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Phosphatase inhibitor cocktails 1 or 3

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Phosphatase inhibitor cocktails 1 and 3 are specialized laboratory reagents used to inhibit the activity of phosphatase enzymes in biological samples. These cocktails contain a combination of chemical compounds that effectively suppress the function of various phosphatases, which play a crucial role in cellular signaling pathways. The cocktails are designed to maintain the phosphorylation state of proteins, allowing researchers to study their regulatory mechanisms and cellular functions.

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Lab products found in correlation

Perchloric acid, by Thermo Fisher Scientific (2 mentions) Medetomidine, by Henry Schein (2 mentions) Sodium dodecyl sulfate (sds), by Teknova (2 mentions) Sodium deoxycholate, by Merck Group (2 mentions) Methanol, by Thermo Fisher Scientific (2 mentions) Trichostatin a, by Merck Group (2 mentions) Halt protease and phosphatase inhibitor cocktail, by Thermo Fisher Scientific (2 mentions) 4 2 hydroxyethyl piperazine 1 ethanesulfonic acid hepes, by Merck Group (2 mentions) Asp n, by Roche (2 mentions) Thiamet g, by Bio-Techne (2 mentions) Dimethylamino phenyl n hydroxy 4 6 dimethyl 7 oxo 2 4 heptadienamide, by Merck Group (2 mentions) Niacinamide pyridine 3 carboxylic acid amide, by Merck Group (2 mentions) Proteomic grade trypsin, by Promega (2 mentions) Triton x 100, by Merck Group (2 mentions) Complete mini, by Roche (2 mentions)

2 protocols using phosphatase inhibitor cocktails 1 or 3

1

Protein Extraction and Modification Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
Phosphatase inhibitor cocktails 1 or 3, and 2 (100x, Sigma) and protease inhibitor tablets (cOmplete, EDTA-free and cOmplete-mini, EDTA-free; Roche) were used interchangeably with Halt protease and phosphatase inhibitor cocktails (Thermo Scientific); all were used at 1x according to the manufacturers’ instructions. Thiamet G (4390, Tocris) was used in a range of concentrations, as specified. Trichostatin A ([R-(E,E)]-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxo-2,4-heptadienamide, Sigma) was used at 3 μM and niacinamide (pyridine-3-carboxylic acid amide, Sigma) at 10 mM. Other reagents were ketamine HCl (Bionichepharma), medetomidine (Dexdomitor, Henry Schein), perchloric acid (Fisher), methanol (Fisher), 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid (HEPES, Sigma), sodium chloride (5M, Cellgrow), sodium dodecyl sulfate (from 10% solution, Teknova), TritonX-100 (Sigma), and sodium deoxycholate (Sigma). All reagents for peptide digestions were from Sigma, except proteomic-grade trypsin (Promega) and AspN (Roche).
Morris M., Knudsen G.M., Maeda S., Trinidad J.C., Ioanoviciu A., Burlingame A.L, & Mucke L. (2015). Tau post-translational modifications in wildtype and human amyloid precursor protein transgenic mice. Nature neuroscience, 18(8), 1183-1189.
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2

Protein Extraction and Modification Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
Phosphatase inhibitor cocktails 1 or 3, and 2 (100x, Sigma) and protease inhibitor tablets (cOmplete, EDTA-free and cOmplete-mini, EDTA-free; Roche) were used interchangeably with Halt protease and phosphatase inhibitor cocktails (Thermo Scientific); all were used at 1x according to the manufacturers’ instructions. Thiamet G (4390, Tocris) was used in a range of concentrations, as specified. Trichostatin A ([R-(E,E)]-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxo-2,4-heptadienamide, Sigma) was used at 3 μM and niacinamide (pyridine-3-carboxylic acid amide, Sigma) at 10 mM. Other reagents were ketamine HCl (Bionichepharma), medetomidine (Dexdomitor, Henry Schein), perchloric acid (Fisher), methanol (Fisher), 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid (HEPES, Sigma), sodium chloride (5M, Cellgrow), sodium dodecyl sulfate (from 10% solution, Teknova), TritonX-100 (Sigma), and sodium deoxycholate (Sigma). All reagents for peptide digestions were from Sigma, except proteomic-grade trypsin (Promega) and AspN (Roche).
Morris M., Knudsen G.M., Maeda S., Trinidad J.C., Ioanoviciu A., Burlingame A.L, & Mucke L. (2015). Tau post-translational modifications in wildtype and human amyloid precursor protein transgenic mice. Nature neuroscience, 18(8), 1183-1189.
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