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).
The figure above shows coupling of a GST-tagged protein/peptide to glutathione plates. GSH = Glutathione; GST = Glutathione-S-transferase
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.
A selection of FAQs is listed below. For more technical information and FAQs, please visit our Solid Phase Guide ›
The Immobilizer Glutathione plates are designed for optimal detection of glutathione-S-transferase (GST)-tagged proteins or purified GST.
We recommend using transparent polystyrene plates for colorimetric assays, white polystyrene plates for bio and chemi-luminescence assays, and black polystyrene plates for fluorescence assays.
The background is extremely low when using the Immobilizer Glutathione plates. This results in a high signal-to-noise ratio and a low detection limit which in general means that the detection limit (OD 0.5) is 3ng per well (100 μL).
For Research Use Only. Not for use in diagnostic procedures.