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Protein Expr Purif. 1999 Feb;15(1):34-9.

Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors.

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Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, 22908, USA.


We describe the construction of expression vectors based on three of the most frequently used gene fusion affinity tags [glutathione S-transferase (GST), maltose binding protein (MBP), and the His6 peptide]. The polylinkers of pGEX4T1, pMal-c2, and a pET vector were replaced with the polylinker isolated from the baculovirus expression plasmid pFastBac. Once appropriate restriction sites have been introduced into a gene, it can be fused to all three affinity tags with little effort, allowing expression-screening experiments to be performed efficiently. We discuss the development and use of these vectors with respect to overcoming purification problems encountered for the RhoA GDP/GTP nucleotide dissociation inhibitor (RhoGDI) and their advantages over commercially available expression vectors.

[Indexed for MEDLINE]

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