| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPARd |
| Uniprot No | Q03181 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 165-441aa |
| 氨基酸序列 | GSQYNPQVADLKAFSKHIYNAYLKNFNMTKKKARSILTGKASHTAPFVIHDIETLWQAEKGLVWKQLVNGLPPYKEISVHVFYRCQCTTVETVRELTEFAKSIPSFSSLFLNDQVTLLKYGVHEAIFAMLASIVNKDGLLVANGSGFVTREFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGDRPGLMNVPRVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRIKKTETETSLHPLLQEIYKDMY |
| 预测分子量 | 49.8 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PPARδ重组蛋白的3篇代表性文献摘要概括：
1. **文献名称**: "Purification and characterization of the human PPARδ ligand-binding domain produced in Escherichia coli"
**作者**: Chandra Shekar, V. et al.
**摘要**: 该研究成功在大肠杆菌中表达并纯化了人源PPARδ配体结合域(LBD)。通过优化诱导条件获得可溶性蛋白，并利用亲和层析和凝胶过滤技术纯化，证实其具有配体结合活性，为体外药物筛选奠定基础。
2. **文献名称**: "Crystal structure of the PPARδ ligand-binding domain in complex with a selective agonist"
**作者**: Xu, H.E. et al.
**摘要**: 报道了PPARδ-LBD重组蛋白与选择性激动剂GW501516的复合物晶体结构(分辨率2.3 Å)，揭示了配体结合口袋的构象变化及关键氨基酸相互作用，为设计高选择性PPARδ调节剂提供结构依据。
3. **文献名称**: "Functional analysis of PPARδ using recombinant adenovirus: lipid uptake regulation in macrophages"
**作者**: Lee, C.H. et al.
**摘要**: 通过重组腺病毒系统过表达PPARδ，发现其显著增强巨噬细胞中CD36表达及氧化低密度脂蛋白摄取，证明PPARδ在脂代谢调控中的核心作用，提示其与动脉粥样硬化病理过程相关。
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**领域动态**：近年研究聚焦于PPARδ重组蛋白的高效表达系统开发(如哺乳动物/昆虫细胞体系)、冷冻电镜结构解析(如Nature 2021年报道的全长受体结构)，以及基于重组蛋白的高通量药物筛选平台构建。建议通过PubMed检索关键词“PPARdelta recombinant protein structural/functional study”获取最新文献。
Peroxisome proliferator-activated receptor delta (PPARδ), a member of the nuclear receptor superfamily, plays a pivotal role in regulating metabolic homeostasis, inflammation, and cellular differentiation. As one of three PPAR isoforms (α, γ, δ), PPARδ is ubiquitously expressed but particularly abundant in tissues with high oxidative capacity, such as skeletal muscle, adipose tissue, and the heart. It functions as a ligand-activated transcription factor, binding to specific DNA response elements to modulate gene networks involved in lipid metabolism, glucose homeostasis, and energy expenditure. Its activation enhances fatty acid oxidation, improves insulin sensitivity, and promotes mitochondrial biogenesis, making it a therapeutic target for metabolic disorders.
Recombinant PPARδ protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., E. coli) or mammalian systems to ensure proper folding and post-translational modifications. This engineered protein retains key functional domains: a DNA-binding domain (DBD) and a ligand-binding domain (LBD), enabling researchers to study receptor-ligand interactions, coactivator recruitment, and DNA binding mechanisms in vitro. Purification methods often involve affinity tags (e.g., His-tag) followed by chromatography to achieve high purity.
In drug discovery, recombinant PPARδ serves as a critical tool for screening synthetic or natural agonists/antagonists. Its role in mitigating atherosclerosis, obesity, and type 2 diabetes has driven pharmaceutical interest, though clinical applications remain cautious due to pleiotropic effects. Structural studies using recombinant PPARδ have revealed conformational changes during activation, informing the design of selective modulators. Ongoing research also explores its neuroprotective and anti-cancer potentials, expanding its therapeutic relevance beyond metabolic diseases.
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