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· 8 min read
NAD+ is not a peptide. That observation is less obvious than it sounds, given that it sits in a research-reagent catalogue alongside peptide molecules, but the distinction matters at the bench: NAD+ (nicotinamide adenine dinucleotide, PubChem CID 5892) is a small-molecule dinucleotide coenzyme with a molecular weight of 663.43 g/mol and no amino-acid backbone in sight. It carries two mechanistic roles in the published biochemistry - electron carrier and consumed co-substrate - and a research literature with enough depth to fill several Cell papers. Everything on this page describes what published studies have investigated, not any human use. Kovalabs supplies NAD+ strictly as a research reagent; see the NAD+ product listing in the cellular research category for supply details.
| Compound | Nicotinamide adenine dinucleotide (NAD+, oxidised form) |
|---|---|
| Synonyms | NAD+, nadide, coenzyme I, diphosphopyridine nucleotide (DPN) |
| Class / mechanism | Small-molecule dinucleotide coenzyme; redox cofactor and substrate for NAD+-consuming enzymes (not a peptide) |
| Molecular formula | C21H27N7O14P2 |
| Molecular weight | 663.43 g/mol |
| CAS number | 53-84-9 |
| PubChem CID | 5892 |
| InChIKey | BAWFJGJZGIEFAR-NNYOXOHSSA-N |
| Supply status | Research use only; not for human or veterinary use |
The structure is worth spending a moment on, because getting the identity right requires navigating a small PubChem ambiguity. NAD+ is built from two nucleotides joined at their phosphate groups: an adenosine 5'-monophosphate moiety connected through a pyrophosphate (diphosphate) bridge to nicotinamide mononucleotide. The canonical record resolves to PubChem CID 5892, CAS 53-84-9, molecular formula C21H27N7O14P2, molecular weight 663.43 g/mol, and InChIKey BAWFJGJZGIEFAR-NNYOXOHSSA-N. The IUPAC name contains a 3-carbamoylpyridin-1-ium fragment, confirming the positively charged (oxidised) nicotinamide ring of NAD+ rather than the reduced coenzyme NADH - a distinction that matters immediately at the assay level.
Here is the database wrinkle worth knowing: PubChem also hosts CID 925 (beta-NAD), a stereo/charge variant of the same molecule. Search for 'NAD' and CID 925 will surface alongside CID 5892. The identifiers above - and the figures in the key facts table - derive from the canonical name-resolved parent record CID 5892. Using CID 925 in a citation is not wrong, but it is a different record; verify which one the source was using before cross-referencing. The lot-specific certificate of analysis is the definitive identity and purity reference for the supplied material.
NAD+ participates in cell biochemistry in two mechanistically distinct ways, and conflating them is a surprisingly common shortcut in lay coverage. A narrative review by Braidy et al. (Antioxid Redox Signal, 2018; PMID 29634344) maps both roles alongside the kynurenine de novo and salvage biosynthetic pathways that replenish the intracellular pool.
The first role is redox. NAD+ is the oxidised member of the NAD+/NADH couple; it accepts a hydride to become NADH, acting as an electron-carrying cofactor for oxidoreductase (dehydrogenase) enzymes across glycolysis and oxidative phosphorylation. In this capacity it is regenerated rather than consumed - the same NAD+ molecule cycles between oxidised and reduced forms. This is molecular and biochemical context only; no physiological effect in any organism is asserted.
The second role is distinct: NAD+ is a consumed co-substrate for three classes of NAD+-cleaving enzymes. The sirtuin (SIRT) NAD+-dependent deacylases, the poly(ADP-ribose) polymerases (PARPs), and the NAD+ glycohydrolase CD38 all hydrolyse the nicotinamide-ribosyl bond to transfer or release ADP-ribose. Because these enzymes use NAD+ up rather than recycle it, the intracellular pool is permanently diminished by each catalytic cycle. A review by Colombo et al. (Front Pharmacol, 2021; PMID 34880756) frames this substrate relationship and surveys NAMPT as the rate-limiting salvage enzyme that sustains the pool. Both citations are narrative reviews of enzyme biochemistry; no human-outcome endpoint is asserted.
| Property | NAD+ (oxidised) | NADH (reduced) |
|---|---|---|
| Redox role in the couple | Electron / hydride acceptor | Electron / hydride donor |
| Charge on nicotinamide ring | Quaternary 3-carbamoylpyridin-1-ium cation | Neutral, reduced dihydropyridine ring |
| PubChem CID (oxidised parent record) | 5892 | - |
| Characteristic UV absorbance | ~260 nm (adenine) only | ~260 nm (adenine) and ~340 nm |
| Typical assay use | Substrate fed into dehydrogenase reactions | Product followed at ~340 nm in dehydrogenase assays |
One structural point to flag before reading the trial literature: the published clinical studies investigated NAD+ precursors - chiefly nicotinamide riboside - not NAD+ itself. NAD+ remains the molecular subject of the pathway under study; the trials are cited here only to document study design and the names of pre-specified endpoints. No result, effect or benefit is described, and none of the trials is cited as evidence for any human-use recommendation.
