| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADHR |
| Uniprot No | P30518 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-371aa |
| 氨基酸序列 | MLMASTTSAVPGHPSLPSLPSNSSQERPLDTRDPLLARAELALLSIVFVAVALSNGLVLAALARRGRRGHWAPIHVFIGHLCLADLAVALFQVLPQLAWKATDRFRGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGSGAHWNRPVLVAWAFSLLLSLPQLFIFAQRNVEGGSGVTDCWACFAEPWGRRTYVTWIALMVFVAPTLGIAACQVLIFREIHASLVPGPSERPGGRRRGRRTGSPGEGAHVSAAVAKTVRMTLVIVVVYVLCWAPFFLVQLWAAWDPEAPLEGAPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCARGRTPPSLGPQDESCTTASSSLAKDTSS |
| 预测分子量 | 40.2kDa |
| 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V重组蛋白的3篇代表性文献的简化示例(注：文献为虚构概括，仅供参考)：
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1. **文献名称**: *Structural and functional analysis of recombinant V protein in viral immune evasion*
**作者**: Smith A, et al.
**摘要**: 研究解析了V重组蛋白的晶体结构，揭示其通过结合宿主STAT蛋白抑制干扰素信号通路，为抗病毒药物设计提供靶点。
2. **文献名称**: *Development of a V protein-based subunit vaccine against paramyxovirus*
**作者**: Chen L, et al.
**摘要**: 利用重组V蛋白作为疫苗抗原，在小鼠模型中诱导中和抗体和T细胞免疫，证实其对副黏病毒感染的防护效果。
3. **文献名称**: *High-yield expression and purification of recombinant V protein for diagnostic applications*
**作者**: Kim J, et al.
**摘要**: 优化了大肠杆菌表达系统，实现V重组蛋白的高效可溶表达，并验证其用于血清学检测的灵敏度和特异性。
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**注**：实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“recombinant V protein”或结合具体病毒名称(如麻疹病毒V蛋白)。
**Background of Recombinant V Proteins**
Recombinant proteins, including V proteins, are engineered through genetic modification to express specific viral, bacterial, or eukaryotic proteins in heterologous host systems. The term "V protein" often refers to viral proteins, such as the non-structural V protein of paramyxoviruses (e.g., measles, mumps), which play roles in immune evasion by inhibiting interferon signaling. Recombinant versions are produced by cloning the target gene into expression vectors, followed by transfection into hosts like *E. coli*, yeast, or mammalian cells. These systems enable scalable production of proteins for research, diagnostics, or therapeutics.
The development of recombinant V proteins gained momentum with advances in molecular biology in the late 20th century. For example, recombinant viral proteins are critical in vaccine development, such as hepatitis B surface antigen (HBsAg) vaccines. Similarly, V proteins from pathogens like SARS-CoV-2 (e.g., spike protein) were pivotal in COVID-19 vaccine design. Their recombinant forms allow safe antigen production without handling live viruses.
Challenges include ensuring proper folding, post-translational modifications (e.g., glycosylation), and stability, often necessitating mammalian expression systems. Innovations in protein engineering, such as codon optimization and fusion tags, enhance yield and functionality.
Today, recombinant V proteins are tools for structural studies, antibody production, and understanding host-pathogen interactions. They also hold therapeutic potential, such as interferons or monoclonal antibodies targeting viral proteins. Ongoing research focuses on optimizing expression platforms and expanding applications in precision medicine.
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