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Merck

70794

BugBuster® GST-Bind Purification Kit

Affinity purification of GST fusion proteins

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UNSPSC Code:
41106500
NACRES:
NA.32

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manufacturer/tradename

Novagen®

storage condition

OK to freeze

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Este artículo
7092270584-M70751
manufacturer/tradename

Novagen®

manufacturer/tradename

Novagen®

manufacturer/tradename

Novagen®

manufacturer/tradename

Novagen®

storage condition

OK to freeze

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze

General description

Affinity purification of GST fusion proteins
The BugBuster® GST•Bind<TMSYMBOL></TMSYMBOL> Purification Kit combines the GST•Bind Resin, GST•Bind Buffer Kit reagents and BugBuster Protein Extraction Reagent for convenient preparation of soluble cell extracts and affinity purification of GST•Tag<TMSYMBOL></TMSYMBOL> fusion proteins. BugBuster Protein Extraction Reagent is formulated for the gentle disruption of the cell wall of E. coli, resulting in the liberation of soluble protein. Cells are harvested by centrifugation as usual, followed by suspension in BugBuster Reagent. During a brief incubation, soluble proteins are released. The extract is clarified by centrifugation, which removes cell debris and insoluble proteins. The clarified extract is ready to apply to GST•Bind Resin.

Other Notes

•2 x 100 mlBugBuster Protein Extraction Reagent

•10,000 UBenzonase Nuclease, purity >90%

•10 mlGST•Bind Resin

•pkg/4Chromatography Columns

•2 x 100 ml10X GST Bind/Wash Buffer

•40 ml10X Glutathione Reconstitution Buffer

•1 gGlutathione, Reduced

Legal Information

BUGBUSTER is a registered trademark of Merck KGaA, Darmstadt, Germany
NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Multiple Toxicity Values, refer to MSDS (O)

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Warning

hcodes

Hazard Classifications

Flam. Liq. 3

Clase de almacenamiento

3 - Flammable liquids

flash_point_f

96.8 °F

flash_point_c

36 °C


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Contenido relacionado

Traditionally, protein purification from E. coli consists of four distinct phases: harvest, bacterial cell lysis, lysate clarification and protein purification. Bacterial lysis typically requires several time-consuming, hands-on steps, such as freeze/thaw cycles and sonication. These harsh lysis techniques may negatively impact protein quality and contribute to sample-to-sample variability. To maintain protein activity and integrity, detergent-based lysis buffers are routinely used to avoid mechanical protein extraction methods. Regardless of the lysis method used, centrifugation is traditionally required to pellet unwanted cell debris and permit recovery of the clarified lysate. The final step, purification, is frequently performed using affinity media specific for expressed epitope tags. Agarose-based media have typically been used, either as a slurry in microcentrifuge tubes or packed into gravity-driven or spin columns. While easier to manipulate, columns are greatly affected by lysate consistency and carryover of cell debris, which can lead to clogging of the column frits.

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