NAD+ (Nicotinamide Adenine Dinucleotide) is a fundamental coenzyme present in all living cells, central to redox reactions and cellular energy metabolism. Research has established NAD+ as a critical regulator of sirtuin activity, PARP function, and mitochondrial biogenesis. Levels decline with age in multiple tissues, making NAD+ repletion a major area of contemporary longevity research.
NAD+ (Nicotinamide Adenine Dinucleotide) is a fundamental coenzyme present in all living cells, central to redox reactions and cellular energy metabolism. Research has established NAD+ as a critical regulator of sirtuin activity, PARP function, and mitochondrial biogenesis. Levels decline with age in multiple tissues, making NAD+ repletion a major area of contemporary longevity research.
NAD+ (Nicotinamide Adenine Dinucleotide) is supplied strictly as a reference material for in vitro and preclinical investigation. All characterization data described here is drawn from peer-reviewed literature and laboratory analysis; nothing herein constitutes a claim of clinical effect in humans.
The following domains summarize directions explored across published studies and laboratory models. Each reflects observations reported in rodent models, in vitro systems, or the peer-reviewed record.
NAD+ is the primary electron carrier in mitochondrial oxidative phosphorylation. Research has extensively characterized its role in the TCA cycle, electron transport chain function, and ATP production across multiple tissue types.
NAD+ is an obligate substrate for sirtuin deacylases (SIRT1–7). Studies have examined how NAD+ repletion restores sirtuin activity in aged tissues and the downstream effects on mitochondrial biogenesis and stress resistance.
PARP enzymes consume NAD+ during DNA damage repair. Research has examined the competition between PARP and sirtuins for NAD+ in the context of aging, neurodegeneration, and metabolic disease models.
Research has examined NAD+ repletion in models of neurodegeneration, including Parkinson's and Alzheimer's disease models in rodents, with studies documenting neuroprotective effects via sirtuin and PARP pathways.
Mechanistic steps below are hypothesized from in vitro assays and animal-model data reported in the literature. They describe biochemical interactions observed under controlled experimental conditions.
NAD+ accepts electrons from metabolic substrates to form NADH, which donates electrons to Complex I of the mitochondrial electron transport chain, driving ATP synthesis via oxidative phosphorylation.
NAD+ is consumed stoichiometrically by sirtuin deacylases during protein deacetylation reactions. Sirtuin activity is directly limited by NAD+ availability, linking metabolic state to epigenetic regulation.
PARP-1 uses NAD+ to synthesize poly-ADP-ribose chains at sites of DNA strand breaks, facilitating repair factor recruitment. NAD+ depletion through PARP hyperactivation has been studied as a mechanism of cell death.
CD38, an NAD+ hydrolase, converts NAD+ to cyclic ADP-ribose (cADPR), a second messenger for calcium signaling. Research has examined the NAD+/CD38/cADPR axis in immune function and muscle contraction models.
| Amino Acid Sequence | N/A |
|---|---|
| Molecular Weight | 663.4 g/mol |
| Molecular Formula | C₂₁H₂₇N₇O₁₄P₂ |
| CAS Number | 53-84-9 |
| Storage | −20°C long-term, 4°C short-term up to 2 weeks, protect from light |
The following peer-reviewed references informed the research summaries on this page. Citations are provided for scientific context only.
This product is intended strictly for laboratory research purposes only. It is not a drug, food, cosmetic, or dietary supplement and is not intended to diagnose, treat, cure, or prevent any disease. It is not for human or animal consumption. All information presented is derived from published scientific literature and is provided for educational reference only. By purchasing, the buyer affirms they are a qualified researcher or institution and assume full responsibility for the safe and lawful handling of this material.