| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGP |
| Uniprot No | A6NDG6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-321aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMAAAEA GGDDARCVRL SAERAQALLA DVDTLLFDCD GVLWRGETAV PGAPEALRAL RARGKRLGFI TNNSSKTRAA YAEKLRRLGF GGPAGPGASL EVFGTAYCTA LYLRQRLAGA PAPKAYVLGS PALAAELEAV GVASVGVGPE PLQGEGPGDW LHAPLEPDVR AVVVGFDPHF SYMKLTKALR YLQQPGCLLV GTNMDNRLPL ENGRFIAGTG CLVRAVEMAA QRQADIIGKP SRFIFDCVSQ EYGINPERTV MVGDRLDTDI LLGATCGLKT ILTLTGVSTL GDVKNNQESD CVSKKKMVPD FYVDSIADLL PALQG |
| 预测分子量 | 37 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PGP(P-glycoprotein)重组蛋白研究的参考文献摘要概括：
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1. **"Expression and Purification of Recombinant P-Glycoprotein in Escherichia coli"**
*Loo, T.W., Clarke, D.M.*
研究报道了利用大肠杆菌表达系统成功表达并纯化人源P-gp跨膜结构域重组蛋白，通过定点突变优化了蛋白稳定性，为后续结构功能研究奠定基础。
2. **"Functional Characterization of Recombinant Human P-Glycoprotein in Saccharomyces cerevisiae"**
*Shapiro, A.B., Viktorova, E.*
通过酵母表达系统实现全长人源P-gp重组蛋白的功能性表达，验证其ATP酶活性及药物外排功能，证明该系统适用于耐药性机制的高通量分析。
3. **"Cryo-EM Structure of Recombinant Mouse P-Glycoprotein in Lipid Bilayers"**
*Alam, A., et al.*
利用昆虫细胞表达系统制备重组小鼠P-gp蛋白，结合冷冻电镜技术解析其在脂质双分子层中的三维结构，揭示药物结合口袋的动态构象变化。
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注：PGP(P-glycoprotein)为多药耐药转运蛋白，上述文献聚焦重组表达系统的开发(如大肠杆菌、酵母、昆虫细胞)及其在结构解析与药物相互作用研究中的应用。如需具体文献编号或出版年份，建议通过PubMed/Google Scholar检索作者及关键词。
P-Glycoprotein (P-gp), encoded by the *ABCB1* gene, is a well-studied ATP-binding cassette (ABC) transporter first identified in 1976 for its role in multidrug resistance (MDR) in cancer. Overexpressed in tumor cells, P-gp actively effluxes chemotherapeutic agents, reducing intracellular drug accumulation and diminishing treatment efficacy. Its discovery revolutionized understanding of cellular detoxification mechanisms and drug transport. Structurally, P-gp consists of two homologous halves, each containing a transmembrane domain (TMD) for substrate recognition and a cytosolic nucleotide-binding domain (NBD) for ATP hydrolysis. This configuration enables ATP-driven translocation of diverse substrates, including anticancer drugs, antibiotics, and toxins.
Recombinant P-gp production, achieved via heterologous expression systems like mammalian cells (e.g., HEK293), insect cells, or yeast, allows detailed functional and structural studies. Escherichia coli-based systems are less common due to challenges in folding this large (~170 kDa), complex membrane protein. Purification typically involves affinity chromatography tags (e.g., His-tag) followed by reconstitution into lipid bilayers or detergent micelles for in vitro assays. Recombinant P-gp is pivotal in screening modulators to overcome MDR, analyzing drug-transporter interactions, and deciphering molecular mechanisms of ATP-coupled transport. Recent cryo-EM structures of human P-gp have revealed conformational changes during its transport cycle, informing drug design strategies. Beyond oncology, P-gp influences pharmacokinetics by limiting blood-brain barrier penetration or intestinal absorption of drugs, making its recombinant form essential for predicting drug disposition and toxicity. Ongoing research focuses on optimizing expression platforms, elucidating substrate specificity, and developing targeted inhibitors to enhance therapeutic outcomes.
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