纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | UBC10 |
Uniprot No | P35133 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-148aa |
氨基酸序列 | MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPSESPYAGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDKNKYESTARSWTQKYAMG |
预测分子量 | 20.6 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UBC10重组蛋白的3篇参考文献示例(部分信息为模拟生成,实际文献需通过学术数据库验证):
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1. **文献名称**: *Functional Characterization of Arabidopsis UBC10 as a Ubiquitin-Conjugating Enzyme in DNA Damage Response*
**作者**: Smith J, et al.
**摘要**: 本研究通过重组表达拟南芥UBC10蛋白,证实其在DNA损伤修复中的关键作用。实验表明,UBC10通过泛素化修饰靶标蛋白,调控同源重组修复途径,缺乏UBC10的突变体对辐射敏感性显著增加。
2. **文献名称**: *Recombinant UBC10 Protein Mediates Salt Stress Tolerance via Modulating Ion Homeostasis*
**作者**: Li Y, et al.
**摘要**: 作者利用重组UBC10蛋白进行功能分析,发现其通过泛素化降解钠离子转运蛋白的抑制因子,增强拟南芥对盐胁迫的耐受性,揭示了UBC10在植物逆境响应中的新机制。
3. **文献名称**: *In Vitro Ubiquitination Assay of Recombinant UBC10 Reveals Substrate Specificity in the Plant Ubiquitin-Proteasome System*
**作者**: Tanaka K, et al.
**摘要**: 该研究建立了一种体外泛素化实验体系,利用重组UBC10蛋白筛选其特异性底物,发现UBC10偏好结合含有K63泛素链的靶蛋白,为阐明植物泛素化网络提供了实验依据。
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**注意**:以上文献信息为示例,实际研究中请通过PubMed、Google Scholar等平台以关键词“UBC10 recombinant protein”或“Arabidopsis UBC10 ubiquitin”检索最新文献。若需具体文献协助,可提供更详细的研究背景。
**Background of UBC10 Recombinant Protein**
UBC10. a member of the ubiquitin-conjugating enzyme (E2) family, plays a critical role in the ubiquitin-proteasome system (UPS), a primary pathway for targeted protein degradation in eukaryotic cells. Ubiquitination involves a cascade of enzymes: E1 (activating), E2 (conjugating), and E3 (ligase). UBC10 functions as an E2 enzyme, transferring ubiquitin from E1 to substrate proteins marked for degradation, often in collaboration with specific E3 ligases. This post-translational modification regulates diverse cellular processes, including cell cycle progression, DNA repair, and stress responses.
The recombinant UBC10 protein is engineered through molecular cloning, typically expressed in *E. coli* or other host systems, ensuring high purity and activity for experimental use. Recombinant technology allows large-scale production, enabling studies on UBC10’s structure, enzymatic mechanisms, and interactions. Researchers utilize UBC10 recombinant protein to dissect UPS dynamics, investigate disease mechanisms linked to dysregulated protein turnover (e.g., cancer, neurodegenerative disorders), and screen for modulators of ubiquitination pathways.
UBC10’s conservation across species underscores its biological importance, though its specific roles may vary. In plants, for example, UBC10 homologs contribute to stress adaptation, while in humans, aberrant UBC10 activity is implicated in tumorigenesis. Studies leveraging recombinant UBC10 have advanced understanding of substrate specificity, E2-E3 partnerships, and potential therapeutic targets. By reconstituting ubiquitination cascades *in vitro*, this tool bridges molecular insights with translational applications, offering a platform for drug discovery and mechanistic enzymology.
Overall, UBC10 recombinant protein serves as a vital resource for probing UPS functionality and developing strategies to manipulate protein stability in research and medicine.
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