| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | E6 |
| Uniprot No | Q16553 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-131aa |
| 氨基酸序列 | MKIFLPVLLAALLGVERASSLMCFSCLNQKSNLYCLKPTICSDQDNYCVTVSASAGIGNLVTFGHSLSKTCSPACPIPEGVNVGVASMGISCCQSFLCNFSAADGGLRASVTLLGAGLLLSLLPALLRFGP |
| 预测分子量 | 13,5 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篇关于HPV E6重组蛋白研究的代表性文献摘要：
1. **《Expression and purification of HPV16 E6 oncoprotein in Escherichia coli》**
作者：Smith J, et al.
摘要：报道在大肠杆菌中高效表达HPV16 E6重组蛋白，利用His标签亲和层析纯化，并通过Western blot验证其抗原性，为后续抗体开发提供材料。
2. **《Structural analysis of HPV18 E6 recombinant protein reveals key functional domains》**
作者：Chen L, et al.
摘要：通过X射线晶体学解析HPV18 E6重组蛋白结构，发现其锌指结构域对p53结合至关重要，揭示了E6介导的致癌机制的结构基础。
3. **《Development of a yeast-based system for high-yield production of recombinant HPV E6 protein》**
作者：Garcia R, et al.
摘要：构建毕赤酵母表达系统规模化生产HPV E6重组蛋白，优化发酵条件使产量达120mg/L，并通过质谱验证翻译后修饰的完整性。
注：以上文献信息为示例性质，实际文献可通过PubMed(https://pubmed.ncbi.nlm.nih.gov)搜索关键词"HPV E6 recombinant protein"获取。建议优先选择近5年发表于《Virology》《Journal of Biotechnology》等期刊的研究。
**Background of E6 Recombinant Protein**
The E6 recombinant protein is derived from the E6 oncoprotein of human papillomavirus (HPV), a family of viruses linked to various cancers, notably cervical cancer. HPV E6 is a key viral protein involved in oncogenesis, primarily by degrading the tumor suppressor p53 through ubiquitin-mediated proteolysis. This disruption of p53 impairs cell cycle regulation and apoptosis, promoting uncontrolled cellular proliferation and genomic instability.
Recombinant E6 proteins are engineered using genetic recombination techniques, where the E6 gene is cloned into expression vectors (e.g., bacterial, yeast, or mammalian systems) to produce purified proteins for research and therapeutic applications. Bacterial systems like *E. coli* are cost-effective for large-scale production, while eukaryotic systems ensure proper post-translational modifications for functional studies.
In research, E6 recombinant proteins are critical tools for studying HPV pathogenesis, host-virus interactions, and mechanisms of immune evasion. They facilitate structural analyses, antibody development, and screening of antiviral compounds. For instance, E6’s interaction with host proteins like E6AP (E6-associated protein) is a focus for understanding oncogenic signaling.
Clinically, recombinant E6 proteins are explored in diagnostic kits to detect HPV-specific antibodies and in therapeutic vaccines. Despite progress, challenges remain, such as E6’s high variability across HPV strains and its immunosuppressive properties. Current efforts aim to design multivalent vaccines or small-molecule inhibitors targeting conserved E6 regions.
Overall, E6 recombinant proteins bridge virology, oncology, and immunology, offering insights into HPV-related malignancies and paving the way for novel diagnostics and therapies.
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