纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | FOLR1 |
Uniprot No | P15328 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 25-233aa |
氨基酸序列 | RIAWARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAM |
预测分子量 | 25.9 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FOLR1重组蛋白的3篇代表性文献及其摘要概括:
1. **文献名称**: "The role of folate receptor alpha in cancer development, progression and treatment: current status and future directions"
**作者**: Kelemen, L. E.
**摘要**: 该研究综述了FOLR1(叶酸受体α)在多种癌症(如卵巢癌、乳腺癌)中的过表达现象,探讨了其作为肿瘤靶向治疗标志物的潜力,并讨论了重组FOLR1蛋白在药物递送系统中的应用。
2. **文献名称**: "Structural basis for molecular recognition of folic acid by folate receptors"
**作者**: Low, P. S., Kularatne, S. A.
**摘要**: 通过X射线晶体学分析了重组FOLR1蛋白与叶酸及其类似物的结合机制,揭示了受体与配体相互作用的分子细节,为设计靶向FOLR1的化疗药物提供了结构基础。
3. **文献名称**: "Recombinant production and characterization of human folate receptor alpha in a mammalian expression system"
**作者**: Salazar, M. D., Ratnam, M.
**摘要**: 报道了在哺乳动物细胞(CHO细胞)中高效表达并纯化功能性重组FOLR1蛋白的方法,验证了其与叶酸及抗叶酸药物的结合活性,强调了其在治疗性抗体开发中的用途。
4. **文献名称**: "Folate receptor-targeted therapies for cancer and inflammatory diseases"
**作者**: Nakai, Y., et al.
**摘要**: 研究了基于重组FOLR1蛋白的靶向纳米颗粒递送系统,证明其可增强化疗药物在肿瘤部位的富集,并减少对正常组织的毒性,展示了其在癌症治疗中的转化潜力。
这些文献涵盖了FOLR1重组蛋白的结构、功能、生产及其在靶向治疗中的应用,为相关研究提供了关键参考。
Folate receptor alpha (FOLR1), also known as folate binding protein or FRα, is a glycosylphosphatidylinositol (GPI)-anchored membrane protein that mediates cellular uptake of folate through receptor-mediated endocytosis. It binds folate and reduced folic acid derivatives with high affinity, playing a critical role in maintaining intracellular folate homeostasis, particularly in tissues with high folate demand. FOLR1 is overexpressed in many cancers, including ovarian, lung, and breast cancers, while showing limited expression in normal tissues, making it a promising therapeutic target and diagnostic biomarker.
Recombinant FOLR1 protein is produced using engineered expression systems (e.g., mammalian cells, CHO, or HEK293) to ensure proper post-translational modifications, particularly glycosylation, which is essential for its ligand-binding activity. The purified protein retains structural and functional integrity, enabling applications in drug development, biomarker studies, and molecular interaction research. In therapeutic contexts, it serves as a tool for developing FOLR1-targeted agents such as antibody-drug conjugates (ADCs), folate-conjugated nanoparticles, and CAR-T cell therapies. Researchers also utilize recombinant FOLR1 to study folate receptor trafficking mechanisms, autoantibody detection in cerebral folate deficiency syndromes, and folate uptake regulation in physiological/pathological conditions. Its standardized production supports assay development for high-throughput screening of FOLR1 inhibitors or diagnostic kits for cancer detection. Recent advances in recombinant protein engineering have improved yield and stability, facilitating both basic research and translational applications in precision medicine.
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