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Colloidal coomassie

Manufactured by Merck Group
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Colloidal Coomassie is a laboratory reagent used for the detection and quantification of proteins in biological samples. It is a dye-based colorimetric assay that binds to proteins, resulting in a color change that can be measured using a spectrophotometer. The intensity of the color is proportional to the amount of protein present in the sample.

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Lab products found in correlation

Protease inhibitor, by Merck Group (2 mentions) Pro q diamond, by Thermo Fisher Scientific (1 mentions) Phosstop, by Roche (1 mentions) Dynabeads protein g, by Thermo Fisher Scientific (1 mentions) Phosphatase inhibitor, by Merck Group (1 mentions) Precast gel, by Bio-Rad (1 mentions)

Close spelling variants of this product

Colloidal Coomassie brilliant blue Brilliant Blue G-colloidal Coomassie Colloidal Coomassie blue stain Colloidal Coomassie blue Colloidal Coomassie Brilliant Blue (R-250) Colloidal Coomassie blue G-250

3 protocols using colloidal coomassie

1

In Vitro Mps1 and ARHGEF17 Phosphorylation

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200 nM of Mps1 and ARHGEF17 or BSA with 200 nM of each were incubated with kinase buffer containing 12.5 mM Tris-Cl, pH 7.5, 35 mM KCl, 1 mM MgCl2, 50 µM EGTA, 100 µM DTT, and 1× phosStop (Roche) at 30°C for 3 h in the absence or presence of ATP/Mg cocktail (0.25 mM ATP; Merck). The reaction was stopped with 20 mM EDTA. The samples were separated by SDS-PAGE gel and stained with colloidal Coomassie (Sigma-Aldrich), or they were blotted and the phosphorylated protein was visualized with Pro-Q Diamond (Life Technologies) and visualized using the Typhoon imaging device (Fuji).
Isokane M., Walter T., Mahen R., Nijmeijer B., Hériché J.K., Miura K., Maffini S., Ivanov M.P., Kitajima T.S., Peters J.M, & Ellenberg J. (2016). ARHGEF17 is an essential spindle assembly checkpoint factor that targets Mps1 to kinetochores. The Journal of Cell Biology, 212(6), 647-659.
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2

Proteomic Analysis of UTX Interactome

Cited 1 time
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107 416B cells were lysed in the whole cell lysis buffer (50 mM Tris-HCl pH=8, 150 mM NaCl, 0.1% NP-40, 1 mM EDTA), supplemented with 1 mM DTT, protease inhibitors (Sigma), and phosphatase inhibitors (Sigma). Cell were homogenized and lysate cleared by centrifugation. UTX immunoprecipitation was performed in the whole cell lysis buffer with 16 ug of antibody bound to 100ul of Dynabeads Protein G (Thermo Fisher Scientific) and incubated for 1,5h at 4°C with rotation. IP was washed five times with IP wash buffer (10 mM Tris-HCl pH=8, 150 mM NaCl, 0.1% NP-40, 1 mM EDTA), supplemented with protease inhibitor (Sigma). UTX immunoprecipitates were eluted by boiling in 1x LDS loading buffer, reduced with 5 mM TCEP, alkylated with 10 mM iodoacetamide and electrophoresed in Novex NuPAGE Bis-Tris 4%–12% gels (Life Technologies). Gels were stained with colloidal Coomassie (Sigma). Whole lanes were cut in slices and samples processed for MS analysis as described previously65 (link).
Gozdecka M., Meduri E., Mazan M., Tzelepis K., Dudek M., Knights A.J., Pardo M., Yu L., Choudhary J.S., Metzakopian E., Iyer V., Yun H., Park N., Varela I., Bautista R., Collord G., Dovey O., Garyfallos D.A., De Braekeleer E., Kondo S., Cooper J., Göttgens B., Bullinger L., Northcott P.A., Adams D., Vassiliou G.S, & Huntly B.J. (2018). UTX-mediated enhancer and chromatin remodeling suppresses myeloid leukemogenesis through noncatalytic inverse regulation of ETS and GATA programs. Nature genetics, 50(6), 883-894.
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3

Isolation and Analysis of Small-EVs

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60 µg of protein from ascites and 200 µg of protein from cell‐derived small‐EVs were solubilized in Laemly buffer. The protein lysates were separated by 4–20% precast gel (Biorad). After electrophoresis, the gel was fixed with 40% ethanol and 10% acetic acid for 12 h. The gel was then stained with colloidal Coomassie (Sigma) for 48 h, and, after staining, the gel was destained with deionized water. Bands (spots) of interest were excised with a clean scalpel.
Bortot B., Apollonio M., Rampazzo E., Valle F., Brucale M., Ridolfi A., Ura B., Addobbati R., Di Lorenzo G., Romano F., Buonomo F., Ripepi C., Ricci G, & Biffi S. (2021). Small extracellular vesicles from malignant ascites of patients with advanced ovarian cancer provide insights into the dynamics of the extracellular matrix. Molecular Oncology, 15(12), 3596-3614.
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