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Merck

LSKMAGS08

PureProteome Magnetic Stand

The PureProteome Magnetic Stand is designed to rapidly & easily isolate magnetic particles from up to eight 1. 5 mL or 2. 0 mL tubes.

Synonym(s):

Magnetic Bead Stand, Magnetic Separation Stand

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About This Item

UNSPSC Code:
41116133
eCl@ss:
32011202
NACRES:
NA.56

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material

self-standing

feature

binder

manufacturer/tradename

PureProteome

technique(s)

RNA purification: suitable (with magnetic beads)
protein purification: suitable

shipped in

ambient

General description

PureProteome Magnetic Stand contains a removable magnet.

Application

Research Category
Cell Culture

Features and Benefits

  • Enables reproducible process
  • Comparable results with standard protocols

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Articles

Comparison of elution techniques for small-scale protein purification of FLAG® tag proteins using anti-FLAG® M2 magnetic beads.

PureProteome™ Protein A and G Magnetic beads provide a rapid and reproducible means to purify immunoglobulins (IgG) using the KingFisher Duo particle processor.

Related Content

Immunoprecipitation (IP) is a powerful technique for proteomic screening, biomarker discovery, and signaling network elucidation. It is frequently used to enrich target proteins from complex samples such as cell lysates or extracts. Traditional IP protocols use Protein A, Protein G or a mixture of Protein A and G coupled to a solid support resin, such as agarose beads, to capture an antigen/antibody complex in solution. As the number of samples increase, the traditional, manual IP method can be time-consuming. Processing of multiple IP reactions in parallel can introduce complexity, variability and pipetting errors, which may affect reproducibility.

Purification of recombinant proteins expressed in E.coli requires many time-consuming steps. To liberate the protein of interest, traditional bacterial lysis relies on the addition of lysozyme and a combination of sonication and repeated freeze/thaw cycles to break the bacterial cell wall. Disruption of the cell is accompanied by an increase in the viscosity of the suspension, due to the release of DNA. An endonuclease is added to digest the DNA, thus reducing the viscosity of the lysate. Finally, to render the lysate compatible with traditional purification methods, insoluble cell debris must be removed by centrifugation.

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