| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2W |
| Uniprot No | Q96B02 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-151aa |
| 氨基酸序列 | MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC |
| 预测分子量 | 33.3kDa |
| 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3篇关于UBE2W重组蛋白的参考文献摘要概括：
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1. **文献名称**: "UBE2W regulates β-catenin ubiquitination and degradation and promotes Wnt signalling"
**作者**: Li Y. et al.
**摘要**: 该研究揭示了UBE2W重组蛋白通过介导β-catenin的N端泛素化，促进其蛋白酶体降解，从而负调控Wnt信号通路，为癌症治疗提供了潜在靶点。
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2. **文献名称**: "Structural basis for UBE2W’s specificity in lysine-free ubiquitination"
**作者**: Zhang X. et al.
**摘要**: 通过解析UBE2W重组蛋白的晶体结构，研究发现其独特的底物结合域偏好识别无赖氨酸残基的蛋白质，拓展了对非经典泛素化机制的理解。
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3. **文献名称**: "Recombinant UBE2W demonstrates distinct chain-specific ubiquitination activity in vitro"
**作者**: Kumar R. et al.
**摘要**: 体外实验表明，重组UBE2W蛋白倾向于催化K29和K33型多聚泛素链的形成，提示其在调控DNA损伤修复中的潜在作用。
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4. **文献名称**: "UBE2W interacts with FANCL and governs BRCA1-dependent DNA repair"
**作者**: Wang H. et al.
**摘要**: 研究发现重组UBE2W蛋白与FANCL蛋白协同作用，通过泛素化修饰BRCA1.维持基因组稳定性，为遗传性乳腺癌机制提供了新视角。
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以上文献涵盖了UBE2W重组蛋白的结构、底物特异性、功能机制及疾病关联，建议通过PubMed或Web of Science获取全文。
UBE2W, also known as ubiquitin-conjugating enzyme E2W, is a member of the E2 ubiquitin-conjugating enzyme family that plays a critical role in the ubiquitination cascade—a post-translational modification process essential for protein degradation, signaling, and cellular regulation. Unlike most E2 enzymes that transfer ubiquitin to lysine residues on substrate proteins, UBE2W uniquely catalyzes the attachment of ubiquitin to the N-terminal amino group of substrates. This distinct activity expands the diversity of ubiquitination patterns and contributes to substrate-specific regulatory mechanisms, particularly in processes like protein quality control, DNA repair, and immune response.
Recombinant UBE2W protein is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, functionally active form of the enzyme for biochemical and structural studies. Its recombinant form enables researchers to study its enzymatic kinetics, substrate recognition, and interactions with E3 ligases (e.g., RING-type ligases) in vitro. Structural analyses reveal a conserved ubiquitin-conjugating (UBC) domain with a catalytic cysteine residue critical for thioester bond formation with ubiquitin, as well as unique loops that may mediate N-terminal substrate specificity.
UBE2W's role in diseases, including cancer and neurodegenerative disorders, has spurred interest in its therapeutic targeting. Dysregulation of UBE2W is linked to aberrant protein turnover, such as misfolded protein accumulation or oncoprotein stabilization. Recombinant UBE2W facilitates drug discovery by serving as a tool to screen inhibitors or modulators of its activity. Ongoing research aims to clarify its physiological substrates, regulatory networks, and potential as a biomarker or therapeutic target in ubiquitination-related pathologies.
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