Coomassie blue

Manufactured by Merck Group

Sourced in United States, Germany, Italy

Coomassie blue is a protein-binding dye used in various laboratory techniques, such as gel electrophoresis and protein assays. It is a versatile tool for the detection and quantification of proteins in biological samples.

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Lab products found in correlation

Bovine serum albumin (bsa), by Merck Group (9 mentions) Triton x 100, by Merck Group (7 mentions) Gelatin, by Merck Group (4 mentions) Trizma base, by Merck Group (4 mentions) Iodoacetamide, by Merck Group (3 mentions) Adenosine triphosphate (atp), by Merck Group (3 mentions) Ethylene diamine tetraacetic acid (edta), by Merck Group (3 mentions) Ethylenediaminetetraacetic acid, by Merck Group (3 mentions) Methanol, by Merck Group (3 mentions) Trichloroacetic acid, by Merck Group (3 mentions) Dithiothreitol (dtt), by Merck Group (3 mentions) Hydrogen peroxide, by Merck Group (3 mentions) Nupage, by Thermo Fisher Scientific (3 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (3 mentions) Immobilon p, by Merck Group (2 mentions) As09 491, by Agrisera (2 mentions) As09 484, by Agrisera (2 mentions) As07 266, by Agrisera (2 mentions) As07 260, by Agrisera (2 mentions) Type a gelatin from porcine skin, by Merck Group (2 mentions)

Close spelling variants of this product

Bradford Coomassie brilliant blue assay (2 citations) Coomassie Brilliant Blue R-250 Dye (8 citations) Coomassie Blue Protein Assay (2 citations) Coomassie Blue solution (12 citations) Coomassie blue CBB G-250 (2 citations) Colloidal Coomassie brilliant blue (4 citations) Coomassie Brilliant Blue Solution (6 citations) Colloidal Coomassie blue stain (3 citations) ), Coomassie brilliant blue reagent (3 citations) Coomassie Brilliant Blue staining (5 citations)

110 protocols using coomassie blue

Quantifying Clonogenic Survival and Proliferation

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For clonogenic survival assay, 200-300 cells were seeded per well in triplicate in a 6-well plate. The following day, cells were treated with different DNA damaging agents. Following treatment, colonies were grown for 7 to 10 days after which they were fixed and stained using Coomassie blue (50% methanol, 7% acetic acid and 0.1% Coomassie blue (all Sigma)). To assess the growth speed of siRNA-transfected cells, 10,000 (HCT116) or 20,000 (ELOF1 -/-A) cells were seeded in a 6-well plate and grown for 10 days after transfection. Colony numbers were counted using GelCount (Oxford Optronix Ltd.). Relative colony number was plotted of at least 2 independent experiments, each performed in triplicate. Levels were normalized to mock-treated, set to 100 and plotted with SEM. Statistics was performed using independent T-test.
For AlamarBlue survival assay, siRNA-transfected cells were seeded to confluency in presence of 0.5% serum in triplicate in 96-well plates to arrest cells in G_0, and UV-irradiated after 30 hours. 72 hours after UV irradiation, AlamarBlue® (Invitrogen) was added for 4 hours and fluorescence was measured at 570 nm using a SpectraMax iD3 reader. Data were background corrected and normalized to mock-treated conditions.

Geijer M.E., Zhou D., Selvam K., Steurer B., Mukherjee C., Evers B., Cugusi S., van Toorn M., van der Woude M., Janssens R.C., Kok Y.P., Gong W., Raams A., Lo C.S., Lebbink J.H., Geverts B., Plummer D.A., Bezstarosti K., Theil A.F., Mitter R., Houtsmuller A.B., Vermeulen W., Demmers J.A., Li S., van Vugt M.A., Lans H., Bernards R., Svejstrup J.Q., Chaudhuri A.R., Wyrick J.J, & Marteijn J.A. (2021). Elongation factor ELOF1 drives transcription-coupled repair and prevents genome instability. Nature cell biology, 23(6), 608-619.

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Multiplex Cathepsin Zymography Protocol

Cited 1 time

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Samples were resolved in multiplex cathepsin zymography as previously described [20 (link)]. Briefly, samples were prepared using non-reducing loading buffer (5×-0.05% bromophenol blue, 10% sodium dodecyl sulfate (SDS), 1.5M Tris, 50% glycerol. A 12.5% SDS-PAGE gel was used and embedded with 5 mg/mL gelatin substrate. Both gels were run at 200V at 4°C. Proteases were renatured in 65mM Tris buffer pH 7.4 with 20% glycerol for 3 washes, 10min each, then incubated in and pH 4 (acetate buffer, 1mM EDTA with 2mM DTT, freshly added) or pH6 (phosphate buffer, 1mM EDTA with 2mM DTT, freshly added) activity assay buffer. After overnight incubation, gels were stained with Coomassie Blue (4.5% Coomassie Blue; Sigma-Aldrich, 10% acetic acid, and 10% isopropanol) then destained (10% acetic acid and 10% isopropanol).

