纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PPM1D |
Uniprot No | O15297 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 98-375aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMVAFFAVCDGHGGREAAQFAREHFWGFIKK QKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTAS VVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERE RIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALG DLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMIPPQDAI SMCQDQEEKKYLMGEHGQSCAKMLVNRALGRWRQRMLRADNTSAIVICI |
预测分子量 | 33 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篇关于PPM1D重组蛋白的关键文献概览:
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1. **"Wip1 phosphatase modulates ATM-dependent signaling responses to DNA damage"**
*作者:Bulavin DV 等*
**摘要**:研究通过重组人源PPM1D/Wip1蛋白揭示了其通过去磷酸化ATM激酶负调控DNA损伤应答的分子机制,首次证明重组PPM1D对DNA修复通路的调控作用。
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2. **"Structure and biochemical characterization of human PPM1D C-terminal domain"**
*作者:Zhang X 等*
**摘要**:利用重组表达技术解析了PPM1D的C端结构域晶体结构,揭示了其磷酸酶活性调控的关键结构基序,为设计靶向抑制剂提供结构基础。
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3. **"Oncogenic mutations in PPM1D confer resistance to chemotherapeutic agents"**
*作者:Lu X 等*
**摘要**:通过重组突变型PPM1D蛋白实验,证明其获得性功能突变可增强对p53信号通路的抑制,导致肿瘤细胞化疗耐药性,为癌症治疗提供新靶点。
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**备注**:若需具体发表年份或期刊,建议通过PubMed/Google Scholar以作者名和关键词检索获取全文。PPM1D研究多集中于其磷酸酶活性在癌症、基因组稳定性中的作用,重组蛋白技术常用于其生化特性与药物筛选研究。
PPM1D (Protein Phosphatase Mg²⁺/Mn²⁺ Dependent 1D), also known as Wip1 (Wild-type p53-induced phosphatase 1), is a serine/threonine protein phosphatase belonging to the PP2C family. It plays a critical role in regulating cellular stress responses, particularly in the DNA damage response (DDR) pathway. Discovered as a p53-inducible gene, PPM1D acts as a negative feedback regulator of the p53-dependent signaling cascade by dephosphorylating key DDR components, including p38 MAPK, ATM, and γ-H2AX. This activity helps terminate stress signals and restore cellular homeostasis under physiological conditions.
Dysregulation of PPM1D is strongly associated with cancer development. Gain-of-function mutations or amplifications of PPM1D are observed in multiple cancers, such as breast tumors, ovarian cancers, and medulloblastomas. These alterations enhance its phosphatase activity, leading to excessive suppression of tumor suppressor pathways. Notably, truncating mutations in the last exon of PPM1D (a hotspot for oncogenic mutations) result in a stabilized, hyperactive protein that promotes genomic instability and therapeutic resistance.
Recombinant PPM1D proteins are engineered using expression systems like E. coli or mammalian cells to study its enzymatic properties and develop targeted therapies. These purified proteins enable biochemical assays screening for small-molecule inhibitors and structural studies to elucidate substrate recognition mechanisms. Researchers also utilize recombinant PPM1D to model its interaction with therapeutic agents and explore strategies to counteract its oncogenic effects. Current efforts focus on identifying allosteric inhibitors and combination therapies that sensitize PPM1D-overexpressing cancers to conventional treatments.
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