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E6406

Millipore

EZview™ Red Glutathione Affinity Gel

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About This Item

MDL number:
MFCD05665380
UNSPSC Code:
41106500
NACRES:
NA.56

analyte chemical class(es)

proteins (GST)

technique(s)

immunoprecipitation (IP): suitable
protein purification: suitable

storage temp.

2-8°C

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General description

EZviewä Red Glutathione Affinity Gel is a highly visible, red colored glutathione agarose affinity gel. The affinity resin is composed of glutathione covalently attached through the sulfur to epoxy-activated 4% cross-linked agarose beads, resulting in a 12-atom spacer.

Application

The product is used for affinity capture, molecular pull-down, or IP of proteins containing glutathione binding sequences, such as glutathione S-transferase, glutathione peroxidase and glyoxalase I.
When performing small-scale affinity capture, such as immunoprecipitation, the affinity matrix is difficult to see in the microcentrifuge tubes. Accidental aspiration of the resin leads to quantitative variability in results. The EZview™ Red Affinity Gels greatly reduce the risk of pellet loss. EZview™ resins perform as well as conventional non-colored affinity gels, but allow the user to easily differentiate pellet from supernatant. This correlates to more accurate data because less protein is lost.

Features and Benefits

  • Increased visibility - Red color reduces risk of incidental aspiration
  • Improved recovery of target protein by reduced accidental loss
  • Higher reproducibility - More consistent yields

Physical form

1:1 (v/v) suspension in PBS containing 50% glycerol and 15 ppm Kathon

Legal Information

EZview is a trademark of Sigma-Aldrich Co. LLC

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

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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S K Jang et al.
Journal of virology, 62(8), 2636-2643 (1988-08-01)
Picornavirus RNAs are uncapped messengers and have unusually long 5' nontranslated regions (5'NTRs) which contain many noninitiating AUG triplets. The translational efficiency of different picornavirus RNAs varies between different cell-free extracts and even in the same extract, such as micrococcal
P L Hallauer et al.
BMC genetics, 1, 1-1 (2000-10-19)
Versatile transgenic manipulation of skeletal muscle requires knowledge of the expression profiles of diverse promoter/enhancer elements in the transcriptionally specialized fiber types of which muscle is composed. "Universal" viral promoters/enhancers, e.g., cytomegalovirus IE1 (CMV IE1), are of interest as reagents
S Andersson et al.
The Journal of biological chemistry, 264(14), 8222-8229 (1989-05-15)
The conversion of cholesterol into bile acids in the liver represents the major catabolic pathway for the removal of cholesterol from the body. In this complex biosynthetic pathway, at least 10 enzymes modify both the ring structure and side chain
D R Thomsen et al.
Proceedings of the National Academy of Sciences of the United States of America, 81(3), 659-663 (1984-02-01)
The DNA templates containing immediate early (IE) genes of human cytomegalovirus (CMV) were transcribed in vitro by using a HeLa cell extract. When IE region 1, 2, and 3 were used, transcription was detected qualitatively only from IE region 1.

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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.

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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