| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PI3 |
| Uniprot No | P19957 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 61-117aa |
| 氨基酸序列 | AQEPVKGPVSTKPGSCPIILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQ |
| 预测分子量 | 22.0kDa |
| 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PI3K重组蛋白的参考文献示例(内容为虚构，仅作格式参考)：
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1. **"Functional expression and purification of recombinant PI3Kγ for structural studies"**
*Johnson, A. et al.*
该研究利用杆状病毒-昆虫细胞系统成功表达并纯化了具有活性的PI3Kγ重组蛋白，通过冷冻电镜解析其三维结构，为靶向该激酶的药物设计提供了基础。
2. **"Optimization of PI3Kα recombinant protein production in mammalian cells for kinase activity screening"**
*Chen, L. & Wang, H.*
作者开发了一种HEK293细胞表达系统，高效制备PI3Kα重组蛋白，并验证其在体外激酶活性检测及小分子抑制剂筛选中的应用，提升了药物研发效率。
3. **"Site-specific phosphorylation analysis of recombinant PI3Kβ in cancer signaling pathways"**
*Martinez, R. et al.*
研究通过大肠杆菌表达体系获得非磷酸化PI3Kβ重组蛋白，结合质谱技术分析其酪氨酸磷酸化位点，揭示了该蛋白在肿瘤细胞异常活化中的调控机制。
4. **"A high-yield method for purifying active PI3Kδ heterodimer from E. coli inclusion bodies"**
*Saito, K. et al.*
报道了一种通过原核表达系统规模化制备PI3Kδ异源二聚体重组蛋白的策略，利用包涵体重折叠技术获得高纯度活性蛋白，降低了体外研究成本。
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注：以上文献为示例，实际引用时请以真实论文数据为准，并核对期刊名称、年份及作者信息。
**Background of PI3 Recombinant Protein**
Phosphoinositide 3-kinases (PI3Ks) are a family of lipid kinases critical for regulating cellular processes such as growth, survival, metabolism, and motility. Among them, the class I PI3K isoforms (e.g., PI3Kα, β, δ, γ) are particularly notable for their roles in signal transduction downstream of receptor tyrosine kinases and G-protein-coupled receptors. Dysregulation of PI3K signaling is implicated in numerous diseases, including cancer, immune disorders, and diabetes, making PI3K a key therapeutic target.
Recombinant PI3K proteins are engineered versions produced via heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*) to study their structure, function, and interactions. These proteins retain enzymatic activity and structural integrity, enabling *in vitro* assays, drug screening, and mechanistic studies. The development of recombinant PI3K has been pivotal in deciphering the molecular basis of PI3K-AKT-mTOR pathway activation and inhibition.
Advances in protein engineering, such as codon optimization, fusion tags (e.g., GST, His-tag), and post-translational modification mimicry, have enhanced the stability and solubility of recombinant PI3K. This has facilitated high-resolution structural studies (e.g., X-ray crystallography, cryo-EM), revealing conformational changes during lipid substrate binding and inhibitor interactions.
Clinically, recombinant PI3K proteins are used to screen and validate inhibitors (e.g., idelalisib, alpelisib) targeting specific isoforms, aiding personalized therapies. However, challenges remain, including maintaining native folding in heterologous systems and reproducing complex regulatory interactions with partners like RAS or regulatory subunits.
Overall, recombinant PI3K proteins serve as indispensable tools for basic research and drug development, bridging molecular insights with therapeutic innovation in precision medicine.
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