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.
Table 1: Glutathione Working Conditions
Volumetric flow rate (mL / min) |
||||
Column diameter
|
Bed volume
|
Packing |
Equilibration/Washing/Elution |
Binding |
6.6 |
1.0 |
1.4 |
1.0 |
0.3 - 1.0 |
16 |
10 |
7.0 |
5.0 |
0.5 - 5.0 |
Linear flow rate (cm/h) |
||||
<250 |
<180 |
<180 |
Store at 4°C. Do not freeze.
Catalog ID | G-250 |
---|---|
Name(s) | Glutathione Agarose Resin |
Bead Size | Spherical, Standard: ~50-150 μm (approx.) |
Cross-linking | No |
Agarose % | 4% agarose |
Ligand | Glutathione, linked via sulfur atom |
Binding/Loading Capacity | ≥8 mg recombinant GST / mL gel |
Temperature Stability | Do not autoclave |
Storage Buffer | 20% Ethanol |
Storage/Handling | Store at 4°C. Do NOT freeze. |
Previously, we’ve been discussing the function of various reducing agents. There are a number of red...
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