GST-Binding Plates

Assay GST-fusion proteins

A glutathione peptide, crosslinked to the polymer surface via a spacer arm, enables binding by specific affinity interaction of GST, which is typically genetically engineered into a fusion protein. The spacer arm maximizes surface reactivity while minimizing non-specific binding, and the covalent linkage reduces the occurrence of leaching. The surface does not need to be blocked and therefore a high S/N ratio is obtained.

These glutathione-coated plates can be used in the analysis of cell lysates to determine the presence and concentration of the GST-fusion protein produced in an expression system. Alternatively, the plates can be used to capture and coat fusion proteins via their GST tag for subsequent binding assays involving the recombinant protein (either protein interactions or a specific antibody).

Protein purification with affinity tags such as glutathione S-transferase (GST), histidine (HIS), and other affinity tags, enables purification of proteins with both known and unknown biochemical properties. Therefore, this methodology has become a widely used research tool for determining the biological function of uncharacterized proteins.