MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台
MCL单分子成像RM21™显微镜平台

¥100万 - 150万

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RM21™ Microscope Platform

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美洲

  • 金牌
  • 第17年
  • 授权经销商
  • 营业执照已审核
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RM21™: Microscope Platform for the Future


RM21™ is a precision aligned microscope platform for epifluorescence microscopy. The RM21™ has been designed for maximum user accessibility. This feature offers users the opportunity to develop flexible configuration microscopy instruments with ease. It has been manufactured with high precision to allow easy alignment of microscopy and optical components within its three dimensional space. In addition, all posts and fixturing points are referenced to a known datum. With a robust design, precision manufacturing and assembly, the RM21™ is the ideal platform for a range of microscopy applications such as super resolution (SR) microscopy, fluorescence microscopy and TIRF.

The RM21™ includes the precision platform with an axial, motorized Z axis approach suitable for lens positioning, manual or motorized XY micropositioner for sample positioning (manual version and accessories not pictured above). The Z axis has a displacement of 2 inches (50mm) with a 95nm step size. A customized platform version without XY micropositioners is available. Optional encoders can be added to motorized X, Y, and Z for accurate micropositioner displacement readouts.

The RM21™ can be seamlessly integrated with the Nano-Cyte® 3D microscope stability system. The RM21™ can also interface with other Mad City Labs products like closed loop nanopositioning systems, including the Nano-LPS Series(shown above) and high speed Nano-LPQ. The Nano-OP Series and the Nano-F Series objective nanopositioners can be added on for control of focus down to the subnanometer level. The ease of integration with Mad City Labs nanopositioning and microspositioning systems provides the researcher with a flexible microscopy platform with high precision performance for the most demanding microscopy techniques.



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  • In hemodynamics, the inherent intermittency of two-phase cellular-level flow has received little attention. Unsteadiness is reported and quantified for the first-time in the literature using a combination of fluorescent dye labelling, time-resolved scanning confocal microscopy, and micro-particle image velocimetry (μPIV). The near-wall red blood cell (RBC) motion of physiologic high-hematocrit blood in a rectangular microchannel was investigated under pressure driven flow. Intermittent flow was associated with (1) the stretching of RBCs as they passed through RBC clusters with twisting motions; (2) external flow through local obstacles; and (3) transitionary rouleaux formations. Velocity profiles are presented for these cases. Unsteady flow clustered in local regions. Extra-cellular fluid flow generated by individual RBCs was examined using submicron fluorescent microspheres. The capabilities of confocal μPIV post-processing were verified using synthetic raw PIV data for validation. Cellular interactions and oscillating velocity profiles are presented and 3D data are made available for computational model validation.

    医疗/卫生 2012-01-14

  • 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

  • In hemodynamics, the inherent intermittency of two-phase cellular-level flow has received little attention. Unsteadiness is reported and quantified for the first-time in the literature using a combination of fluorescent dye labelling, time-resolved scanning confocal microscopy, and micro-particle image velocimetry (μPIV). The near-wall red blood cell (RBC) motion of physiologic high-hematocrit blood in a rectangular microchannel was investigated under pressure driven flow. Intermittent flow was associated with (1) the stretching of RBCs as they passed through RBC clusters with twisting motions; (2) external flow through local obstacles; and (3) transitionary rouleaux formations. Velocity profiles are presented for these cases. Unsteady flow clustered in local regions. Extra-cellular fluid flow generated by individual RBCs was examined using submicron fluorescent microspheres. The capabilities of confocal μPIV post-processing were verified using synthetic raw PIV data for validation. Cellular interactions and oscillating velocity profiles are presented and 3D data are made available for computational model validation.

    医疗/卫生 2012-01-14

  • 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

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