纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PDP2 |
Uniprot No | Q9P2J9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 67-529aa |
氨基酸序列 | STEEDDFHLQLSPEQINEVLRAGETTHKILDLESRVPNSVLRFESNQLAANSPVEDRRGVASCLQTNGLMFGIFDGHGGHACAQAVSERLFYYVAVSLMSHQTLEHMEGAMESMKPLLPILHWLKHPGDSIYKDVTSVHLDHLRVYWQELLDLHMEMGLSIEEALMYSFQRLDSDISLEIQAPLEDEVTRNLSLQVAFSGATACMAHVDGIHLHVANAGDCRAILGVQEDNGMWSCLPLTRDHNAWNQAELSRLKREHPESEDRTIIMEDRLLGVLIPCRAFGDVQLKWSKELQRSILERGFNTEALNIYQFTPPHYYTPPYLTAEPEVTYHRLRPQDKFLVLASDGLWDMLSNEDVVRLVVGHLAEADWHKTDLAQRPANLGLMQSLLLQRKASGLHEADQNAATRLIRHAIGNNEYGEMEAERLAAMLTLPEDLARMYRDDITVTVVYFNSESIGAYYKGG |
预测分子量 | 56.4 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PDP2(丙酮酸脱氢酶磷酸酶2)重组蛋白的模拟参考文献示例,供参考:
1. **文献名称**:*Recombinant Expression and Functional Characterization of Human Pyruvate Dehydrogenase Phosphatase 2*
**作者**:Smith, J. et al.
**摘要**:报道了在大肠杆菌中成功表达并纯化重组人源PDP2.验证其通过去磷酸化激活丙酮酸脱氢酶复合体的功能,并分析其酶动力学特性。
2. **文献名称**:*Structural Insights into PDP2 Regulation of Mitochondrial Energy Metabolism*
**作者**:Lee, H. et al.
**摘要**:通过X射线晶体学解析了PDP2的三维结构,揭示了其与丙酮酸脱氢酶复合体的相互作用界面及Mg²⁺依赖性催化机制。
3. **文献名称**:*Role of PDP2 in Insulin Resistance: Evidence from Recombinant Protein-Based Assays*
**作者**:Johnson, R. et al.
**摘要**:利用重组PDP2蛋白进行体外实验,证明其在胰岛素抵抗模型中通过调节糖代谢关键酶活性影响葡萄糖稳态。
4. **文献名称**:*Development of a High-Throughput Screening Assay for PDP2 Activators Using Recombinant Protein*
**作者**:Chen, L. et al.
**摘要**:基于重组PDP2建立药物筛选平台,发现小分子激活剂可增强其磷酸酶活性,为代谢性疾病治疗提供新策略。
**注意**:以上为模拟文献,实际研究中请通过PubMed、Google Scholar等平台检索最新文献(关键词:PDP2、PDHP phosphatase 2、recombinant protein)。
**Background of PDP2 Recombinant Protein**
The PDP2 (Pyruvate Dehydrogenase Phosphatase 2) recombinant protein is a engineered form of the regulatory enzyme involved in mitochondrial energy metabolism. PDP2 specifically dephosphorylates and reactivates the pyruvate dehydrogenase complex (PDC), a critical multienzyme system that converts pyruvate to acetyl-CoA, linking glycolysis to the tricarboxylic acid (TCA) cycle. PDC activity is tightly regulated by phosphorylation (inactivation) by pyruvate dehydrogenase kinases (PDKs) and dephosphorylation (activation) by PDPs. PDP2. one of two known PDP isoforms, plays a key role in maintaining metabolic flexibility, particularly in tissues with high energy demands like liver, muscle, and heart.
Recombinant PDP2 is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable large-scale purification for research and therapeutic applications. Its production allows detailed study of PDP2’s structure-function relationships, regulatory mechanisms, and interactions with PDC components. Dysregulation of PDP2 is linked to metabolic disorders, such as insulin resistance, diabetes, and cancer, where altered glucose oxidation impacts disease progression. For example, reduced PDP2 activity may suppress PDC function, shifting cells toward glycolytic metabolism—a hallmark of cancer (Warburg effect).
Research on PDP2 recombinant protein also explores its potential as a therapeutic target. Modulating PDP2 activity could restore metabolic balance in diseases characterized by mitochondrial dysfunction. However, challenges remain in understanding tissue-specific regulation and avoiding off-target effects. Current studies leverage recombinant PDP2 to screen for activators/inhibitors and develop precision therapies. Overall, PDP2 recombinant protein serves as a vital tool for dissecting metabolic pathways and advancing treatments for metabolic and degenerative diseases.
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