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NAD+ (Nicotinamide Adenine Dinucleotide) 100 mg

NAD+ (Nicotinamide Adenine Dinucleotide) is a crucial coenzyme involved in oxidation-reduction (redox) reactions, serving as an electron carrier in cellular bioenergetics.

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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

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NAD+ 100mg1 vial | KIT (10 vials)
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
NAD+ (nicotinamide adenine dinucleotide) is an oxidized dinucleotide consisting of nicotinamide mononucleotide (NMN) and adenosine monophosphate (AMP) linked by a pyrophosphate bridge. As a redox-active cofactor, NAD+ participates in electron-transfer reactions and oxidation-reduction processes throughout numerous biochemical systems, where it is reversibly converted between oxidized (NAD+) and reduced (NADH) states. The NAD+/NADH ratio is a widely studied regulatory parameter that influences the activity of redox-sensitive enzymes, signaling proteins, and cofactor-dependent biochemical pathways. Beyond redox cycling, NAD+ serves as an obligate substrate for three major enzyme families: PARP-1/-2 (poly(ADP-ribose) polymerases), sirtuins (SIRT1–7, NAD+-dependent deacylases), and CD38/CD157 (ADP-ribosyl cyclases). These enzymes utilize NAD+ in processes involving protein modification, signal transduction, regulatory pathway activation, and cofactor-dependent enzymatic activity. The central role of NAD+ in redox biology and enzyme-cofactor interactions has established it as a valuable research tool for investigating NAD+-dependent signaling networks, sirtuin pharmacology, PARP-associated pathways, and the molecular mechanisms governing cofactor-regulated biochemical systems. Independently third-party HPLC-tested; COA available per batch.

Results refer to the tested sample. Check the batch and date in the report.

HPLC NAD+ (2607-ED-NA)
September 24, 2026
HPLC NAD+ (2607-CY-NA)
September 13, 2026
HPLC NAD+ (2608-CY-NA)
September 13, 2026
HPLC NAD+ (2605-ED-NA)
July 16, 2026
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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