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GST-beads para purificación de proteínas

El método óptimo para la purificación de proteínas con el tag GST (glutathione S-transferase)

Según descripción del fabricante:

GST-Agarose Products

Fusion proteins expressed from pGEX vectors contain a glutathione S-transferase (GST) moiety and can be purified to near-homogeneity by affinity chromatography on glutathione (g-glutamylcysteinylglycine) as a substrate to inactivate toxic small molecules via formation of mercapturic acid.

Because affinity of GST for its substrate is in the submillimolar range, immobilization of glutathione on an agarose matrix makes it a highly efficient affinity chromatography resin.

Glutathione has been covalently linked for use in affinity purification of glutathione-S-transferase (GST) and GST fusion proteins. 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.
Biontex offers the glutathione beads with an agarose percentage type (4% agarose).

El rango de productos comprende dos formatos diferentes, en función de la aplicación:

 GST beads (Agarose Resin) GST Agarose Cartridge
Bulk Resins
(10, 50, 100, 500, 1000 ml etc.)
(5 x 1 ml)
Binding Capacity     > 8 mg recombinant GST/ml gel ~ 10 mg recombinant GST/cartridge
Application Batch, Gravity, MPLC, FPLCTM
Peristaltic pump, syringe, MPLC, FPLCTM, ÄKTA designTM

*Sepharose, ÄKTA, FPLC are registered trademarks of Amersham Pharmacia Biotech AB.

Características de las GST-beads:


Biontex GST Agarose is designed for the efficient, highly selective purification of recombinant glutathion S-transferase fusion proteins and is a key constituent of the integrated GST gene fusion system which is widespread in cell laboratories. The system comprises expression, purification and detection of fusion proteins expressed from bacterial, yeast, mammalian or insect cells, and, due to the high affinity of glutathion S-transferase to glutathion, is distinguished by extremely high selectivity and purity of the fusion proteins.

Biontex GST Agarose consists of 4% agarose, to which glutathion is covalently bound and linked via sulphur atom.

A major advantage is that it can be used multiple times without the need for further regeneration measures. Biontex GST Agarose meets the highest quality standards and is outstandingly easy and flexible to use. It features high pH stability and enables purification to be undertaken directly from the raw lysates.

Disponibles también en grandes cantidades (500 mL, 1000 mL, 2000 mL...)

Product Specifications
Application Affinity chromatography of glutathion S-transferase fusion proteins in batch, gravity flow, MPLC or FPLC process
Formulation 75% (v/v) aqueous suspension containing 20% ethanol (1 ml gel corresponds to 1.333 ml of original 75 % suspension)
Binding capacity > 8 mg GST-tagged fusion protein per 1 ml agarose (only a benchmark, will vary for each GST-tagged protein)
Bead structure 4% agarose (not cross-linked: do not autoclave the gel)
Bead size 50 – 150 µm, spherical
Max. linear flow rate 250 cm / h
Max. pressure 0.18 bar (2.6 psi)
Matrix Stable in 0.1M acetate pH 4.0, 0.1M NaOH, 70% ethanol or 6M guanidine hydrochloride for 2 hours at room temperature
Antimicrobial agent
20 % ethanol
Shipping At room temperature
Storage 4 - 8°C
Shelf life 3 years (after date of certificate of analysis)

*Sepharose, ÄKTA, FPLC are registered trademarks of Amersham Pharmacia Biotech AB. 


Description Cat. #
GST Agarose
5 ml resin
For purification of glutathione-S-transferase fusion proteins
GST Agarose
2 x 5 ml resin
For purification of glutathione-S-transferase fusion proteins (GST)
GST Agarose
50 ml resin
For purification of glutathione-S-transferase fusion proteins
GST Agarose
2 x 50 ml resin
For purification of glutathione-S-transferase fusion proteins


Para informarse de disponibilidad y precio, contacte con nosotros.




© AttendBio Research S.L. 2012