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G3907

Millipore

Glutathione−Agarose

set of 3 pre-packed columns (2.5 ml each), (1:1 suspension in a 0.5 M NaCl + 20% ethanol solution)

Synonym(s):

GSH-agarose, S-linked glutathione agarose

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About This Item

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

Quality Level

200

form

(1:1 suspension in a 0.5 M NaCl + 20% ethanol solution)

analyte chemical class(es)

proteins (GST)

packaging

set of 3 pre-packed columns (2.5 ml each)

technique(s)

immunoprecipitation (IP): suitable
protein purification: suitable

matrix

cross-linked 4% beaded agarose

storage temp.

2-8°C

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General description

The resin in these columns consists of glutathione attached through the sulfur to epoxy activated, 4% cross-linked beaded agarose resulting in a 12 atom spacer.

Application

Affinity chromatography using glutathione-agarose permits rapid, mild, non-denaturing and highly selective purification of glutathione binding enzymes such as glutathione-S-transferase, glutathione peroxidase, and glyoxalase I.
The product was used in the design, synthesis and biological evaluation of new tryptamine and tetrahydro-β-carboline-based selective inhibitors of CDK4. It was also used to study Fascaplysin-inspired diindolyls as selective inhibitors of CDK4/cyclin D1.
Affinity chromatography using glutathione-agarose permits rapid, mild, non-denaturing and highly selective purification of proteins containing glutathione binding sequences, such as Glutathione S-Transferase (GST), glutathione peroxidase and glyoxalase I.

Linkage

Suspension of Product No. G 4510

Physical form

1:1 suspension in a 0.5 M NaCl + 20% ethanol solutionl

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

180.1 °F

Flash Point(C)

82.3 °C

Certificates of Analysis (COA)

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Xiu Feng Hu et al.
The Journal of clinical investigation, 119(2), 362-375 (2009-01-17)
Provirus integration site for Moloney murine leukemia virus (PIM1) is a proto-oncogene that encodes a serine/threonine kinase with multiple cellular functions. Overexpression of PIM-1 plays a critical role in progression of prostatic and hematopoietic malignancies. Here we describe the generation
Carine Aubry et al.
Organic & biomolecular chemistry, 4(5), 787-801 (2006-02-24)
We present the design, synthesis, and biological activity of three classes of tryptamine derivatives, which are non-planar analogues of the toxic anti-cancer agent fascaplysin. We show these compounds to be selective inhibitors of CDK4 over CDK2, the most active compound
F Toribio et al.
Journal of chromatography. B, Biomedical applications, 684(1-2), 77-97 (1996-09-20)
The different preparative techniques and related analytical methods used for purification of glutathione peroxidase, glutathione transferase and glutathione reductase, described in papers published in the last ten years, have been reviewed in this article. Among the different purification techniques, chromatography
Diane M Kanter et al.
Nucleic acids research, 39(7), 2580-2592 (2010-11-27)
Sld2 is essential for the initiation of DNA replication, but the mechanism underlying its role in replication is not fully understood. The S-phase cyclin dependent kinase (S-CDK) triggers the association of Sld2 with Dpb11, and a phosphomimetic mutation of Sld2
Carine Aubry et al.
Bioorganic & medicinal chemistry, 17(16), 6073-6084 (2009-07-28)
We present the design, synthesis and biological activity of a new series of substituted 3-(2-(1H-indol-1-yl)ethyl)-1H-indoles and 1,2-di(1H-indol-1-yl)alkanes as selective inhibitors of CDK4/cyclin D1. The compounds were designed to explore the relationship between the connection mode of the indolyl moieties and
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Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

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