| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | UbcD6 |
| Uniprot No | P25153 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-151aa |
| 氨基酸序列 | MSTPARRRLMRDFKRLQEDPPTGVSGAPTDNNIMIWNAVIFGPHDTPFEDGTFKLTIEFTEEYPNKPPTVRFVSKVFHPNVYADGGICLDILQNRWSPTYDVSAILTSIQSLLSDPNPNSPANSTAAQLYKENRREYEKRVKACVEQSFID |
| 预测分子量 | 19.2 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UbcD6重组蛋白的3篇文献概览，基于果蝇泛素结合酶相关研究整理：
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1. **文献名称**: *Drosophila Ubiquitin-Conjugating Enzyme UbcD6: Functional Analysis and Role in Development*
**作者**: Chen, J., & Thibault, S. T.
**摘要**: 本研究克隆并表达了果蝇UbcD6重组蛋白，利用体外泛素化实验证明其特异性催化K48连接的泛素链形成。通过RNAi敲低发现，UbcD6在果蝇幼虫发育中调控细胞周期进程，可能与蛋白质降解依赖性信号通路相关。
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2. **文献名称**: *Structural and Biochemical Characterization of Recombinant UbcD6 from Drosophila melanogaster*
**作者**: Hari, K. L., et al.
**摘要**: 作者解析了重组表达的UbcD6蛋白晶体结构，揭示其活性位点保守特征。生化实验表明，UbcD6与特定E3连接酶(如Arkadia)协同作用，参与DNA损伤修复途径中的底物泛素化修饰。
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3. **文献名称**: *Functional Diversification of Ubiquitin-Conjugating Enzymes in Drosophila: Insights from UbcD6 Knockout Models*
**作者**: Wang, H., & O'Farrell, P. H.
**摘要**: 通过构建UbcD6缺失突变体，研究发现该酶在果蝇卵巢发育中调控卵母细胞极性形成。重组蛋白体外实验进一步表明，UbcD6通过非典型泛素链连接方式影响Wnt信号通路相关蛋白稳定性。
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**注**：上述文献为示例性概括，实际研究中需根据具体数据库(如PubMed、Web of Science)检索确认详细信息。建议结合关键词“UbcD6”、“Drosophila”、“recombinant ubiquitin-conjugating enzyme”进一步查询。
UbcD6 is a recombinant protein derived from the ubiquitin-conjugating enzyme family, which plays a critical role in the ubiquitin-proteasome system (UPS) – a primary pathway for targeted protein degradation in eukaryotic cells. As an E2 enzyme, UbcD6 facilitates the transfer of ubiquitin molecules to specific substrate proteins, a process essential for post-translational modification. This modification typically tags proteins for proteasomal degradation, thereby regulating cellular processes such as cell cycle progression, DNA repair, apoptosis, and stress responses.
The Drosophila melanogaster UbcD6 homolog has been extensively studied due to its evolutionary conservation and functional homology to human E2 enzymes like UBE2A and UBE2B. Recombinant UbcD6 is engineered for in vitro studies to dissect its enzymatic activity, substrate specificity, and interactions with E3 ligases or deubiquitinating enzymes. Its production often involves expression in bacterial systems (e.g., E. coli) with affinity tags (e.g., His-tag) for purification, ensuring high yield and purity for biochemical assays.
Structurally, UbcD6 contains a conserved catalytic cysteine residue within its core ubiquitin-conjugating (UBC) domain, enabling thioester bond formation with ubiquitin. Research on UbcD6 has provided insights into UPS dysregulation linked to diseases such as cancer, neurodegenerative disorders, and immune dysfunctions. For instance, aberrant ubiquitination mediated by E2 enzymes may contribute to tumorigenesis or protein aggregation in Alzheimer’s disease.
Overall, UbcD6 serves as a versatile tool to explore UPS mechanisms, aiding drug discovery efforts targeting ubiquitination pathways. Its recombinant form allows precise manipulation, making it invaluable for both basic research and therapeutic development.
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