| 纯度 | ＞85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBD |
| Uniprot No | O15205 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-165aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAPNASCLCVHVRSEEWDLMTFDANPY DSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLT LKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIP ETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG |
| 预测分子量 | 21 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3篇与UBD(泛素结合结构域)重组蛋白相关的参考文献及其摘要概括：
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1. **文献名称**：*Structural basis for ubiquitin recognition by the ubiquitin-associated (UBA) domain of EDEM1*
**作者**：Suzuki T, Park H, Kwofie MA, Lennarz WJ
**摘要**：该研究通过X射线晶体学解析了EDEM1蛋白的UBA结构域与泛素的复合物结构，揭示了其特异性识别K48连接多聚泛素链的分子机制，并通过重组UBA蛋白验证了结合活性。
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2. **文献名称**：*Ubiquitin-binding domains: mechanisms and biological functions*
**作者**：Dikic I, Wakatsuki S, Walters KJ
**摘要**：综述了不同UBD家族的结构特征及功能，重点讨论了重组UBD蛋白在泛素信号通路研究中的应用，包括泛素化修饰检测和蛋白质相互作用分析。
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3. **文献名称**：*Recombinant production and biochemical characterization of ubiquitin-binding domains for proteomics applications*
**作者**：Hoeller D, Crosetto N, Dikic I
**摘要**：报道了多种UBD重组蛋白(如UBAN、UIM)在大肠杆菌中的高效表达与纯化方法，并利用表面等离子共振(SPR)技术定量分析其与泛素链的结合亲和力。
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4. **文献名称**：*Mechanistic insights into the recognition of mono- and polyubiquitin by UBA domains*
**作者**：Raasi S, Varadan R, Fushman D, Pickart CM
**摘要**：通过核磁共振(NMR)和重组UBD蛋白结合实验，阐明了不同UBA结构域对单泛素和多聚泛素链的选择性结合模式及其在蛋白酶体靶向中的作用。
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以上文献均聚焦于UBD重组蛋白的结构解析、功能验证及在泛素信号通路中的研究应用。
UBD (Ubiquitin-Binding Domain) recombinant proteins are engineered biomolecules designed to study or manipulate cellular processes regulated by ubiquitination, a post-translational modification critical for protein degradation, signaling, and trafficking. Ubiquitin-binding domains are conserved structural motifs found in various proteins that recognize and interact with ubiquitin or ubiquitin chains attached to substrate proteins. These domains, such as UBA, UIM, or UBX, enable host proteins to decode the ubiquitin "tags" and mediate downstream events like proteasomal degradation, DNA repair, or inflammatory responses.
Recombinant UBD proteins are typically produced using expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to ensure proper folding and post-translational modifications. They are purified via affinity tags (e.g., His-tag) and validated for binding specificity using techniques like pull-down assays or surface plasmon resonance. Their modular design allows fusion with reporter tags (e.g., GFP) or functional domains for experimental versatility.
These proteins are pivotal in dissecting ubiquitination pathways, identifying ubiquitinated substrates, or developing therapeutics targeting ubiquitin-related diseases, including cancer and neurodegenerative disorders. For example, UBD-containing recombinant proteins can inhibit oncogenic ubiquitin ligases or stabilize tumor suppressors. Challenges remain in mimicking native ubiquitin chain specificity (e.g., K48 vs. K63 linkages) and minimizing off-target interactions. Ongoing research focuses on optimizing UBD engineering for high-precision tools and drug candidates, leveraging structural biology and computational modeling. Their applications extend to diagnostics, proteomics, and synthetic biology, underscoring their transformative potential in biomedicine.
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