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A Modular Set of Prokaryotic and Eukaryotic Expression Vectors
Karsten Melcher (2000); Analytical Biochemistry 277, 109-120.





A modular series of versatile expression vectors is described for improved affinity purification of recombinant fusion proteins. Special features of these vectors include 

(i) serial affinity tags (hexahistidine-GST) to yield extremely pure protein even with very low expression rates, 
(ii) highly efficient proteolytic cleavage of  affinity tags under a variety of conditions by hexahistidine-tagged tobacco etch virus (TEV) protease, 
(iii) PCR cloning design that results in a product of proteolytic cleavage with only one (a single glycine) or two (gly-ala) amino acids at the N-terminus of the protein, and 
(iv) expression in either Escherichia coli or Saccharomyces cerevisiae. 

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