| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBC8 |
| Uniprot No | O14933 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-153aa |
| 氨基酸序列 | MMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPEYPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREPLRMDLADLLTQNPELFRKNAEEFTLRFGVDRPS |
| 预测分子量 | 17,7 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UBC8重组蛋白的3篇参考文献示例(文献信息为模拟示例，仅供参考)：
---
1. **文献名称**: *"Functional Analysis of Arabidopsis UBC8 in the Ubiquitin-Proteasome Pathway"*
**作者**: Smith, J., et al.
**摘要**: 本研究利用重组表达的拟南芥UBC8蛋白，验证其作为泛素结合酶(E2)的活性，并证明其在体内外介导特定底物蛋白的泛素化降解，参与光形态建成调控。
2. **文献名称**: *"Crystal Structure of Recombinant Yeast UBC8 Reveals Catalytic Mechanism"*
**作者**: Lee, H., et al.
**摘要**: 通过大肠杆菌表达系统获得高纯度酵母UBC8重组蛋白，解析其晶体结构，揭示了其与泛素(Ub)及E3连接酶相互作用的关键位点，为泛素化机制提供结构基础。
3. **文献名称**: *"Optimization of Recombinant UBC8 Production for Drug Screening Assays"*
**作者**: Chen, L., et al.
**摘要**: 开发了一种高效表达和纯化人源UBC8重组蛋白的工艺，验证其在体外泛素化反应体系中的功能，并应用于筛选靶向泛素通路的抑制剂。
---
**备注**：以上文献为示例性内容，实际研究中建议通过学术数据库(如PubMed、Web of Science)以关键词“UBC8 recombinant protein”“UBC8 ubiquitination”等检索最新文献。
**Background of UBC8 Recombinant Protein**
UBC8 (Ubiquitin-Conjugating Enzyme 8) belongs to the E2 enzyme family, which plays a central role in the ubiquitination cascade—a post-translational modification process critical for regulating protein degradation, cellular signaling, and stress responses. In *Arabidopsis thaliana*, UBC8 is one of 37 E2 enzymes that collaborate with E3 ubiquitin ligases to transfer ubiquitin molecules onto target proteins, marking them for proteasomal degradation or functional modulation.
Structurally, UBC8 contains a conserved catalytic core domain typical of E2 enzymes, including an active-site cysteine residue essential for forming a thioester bond with ubiquitin. Studies suggest its involvement in diverse physiological processes, such as hormone signaling, DNA repair, and responses to abiotic stresses. For example, UBC8 interacts with specific E3 ligases to regulate jasmonate signaling and modulate plant defense mechanisms.
The recombinant UBC8 protein is engineered using heterologous expression systems (e.g., *E. coli* or yeast) to enable high-yield production and purification for in vitro studies. Recombinant versions retain enzymatic activity, allowing researchers to dissect ubiquitination mechanisms, screen E3 ligase partners, or study substrate specificity. Its soluble expression and stability make it a valuable tool for structural studies, including crystallography and NMR, to elucidate E2-E3-substrate interactions.
Notably, UBC8 exhibits functional redundancy with other E2 enzymes, complicating genetic studies but highlighting the robustness of the ubiquitin system. Research on recombinant UBC8 continues to advance understanding of ubiquitin-mediated regulation in plants and its potential biotechnological applications, such as engineering stress-tolerant crops or targeting disease-related ubiquitination pathways.
×
