| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRUNE |
| Uniprot No | Q86TP1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-168aa |
| 氨基酸序列 | MLRKDQKTIYRQGVKVAISAIYMDLEICEVLERSHSPPLKLTPASSTHPNLHAYLQGNTQVSRKKLLPLLQEALSAYFDSMKIPSGQPETADVSREQVDKELDRASNSLISGLSQDEEDPPLPPTPMNSLVDECPLDQGLPKLSAEAVFEKCSQISLSQSTTASLSKK |
| 预测分子量 | 22.5 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PRUNE重组蛋白的3篇参考文献(基于模拟数据，非真实文献)：
1. **文献名称**: *PRUNE promotes TGF-β-induced epithelial-mesenchymal transition in colorectal cancer*
**作者**: Carotenuto, M. et al.
**摘要**: 研究揭示了PRUNE通过激活TGF-β/Smad信号通路促进结直肠癌细胞的上皮-间质转化(EMT)，增强侵袭和转移能力，提示其作为癌症治疗靶点的潜力。
2. **文献名称**: *Structural insights into the catalytic mechanism of PRUNE protein in neurodevelopmental disorders*
**作者**: Bessette, P.H. et al.
**摘要**: 通过X射线晶体学解析PRUNE蛋白的三维结构，阐明其磷酸酶活性位点及突变导致的功能异常，为神经发育疾病(如小头畸形)的机制研究提供依据。
3. **文献名称**: *PRUNE1 deficiency drives neurodegenerative phenotypes via dysregulated mitochondrial dynamics*
**作者**: Smith, J. et al.
**摘要**: 在小鼠模型中证明PRUNE1缺失通过扰乱线粒体动力学和能量代谢导致神经元退行性变，强调了PRUNE在维持神经元稳态中的关键作用。
4. **文献名称**: *Targeting PRUNE with small-molecule inhibitors for metastatic breast cancer therapy*
**作者**: Zhang, L. et al.
**摘要**: 开发特异性靶向PRUNE的小分子抑制剂，在乳腺癌模型中有效抑制肿瘤转移并延长生存期，验证了PRUNE作为治疗转移性癌症的可行性。
(注：以上文献为示例性质，实际研究中请通过学术数据库核实具体信息。)
PRUNE recombinant protein is derived from the human PRUNE (prune exopolyphosphatase) protein, a member of the DHH phosphoesterase superfamily. Initially identified for its role in Drosophila development, human PRUNE is implicated in cellular processes such as proliferation, migration, and metastasis. Structurally, PRUNE contains conserved DHH and DHHA2 domains critical for its enzymatic activity, which includes phosphatase and exopolyphosphatase functions. Dysregulation of PRUNE is linked to cancer progression, particularly in tumors like breast cancer, neuroblastoma, and glioblastoma, where it often correlates with poor prognosis and metastatic potential.
Research highlights PRUNE's interaction with key signaling pathways, including TGF-β and BMP-Smad cascades. For instance, PRUNE binds to BMPR1A, modulating Smad1/5/8 phosphorylation to enhance cell invasiveness. Its overexpression is associated with upregulated oncogenic drivers (e.g., MYC, AKT) and suppression of tumor suppressors (e.g., PTEN). PRUNE also interacts with non-coding RNAs, such as miR-30c-2-3p, creating feedback loops that sustain its pro-metastatic activity.
Recombinant PRUNE protein is engineered for functional studies, enabling researchers to explore its biochemical properties, substrate specificity, and role in cancer biology. It serves as a tool to screen inhibitors targeting PRUNE's enzymatic or interaction domains, with therapeutic potential. Additionally, recombinant forms aid in antibody development for diagnostic assays. Despite progress, PRUNE's full mechanistic spectrum—particularly its non-catalytic roles and tissue-specific functions—remains under investigation, driving ongoing interest in its utility as a biomarker or therapeutic target in precision oncology.
×
