| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2D3 |
| Uniprot No | P61077 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-147aa |
| 氨基酸序列 | MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVF FLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTIS KVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM |
| 预测分子量 | 17 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UBE2D3重组蛋白的假设性参考文献示例(仅供参考，实际文献需通过学术数据库检索确认)：
---
1. **文献名称**: *"Structural Basis of UBE2D3 and E3 Ligase RNF38 Interaction in Ubiquitination"*
**作者**: Li, X. et al.
**摘要**: 本研究通过重组UBE2D3蛋白的晶体结构解析，揭示了其与E3连接酶RNF38的相互作用界面，阐明了其催化泛素转移的分子机制，为靶向泛素化通路的药物设计提供了结构基础。
2. **文献名称**: *"Recombinant UBE2D3 Expression and Functional Characterization in Parkin-Mediated Mitophagy"*
**作者**: Chen, J. et al.
**摘要**: 文章报道了重组UBE2D3蛋白在大肠杆菌中的高效表达与纯化方法，并通过体外泛素化实验验证了其与Parkin协同调控线粒体自噬的功能，强调了UBE2D3在神经退行性疾病中的潜在作用。
3. **文献名称**: *"UBE2D3 Enhances p53 Degradation via MDM2 in Breast Cancer Cells"*
**作者**: Wang, Y. et al.
**摘要**: 利用重组UBE2D3蛋白进行体外泛素化分析，研究表明UBE2D3通过促进MDM2介导的p53泛素化降解，调控乳腺癌细胞增殖，为癌症治疗提供了新的靶点。
---
**注意**：以上文献为示例，实际引用时请通过PubMed、Web of Science或Google Scholar等平台检索真实文献并核对信息。
UBE2D3. also known as ubiquitin-conjugating enzyme E2 D3. is a member of the E2 ubiquitin-conjugating enzyme family involved in the ubiquitin-proteasome system (UPS), a critical pathway for targeted protein degradation in eukaryotic cells. As a key mediator of ubiquitination, UBE2D3 facilitates the transfer of ubiquitin molecules from E1 activating enzymes to substrate proteins, often in collaboration with E3 ubiquitin ligases. This post-translational modification typically marks proteins for proteasomal degradation, though it can also regulate cellular processes like DNA repair, signal transduction, and trafficking.
Recombinant UBE2D3 protein is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce high-purity, functional enzyme for *in vitro* studies. Its conserved catalytic core contains a cysteine residue critical for thioester bond formation with ubiquitin. Structural studies reveal a conserved α/β fold typical of E2 enzymes, with surface regions enabling interactions with diverse E3 ligases, including RING-finger and HECT-domain types.
Research applications of recombinant UBE2D3 span mechanistic studies of ubiquitination cascades, drug discovery screening for UPS-targeted therapies, and disease modeling. It is particularly relevant in cancer research, where dysregulated ubiquitination contributes to oncoprotein stabilization (e.g., cyclins, c-Myc) or tumor suppressor degradation. In neurodegenerative diseases like Alzheimer's, altered UBE2D3 activity may influence amyloidogenic protein clearance. Mutant variants of UBE2D3 are also used to dissect structure-function relationships and substrate specificity. The recombinant protein's standardized activity enables quantitative comparisons in biochemical assays, making it a vital tool for deciphering UPS dynamics and developing therapeutic strategies.
×
