{"id":{"repo_id":"mit","oai_identifier":"oai:dspace.mit.edu:1721.1/27143"},"canonical_url":"https://search.dev.ndltd.org/etd/mit/oai:dspace.mit.edu:1721.1/27143","repository":{"repo_id":"mit","name":"MIT","base_url":"https://dspace.mit.edu/oai/request"},"display":{"title":"On-chip multi-dimensional biomolecule separation using multi-layer microfabricated valves","abstract":"Recent proteomics researches require a sensitive, high-speed, and automatic protein separation tool that far exceeds the capability of traditional two dimensional (2D) protein gel electrophoresis. Methods are described to achieve multi-dimensional biomolecule separation in a microfluidic channel. The new methods couple isoelectric focusing (IEF) with high ionic strength capillary electrophoresis (CE) by active micro valve control in a microchip. Several experiments demonstrating independent 2D separation were performed, and critical parameters for better chip performance were identified; including channel passivation, electroosmosis control, IEF linearity control, and detection enhancement. The result can be used for the filtration of high-abundance proteins, which used to be done by affinity columns. Also, it can be used for much possible integration between different heterogeneous separation/analysis techniques such as IEF, polyacrylamide gel electrophoresis (PAGE), CE, reverse-phase chromatography, and mass spectrometry (MS).","abstract_html":"Recent proteomics researches require a sensitive, high-speed, and automatic protein separation tool that far exceeds the capability of traditional two dimensional (2D) protein gel electrophoresis. Methods are described to achieve multi-dimensional biomolecule separation in a microfluidic channel. The new methods couple isoelectric focusing (IEF) with high ionic strength capillary electrophoresis (CE) by active micro valve control in a microchip. Several experiments demonstrating independent 2D separation were performed, and critical parameters for better chip performance were identified; including channel passivation, electroosmosis control, IEF linearity control, and detection enhancement. The result can be used for the filtration of high-abundance proteins, which used to be done by affinity columns. Also, it can be used for much possible integration between different heterogeneous separation/analysis techniques such as IEF, polyacrylamide gel electrophoresis (PAGE), CE, reverse-phase chromatography, and mass spectrometry (MS).","abstract_has_math":false,"creators":["Wang, Ying-Chih, 1977-"],"institution":"Massachusetts Institute of Technology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Massachusetts Institute of Technology. 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