78602
PIER78602EA
718
EUR
InStock
PIER78602
Glutathione magnetic agarose, Pierce™
Protéines purification
Protein Purification Magnetic Beads
These beads provide a fast, convenient method for purification of glutathione-S-transferase (GST) from a bacterial, yeast, or mammalian crude cell lysate.
- 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 immobilised to particles, enabling leach-resistance and clean purification products
- High capacity: Binding capacity is sufficient for both routine and demanding purification procedures
The 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 immobilised 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 immobilised glutathione.
These 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. Automated instruments are especially useful for higher throughput purification and screening of purification conditions.
Information de livraison: Supplied at 25% v/v suspension in 20% ethanol. Accessories not included.
Attention: For research use only. Not for use in diagnostic procedures.