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G0924

Millipore

Glutathione High Capacity Magnetic Agarose Beads

(1:1 suspension in a 30% ethanol solution)

Sinónimos:

Magnetic agarose beads

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About This Item

MDL number:
MFCD00131200
UNSPSC Code:
41106500
NACRES:
NA.56

conjugate

magnetic beads

Quality Level

200

form

(1:1 suspension in a 30% ethanol solution)

analyte chemical class(es)

proteins (GST)

technique(s)

immunoprecipitation (IP): suitable
protein purification: suitable

matrix

4% beaded magnetic agarose

matrix spacer

12 atoms

capacity

≥15 μmol/mL, agarose binding capacity

shipped in

wet ice

storage temp.

2-8°C

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General description

Glutathione Magnetic Agarose Beads consist of a paramagnetic 4% beaded agarose. Glutathione is covalently attached through the sulfur to epoxy-activated agarose resulting in a 12 atom (10 carbon) spacer.

The Glutathione Magnetic Agarose Beads are useful for affinity capture, molecular pull-down, or immunoprecipitation (IP) of proteins containing glutathione binding sequences, such as native glutathione S-transferase (GST), glutathione peroxidase, and glyoxalase I, or GST-tagged recombinant fusion proteins from cell lysates or other biochemical solutions while exhibiting low non-specific binding of other proteins. Recombinant GST-tagged proteins, bound to the affinity resin are separated with the use of a magnet. The magnetic properties allow for very rapid processing, as well as aid in manipulations, such as repetitive washings and recovery of the desired protein. This leads to faster recovery, experimental reproducibility, and more accurate quantitation of the proteins of interest.

The matrix of the magnetic beads is a 4% beaded agarose with an average diameter of 50 μ and a diameter range of 20-75 μ. Paramagnetic iron is impregnated within the beads.

Application

Useful for affinity capture, molecular pull-down, or immunoprecipitation (IP) of proteins containing glutathione binding sequences, such as recombinant GST-tagged fusion proteins or native glutathione S-transferase, glutathione peroxidase and glyoxalase I from cell lysates and other biological samples. Can be used for purification in single tubes or for high throughput in 96-well multiwell plates. The magnetic properties of the beads aid in manipulations, such as repetitive washings and recovery of the protein. This leads to greater experimental reproducibility and more accurate quantitation of the proteins of interest.

Physical form

1:1 suspension in a 30% ethanol solution

pictograms

Flame
GHS02

signalword

Danger

hcodes

H225

Hazard Classifications

Flam. Liq. 2

Storage Class

3 - Flammable liquids

wgk_germany

WGK 2

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Xueran Chen et al.
Theranostics, 10(3), 998-1015 (2020-01-16)
Rationale: Glioblastoma multiforme (GBM) almost invariably gain invasive phenotype with limited therapeutic strategy and ill-defined mechanism. By studying the aberrant expression landscape of gliomas, we find significant up-regulation of p-MAPK level in GBM and a potent independent prognostic marker for
Yun Wei et al.
Journal of materials chemistry. B, 1(15), 2066-2071 (2013-04-21)
The imidazolium cation was chosen as protein selective affinity group and a kind of ionic liquid magnetic microspheres was developed by immobilizing imidazolium cations onto the surface of silica-coated magnetic microspheres to form imidazolium ionic liquid modified magnetic microspheres (Fe3O4@SiO2@IL).
Reinier F Prosée et al.
PLoS biology, 19(7), e3000968-e3000968 (2021-07-07)
Centromere protein A (CENP-A) is a histone H3 variant that defines centromeric chromatin and is essential for centromere function. In most eukaryotes, CENP-A-containing chromatin is epigenetically maintained, and centromere identity is inherited from one cell cycle to the next. In
Ian Holt et al.
BMC molecular and cell biology, 21(1), 88-88 (2020-12-03)
Popeye domain-containing proteins 1 and 2 (POPDC1 and POPDC2) are transmembrane proteins involved in cyclic AMP-mediated signalling processes and are required for normal cardiac pacemaking and conduction. In order to identify novel protein interaction partners, POPDC1 and 2 proteins were
Yong-Wei Nie et al.
Biochemical and biophysical research communications, 473(1), 249-254 (2016-03-24)
Sorting motifs are involved in the transport of diverse proteins. In the present study, we identified a hydrophobic peptide (WRPWRNFWWSIRVPWRRN) that was able to target enhanced green fluorescent protein- or DsRed2-enriched vesicular-like sub-compartments of the endoplasmic reticulum (ER). Analysis of
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