NAD+
500 MGNAD+ (β-NAD+) — Nicotinamide Adenine Dinucleotide for research on sirtuins
Studied therapeutic interests:
NAD+ (β-nicotinamide adenine dinucleotide, also noted β-NAD+ or NAD plus) is the key pyridine dinucleotide of energy metabolism, ubiquitous cofactor of oxidoreductase enzymes and substrate of sirtuins (SIRT1-SIRT7) NAD+-dependent deacetylases. It is a 663.43 g/mol dinucleotide composed of an adenosine and a nicotinamide ribonucleotide linked by a pyrophosphate bridge. Intracellular concentrations vary from 0.1-1 mM depending on tissue and cellular state.
In fundamental metabolism, NAD+ exists in two interconvertible forms — oxidized (NAD+) and reduced (NADH) — by transferring a hydride during cytosolic and mitochondrial oxidoreduction reactions. The NAD+/NADH ratio is a cellular redox status indicator, regulating glycolysis, the Krebs cycle and oxidative phosphorylation.
Beyond its role as a redox cofactor, NAD+ is the substrate for three major consuming enzymes: sirtuins (SIRT1-SIRT7) NAD+-dependent deacetylases, poly-ADP-ribose polymerases (PARP1/2) in DNA repair, and CD38/CD73 ectoenzymes. NAD+ cellular levels decline with age, contributing to aging phenotype via reduced sirtuin and PARP activity.
Research uses NAD+ to study: sirtuin pathway activation (SIRT1 → PGC-1α, mitochondrial biogenesis), replicative senescence in IMR-90 fibroblasts, oxidative stress response, and SIRT6-mediated DNA repair.
At OSMOSE Research, NAD+ is supplied as a lyophilized powder with HPLC purity ≥ 99.2%, accompanied by a comprehensive certificate of analysis. Delivered to France, Belgium and Switzerland with insulated packaging.
- Preclinical research on sirtuins SIRT1-SIRT7
- Studies on mitochondrial biogenesis and PGC-1α
- Research on cellular senescence in IMR-90
- Preclinical studies on DNA repair via SIRT6/PARP
- Comparative studies NAD+ vs NMN vs NR
- Research on enzymatic reactions of oxidoreduction
- Preclinical models of hepatic steatosis and NAD+
- Studies on cellular longevity
NAD+ is a central molecule in research on the biology of aging and cellular metabolism. The foundational work of Imai, Sinclair, Chini and Baur (2000-present) established its crucial role in regulating sirtuins and aging. Research topics include: activation of SIRT1-SIRT7 deacetylases, regulation of PGC-1α and mitochondrial biogenesis, DNA repair via SIRT6 and PARP, age-related decline of NAD+ levels (50% reduction from age 20 to 70), and comparison with NMN and NR precursors. Replicative senescence studies in IMR-90 fibroblasts and diet-induced obesity models use NAD+ to investigate the role of sirtuins in aging.
- HPLC purity ≥ 99.2% verified by RP-HPLC
- Molecular mass certified by ESI-MS (663.43 g/mol)
- Endotoxin test < 0.5 EU/mg by LAL method
- Sterility validation
- Verification of the β-anomer (not α)
Frequently asked questions
NAD+ is the oxidized form (electron acceptor) while NADH is the reduced form (electron donor). Interconversion occurs by hydride transfer during oxidoreduction reactions. The NAD+/NADH ratio is a cellular redox status indicator: cytosolic NAD+/NADH ~700, mitochondrial ~7-8.
Sirtuins (SIRT1-SIRT7) are NAD+-dependent deacetylases that hydrolyze NAD+ to nicotinamide and 2'-O-acetyl-ADP-ribose while removing an acetyl group from lysines of target proteins. This deacetylation regulates transcription factors, histones and metabolic enzymes.
Age-related decline involves multiple mechanisms: reduced NAMPT expression (key enzyme of the salvage pathway), increased activity of consuming enzymes (CD38 increases 2-3 fold with age), and reduced efficiency of the tryptophan-kynurenine de novo pathway. Levels decrease ~50% between ages 20 and 70.
They are interconverted but with different bioavailabilities. Exogenous NAD+ is rapidly degraded to nicotinamide by membrane NADases (CD38). NMN and NR are more stable precursors, with NMN entering via SLC12A8 transporter and NR via NRK1/NRK2.
For direct enzymatic assays (sirtuins, PARP, dehydrogenases) in vitro: 10-500 µM. For cellular cultures: 100 µM to 1 mM (keeping in mind that NAD+ crosses the membrane poorly, unlike NMN/NR precursors which are more efficient). Intracellular concentrations are 0.1-1 mM.
Lyophilized NAD+ dissolves rapidly in sterile water or PBS at neutral pH. Avoid alkaline pH (> 8) and high temperatures that accelerate hydrolysis. Solutions are stable for 7 days at 4 °C, 1 month at -20 °C aliquoted. Avoid repeated freeze-thaw cycles.
The β-anomer is the biologically active form, recognized by dehydrogenases and sirtuins. The α-anomer is inactive. Our NAD+ is exclusively β-anomer, verified by ¹H NMR and RP-HPLC.
Yes. NAD+ is the obligate substrate for SIRT1-SIRT7 deacetylation reactions. Sirtuin activity is directly proportional to NAD+ concentration in the physiological range (Km ~50-200 µM for SIRT1). An increase in NAD+ levels activates sirtuins without the need for 'activators' such as resveratrol.
Reference models are IMR-90 and WI-38 fibroblasts for replicative senescence, primary hepatocytes for NAFLD/NASH, C2C12 myoblasts for mitochondrial biogenesis, and HEK-293 recombinantly expressing SIRT1-SIRT7 for deacetylation studies.
Purity ≥ 99.2% HPLC is imperative for quantitative enzymatic studies. Synthesis or purification impurities may include NADH (reduced form, co-elutes in some systems), nicotinamide (degradation), and the α-anomer (inactive). Strict β-anomer verification is essential.
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