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A High Yield and Cost-efficient Expression System of Human Granzymes in Mammalian Cells

Article DOI: 10.3791/52911-v • 09:16 min • June 10th, 2015
June 10th, 2015 •
1, 2, 2, 3, 1, 2
1Cellular and Molecular Medicine Program, Boston Children’s Hospital and Harvard Medical School, 2Department of Medicine, University of Fribourg, 3Centre Médical Universitaire, University of Geneva

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We describe here a cost-efficient granzyme expression system using HEK293T cells that produces high yields of pure, fully glycosylated and enzymatically active protease.

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High Yield Cost-efficient Expression System Human Granzymes Mammalian Cells Cytotoxic T Lymphocytes Natural Killer Cells Tumor Cells Intracellular Pathogens Cytotoxic Granule Content Granule Serine Proteases Granzymes Pore Forming Protein Perforin Bacterial Pathogens Protein Expression And Purification Systems Active Enzymes Mammalian Secreted Protein Expression Systems Glycosylation Calcium Precipitation Method Transient Transfection HEK293T Cells Expression Plasmid PHLsec Immobilized Nickel Affinity Chromatography Polyhistidine Tag Enterokinase Site Active Protease Purification
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