of recombinant HIV-1 Vpr"**
*作者：Zhao et al. (2005)*
摘要：通过大肠杆菌表达系统纯化重组Vpr蛋白，结合圆二色光谱和核磁共振(NMR)解析其三维结构，揭示其α-螺旋结构域对细胞周期停滞功能的关键作用。
3. **"HIV-1 Vpr interacts with the human DNA repair protein HHR23A"**
*作者：Withers-Ward et al. (1997)*
摘要：利用重组Vpr蛋白进行体外结合实验，发现Vpr直接结合宿主DNA修复蛋白HHR23A，可能通过干扰DNA损伤修复促进病毒复制和免疫逃逸。
注：以上文献为示例性概括，实际引用需根据具体研究内容选择最新或高影响力论文。建议通过PubMed或Web of Science以"HIV-1 Vpr recombinant protein"为关键词检索近年研究。
**Background of VPR Recombinant Protein**
The Vpr (Viral Protein R) recombinant protein is derived from the human immunodeficiency virus type 1 (HIV-1), where Vpr serves as a critical accessory protein. Vpr plays multifaceted roles in the viral life cycle, including facilitating nuclear import of viral DNA in non-dividing cells, inducing cell cycle arrest at the G2/M phase, and promoting apoptosis. These functions make Vpr essential for viral pathogenesis and immune evasion. Structurally, Vpr is a 14 kDa protein composed of 96 amino acids, characterized by three alpha-helices and a flexible N-terminal domain. Its ability to oligomerize and interact with host proteins, such as components of the nuclear pore complex and DNA repair machinery, underpins its diverse biological activities.
Recombinant Vpr is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or eukaryotic expression systems. This allows large-scale production of the protein for research and therapeutic development. Purification methods often involve affinity chromatography, followed by refolding steps to ensure proper conformational integrity.
Research on Vpr recombinant protein has focused on elucidating its mechanisms in HIV-1 infection, particularly its role in viral replication and immune modulation. Studies explore its interactions with host factors, such as the ubiquitin-proteasome system and mitochondrial pathways, to identify potential therapeutic targets. Additionally, Vpr's ability to permeabilize cell membranes has sparked interest in its application as a delivery tool for biomolecules.
Challenges in working with Vpr include its inherent cytotoxicity and tendency to aggregate, requiring optimized expression and handling protocols. Despite this, Vpr remains a vital tool for understanding HIV-1 biology and developing antiretroviral strategies, including inhibitors targeting its functional domains. Its study also contributes to broader insights into viral-host interactions and cell cycle regulation.
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