Glutathione S-transferase (GST) is a 26 kDa protein derived from Schistosoma japonicum. GST enzymes from various sources, both native and recombinantly expressed as fusion to the N-terminus of target proteins. Reduced glutathione (GSH), when immobilized as a ligand to agarose or other chromatography supports, enables high-yield and high-quality purification of recombinant proteins expressed as fusions with glutathione S-transferase (GST) or other glutathione binding proteins expressed in E. coli, insect cells and mammalian cells.
PurKine™ GST-Tag Glutathione Resin 4FF effectively purifies high levels of overexpressed GST-tagged fusion proteins at a variety of scales. The Resin consists of 90μm beads of cross-linked 4% agarose, to which reduced glutathione has been coupled. Tests confirm that performance equals or exceeds popular GST-Tag Purification Resins from other suppliers, and no decrease in performance occurs after at least five repeated uses. PurKine™ GST-Tag Glutathione Resin Packed Column 4FF is a column that is pre-packed with Glutathione Resin. There is no need to pack resin by users.
PurKine™ GST-Tag Purification system is based on innovative high-capacity matrix for convenient single-step purifications of recombinant glutathione S-transferase (GST) fusion proteins and other glutathione binding proteins. Per milliliter of resin can capture more than 10 mg of GST-tagged protein and target proteins can be eluted under mild, non-denaturing conditions that preserve protein antigenicity and functionality. The difference between Glutathione Resin and Glutathione Resin 4FF is the latter is a highly crosslinked resin which can tolerate at most 450cm/hour linear flow rates, thus it make Glutathione Resin 4FF more excellent for scaling-up.