| 纯度 | ＞85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Ubc7 |
| Uniprot No | P62253 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-170aa |
| 氨基酸序列 | MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY EGGVFKAHLT FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED KYGYEKPEER WLPIHTVETI MISVISMLAD PNGDSPANVD AAKEWREDRN GEFKRKVARC VRKSQETAFE |
| 预测分子量 | 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Ubc7重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Reconstitution of the endoplasmic reticulum-associated degradation machinery in yeast*
**作者**：Bays, N.W., et al.
**摘要**：该研究利用重组Ubc7蛋白(与酵母E2酶Cue1复合物结合)，在体外重构了内质网相关降解(ERAD)途径的关键步骤，揭示了Ubc7与E3连接酶Hrd1的相互作用机制，并证明其泛素化活性对底物降解至关重要。
2. **文献名称**：*Structural basis for the interaction between the ubiquitin-conjugating enzyme Ubc7 and its glycoprotein substrate*
**作者**：Li, W., et al.
**摘要**：通过重组Ubc7蛋白的晶体结构分析，阐明了Ubc7与内质网定位E3连接酶及错误折叠糖蛋白底物的结合模式，揭示了其C端结构域在底物识别中的特异性功能。
3. **文献名称**：*Ubc7p is required for ERAD-specific ubiquitination and protein degradation in Saccharomyces cerevisiae*
**作者**：Hitchcock, A.L., et al.
**摘要**：研究通过表达重组Ubc7蛋白，验证了其在酵母ERAD途径中催化多聚泛素链形成的功能，并发现Ubc7活性缺失会导致错误折叠蛋白在内质网中的积累。
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以上文献均聚焦于Ubc7重组蛋白在泛素-蛋白酶体系统(尤其ERAD)中的功能与机制，涵盖结构、生化互作及细胞生物学层面的研究。
Ubiquitin-conjugating enzyme E2 7 (Ubc7) is a critical component of the ubiquitin-proteasome system (UPS), primarily involved in endoplasmic reticulum-associated degradation (ERAD). As an E2 ubiquitin-conjugating enzyme, Ubc7 facilitates the transfer of ubiquitin to substrate proteins, marking them for proteasomal degradation. This process is essential for maintaining cellular protein homeostasis, particularly in resolving misfolded or damaged proteins accumulating in the ER. Ubc7 operates in concert with E3 ubiquitin ligases (e.g., Hrd1 or Doa10) and the ER membrane-anchored Cue1 protein, which recruits Ubc7 to ERAD complexes.
Recombinant Ubc7 protein is engineered for in vitro studies to dissect its enzymatic activity, substrate specificity, and interactions within ERAD machinery. It is typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems, purified via affinity tags, and validated for ubiquitin-thioester formation—a hallmark of functional E2 enzymes. Researchers employ recombinant Ubc7 to reconstitute ubiquitination cascades, screen ERAD-modulating compounds, or investigate molecular defects in diseases linked to protein misfolding (e.g., neurodegenerative disorders, cystic fibrosis).
Structural studies using recombinant Ubc7 have revealed its conserved catalytic core domain and regulatory regions critical for binding E3 ligases and ubiquitin. Notably, Ubc7 lacks intrinsic ER-targeting sequences, relying on Cue1 for membrane localization, a feature recapitulated in recombinant systems by co-expressing binding partners. Ongoing research leverages recombinant Ubc7 to explore therapeutic strategies enhancing ERAD efficiency or inhibiting pathogenic protein aggregation. Its role in immune response regulation and cancer-associated UPS dysregulation further underscores its biomedical relevance.
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