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Molecular Weight
Purity
Storage
Appearance
Solubility
01
NAD⁺ (β-nicotinamide adenine dinucleotide, oxidised form) is a coenzyme found in all living cells. It is not a peptide: it is made of two nucleotides, one containing adenine and one containing nicotinamide, joined through a pyrophosphate bridge.
NAD⁺ accepts electrons in redox reactions, becoming NADH, and is also consumed as a substrate by enzymes such as sirtuins, PARPs and CD38. These roles make it a standard reagent in enzyme assays and a central analyte in research on cellular metabolism. It is supplied as a solid reference compound for in vitro and analytical use only.
02
NAD⁺ is a small organic molecule with two distinct halves.
Adenosine half
Adenosine 5′-monophosphate provides the adenine ring, which gives NAD⁺ its strong absorbance at 260 nm.
Nicotinamide half
Nicotinamide riboside 5′-phosphate carries the nicotinamide ring, the site where a hydride is added during reduction to NADH.
Pyrophosphate bridge
The two nucleotides are linked through their 5′ phosphates.
Charge
The nicotinamide ring carries a positive charge in NAD⁺, while the pyrophosphate carries two negative charges, so the net charge is about −1 at neutral pH. The molecule is very polar and freely water-soluble.
NAD⁺ versus NADH
Reduction converts the aromatic nicotinamide ring into a dihydropyridine, which adds a new absorbance band at 340 nm and a weak fluorescence.
03
NAD⁺ has two broad roles studied in vitro.
Redox coenzyme
Dehydrogenases transfer a hydride to NAD⁺, forming NADH. Enzymatic cycling assays use this reaction to amplify signals and measure metabolites at low concentrations.
Consumed substrate
Sirtuins (deacylases), poly(ADP-ribose) polymerases and CD38-type enzymes break the nicotinamide–ribose bond of NAD⁺, releasing nicotinamide and using the ADP-ribose portion. NAD⁺ availability therefore affects these signalling and DNA-repair enzymes.
NAD⁺ metabolism
Research on cellular NAD⁺ levels covers the salvage pathway from nicotinamide and the enzymes, such as NNMT, that divert nicotinamide away from it.
These are research contexts only; no effects are claimed for this material.
04
Dehydrogenase assays
The electron acceptor in spectrophotometric assays, where NADH formation is followed at 340 nm (ε ≈ 6,220 M⁻¹ cm⁻¹).
Enzymatic cycling
A reagent in cycling assays that amplify signals for sensitive metabolite measurement.
Sirtuin and PARP assays
A substrate for measuring NAD⁺-consuming enzyme activity.
Metabolome calibration
An external standard for LC and LC-MS methods covering NAD⁺, NADH, nicotinamide, NMN and ADP-ribose.
05
Storage
Store the solid at −20 °C, sealed, desiccated and protected from light. It is hygroscopic; let the container reach room temperature before opening.
pH stability
NAD⁺ is relatively stable in neutral to mildly acidic solution but is rapidly destroyed in alkaline solution, which cleaves the nicotinamide–ribose bond. NADH behaves in the opposite way: it is stable in alkali and destroyed by acid. Prepare NAD⁺ solutions in neutral or slightly acidic buffer.
Reconstitution
Dissolve in cold water or a near-neutral buffer. Solutions are clear and colourless to faintly yellow.
Solutions
Use within hours, or freeze single-use aliquots; avoid repeated freeze–thaw cycles.
Handling
Handle as a laboratory chemical with standard personal protective equipment.
06
NAD⁺ needs nucleotide-style analytical methods rather than peptide methods.
UV detection
Absorbance maximum at 260 nm (ε ≈ 18,000 M⁻¹ cm⁻¹) from the adenine ring. NADH shows an additional band at 340 nm, which NAD⁺ lacks.
HPLC
Its high polarity and charge give poor retention and tailing on plain C18. Ion-pairing reversed-phase methods (for example with tetrabutylammonium or dibutylamine salts), HILIC or mixed-mode anion-exchange columns give good separation from related nucleotides.
Mass spectrometry
Positive-mode ESI gives [M+H]⁺ at m/z 664.1 and [M+Na]⁺ at m/z 686.1 (monoisotopic). Fragments include loss of nicotinamide (m/z 542.1), an ADP-related ion near m/z 428.0, protonated nicotinamide (m/z 123.1) and adenine (m/z 136.1). Negative mode also works well.
Degradation products
The main products are nicotinamide and ADP-ribose, from cleavage of the nicotinamide–ribose bond; pyrophosphate cleavage gives NMN and AMP. Purity methods should resolve all of these, plus NADH.
07
No. It is a dinucleotide coenzyme made of two nucleotides joined by a pyrophosphate bridge. It is included as a reference compound for cellular metabolism research.
By UV: both absorb at 260 nm, but only NADH has a band at 340 nm (and weak fluorescence). They also separate by HPLC, and their different pH stability (NAD⁺ survives mild acid, NADH survives alkali) is used to measure them separately.
It is very polar and charged, so it is barely retained and tails on standard C18. Ion-pairing agents, HILIC or mixed-mode columns provide adequate retention and peak shape.
Mainly nicotinamide and ADP-ribose, from cleavage of the nicotinamide–ribose bond, which is fastest in alkaline solution. Cleavage of the pyrophosphate gives NMN and AMP.
Chromatographic (HPLC) purity shows what proportion of UV-absorbing material is NAD⁺. Enzymatic purity shows how much is actually reducible to NADH by a dehydrogenase, for example alcohol dehydrogenase with ethanol. The two can differ if inactive isomers or salts are present, so both together give the best picture of usable NAD⁺ content.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
NAD+ Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/cellular-research-peptides/nad/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