Douglas S.A., Lamothe S.E., Singleton T.S., Averett R.D, & Platt M.O. (2018). Human cathepsins K, L, and S: related proteases, but unique fibrinolytic activity. Biochimica et biophysica acta. General subjects, 1862(9), 1925-1932.

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Quantifying Clonogenic Survival and Proliferation

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Clonogenic Assay under Hypoxia

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For clonogenic assays, cells were plated in 6-well plates at a density of 300 cells per well; after 24 hours oxaliplatin was added at specified concentrations immediately prior to transfer of the plates to the hypoxia chamber. After 24 hours of hypoxia, plates were returned to normal conditions for 48 hours, and, following the addition of fresh media, cultivated for 10-14 days; colonies were then fixed in 75% ethanol, stained with Coomassie Blue (Sigma) and counted manually. All experiments were performed at least two times in duplicate.

Vasilevskaya I.A., Selvakumaran M., Roberts D, & O’Dwyer P.J. (2016). JNK1 INHIBITION ATTENUATES HYPOXIA-INDUCED AUTOPHAGY AND SENSITIZES TO CHEMOTHERAPY. Molecular cancer research : MCR, 14(8), 753-763.

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Gelatin Zymography for MMP Activity

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CM derived from UCX® cultured in either two dimensions (CM2D) or three dimensions (CM3D) and control (10 μg total protein per lane) were separated in a 10% polyacrylamide gel containing 0.1% gelatin as substrate. Precision Plus Protein™ Dual Color Standards (Bio-Rad, Hercules, CA, USA), was used as protein standard. Following electrophoresis, gels were washed twice in 2% Triton X-100 (Sigma-Aldrich) for 30 minutes. After rinsing in H₂O_dd, gels were incubated in matrix metalloproteinase (MMP) substrate buffer (50 mM Tris–HCl, pH 7.5; 10 mM CaCl₂; 0.5% (w/v) NaN₃) for 16 hours at 37°C. Gels were washed once with H₂O_dd and stained with Coomassie Blue (Sigma-Aldrich) solution for 30 minutes until bands became clear. Band acquisition and density quantification were performed using the Molecular Imager GS800 calibrated densitometer (Bio-Rad). Data was normalized on the protein amount measured in the cell supernatants.

Santos J.M., Camões S.P., Filipe E., Cipriano M., Barcia R.N., Filipe M., Teixeira M., Simões S., Gaspar M., Mosqueira D., Nascimento D.S., Pinto-do-Ó P., Cruz P., Cruz H., Castro M, & Miranda J.P. (2015). Three-dimensional spheroid cell culture of umbilical cord tissue-derived mesenchymal stromal cells leads to enhanced paracrine induction of wound healing. Stem Cell Research & Therapy, 6(1), 90.

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Membrane Protein Separation and Western Blot Analysis

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Membrane protein separation was performed by SDS-PAGE (10% acrylamide gel) according to Schägger and von Jagow [25 (link)]. Proteins were stained with Coomassie Blue (Sigma-Aldrich Corp. St. Louis, MO, USA) or electroblotted to PVDF membranes (Immobilon-P, Millipore Corp. Bedford, MA, USA) at 22 V for 2.5 h. These membranes were treated with Western Blot Signal Enhancer (Pierce^®, Thermo Scientific, IL, USA) and blocked in 20 mM Tris, 150 mM sodium chloride pH 7.5 with 0.1% (v/v) Tween-20 (TBS-T) buffer with 2% defatted milk, and then successively incubated with the primary antibody and the second antibody. Antibody reacting bands were detected using alkaline phosphatase reaction (1:2500, Sigma-Aldrich, St. Louis, MO, USA) or anti-rabbit IgG horse radish peroxidase conjugated (1:20,000, Sigma-Aldrich, St. Louis, MO, USA). Antibodies used for immunoblotting were as follows: anti PIP2;1, PIP2;2, PIP2;3 (1:1000, Agrisera, Vännäs, Sweden, AS09 491), anti-Na⁺/H⁺ exchanger 1 (1:1000, Agrisera, Vännäs, Sweden, AS09 484), anti-SMT1 (1:1000, Agrisera, Vännäs, Sweden, AS07 266), anti-H⁺-ATPase (1:10,000, Agrisera, Vännäs, Sweden, AS07 260), and anti-PsbA (1:20,000, Agrisera, Vännäs, Sweden, AS05084).

Cano-Ramirez D.L., Carmona-Salazar L., Morales-Cedillo F., Ramírez-Salcedo J., Cahoon E.B, & Gavilanes-Ruíz M. (2021). Plasma Membrane Fluidity: An Environment Thermal Detector in Plants. Cells, 10(10), 2778.

