Both of these two types of support are of 4% agarose matrix. Agarose 4FF is rigid, highly cross-linked polymer. It exhibits excellent chemical and physical stability and allows applications using medium pressure (up to 0.3 MPa). Therefore, the recommended flow rate is 300 - 500 cm/hour. Glutathione Agarose is non-cross-linked medium. It offers excellent binding capacity for targeted proteins. It is suitable for applications using gravity flow (with flow rate of 100 - 300 cm/hour).
Efficient, single-step chromatography purification of Glutathione S-Transferase (GST) tagged fusion proteins with high yield and purity. Suitable for other glutathione transferases and glutathione binding proteins. ... Read more
PROTEINDEX™ Glutathione Agarose is an affinity chromatography medium designed for easy, one-step purification of recombinant glutathione S-transferase (GST) fusion proteins and other glutathione binding proteins expressed in E. coli, insect and mammalian cells.
- Highly specific to the GST tag
- High ligand density for greater yield
Purification of GST-tagged protein using ProteIndex™ Glutathione Agarose 4FF resins.
Lanes: (1) MW; (2) Raw cell lysate; (3) Eluate.
||300 μmol Glutathione/g medium|
|Binding capacity||>20 mg GST (26 kDa)/mL medium|
|Matrix||4% agarose supplied as 50% slurry|
|Particle size||45 μm - 165 μm|
||0.1 MPa (1 bar)|
|Recommended flow rate
||Gravity flow, <75 cm/hour|
||2 - 8°C|
Product is shipped at ambient temperature. Upon receipt store at 2 - 8°C. Do not Freeze.
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Q&As and Reviews
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Customers Questions & Answers
Yes. Glutathione Agarose has high binding capacity for GST-tagged fusion proteins or other glutathione binding protein. The medium can be directly added to pre-treated cell lysates to capture target proteins.
There are many factors that can affect the final purification product. First of all, the composition of the buffers being used in binding, washing, and elution may affect greatly the yield and the purity of the final product. These buffers to should be compatible with the medium. Chemicals, such as 1% Triton X-100, 1% Tween-20, 1% CTAB, 0.03% SDS, or 0.1% NP-40, will not significantly affect the binding of GST or GST-fusion protein to Glutathione Beads. Therefore, these chemicals may be used to reduce non-specific binding. Adding DTT to a final concentration of 1 - 10 mM may greatly increase binding of certain GST-tagged proteins to Glutathione Agarose medium. However, while 1 - 10 mM DTT can be included in the binding and elution buffer to increase purity, it may result in lower yield of some target proteins. Binding of GST-tagged proteins to the chromatography medium depends on its size, conformation, as well as its concentration in the sample loaded. Binding of GST to glutathione is also flow dependent. Lower flow rates often increase the binding capacity, whereas higher flow rates decrease the binding efficiency. Therefore, lower flow rates are recommended, in particular, during sample loading. Furthermore, protein characteristics, pH and temperature may also have impact on the binding capacity.
No. GST may not be the suitable tag to use if the fusion protein is aggregated in the inclusion body. Isolation of inclusion body proteins requires the use of denaturing agents, such as urea or guanidine-HCl, which will lead to denaturing of the GST tag and loss of its the binding capacity to the ligand.
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