Reducing Agents (Part 4 of 4) - TCEP-HCl (Tris-(carboxyethyl) phosphine hydrochloride)
Previously, we’ve been discussing the function of various reducing agents. There are a number of red...
Glutathione has been covalently linked for use in affinity purification of glutathione-S-transferase (GST) and GST fusion proteins.
This product is supplied as a 75% (v/v) aqueous suspension in 20% EtOH.
Fusion proteins expressed from pGEX vectors contain a Glutathione S-transferase (GST) moiety and can therefore be purified to near homogeneity by affinity chromatography on glutathione as a substrate in inactivate toxic small molecules via formation of mercapturic acid. Because the affinity of GST for its substrate is in the submillimolar range, immobilization of glutathione on an agarose matrix makes a highly efficient affinity chromatography resin.
This product provides a one-step purification method and permits rapid, mild and highly selective purifications of proteins containing glutathione binding sequences. Bound GST –fusion proteins are easily displaced from the resin by elution with buffers containing reduced glutathione.
Storage/Handling: Store at 4°C. Do not freeze.
|store at 4°C. Do NOT freeze.
Affinity GST Purification of glutathione-fusion proteins
A convenient guide for the compatibility and stability of glutathione agarose resins with reducing agents, denaturing agents, buffers and other reagents.
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