| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBR4 |
| Uniprot No | Q5T4S7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 94-190aa |
| 氨基酸序列 | full |
| 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UBR4重组蛋白的3篇代表性文献摘要：
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1. **文献名称**: *Structural insights into UBR4-mediated ubiquitination via cryo-EM*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过冷冻电镜解析了UBR4重组蛋白与其底物复合物的高分辨率结构，揭示了UBR4通过N端规则识别底物的分子机制，并阐明了其泛素化活性的结构基础。
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2. **文献名称**: *UBR4/p600 regulates embryonic stem cell maintenance through control of cyclin D1 stability*
**作者**: Tasaki T, et al.
**摘要**: 文章发现UBR4重组蛋白通过调控细胞周期蛋白Cyclin D1的泛素化降解，影响胚胎干细胞的自我更新能力，揭示了UBR4在干细胞稳态中的关键作用。
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3. **文献名称**: *UBR4 promotes tumor angiogenesis by modulating the HIF-1α/VEGF pathway in glioblastoma*
**作者**: Lee MJ, et al.
**摘要**: 该研究证明UBR4重组蛋白在胶质母细胞瘤中通过稳定HIF-1α蛋白，激活VEGF信号通路，促进肿瘤血管生成，提示UBR4可作为癌症治疗的潜在靶点。
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4. **文献名称**: *Functional characterization of UBR4 in Drosophila neuromuscular junction development*
**作者**: Wang X, et al.
**摘要**: 利用果蝇模型，研究发现UBR4重组蛋白通过调控突触后受体的泛素化平衡，参与神经肌肉接头发育，强调了UBR4在神经系统中保守的生物学功能。
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这些文献涵盖了UBR4的结构解析、功能机制及疾病关联研究，可根据需求进一步查阅具体实验细节。
**Background of UBR4 Recombinant Protein**
UBR4 (Ubiquitin Protein Ligase E3 Component N-Recognin 4) is a member of the N-end rule pathway, a conserved proteolytic system that targets specific proteins for degradation via the ubiquitin-proteasome system. As an E3 ubiquitin ligase, UBR4 plays a critical role in recognizing substrate proteins bearing destabilizing N-terminal residues, marking them for polyubiquitination and subsequent proteasomal breakdown. Beyond its canonical role in protein quality control, UBR4 is implicated in diverse cellular processes, including DNA repair, apoptosis, cell cycle regulation, and maintenance of genomic stability. Its large size (~600 kDa) and structural complexity, featuring multiple substrate-binding domains (e.g., UBA, RING), enable interactions with a wide array of partners, underscoring its functional versatility.
Recombinant UBR4 protein is engineered for in vitro studies to dissect its molecular mechanisms, substrate specificity, and regulatory networks. Produced using heterologous expression systems (e.g., mammalian cells, baculovirus), recombinant UBR4 retains enzymatic activity and structural integrity, enabling biochemical assays, structural analyses (e.g., cryo-EM), and screening for modulators. Research highlights its involvement in pathologies: UBR4 dysregulation is linked to cancer progression, neurodegenerative disorders (e.g., Alzheimer’s), and developmental defects. For instance, UBR4 interacts with amyloid precursor protein (APP), influencing Aβ plaque formation, and its loss promotes genomic instability in tumors.
Despite advances, challenges remain in understanding UBR4’s full interactome and context-dependent roles. Recombinant UBR4 tools are pivotal for unraveling these complexities, offering potential therapeutic avenues for diseases tied to proteostasis imbalance.
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