Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker.

ABSTRACT: Coupled with over-expression in host organisms, fusion protein systems afford economical methods to obtain large quantities of target proteins in a fast and efficient manner. Some proteases used for these purposes cleave C-terminal to their recognition sequences and do not leave extra amino acids on the target. However, they are often inefficient and are frequently promiscuous, resulting in non-specific cleavages of the target protein. To address these issues, we created a fusion protein system that utilizes a highly efficient enzyme and leaves no residual amino acids on the target protein after removal of the affinity tag. We designed a glutathione S-transferase (GST)-fusion protein vector with a caspase-3 consensus cleavage sequence located between the N-terminal GST tag and a target pro

SUBMITTER: Feeney B 

PROVIDER: S-EPMC3110655 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature