荧光寿命成像显微镜

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JenLab

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TauMap®

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欧洲

北京欧兰科技发展有限公司

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荧光寿命成像显微镜TauMap

荧光寿命成像显微镜（FLIM）/荧光相关光谱（FCS）/ 荧光能量共振转移FRTE

单细胞，细胞膜和组织的时间分辨荧光成像，用于生物，制药和医学研究: 活体内分子和离子动力学的成像观测活体细胞中蛋白质相互作用的可视化倍频和荧光显微镜荧光寿命成像显微镜 (FLIM) 荧光能量共振转移 (FRET)

相关方案

综合医疗/卫生

蛋白中双栖小泡蛋白和N-WASP调节肌蛋白组装的相互作用动力学检测方案(CCD相机)
Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependent fission,wasalsoshownto have a regulatory role in actindynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are requiredforthisstimulation.Acidicliposome-triggered,N-WASPdependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 colocalizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine- containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.
医疗/卫生 2011-03-09

蛋白中双栖小泡蛋白和N-WASP调节肌蛋白组装的相互作用动力学检测方案(CCD相机)
Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependent fission,wasalsoshownto have a regulatory role in actindynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are requiredforthisstimulation.Acidicliposome-triggered,N-WASPdependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 colocalizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine- containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.
医疗/卫生 2011-03-09