| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | WWP2 |
| Uniprot No | O00308 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-870aa |
| 氨基酸序列 | MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLP SETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTAS VNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGN VPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGAS ARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSV VGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPD ALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVD HNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTD HDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGW EMKYTSEGVRYFVDHNTRTTTFKDPRPGFE SGTKQGSPGAYDRSFRWK YHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIM RGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSIN PDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESID PEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTE ENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELM LCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFV TGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYK SYEQLREKLLYAIEETEGFGQE |
| 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WWP2重组蛋白的3篇参考文献及其简要摘要：
1. **《WWP2-mediated ubiquitination of the RNA polymerase II mediates transcriptional regulation》**
- **作者**: Chen C, Sun X, et al.
- **摘要**: 研究揭示了WWP2通过泛素化RNA聚合酶II的Rpb1亚基，调控转录延伸和DNA损伤修复。实验中利用重组WWP2蛋白验证了其E3泛素连接酶活性，并证明其功能缺失导致转录异常。
2. **《WWP2 regulates cartilage development through TGF-β/SMAD signaling》**
- **作者**: Li Y, Wang Y, et al.
- **摘要**: 该研究利用重组WWP2蛋白进行体外实验，发现其通过泛素化SMAD2/3调控TGF-β信号通路，影响软骨细胞分化和骨骼发育，为骨关节炎治疗提供了潜在靶点。
3. **《Structural basis for WWP2 activation by phosphorylation》**
- **作者**: Zhang L, Huang J, et al.
- **摘要**: 通过解析重组WWP2蛋白的晶体结构，研究发现其激酶依赖的磷酸化修饰可激活其泛素连接酶活性，揭示了WWP2在癌症中异常活化的分子机制。
**Background of WWP2 Recombinant Protein**
WWP2 (WW Domain-Containing E3 Ubiquitin Protein Ligase 2) is a member of the HECT-type E3 ubiquitin ligase family, which plays a critical role in post-translational protein modification by mediating the transfer of ubiquitin molecules to specific substrate proteins. This ubiquitination process regulates diverse cellular processes, including protein degradation, signal transduction, DNA repair, and cell cycle progression. WWP2 is characterized by its N-terminal WW domains, which facilitate substrate recognition by binding to proline-rich motifs, and a C-terminal HECT domain responsible for catalytic ubiquitin transfer activity.
Recombinant WWP2 protein is engineered through molecular cloning and expression in heterologous systems (e.g., *E. coli* or mammalian cell lines), allowing large-scale production of purified, biologically active protein for research. Its recombinant form retains the enzymatic activity and structural features required for studying ubiquitination mechanisms *in vitro*. Researchers utilize WWP2 recombinant protein to investigate its interactions with substrates such as SMAD transcription factors (e.g., SMAD2. SMAD7), RUNX2. and PTEN, which are implicated in TGF-β/BMP signaling, osteogenesis, and tumor suppression, respectively. Dysregulation of WWP2 has been linked to diseases like cancer, osteoporosis, and neurological disorders, highlighting its therapeutic relevance.
Studies involving WWP2 recombinant protein also explore its role in modulating pathways like Wnt/β-catenin and Notch, as well as its potential as a drug target. For instance, small-molecule inhibitors targeting WWP2’s HECT domain are being developed to counteract its oncogenic activities. Additionally, structural analyses using recombinant WWP2 have provided insights into substrate-binding specificity and catalytic mechanisms, advancing the understanding of E3 ligase function in health and disease.
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