Journal of Microbial & Biochemical Technology

Department of General Medicine, Graduate School of Medicine Dentistry and Pharmaceutical Sciences, Okayama University Hospital, Okayama University, 700-8558, Japan

Publications

• Review Article   
  The Technique for Excessive-Results of Recombinant Protein Purification led to GST-tag Affinity Chromatography: A Review
  Author(s): Md Asaduzzaman*, Lutfun Nahar, Md. Bakhtiar Lijon, Shahin Imran and Mohammad Saidur Rhaman
  
  Affinity Tags have been performed as the potential tools in the basic biological research field especially for production of recombinant protein and functional proteomics. Those affinity tags were wildly applied to simplify the purification of recombinant protein as well as differentiation of protein complex. Glutathione-S-Transferase (GST) tag has been extensively used in affinity chromatography for purification of fusion/recombinant protein to analysis of structure and function of protein, protein-protein interaction and to produce pharmaceutical product. In this review we describe the advantage of GST-tag in affinity chromatography technique as a method for inducible, high level protein expression and purification of recombinant protein. Recombinant protein which is expressed in a pGEX or pET vectors and that protein with GST-tag encoded at the NH2 or COOH-r.. View more»
  

  DOI: 10.35248/1948-5948.23.15.584

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