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      Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems.

      Applied Microbiology and Biotechnology

      Amino Acid Sequence, Binding Sites, Calmodulin, chemistry, Carrier Proteins, Cellulose, Glutathione Transferase, Histidine, Industry, Maltose-Binding Proteins, Oligopeptides, Peptide Fragments, chemical synthesis, Peptides, Protein Binding, Protein Engineering, Recombinant Fusion Proteins, classification, genetics, Recombinant Proteins, isolation & purification, Ribonucleases

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          Abstract

          In response to the rapidly growing field of proteomics, the use of recombinant proteins has increased greatly in recent years. Recombinant hybrids containing a polypeptide fusion partner, termed affinity tag, to facilitate the purification of the target polypeptides are widely used. Many different proteins, domains, or peptides can be fused with the target protein. The advantages of using fusion proteins to facilitate purification and detection of recombinant proteins are well-recognized. Nevertheless, it is difficult to choose the right purification system for a specific protein of interest. This review gives an overview of the most frequently used and interesting systems: Arg-tag, calmodulin-binding peptide, cellulose-binding domain, DsbA, c-myc-tag, glutathione S-transferase, FLAG-tag, HAT-tag, His-tag, maltose-binding protein, NusA, S-tag, SBP-tag, Strep-tag, and thioredoxin.

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          Journal
          12536251
          10.1007/s00253-002-1158-6

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