Glutathione Separopore® 6B-CL

Glutathione Separopore® 6B-CL

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BW-20182013
Catalog Number: BW-20182013500 mL
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Applications:
Reduced glutathione is covalently linked to High Resolution Separopore® 6B-CL for use in affinity purification of glutathione-S-transferase (GST) and GST-fused proteins. This product provides a one step purification method and permits rapid, mild and highly selective purifications of proteins containing glutathione binding sequences. Glutathione-Separopore is prepared by covalently coupling glutathione to epoxy-activated highly crosslinked 6% agarose beads to form a stable thioether linkage. The coupling was optimized to give a high binding capacity of 5 mg or more of Glutathione-S-transferase (GST) per ml of wet gel. Bound GST –fusion proteins are easily displaced from the resin by elution with buffers containing reduced glutathione. Mild elution conditions preserve protein antigenicity and function. GlutathioneSeparopore®HR ensures the lowest sample dilution and best high-resolution separation.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

References
pCold-GST vector: a novel cold-shock vector containing GST tag for soluble protein production. Protein Expr Purif. (2008) 62: 120-7.
Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. (1997) 6: 2180-7.
Vectors for Cu2+-inducible production of glutathione S-transferase-fusion proteins for single-step purification from yeast. Yeast. (1994) 10: 441-9.
Expression and mutagenesis of recombinant human and murine erythropoietins in Escherichia coli. Biochim Biophys Acta. (1995) 1261: 35-43.
GST fusion vector with caspase-6 cleavage site for removal of fusion tag during column purification. Biotechniques. (2005) 38: 360-364.
Bacterial production of recombinant human poly(ADP-ribose) glycohydrolase. Protein Expr Purif. (2011) 75: 230-5.
Expression of lipase-solubilized bovine liver microsomal cytochrome b5 in Escherichia coli as a glutathione S-transferase fusion protein (GST-cyt b5). Protein Expr Purif. (2006) 45: 352-8.
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. (1988) 67: 31-40.
An automated method for high-throughput protein purification applied to a comparison of His-tag and GST-tag affinity chromatography. BMC Biotechnol. (2003) 3: 12.
A strategy for high-level expression of soluble and functional human interferon alpha as a GST-fusion protein in E. coli. Protein Eng Des Sel. (2007) 20: 201-9.
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