NAD+ is supplied as the free acid or sodium/hydrate salt - a white to off-white, hygroscopic crystalline powder (CAS 53-84-9; C21H27N7O14P2; 663.43 g/mol). Two physical properties combine to make it somewhat demanding to handle: it is hygroscopic and its aqueous solutions are chemically unstable, degrading under alkaline conditions, on warming and on freeze-thaw cycling.
At the bench, working solutions are generally prepared fresh in cold buffer and kept on ice. Aqueous solutions are most stable near neutral to mildly acidic pH. The solid is stored desiccated and protected from light, with long-term storage at -20 C or below; aliquoting minimises repeated freeze-thaw, which is the practical failure mode most often cited in handling notes. The lot-specific certificate of analysis and SDS specify the supplied form and any lot-specific handling requirements - consult those rather than assuming a standard procedure applies.
One assay-specific note: when following dehydrogenase reactions, distinguish the redox states before choosing a wavelength. Only NADH shows the characteristic ~340 nm absorbance used to track many coupled assays; both NAD+ and NADH share the ~260 nm adenine absorbance. Using the wrong wavelength for identity verification gives a misleading result. Handle with standard laboratory PPE (gloves, eye protection) in a controlled laboratory setting.
These are physicochemical handling notes only, not preparation guidance for any use in humans or animals. General bench technique is covered in the reconstitution guide, and lot documentation in the certificates of analysis.
NAD+ itself is the most certain thing on this page: a well-characterised endogenous coenzyme with an unambiguous structure (PubChem CID 5892, CAS 53-84-9, 663.43 g/mol), present in every living cell, with two textbook roles - redox cofactor in the NAD+/NADH couple and consumed co-substrate for sirtuins, PARPs and CD38. Those enzyme and pathway roles are mapped, but mostly in narrative reviews of cell and enzyme biochemistry, which describe the molecule in systems, not in people. The human level carries a specific catch worth naming: the trials cited here studied oral precursors such as nicotinamide riboside rather than NAD+ itself, and they are cited for design and endpoint names only, with no result reported. It is not a licensed medicine, and it has not been shown to produce defined outcomes in humans.
Kovalabs supplies NAD+ for laboratory and in-vitro research use only. It is not a medicine, supplement or food, and it is not for human or veterinary use, ingestion or administration. Nothing on this page describes a clinical effect, benefit or outcome. The precursor trials referenced above are cited solely for their study design and endpoint names, not as evidence of any effect. Purchasers are responsible for handling, storing and using the reagent in accordance with all applicable laws and institutional safety requirements. See the research disclaimer for the full terms.
NAD+ (nicotinamide adenine dinucleotide) is a small-molecule dinucleotide coenzyme: an adenine nucleotide joined to a nicotinamide nucleotide through a pyrophosphate bridge. It is not a peptide and contains no amino-acid backbone. It carries PubChem CID 5892, CAS 53-84-9, formula C21H27N7O14P2 and a molecular weight of 663.43 g/mol.
They are the two members of one redox couple. NAD+ is the oxidised form, carrying a positively charged 3-carbamoylpyridin-1-ium nicotinamide ring; it accepts a hydride to become NADH, the reduced form. In assays, only NADH shows the characteristic ~340 nm absorbance, while both share the ~260 nm adenine absorbance.
The canonical oxidised-form record is PubChem CID 5892, CAS 53-84-9, molecular formula C21H27N7O14P2, molecular weight 663.43 g/mol, and InChIKey BAWFJGJZGIEFAR-NNYOXOHSSA-N. A separate PubChem record, CID 925 (beta-NAD), exists as a variant; the figures here are from CID 5892.
The cited randomised, placebo-controlled trials studied oral NAD+ precursors (nicotinamide riboside), not NAD+ itself in humans. Their pre-specified endpoints, named here only, included whole-blood NAD+ concentration, the NAD+ metabolome, tolerability and safety, and further measures listed by measurement method only. No result, effect or benefit is described, and these are cited only to evidence study design.
No. Kovalabs supplies NAD+ strictly for laboratory and in-vitro research use only. It is not a medicine, supplement or food, and it is not for human or veterinary use, ingestion or administration.
As bench handling of a research reagent only: the hygroscopic, oxidation-sensitive powder is generally stored desiccated, protected from light, at -20 C or below, and aliquoted to limit freeze-thaw. Aqueous solutions are unstable and most stable near neutral to mildly acidic pH, so working solutions are usually prepared fresh in cold buffer and kept on ice. Always follow the lot-specific certificate of analysis and SDS. See the reconstitution guide for general bench technique.