纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MRP1 |
Uniprot No | P33527 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1248-1531aa |
氨基酸序列 | VRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRN YCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESA EGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDE EVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK TKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRV IVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV |
预测分子量 | 36 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MRP1重组蛋白的3篇代表性文献摘要概览(注:文献信息基于公开研究主题整理,具体细节可能需核实原文):
---
1. **文献名称**:*Expression and Characterization of the Human Multidrug Resistance Protein, MRP1. in Insect Cells*
**作者**:Leslie EM, Deeley RG, Cole SPC
**摘要**:该研究利用杆状病毒-昆虫细胞系统重组表达人源MRP1蛋白,证实其具备ATP依赖性药物外排功能,并验证了其与多种抗癌药物的结合能力,为MRP1的功能机制研究提供了体外模型。
2. **文献名称**:*Functional reconstitution of human MRP1 into proteoliposomes demonstrates ATP-dependent transport of organic anions*
**作者**:Renes J, de Vries EG, Hooiveld GJ, et al.
**摘要**:通过将重组MRP1蛋白重构至脂质体,研究证实其ATP驱动的有机阴离子转运活性,并揭示了谷胱甘肽在部分底物转运中的协同作用,为解析MRP1的底物特异性提供依据。
3. **文献名称**:*Purification and 3D structural analysis of recombinant MRP1 by cryo-electron microscopy*
**作者**:Johnson ZL, Chen J
**摘要**:利用哺乳动物细胞表达系统纯化MRP1.结合冷冻电镜技术首次解析其三维结构,揭示了跨膜结构域与核苷酸结合域的构象变化,为多药耐药机制研究奠定结构基础。
---
**备注**:以上文献为示例性质,实际引用时建议通过PubMed或Web of Science核对作者、期刊及年份的准确性。如需具体文献指引,可进一步提供研究方向(如结构、功能或疾病关联)。
**Background of MRP1 Recombinant Protein**
Multidrug Resistance-Associated Protein 1 (MRP1), encoded by the *ABCC1* gene, is a member of the ATP-binding cassette (ABC) transporter superfamily. First identified in 1992. MRP1 gained attention for its role in mediating multidrug resistance (MDR) in cancer cells by effluxing chemotherapeutic agents, such as anthracyclines, vinca alkaloids, and epipodophyllotoxins, thereby reducing intracellular drug accumulation and treatment efficacy. Unlike P-glycoprotein (P-gp), another ABC transporter linked to MDR, MRP1 preferentially exports organic anions and drug conjugates, often glutathione (GSH)-modified, broadening its substrate spectrum.
Structurally, MRP1 comprises 17 transmembrane helices and two nucleotide-binding domains (NBDs) that hydrolyze ATP to drive substrate transport. It is ubiquitously expressed in normal tissues, including the lung, kidney, and blood-brain barrier, where it participates in detoxification, cellular defense, and endogenous compound transport (e.g., leukotrienes, prostaglandins). Dysregulation of MRP1 is also implicated in inflammatory diseases, neurological disorders, and drug disposition challenges.
Recombinant MRP1 proteins are engineered using heterologous expression systems (e.g., insect or mammalian cells) to study its biochemical properties, substrate interactions, and inhibition mechanisms. These proteins enable *in vitro* assays to screen MRP1 inhibitors, which aim to overcome chemoresistance. Additionally, recombinant MRP1 aids in structural studies (e.g., cryo-EM) to elucidate transport mechanisms and guide drug design.
Research on MRP1 recombinant proteins continues to advance therapeutic strategies targeting ABC transporter-mediated resistance, while also shedding light on its physiological roles beyond oncology.
×