Pierce™ Glutathione Magnetic Agarose Beads (Thermo Scientific™)

Thermo Scientific™ Pierce™ Glutathione Magnetic Agarose Beads provide a fast, convenient method for purification of glutathione-S-transferase (GST) from a bacterial, yeast, or mammalian crude cell lysate. Pierce™ Glutathione Magnetic Agarose Beads are well suited for purifying GST fusion proteins from a soluble protein extract and are ideal for the purification of proteins expressed at low levels from diluted supernatants. The beads can be used in manual applications with a magnetic stand or automated applications with an instrument such as the Thermo Scientific™ KingFisher™ Flex Magnetic Particle Processor. Automated instruments are especially useful for higher throughput purification and screening of purification conditions.

Download the KingFisher™ Duo BindIt™ Software protocol (.bdz) >
Download the KingFisher™ Flex BindIt™ Software protocol (.bdz) >

Features of Glutathione Magnetic Agarose Beads:
• High-performance beads—non-aggregating, magnetite (Fe₃O₄), superparamagnetic beads provide exceptional uniformity for both manual and automated HTS applications
• Stable affinity ligand—glutathione is covalently immobilized to particles, enabling leach-resistance and clean purification products
• High capacity—binding capacity is sufficient for both routine and demanding purification procedures

The high-performance, magnetite, superparamagnetic particles are validated and optimized for use with high-throughput magnetic platforms, such as the KingFisher™ 96 and KingFisher™ Flex magnetic particle processors, but the beads also enable premium performance for simple benchtop purification applications using an appropriate magnetic stand.

Glutathione S-transferase (GST) is a protein that is commonly added to the end of recombinant proteins to aid in their purification or detection. To make an affinity support, glutathione is immobilized through its central carbon, preserving the essential structure necessary for efficient GST binding. Addition of reduced glutathione in a physiologic buffer is sufficient to competitively displace and recover the GST fusion protein from the immobilized glutathione.