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Nicotinamide adenine dinucleotide nad

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Nicotinamide adenine dinucleotide (NAD+) is a coenzyme found in all living cells. It is involved in redox reactions, participating in the transfer of electrons during cellular processes such as energy metabolism and DNA repair.

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Lab products found in correlation

S 1 2 3 4 tetrahydro 1 naphthol s tetralol, by Merck Group (3 mentions) Nicotinamide adenine dinucleotide phosphate nadp, by Roche (3 mentions) Androsterone, by Steraloids (1 mentions) Rotenone, by Merck Group (1 mentions) 1 acenaphthenol, by Merck Group (1 mentions) Penicillin, by Roche (1 mentions)

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Nicotinamide adenine dinucleotide

5 protocols using nicotinamide adenine dinucleotide nad

1

Recombinant Enzyme Assay for S-Tetralol

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Reagents were of ACS grade or higher and were purchased from Fisher Scientific (Pittsburgh, PA) and used without further purification. (S)-(+)-1,2,3,4-tetrahydro-1-naphthol (S-tetralol) was purchased from Sigma-Aldrich (St. Louis, MO). Nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+) were purchased from Roche Diagnostics (Indianapolis, IN). Homogeneous recombinant enzymes AKR1C3 and AKR1C2 were prepared and purified as previously described [28 (link)]. The specific activities of AKR1C3 and AKR1C2 for the NAD+ dependent oxidation of S-tetralol are 2.0 and 1.5 μmol min−1 mg−1, respectively.
Zang T., Verma K., Chen M., Jin Y., Trippier P.C, & Penning T.M. (2014). Screening Baccharin Analogs as Selective Inhibitors Against Type 5 17β-Hydroxysteroid Dehydrogenase (AKR1C3). Chemico-biological interactions, 234, 339-348.
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2

Enzymatic Reduction of S-Tetralol

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(S)-(+)-1,2,3,4-tetrahydro-1-naphthol (S-tetralol) was purchased from Sigma-Aldrich (St. Louis, MO). Nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+) were purchased from Roche Diagnostics (Indianapolis, IN). Homogeneous recombinant enzymes AKR1C1, AKR1C2, AKR1C3 and AKR1C4 were prepared and purified as previously described39 (link). The specific activities of AKR1C1, AKR1C2, and AKR1C3 for the oxidation of S-tetralol were 1.4, 2.5 and 3.6 μmol/(min mg), respectively.
Carmona A.V., Jonnalagadda S., Case A.M., Maddeboina K., Jonnalagadda S.K., Dow L.F., Duan L., Penning T.M, & Trippier P.C. (2024). Discovery of an Aldo-Keto reductase 1C3 (AKR1C3) degrader. Communications Chemistry, 7, 95.
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3

Kinetics of AKR1C3 and AKR1C2 Catalysis

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(S)-(+)-1,2,3,4-tetrahydro-1-naphthol (S-tetralol) was purchased from Sigma-Aldrich (St. Louis, MO). Nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+) were purchased from Roche Diagnostics (Indianapolis, IN). Homogeneous recombinant enzymes AKR1C1, AKR1C2, AKR1C3 and AKR1C4 were prepared and purified as previously described.70 (link) The specific activities of AKR1C3 and AKR1C2 for the oxidation of S-tetralol are 2.0 and 1.5 μmol/(min mg), respectively.
Verma K., Zang T., Penning T.M, & Trippier P.C. (2019). Potent and Highly Selective Aldo-Keto Reductase 1C3 (AKR1C3) Inhibitors Act as Chemotherapeutic Potentiators in Acute Myeloid Leukemia and T-Cell Acute Lymphoblastic Leukemia. Journal of medicinal chemistry, 62(7), 3590-3616.
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4

Synthesis and Characterization of Nitro-Aromatic Compounds

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3-NBA, N-OH-3-ABA, and 3-ABA were synthesized as
described previously.31 (link),57 (link),58 (link) The synthesis of 3-NOBA was performed from 3-ABA
following the experimental protocol reported by Fifer et al. for the synthesis
of similar nitroso-PAHs.59 (link) The
purity and identity of these compounds were verified by UV spectroscopy, high
resolution mass spectrometry, and high-field 1 (link) H NMR spectroscopy. All other chemicals were of the
highest grade available, and all solvents were of HPLC grade.
(S)-(+)-1,2,3,4-Tetrahydro-1-naphthol
(S-tetralol), flavin adenine dinucleotide (FAD), dithiothreitol
(DTT), 1-acenaphthenol, dicoumarol (Dic), allopurinol, rotenone, and
D-glucose-6-phosphate (G6P) were purchased from Millipore-Sigma (St. Louis, MO).
Nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine
dinucleotide phosphate (NADP+) were purchased from Roche Diagnostics
(Indianapolis, IN). Glucose-6-phosphate dehydrogenase (G6PD) was purchased from
Worthington Biochemical Corporation (Lakewood, NJ). Androsterone was purchased
from Steraloids (Wilton, NH); 2,6-dichloroindophenol (DCPIP) and salicylic acid
were purchased from Acros Organics (Geel, Belgium). Flufenamic acid (FA),
ursodeoxycholate, and indomethacin were purchased from ICN Biomedicals, Inc.
(Aurora, Ohio).
Murray J.R., Mesaros C.A., Arlt V.M., Seidel A., Blair I.A, & Penning T.M. (2018). Role of Human Aldo-Keto Reductases in the Metabolic Activation of the Carcinogenic Air Pollutant 3-Nitrobenzanthrone. Chemical research in toxicology, 31(11), 1277-1288.
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5

Isolation and Identification of M. synoviae

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For primary isolation, the specimens were diluted and filtered by 0.45μL syringe filter (Nunk, Denmark) in fresh PPLO broth and inoculated onto PPLO agar medium (BBL, Becton Dickinson and company Cockeyville, Sparks, MD, USA). The media was supplemented with 12% of equal volumes of inactivated horse or swine sera. Thallium acetate (1:4000) and penicillin (Roche company, Germany) (1000 IU/mL) as fungal and bacterial inhibitors, nicotinamide adenine dinucleotide (NAD) (Roche company, Germany) (1:10000 w/v) as a necessary requirement of M. synoviae, and cysteine hydrochloride (1:10000 w/v) (Roche company, Germany) as a reducing agent for NAD were also added to the media. Inoculated broth and agar media were incubated under microaerophilic condition (7% CO2) at 37ºC with 98% relative humidity and checked for color change of broth and typical Mycoplasma colonies on agar. As soon as the phenol red indicator changed to yellow, the subculture onto the fresh broth and agar were carried out (7 (link), 15 ). Several passages until 21 to 28 days were subcultured. Identification of the M. synoviae samples was carried out by serological methods, after appearing the specific colonies of Mycoplasma.
Tebyanian H., Mirhosseiny S.H., Kheirkhah B., Hassanshahian M, & farhadian H. (2014). Isolation and Identification of Mycoplasma synoviae From Suspected Ostriches by Polymerase Chain Reaction, in Kerman Province, Iran. Jundishapur Journal of Microbiology, 7(9), e19262.
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