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10 September 1998 Biological transport in a microfabricated device: active immunochromatography with motorized antibodies
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Proceedings Volume 3515, Microfluidic Devices and Systems; (1998)
Event: Micromachining and Microfabrication, 1998, Santa Clara, CA, United States
Kinesin motor proteins transduce chemical energy released by adenosine triphosphate hydrolysis into mechanical force and motion along microtubule tracks. Biological cells use kinesin motors to transport intracellular components to specific cellular locations. Our goal is to mimic some aspects of kinesin's cellular function and apply them to an active separation microdevice. Here we report the coupling of cargo-binding domains to recombinant kinesin. Metal- chelating Pluronic surfactants were used to specifically co- immobilize recombinant kinesin motor proteins and two immunoglobulin-(IgG) binding domains of protein A on the surface of polystyrene beads. Monoclonal antibodies, the cargo-binding domains, were indirectly coupled to kinesin on the beads through the IgG-binding domains. These motorized antibodies are capable of specifically binding virtually any cargo (antigens) and transporting them along microtubule tracks to different locations or compartments in an active separation microdevice.
© (1998) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Loren Limberis and Russell J. Stewart "Biological transport in a microfabricated device: active immunochromatography with motorized antibodies", Proc. SPIE 3515, Microfluidic Devices and Systems, (10 September 1998);

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