NAD+

NAD+ is a redox coenzyme and the consumed substrate of sirtuins, PARPs, and CD38, studied extensively in metabolic and aging biology.

Yes. 1 third party certificate for NAD+ are published on this site, covering endotoxin, purity and sterility. Each one is the report as the testing laboratory issued it, not a retyped summary, and the most recent lot is 500mg · Oct 2025. Match the batch on your vial to the batch on the report.

53-84-9. It is printed in the specification table on this page so it can be checked against your own records before ordering.

Refrigerate (2-8 deg C) Lyophilized powder is the stable form; once reconstituted, a solution is far more fragile and should be aliquoted rather than repeatedly frozen and thawed.

>=99% by HPLC. The released figure for any given lot is on that lot's certificate rather than taken from this page, because purity is a property of a batch and not of a product line.

No. This is sold for laboratory research use only. It is not a drug, not a supplement, and not approved by the FDA for human or veterinary use. We do not provide dosing, administration, or protocol guidance, by phone, by email, or through the assistant on this site.

No. NAD+ is a dinucleotide coenzyme, not a peptide, even though it is frequently listed alongside peptides in research catalogs. It consists of adenosine monophosphate and nicotinamide mononucleotide joined by a pyrophosphate bridge, and its handling and stability requirements differ from those of peptides.

Because NAD+ is large and highly charged and is not efficiently taken up by cells intact. Extracellular NAD+ is degraded at the cell surface by CD38 and CD73 into nicotinamide mononucleotide and nicotinamide riboside, which are then transported and reassembled into NAD+ inside the cell. Study designs use precursors because that is the route the biology actually takes.

Human trials in this field have studied the precursors nicotinamide riboside and nicotinamide mononucleotide, not NAD+ itself. Those trials have generally been small and short, have shown that precursors raise blood NAD metabolite levels and are tolerated over the durations studied, and have produced mixed results on functional endpoints. There is no controlled human trial evidence for NAD+ administration itself.

NADP+ carries an additional phosphate on the adenosine ribose and serves a different function. The NAD+ and NADH pool is kept largely oxidized to accept electrons from fuel breakdown, while the NADP+ and NADPH pool is kept largely reduced to donate electrons for biosynthesis and for regenerating the glutathione and thioredoxin systems. They are not interchangeable in assays.

Spectrophotometrically. NADH absorbs strongly at 340 nm with an extinction coefficient of approximately 6220 per molar per centimeter while NAD+ does not, which allows direct determination of oxidation state and is the basis of coupled dehydrogenase assays. Because aqueous NAD+ loses titer over days, concentration should be measured rather than calculated from mass for any assay where cofactor level is a variable.

Largely because of methodology. NAD+ degrades quickly during sample processing, and extraction methods differ in how well they preserve the oxidized and reduced species separately. Differences in extraction and detection between laboratories are often larger than the biological effects reported, so quantification methods should be compared before the numbers are.