| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | E3 |
| Uniprot No | Q7Z769 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-313aa |
| 氨基酸序列 | MALLVDRVRGHWRIAAGLLFNLLVSICIVFLNKWIYVYHGFPNMSLTLVHFVVTWLGLYICQKLDIFAPKSLPPSRLLLLALSFCGFVVFTNLSLQNNTIGTYQLAKAMTTPVIIAIQTFCYQKTFSTRIQLTLIPITLGVILNSYYDVKFNFLGMVFAALGVLVTSLYQVWVGAKQHELQVNSMQLLYYQAPMSSAMLLVAVPFFEPVFGEGGIFGPWSVSALLMVLLSGVIAFMVNLSIYWIIGNTSPVTYNMFGHFKFCITLFGGYVLFKDPLSINQALGILCTLFGILAYTHFKLSEQEGSRSKLAQRP |
| 预测分子量 | 35 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E3重组蛋白的3篇参考文献的简要概括(文献信息为示例，非真实存在)：
1. **《Structural Insights into E3 Ubiquitin Ligase-Recombinant Protein Complexes》**
- 作者：Zhang, Y. et al.
- 摘要：本研究通过X射线晶体学解析了E3泛素连接酶与重组靶蛋白的复合物结构，揭示了E3连接酶识别底物的分子机制，为设计调控蛋白质降解的重组药物提供了结构基础。
2. **《Engineering Recombinant E3 Ligases for Targeted Protein Degradation》**
- 作者：Smith, J.R. & Brown, K.L.
- 摘要：文章报道了一种基于CRISPR-Cas9筛选平台改造重组E3连接酶的方法，成功开发出可特异性降解致癌蛋白的工程化E3分子，并在体外模型中验证了其抗肿瘤活性。
3. **《Adenovirus E3 Recombinant Protein Modulates Host Immune Response》**
- 作者：Jones, M. et al.
- 摘要：该研究利用重组腺病毒E3蛋白分析其与宿主免疫系统的相互作用，发现E3蛋白通过抑制MHC-I类分子递呈途径帮助病毒逃逸免疫监视，为病毒治疗载体优化提供了新策略。
4. **《High-Yield Production of Functional E3 Recombinant Protein in Escherichia coli》**
- 作者：Lee, S. et al.
- 摘要：本文优化了大肠杆菌表达系统中E3重组蛋白的溶解性和折叠条件，成功实现高产量制备具有酶活性的E3连接酶，为大规模工业应用奠定了基础。
注：以上文献为模拟内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体论文。
**Background of E3 Recombinant Proteins**
E3 recombinant proteins are engineered variants of E3 ubiquitin ligases, a critical component of the ubiquitin-proteasome system (UPS) responsible for targeted protein degradation in eukaryotic cells. E3 ligases function as molecular scaffolds that recognize specific substrate proteins and mediate their ubiquitination—a process where ubiquitin molecules are covalently attached to mark the substrate for proteasomal destruction. This system regulates diverse cellular processes, including cell cycle progression, DNA repair, and apoptosis.
The development of recombinant E3 ligases emerged from advances in molecular cloning and protein engineering. By isolating and modifying genes encoding E3s (e.g., CRL, APC/C, or HECT-domain families), researchers produce these proteins in heterologous systems like *E. coli*, yeast, or mammalian cells. Recombinant technology allows precise control over E3 expression, purification, and functional characterization, enabling studies on substrate specificity, enzymatic mechanisms, and interactions with E2 ubiquitin-conjugating enzymes.
E3 recombinant proteins have become indispensable tools in both basic research and therapeutic development. In drug discovery, they are leveraged to design proteolysis-targeting chimeras (PROTACs)—bifunctional molecules that recruit E3 ligases to degrade disease-causing proteins, such as oncogenic or misfolded aggregates. Additionally, recombinant E3s aid in high-throughput screening for small-molecule modulators to correct UPS dysregulation linked to cancers, neurodegenerative disorders, and autoimmune diseases.
Despite their utility, challenges persist, including maintaining the structural integrity and activity of recombinant E3s *in vitro* and achieving tissue-specific targeting *in vivo*. Ongoing innovations in protein engineering and structural biology continue to refine their applications, positioning E3 recombinant proteins as pivotal agents in understanding and manipulating cellular protein homeostasis.
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