Glutathione Separopore® Microbeads

Application: Reduced glutathione is covalently linked Separopore® 4B Microbeads 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 4% crosslinked 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.

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

Technical Specifications:
Ligand: Reduced glutathione (GSH)
Matrix: Separopore® 4B (agarose microbeads, 4%)
Particle size range: 25 – 50 µm
Molecular weight range: 6 x 104 – 2 x 107
Matrix activation: Epoxy
Matrix spacer: 12 atoms
Ligand density: 5 – 10 mg GST / ml drained gel
Binding capacity: 5 – 10 mg recombinant GST-tagged protein / ml drained gel
pH stability: 4 – 13
Storage: 4 °C – 30 °C
Supplied as suspension in 20% ethanol

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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Usage: bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product , food additive or as a household chemical.

Hazmat Shipping: Non-hazardous
Storage: 2-8°C
Appearance Form: Liquid
Appearance Color: Cloudy, colorless
Brand Name: bioPLUS™, Separopore®