pALEX, a dual-tag prokaryotic expression vector for the purification of full-length proteins

pALEX, a prokaryotic expression vector, was constructed in which the multiple cloning site (MCS, polylinker) is flanked by sequences encoding glutathione S-transferase (GST) at the 5' end and a His 6 residue tag at the 3′ end. Open reading frames cloned into this vector can direct production of...

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Bibliographic Details
Published in:Gene 1995-10, Vol.164 (1), p.45-47
Main Authors: Panagiotidis, Christos A., Silverstein, Saul J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Cloning, Molecular - methods
fusion protein
Genetic Vectors
Glutathione Transferase - genetics
Immediate-Early Proteins - biosynthesis
Immediate-Early Proteins - genetics
Immediate-Early Proteins - isolation & purification
Molecular Sequence Data
Prokaryotic Cells
protein purification
Recombinant DNA
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - isolation & purification
Ubiquitin-Protein Ligases
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Description
Summary:pALEX, a prokaryotic expression vector, was constructed in which the multiple cloning site (MCS, polylinker) is flanked by sequences encoding glutathione S-transferase (GST) at the 5' end and a His 6 residue tag at the 3′ end. Open reading frames cloned into this vector can direct production of fusion proteins with GST at their N terminus and a His 6 tag at their C terminus. This allows for the purification of full-size fusion proteins by a sequential two-step procedure on glutathione-agarose and Ni 2+-agarose columns.
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(95)00417-5