Bio-Rad Laboratories
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Website: http://www.bio-rad.com
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Expedited Analysis And Purification Of A GST-Tagged Recombinant Protein:
Synergistic Application Of Two Disparate Technologies
Laura Kronbetter and Mary Grace Brubacher
Introduction
The use of affinity tags for purification of recombinant proteins is a widely accepted technique. One of the more commonly employed tags is glutathione S-transferase (GST). Protein fused to GST can be purified from crude bacterial lysates under nondenaturing conditions by affinity chromatography on an immobilized glutathione column. After capture of the protein and removal of the contaminants by washing, the tagged protein is eluted from the GST column (released), collected and desalted for further data analysis or experimentation. The GST tag can be removed from the purified protein by digestion with an appropriate protease. Whether the task involves method development for the purification of a new protein analyte or quality control of an existing method, there is a concomitant need to monitor protein quality at each step of the purification.
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