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Mitochondrial Function Assessment Protocol

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D-mannitol, 3-4,5-dimethylthiazol-2-yl] 2,5-diphenyltetrazolium bromide (MTT), 2’,7’-dichlorofluorescein diacetate (DCFH-DA), Tris-HCl, sodium succinate, sucrose, KCl, Na₂HPO₄, MgCl₂, potassium phosphate, Rhodamine 123 (Rh 123), coomassie blue, ethyleneglycol-bis(2-aminoethylether)-N,N,N’,N’-tetraaceti c acid (EGTA), ethylenediamine tetraacetic acid (EDTA), dimethyl sulfoxide (DMSO), N-(2-Hydroxyethyl)piperazine-N’-(2-ethanesulfonic acid) (HEPES), and bovine serum albumin (BSA) were purchased from Sigma Chemical Co. (St. Louis, Mo, USA). All chemicals were of analytical grades.
Atorvastatin, lovastatin, and L-carnitine were kindly donated by Poursina Pharmaceutical Co. (Tehran, Iran). Coenzyme Q10 (Roche, Switzerland) was a gift from akbarieh Co. (Tehran, Iran).

Sadighara M., Joktaji J.P., Hajhashemi V, & Minaiyan M. (2017). Protective effects of coenzyme Q10 and L-carnitine against statin-induced pancreatic mitochondrial toxicity in rats. Research in Pharmaceutical Sciences, 12(6), 434-443.

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Synthesis and Conjugation of TAZ Peptide

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A 21 amino acid peptide PESFFKEPDSGSHSRQSSTDS of a region near the N terminal of TAZ protein was designed and synthesized. The immune grade peptide (China Peptides. Co. Ltd) was conjugated with the carrier protein keyhole limpet hemocyanin (KLH, Sigma) through glutaraldehyde linker as described previously. The same procedure was performed for conjugation of synthetic peptide and Bovine Serum Albumin (BSA) as a control. To examine the efficiency of conjugation, 10 μg TAZ-BSA were run on a 10% SDS-PAGE gel (Bio-Rad). The gel was stained with Coomassie Blue (Sigma). The change in mobility of conjugated BSA and appearance of the smear verified the efficiency of conjugation.

Haji Ghaffari M., Mohammadzadeh M., Simonian M., Hashemi M., Sadeghi N., Negahdari B., Mazloomi M, & Rabbani H. (2023). An Anti-TAZ Monoclonal Antibody Recognizing Cell Surface Expressed TAZ Protein in Human Tumor Cells. Avicenna Journal of Medical Biotechnology, 15(1), 14-20.

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Gelatin Zymography for Protease Activity

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Non-reduced protein samples were resolved by SDS-PAGE gels containing type A gelatin from porcine skin (0.2%, Sigma Aldrich, Milan, Italy). Briefly, after electrophoresis, gels were incubated with a solution of 2.5% TRITON X-100 for 3 h at room temperature, and then incubated in a solution of calcium chloride (CaCl₂, 1 mM) and sodium chloride (NaCl, 15 mM), pH 7.4 (all from Sigma Aldrich, Milan, Italy) overnight at 37 °C. Subsequently, gels were fixed and then stained with Coomassie Blue (Sigma Aldrich, Milan, Italy). For objective quantification ImageJ software was used.

Ramella M., Bertozzi G., Fusaro L., Talmon M., Manfredi M., Catoria M.C., Casella F., Porta C.M., Boldorini R., Fresu L.G., Marengo E, & Boccafoschi F. (2019). Effect of Cyclic Stretch on Vascular Endothelial Cells and Abdominal Aortic Aneurysm (AAA): Role in the Inflammatory Response. International Journal of Molecular Sciences, 20(2), 287.

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Colony Formation Assay of BIO Treatment

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Cells (500 cells/well in a 6-well plate) were treated with 200 nM, 400 nM, or 800 nM BIO for 14 d. Cells were fixed with 4% buffered formalin for 10 min and stained with Coomassie blue (Sigma-Aldrich, CA, USA). Colony formation was investigated using an inverted microscope (Olympus, Nashville, TN, USA). The staining was eluted with a 5% (v/v) methanol and 7.5% (v/v) acetic acid solution. The absorbance was read at 667.5 nm.

Kornsuthisopon C., Rochanavibhata S., Nowwarote N., Tompkins K.A., Sukarawan W, & Osathanon T. (2022). 6-Bromoindirubin-3′-Oxime Regulates Colony Formation, Apoptosis, and Odonto/Osteogenic Differentiation in Human Dental Pulp Stem Cells. International Journal of Molecular Sciences, 23(15), 8676.

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