纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | UBE2K |
Uniprot No | P61086 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-200aa |
氨基酸序列 | ANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN |
预测分子量 | 26.3kDa |
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UBE2K重组蛋白的模拟参考文献示例(仅供学术参考,实际文献需通过数据库核实):
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1. **文献名称**: "UBE2K Mediates Huntington Aggregation via Lysine-63-linked Ubiquitination"
**作者**: Smith A, et al.
**摘要**: 研究报道了重组UBE2K蛋白通过K63位泛素链修饰亨廷顿蛋白(Huntingtin),促进其聚集并影响神经细胞毒性,揭示了其在神经退行性疾病中的作用机制。
2. **文献名称**: "Structural Insights into UBE2K Catalytic Mechanism by Crystal Analysis"
**作者**: Chen L, et al.
**摘要**: 通过解析重组UBE2K的晶体结构,阐明了其催化结构域的关键氨基酸残基(如Cys86)在泛素转移反应中的作用,为靶向UBE2K的药物设计提供依据。
3. **文献名称**: "UBE2K Regulates Proteasome-dependent Protein Degradation via Autoubiquitination"
**作者**: Kim J, et al.
**摘要**: 利用体外重组实验证明UBE2K具有自泛素化活性,其通过形成多聚泛素链标记底物蛋白,增强蛋白酶体依赖性降解效率,调控细胞稳态。
4. **文献名称**: "Functional Interaction Between UBE2K and PARKIN in Mitochondrial Quality Control"
**作者**: Wang Y, et al.
**摘要**: 研究发现重组UBE2K与E3连接酶PARKIN协同作用,参与线粒体损伤后泛素化信号传导,影响线粒体自噬过程,提示其在帕金森病中的潜在功能。
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注:以上为模拟内容,实际文献需通过PubMed、Web of Science等平台检索关键词(如“UBE2K recombinant protein”“UBE2K ubiquitination”)获取。
UBE2K, also known as ubiquitin-conjugating enzyme E2K, is a member of the E2 enzyme family involved in the ubiquitin-proteasome system (UPS), a critical pathway for targeted protein degradation in eukaryotic cells. It plays a role in transferring ubiquitin molecules to specific substrate proteins, marking them for proteasomal destruction. UBE2K functions in conjunction with E3 ubiquitin ligases, which provide substrate specificity, and is particularly associated with the ubiquitination of misfolded or damaged proteins in endoplasmic reticulum-associated degradation (ERAD) and stress response pathways. Dysregulation of UBE2K activity has been implicated in neurodegenerative diseases, cancer, and other disorders linked to protein homeostasis.
Recombinant UBE2K protein is produced using biotechnological methods, typically by expressing the cloned *UBE2K* gene in bacterial (e.g., *E. coli*) or mammalian cell systems. The recombinant form retains the enzyme’s catalytic core structure, including the conserved cysteine residue required for ubiquitin-thioester intermediate formation. Purification often involves affinity tags (e.g., His-tag) for ease of isolation. Researchers use recombinant UBE2K to study ubiquitination mechanisms, screen modulators of UPS activity, or investigate its interactions with E3 ligases and substrates in vitro. Its applications extend to drug discovery, particularly in targeting diseases caused by aberrant protein aggregation. Structural and functional studies of recombinant UBE2K have also clarified its role in mediating Lys48-linked polyubiquitin chains, which signal proteasomal degradation. However, challenges remain in maintaining its stability and activity during experimental workflows, necessitating optimized buffer conditions. Overall, recombinant UBE2K serves as a vital tool for decoding UPS-related cellular processes and developing therapeutic strategies.
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