| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PEA15 |
| Uniprot No | Q15121 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-130aa |
| 氨基酸序列 | GSHMAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFS FLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDT KLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA |
| 预测分子量 | 15 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PEA15重组蛋白的3篇文献概览(基于公开信息及模拟示例)：
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1. **文献名称**: *"Recombinant PEA-15 protein suppresses tumor growth through inhibition of Erk-mediated cell proliferation"*
**作者**: Trencia A. et al.
**摘要**: 研究利用重组PEA15蛋白，证明其通过抑制Erk信号通路降低癌细胞增殖能力，并在小鼠模型中显著抑制肿瘤生长，提示其潜在抗肿瘤应用价值。
2. **文献名称**: *"Expression and purification of functionally active PEA15 in Escherichia coli for apoptosis regulation studies"*
**作者**: Sharif A. et al.
**摘要**: 描述了在大肠杆菌中高效表达并纯化重组PEA15蛋白的方法，验证其与FADD蛋白的相互作用能力，证实其在调控细胞凋亡中的功能活性。
3. **文献名称**: *"PEA15 modulates lipid metabolism via binding to phospholipase D1 and protects against oxidative stress in astrocytes"*
**作者**: Kim S.K. et al.
**摘要**: 发现重组PEA15通过与磷脂酶D1结合调控脂代谢，并在星形胶质细胞中缓解氧化应激损伤，为神经退行性疾病机制研究提供新方向。
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**注意**：以上文献信息为模拟示例，实际引用请通过PubMed、Web of Science等数据库检索真实文献(如搜索关键词“PEA15 recombinant”或“PEA15 overexpression”)。
PEA15 (Phosphoprotein Enriched in Astrocytes 15), also known as PED (Phosphoprotein Enriched in Diabetes), is a 15 kDa cytoplasmic protein initially identified for its high expression in astrocytes and its role in cellular processes such as apoptosis, proliferation, and glucose metabolism. Structurally, it contains an N-terminal death effector domain (DED) that mediates interactions with apoptotic signaling components like FADD (Fas-associated death domain) and caspase-8. and a C-terminal tail with phosphorylation sites (Ser-104 and Ser-116) regulating its subcellular localization and function.
PEA15 acts as a molecular scaffold, modulating extracellular signal-regulated kinase (ERK)-dependent pathways. By sequestering ERK in the cytoplasm, it inhibits ERK nuclear translocation, thereby attenuating cell proliferation and differentiation. Its anti-apoptotic activity arises from blocking the formation of the death-inducing signaling complex (DISC) in death receptor pathways, promoting cell survival. These dual roles link PEA15 to pathologies like cancer, where its overexpression in gliomas, breast, and ovarian cancers correlates with therapy resistance and poor prognosis. Conversely, in type 2 diabetes, elevated PEA15 levels impair insulin-stimulated glucose uptake by interfering with Akt activation, contributing to insulin resistance.
Recombinant PEA15 proteins are engineered using bacterial (e.g., E. coli) or eukaryotic expression systems to study its structure-function relationships, post-translational modifications, and interactions. These tools enable research into PEA15’s pathophysiological roles and its potential as a therapeutic target. For instance, disrupting PEA15-ERK interactions or restoring apoptotic signaling in cancers, or modulating its activity in metabolic disorders, represents emerging strategies. Studies using recombinant PEA15 have also clarified its phosphorylation-dependent regulation and tissue-specific roles, highlighting its importance in both neurological and systemic diseases.
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