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NAD+ (Nicotinamide Adenine Dinucleotide) 100 mg
During our packaging transition, you may receive products with either our previous or updated label. Rest assured, the formulation, purity and quality remain exactly same as standards.
NAD+ (Nicotinamide Adenine Dinucleotide) is a crucial coenzyme involved in oxidation-reduction (redox) reactions, serving as an electron carrier in cellular bioenergetics. It plays a fundamental role in metabolic pathways, including glycolysis, the citric acid cycle, and oxidative phosphorylation.
This pyridine nucleotide exists in both oxidized (NAD⁺) and reduced (NADH) states, enabling its function in enzymatic catalysis and cofactor-dependent biochemical reactions. NAD+ is metabolized through enzymatic cleavage, salvage pathways, and poly(ADP-ribose) polymerase (PARP) activity, with primary clearance via renal and hepatic pathways.
NAD+ 100 mg should be reconstituted with bacteriostatic water (BAC).
- High Purity – 99% Purity Guaranteed
- Independently Lab Tested
- Research Grade Quality
- For Laboratory Research Use Only
3D Molecular Structure
Drag to rotate · scroll to zoom| Chemical Formula | C21H27N7O14P2 |
|---|---|
| Synonyms | nadide, coenzyme I, beta-NAD, beta-nicotinamide adenine dinucleotide |
| Molar Mass | 663.43 g/mol |
| CAS Number | 53-84-9 |
| PubChem CID | 5892 |
| Total Compound Content | 100 mg per vial |
| Shelf Life | 24 months |
Every batch is independently lab tested for identity, purity and potency. View our lab testing program →
How does NAD+ differ from NAD+ precursor compounds in biochemical research?
NAD+ is the oxidized dinucleotide cofactor itself, whereas compounds such as nicotinamide mononucleotide (NMN) and nicotinamide riboside (NR) participate in NAD+ biosynthetic pathways. This distinction makes NAD+ a useful research tool for investigating NAD+-dependent enzymatic reactions, cofactor utilization mechanisms, redox system dynamics, and the biochemical relationships between NAD+ and precursor-associated pathways.
Which enzyme families utilize NAD+ as a substrate?
NAD+ serves as an obligate substrate for three major enzyme families: poly(ADP-ribose) polymerases (PARPs), sirtuins (SIRT1–7), and CD38/CD157 ADP-ribosyl cyclases. These enzymes utilize NAD+ in processes involving protein modification, enzymatic regulation, signal transduction, and cofactor-dependent biochemical activity. Their dependence on NAD+ has made them important targets for investigations of enzyme-cofactor interactions and NAD+-associated regulatory mechanisms.
Why is NAD+ widely used in biochemical research?
NAD+ occupies a central role in both redox chemistry and enzyme-mediated regulatory systems. In addition to functioning as a reversible electron carrier, it participates directly in the catalytic activity of multiple NAD+-dependent enzyme families. These characteristics have established NAD+ as a valuable research tool for investigating redox biology, enzyme kinetics, cofactor-dependent catalysis, sirtuin pharmacology, PARP biochemistry, CD38-associated pathways, and the molecular mechanisms governing NAD+-dependent biochemical processes.
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