NAD+ is nicotinamide adenine dinucleotide — a small molecule, not a peptide. Molecular formula C21H27N7O14P2, molecular weight 663.43 g/mol. It sits in this catalogue alongside research peptides but belongs to an entirely different chemical class, and it behaves differently in handling as a result.
Structurally it is a dinucleotide: nicotinamide mononucleotide joined to adenosine monophosphate through a pyrophosphate bridge. That pyrophosphate linkage is the vulnerable point in the molecule and the reason storage conditions matter.
Research context
NAD+ is a coenzyme rather than a signalling peptide, and its research interest divides along two lines.
The classical role is redox chemistry: NAD+ accepts a hydride ion to become NADH, and this couple drives the oxidation reactions of glycolysis, the citric acid cycle and fatty acid oxidation. Here it is consumed and regenerated cyclically.
The second role is consumptive rather than catalytic, and it is where most current research attention sits. Sirtuins, PARPs and CD38 all cleave NAD+ and consume it — sirtuin deacetylation of histones and metabolic enzymes, PARP activity in DNA damage response. Because these enzymes destroy the molecule rather than recycle it, cellular NAD+ availability becomes a limiting factor, which is the basis for research into NAD+ decline and its relationship to metabolic and age-related endpoints.
For a fuller treatment of the sequence, published models and technical data, see the NAD+ research guide.
Specification
CAS number 53-84-9. Supplied as a lyophilized powder, soluble in water. 99%+ purity, HPLC verified at ILS Lab. Available in 500mg and 1000mg presentations.
Handling
NAD+ is less stable than the peptides in this catalogue and hydrolyses readily in aqueous solution, particularly at alkaline pH and elevated temperature. Prepare solutions fresh where the protocol allows rather than storing reconstituted material for extended periods.
Reconstitute with sterile or bacteriostatic water, swirling gently. Store lyophilized at −20°C protected from light and moisture — the powder is hygroscopic and moisture ingress degrades it.
Ships with a batch-specific Certificate of Analysis. Cross-check the batch ID printed on your vial against the CoA before use — see the guide to reading a CoA if you are unfamiliar with the format.
Frequently asked questions about NAD+
Is NAD+ a peptide?
No. It is a dinucleotide — nicotinamide mononucleotide joined to adenosine monophosphate through a pyrophosphate bridge — and belongs to an entirely different chemical class from everything else in this catalogue. That matters practically: it is less stable in aqueous solution than the peptides here and requires different handling assumptions.
Why is NAD+ less stable than the peptides?
The pyrophosphate bridge hydrolyses readily in water, particularly at alkaline pH and elevated temperature. Peptide bonds are considerably more robust. The practical consequence is that reconstituted NAD+ has a shorter useful life than a reconstituted peptide — prepare solutions fresh where the protocol allows rather than storing them for extended periods.
What is the difference between the redox and consumptive roles?
In redox chemistry, NAD+ accepts a hydride to become NADH and is regenerated cyclically — it is a catalyst, not consumed. But sirtuins, PARPs and CD38 cleave NAD+ and destroy it. Because those enzymes consume rather than recycle, cellular NAD+ availability becomes a limiting factor for their activity. That consumptive pathway is where most current research attention sits.
How should NAD+ powder be stored?
At −20°C, protected from light and — importantly — from moisture. The powder is hygroscopic, meaning it draws water from the air, and moisture ingress degrades it. Keep the vial sealed, minimise the time it spends open, and avoid returning it to a warm environment before it has fully equilibrated, which promotes condensation inside the vial.
Research use only. Not for human or veterinary use, not for use in diagnostic procedures, and not evaluated by the U.S. Food and Drug Administration.
