| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VIL |
| Uniprot No | P09327 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-827aa |
| 氨基酸序列 | MTKLSAQVKGSLNITTPGLQIWRIEAMQMVPVPSSTFGSFFDGDCYIILAIHKTASSLSYDIHYWIGQDSSLDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESEAFRGYFKQGLVIRKGGVASGMKHVETNSYDVQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESTRMERLRGMTLAKEIRDQERGGRTYVGVVDGENELASPKLMEVMNHVLGKRRELKAAVPDTVVEPALKAALKLYHVSDSEGNLVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKKANEQEKKGAMSHALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTASNRTSGLGKTHTVGSVAKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHFYGGDCYLLLYTYLIGEKQHYLLYVWQGSQASQDEITASAYQAVILDQKYNGEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRTNNLETGPSTRLFQVQGTGANNTKAFEVPARANFLNSNDVFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENLVITPRLFECSNKTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKHANEEEKKAAATTAQEYLKTHPSGRDPETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYEDLKAELGNSRDWSQITAEVTSPKVDVFNANSNLSSGPLPIFPLEQLVNKPVEELPEGVDPSRKEEHLSIEDFTQAFGMTPAAFSALPRWKQQNLKKEKGLF |
| 预测分子量 | 92,6 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VIL重组蛋白的参考文献示例，基于假设VIL指代与细胞骨架相关的Villin蛋白家族：
1. **"Expression and functional analysis of recombinant villin headpiece in actin polymerization"**
- **作者**: Smith J, et al.
- **摘要**: 研究重组Villin头部结构域(VIL-HP)在体外对肌动蛋白聚合的调控作用，揭示其通过特定结构域促进细胞骨架重塑的机制。
2. **"High-yield purification of recombinant human villin for structural studies"**
- **作者**: Zhang L, et al.
- **摘要**: 提出一种在大肠杆菌中高效表达并纯化重组人源Villin蛋白的方法，通过质谱和圆二色光谱验证其正确折叠及生物活性。
3. **"Villin’s role in intestinal epithelial cell migration: Insights from recombinant protein assays"**
- **作者**: Brown K, et al.
- **摘要**: 利用重组Villin蛋白进行细胞实验，证明其通过调控肌动蛋白网络影响肠道上皮细胞的迁移能力，为癌症转移研究提供依据。
4. **"Structural dynamics of the villin headpiece domain using NMR spectroscopy"**
- **作者**: Bäuerle SC, et al.
- **摘要**: 通过核磁共振(NMR)分析重组Villin头部结构域在溶液中的动态构象变化，阐明其与肌动蛋白结合的分子机制。
**注**：以上文献为示例性质，实际研究需通过学术数据库(如PubMed、Google Scholar)以关键词“villin recombinant protein”或“VIL重组蛋白”检索最新或相关论文。
**Background of VIL Recombinant Proteins**
VIL (Vaccinia virus Immune evasion Ligase) recombinant proteins are engineered molecules derived from the vaccinia virus, a member of the poxvirus family. Vaccinia virus has historically been pivotal in vaccine development, most notably as the live-virus vaccine used to eradicate smallpox. Its genome encodes numerous immunomodulatory proteins, including VIL, which evolved to subvert host immune responses. VIL, specifically, is a viral E3 ubiquitin ligase that targets major histocompatibility complex class I (MHC-I) molecules for degradation, thereby inhibiting antigen presentation to cytotoxic T-cells—a key immune evasion strategy.
Recombinant VIL proteins are produced via genetic engineering, typically by cloning the VIL gene into expression vectors (e.g., bacterial, insect, or mammalian systems) to enable large-scale production. These proteins retain the functional domains of native VIL, allowing researchers to study their molecular mechanisms, such as ubiquitination pathways and immune suppression. Beyond basic research, VIL recombinant proteins are tools for developing antiviral therapies or improving vaccine platforms. For instance, understanding VIL’s interaction with host proteins informs strategies to block viral immune evasion or engineer attenuated viruses with enhanced immunogenicity.
Additionally, VIL’s unique enzymatic properties have broader biotechnological applications. Its ability to ubiquitinate specific substrates makes it valuable in targeted protein degradation studies, a growing field in drug discovery. The development of VIL recombinant proteins exemplifies the intersection of virology, immunology, and synthetic biology, offering insights into host-pathogen interactions while enabling innovative therapeutic approaches. Overall, VIL recombinant proteins serve as both a model for studying viral immune evasion and a versatile tool in biomedical research and biotechnology.
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