| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | UBC11 |
| Uniprot No | P52492 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-156aa |
| 氨基酸序列 | MAVEEGGCVT KRLQNELLQL LSSTTESISA FPVDDNDLTY WVGYITGPKD TPYSGLKFKV SLKFPQNYPF HPPMIKFLSP MWHPNVDKSG NICLDILKEK WSAVYNVETI LLSLQSLLGE PNNRSPLNAV AAELWDADME EYRKKVLACY EEIDDY |
| 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UBC11重组蛋白的3篇参考文献概览(注：UBC11相关研究较少，以下为模拟示例，实际文献需根据具体研究方向检索验证)：
---
1. **文献名称**：*Functional characterization of Arabidopsis UBC11 in abiotic stress tolerance via recombinant protein analysis*
**作者**：Smith, J., et al.
**摘要**：研究通过原核表达系统(大肠杆菌)成功纯化拟南芥UBC11重组蛋白，并验证其作为泛素结合酶(E2)的活性。实验表明UBC11通过调控特定底物泛素化参与植物盐胁迫响应通路。
2. **文献名称**：*Structural insights into UBC11 catalytic mechanism using recombinant protein crystallography*
**作者**：Lee, S., & Kim, D.
**摘要**：通过真核表达系统(昆虫细胞)获得高纯度UBC11重组蛋白，利用X射线晶体学解析其三维结构，揭示其催化活性位点及与其他E3连接酶的相互作用机制。
3. **文献名称**：*Recombinant UBC11 enhances protein degradation efficiency in vitro*
**作者**：Zhang, Y., et al.
**摘要**：构建UBC11与特定E3连接酶(如RING型)的重组共表达体系，体外实验证明其协同促进靶蛋白的多聚泛素化及蛋白酶体降解，为研究泛素-蛋白酶体系统提供工具。
---
**提示**：实际研究中，建议通过数据库(如PubMed、Web of Science)以关键词“UBC11 recombinant”、“Ubiquitin-conjugating enzyme 11 expression”检索最新文献，并关注其物种(如植物、动物)及功能差异。
Ubiquitin-conjugating enzyme 11 (UBC11), also known as UBE2C or UBCH10. is a member of the E2 ubiquitin-conjugating enzyme family critical for the ubiquitin-proteasome system (UPS), which regulates protein degradation and cellular homeostasis. Functioning as a key mediator in the ubiquitination cascade, UBC11 transfers ubiquitin from E1-activating enzymes to substrate proteins, often in collaboration with E3 ubiquitin ligases. This post-translational modification typically marks target proteins for proteasomal degradation, influencing processes like cell cycle progression, DNA repair, and apoptosis.
Structurally, UBC11 contains a conserved catalytic core domain responsible for binding ubiquitin and E3 ligases. Its activity is particularly notable during the mitotic phase of the cell cycle, where it participates in the degradation of anaphase-promoting complex/cyclosome (APC/C) substrates, ensuring proper chromosome segregation and mitotic exit. Dysregulation of UBC11 has been linked to genomic instability and oncogenesis, with overexpression observed in various cancers, correlating with poor prognosis and therapeutic resistance.
Recombinant UBC11 is engineered for biochemical and functional studies, often expressed in bacterial or mammalian systems to preserve post-translational modifications. Purified recombinant UBC11 enables in vitro ubiquitination assays, structural analyses (e.g., X-ray crystallography), and drug discovery efforts targeting the UPS. Its role in cancer biology has also spurred interest in developing UBC11 inhibitors as potential anticancer agents.
Beyond oncology, UBC11’s involvement in neurodegenerative diseases, where protein aggregation is a hallmark, highlights its broader pathophysiological relevance. Research on recombinant UBC11 continues to unravel its mechanistic nuances, offering insights into cellular regulation and therapeutic opportunities.
×
