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Niacinamide pyridine 3 carboxylic acid amide

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Niacinamide (pyridine-3-carboxylic acid amide) is a chemical compound used in various laboratory applications. It is a form of vitamin B3 and serves as a precursor to the coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), which are essential in cellular metabolism and energy production.

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Lab products found in correlation

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

Spelling variants of this product

Pyridine (718 citations) Niacinamide (18 citations) Carboxylic acids (8 citations)

2 protocols using niacinamide pyridine 3 carboxylic acid amide

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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