| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2H |
| Uniprot No | P62256 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-183aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSSPSPG KRRMDTDVVK LIESKHEVTI LGGLNEFVVK FYGPQGTPYE GGVWKVRVDL PDKYPFKSPS IGFMNKIFHP NIDEASGTVC LDVINQTWTA LYDLTNIFES FLPQLLAYPN PIDPLNGDAA AMYLHRPEEY KQKIKEYIQK YATEEALKEQ EEGTGDSSSE SSMSDFSEDE AQDMEL |
| 预测分子量 | 23 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UBE2H重组蛋白的3篇模拟参考文献示例(注：文献为模拟生成，非真实存在)：
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1. **文献名称**: *Recombinant UBE2H protein production and its role in ubiquitin chain assembly*
**作者**: Harper, J.M., et al.
**摘要**: 本研究报道了人源UBE2H重组蛋白在大肠杆菌中的高效表达与纯化。通过体外泛素化实验，发现UBE2H与E3连接酶CUL4B复合物协同催化K11-linked泛素链的形成，揭示了其在蛋白质降解通路中的特异性作用。
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2. **文献名称**: *Structural and functional analysis of UBE2H in DNA damage response*
**作者**: Tanaka, R., et al.
**摘要**: 利用重组UBE2H蛋白进行晶体结构解析，揭示了其催化结构域的关键活性位点。功能研究表明，UBE2H通过介导BRCA1复合物的泛素化修饰，参与DNA损伤修复调控，为癌症治疗靶点开发提供依据。
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3. **文献名称**: *UBE2H recombinant protein screening for neurodegenerative disease therapeutics*
**作者**: Patel, S., & Lee, C.G.
**摘要**: 通过体外高通量筛选，评估重组UBE2H蛋白在调控α-突触核蛋白泛素化中的作用。实验表明UBE2H过表达可促进错误折叠蛋白的降解，提示其在帕金森病等神经退行性疾病中的潜在治疗价值。
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如需查找真实文献，建议通过PubMed或Google Scholar搜索关键词“UBE2H recombinant protein”或“UBE2H ubiquitination”。
UBE2H, 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. As an E2 enzyme, UBE2H facilitates the transfer of ubiquitin from E1-activating enzymes to substrate proteins, often in coordination with E3 ubiquitin ligases. This post-translational modification regulates diverse cellular processes, including cell cycle progression, DNA repair, signal transduction, and immune responses. Dysregulation of UBE2H has been implicated in neurodegenerative diseases, cancers, and developmental disorders, highlighting its biological and clinical significance.
Recombinant UBE2H protein is engineered through molecular cloning and heterologous expression systems (e.g., E. coli or mammalian cells) to study its structure, enzymatic activity, and interaction networks. Unlike endogenous UBE2H, the recombinant form is typically produced with affinity tags (e.g., His-tag, GST-tag) for simplified purification and detection. Structural studies reveal that UBE2H adopts a conserved ubiquitin-conjugating fold, with a catalytic cysteine residue essential for thioester bond formation during ubiquitin transfer. Researchers utilize recombinant UBE2H in vitro to reconstitute ubiquitination cascades, screen E3 ligase partners, and investigate substrate specificity. Its applications extend to drug discovery, particularly in developing small-molecule modulators targeting UPS components. However, challenges remain in understanding context-dependent regulation, tissue-specific isoforms, and post-translational modifications affecting UBE2H functionality. Ongoing research aims to elucidate its role in disease mechanisms and exploit recombinant UBE2H as a tool for therapeutic innovation.
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