What NAD+ is
Nicotinamide adenine dinucleotide is not a peptide at all — it is a dinucleotide coenzyme, and one of the most fundamental molecules in metabolism. It exists in two interconverting forms: NAD+, the oxidised form, and NADH, the reduced form. The ratio between them is a direct readout of a cell’s metabolic state, which is why it appears in research contexts far removed from one another.
- NAD+Redox cofactor, not a peptide
- Sirtuins (SIRT1-7) and PARPsConsumed as a substrate, not just a carrier
- Deacetylation, DNA repair, redox fluxLevels decline with age
- Metabolic and ageing modelsPreclinical and early clinical
Mechanism as described in published research. Nothing here describes an effect in a person — these compounds are supplied for laboratory research use only.
Two distinct roles
NAD+ does two mechanistically separate jobs, and conflating them is a common source of confusion.
As a redox cofactor it is recycled, not consumed: it accepts electrons in glycolysis and the citric-acid cycle, becomes NADH, delivers those electrons to the respiratory chain and returns to NAD+. In this role the total pool is conserved and only the ratio moves.
As a substrate it is consumed outright. Sirtuins, PARPs and CD38 all cleave NAD+ and release nicotinamide. This is the role that draws the ageing and DNA-repair literature, because consumption means the pool has to be replenished and can, in principle, be depleted. Nearly all research interest in NAD+ availability follows from this second role rather than the first.
What the literature covers
Research areas include:
- Sirtuin-dependent deacetylation — NAD+ as the required cosubstrate.
- PARP activity and DNA repair — NAD+ consumption under genotoxic stress.
- Mitochondrial redox state — the NAD+/NADH ratio as a metabolic readout.
- Salvage-pathway biology — how the pool is regenerated from nicotinamide, and what limits it.
5-Amino-1MQ is studied in the directly adjacent context as an NNMT inhibitor, and MOTS-c in the same mitochondrial-metabolic space.
Identity and verification
NAD+ has the molecular formula C21H27N7O14P2 and a molecular weight of 663.4 g/mol (CAS 53-84-9). Identifiers matter more here than in most categories: research compounds are sold under trade names, development codes and abbreviations that do not always refer to the same molecule, and a formula is unambiguous where a name is not.
The lot we currently hold measured 99.94% for the 500 mg (lot 261807) and 99.97% for the 1000 mg (lot 261807), tested by Freedom Diagnostics. The certificate is published in full, including the raw chromatogram and mass spectrum — so the number can be read off the underlying trace rather than taken on trust.
We use two laboratories because purity and identity are different questions. Vanguard Laboratory is ISO/IEC 17025:2017 accredited (A2LA #6377.01.01) and reports chromatographic purity and net quantity with a stated measurement uncertainty. Freedom Diagnostics reports HPLC-UV purity together with LC-MS identity confirmation — the test that catches a substituted compound rather than merely an impure one. A sample can be 99% pure and still be the wrong molecule. How we test →
Handling, reconstitution and storage
NAD+ ships lyophilized — freeze-dried to a solid and sealed under vacuum — which is what makes it stable in transit rather than a solution racing a clock. Reconstitute with bacteriostatic water, added slowly down the inside wall of the vial rather than directly onto the powder, then swirled gently. Do not shake: mechanical shear is one of the few things that reliably degrades a peptide in the lab.
Final concentration is a function of the volume added, not of the compound, so the same vial can be prepared at very different concentrations. The reconstitution calculator works out the volume for a target concentration and the reconstitution guide covers the procedure. Store lyophilized vials at −20 °C (−4 °F) protected from light; refrigerate once in solution, and see the storage and stability guide for how long reconstituted material holds.
Common questions
Is NAD+ a peptide?
No. NAD+ is a dinucleotide coenzyme, not a peptide. It is stocked alongside research peptides because it appears constantly in the same metabolic and mitochondrial research, but chemically it is an entirely different class of molecule.
What is the difference between NAD+ and NADH?
They are the oxidised and reduced forms of the same molecule. NAD+ accepts electrons to become NADH; NADH delivers them to the respiratory chain and returns to NAD+. The ratio between the two is a direct readout of metabolic state.
Why is NAD+ depletion discussed if it is a cofactor?
Because it has two roles. As a redox cofactor it is recycled and the pool is conserved. But sirtuins, PARPs and CD38 consume it outright as a substrate, releasing nicotinamide — and that consumption is what makes availability a research question at all.
What enzymes consume NAD+?
Principally the sirtuins, the PARP family and CD38. All cleave NAD+ and release nicotinamide, which then re-enters the salvage pathway.
Where to get it
Buy research-grade NAD+ — independently tested, certificate published, shipped from Miami with cold-chain packaging. Current pricing for every size is on the price list, and we ship worldwide.
Research use only
Everything referenced here is supplied strictly for laboratory research. These compounds are not drugs, foods, cosmetics or medical devices, are not for human or veterinary use, and are not approved for diagnostic or therapeutic application. Mechanisms are described as studied in preclinical and laboratory research; nothing above describes dosing, treatment or clinical outcome.
