NAD+ 1000mg

What is NAD+ ?

NAD+ (nicotinamide adenine dinucleotide, also written NAD plus) is the oxidised form of the cell's main redox cofactor. It is a dinucleotide, not a peptide. We supply it as lyophilised powder in 500mg and 1000mg vials.

The formula is C₂₁H₂₇N₇O₁₄P₂, the molecular weight 663.43 g/mol and the CAS number 53-84-9. Nicotinamide mononucleotide is joined to adenosine monophosphate through a pyrophosphate bridge. Redox chemistry happens on the nicotinamide ring, which accepts a hydride to give NADH.

Signalling enzymes such as sirtuins and PARPs consume NAD+ as a substrate (Liu et al., Cell Metab, 2018). Cells rebuild it through salvage pathways from nicotinamide, nicotinic acid or nicotinamide riboside. NAMPT catalyses the first step from nicotinamide (Grozio et al., J Biol Chem, 2013).

NAD+ Research Applications

• Signalling : NAD+ activates sirtuins and supports mitochondrial function, including through the mitochondrial unfolded protein response (Cantó, Menzies and Auwerx, Cell Metab, 2015).
• Turnover : isotope tracing in cell lines showed NAD made from nicotinamide and consumed largely by PARPs and sirtuins (Liu et al., 2018).
• CD38 : Camacho-Pereira and colleagues (Cell Metab, 2016) identified CD38 as the main enzyme degrading the precursor NMN in vivo.

Typical in-vitro uses are dehydrogenase assays read at 340 nm, sirtuin, PARP and CD38 activity assays, and NAD+/NADH ratio measurements in bioenergetics work.

NAD+ vs NMN vs NR (Nicotinamide Riboside)

NAD+ is the finished dinucleotide. NMN (nicotinamide mononucleotide) and NR (nicotinamide riboside) are precursors upstream of it in the salvage pathways. At the cell surface, CD38 converts NMN to nicotinamide and CD73 converts it to NR. In human cells, CD73 enabled extracellular NMN to feed NAD+ synthesis inside the cell, and CD38 impaired it (Grozio et al., 2013). For cell-free and enzyme work, NAD+ is the cofactor added directly.

Research Overview

NAD+ (nicotinamide adenine dinucleotide, oxidised form, often written NAD plus where the charge symbol cannot be rendered) has the molecular formula C₂₁H₂₇N₇O₁₄P₂, a molecular weight of 663.43 g/mol, and CAS number 53-84-9. Structurally it is nicotinamide mononucleotide joined to adenosine monophosphate through a pyrophosphate bridge, and its redox chemistry is confined to the nicotinamide ring: reduction is a stereospecific two-electron hydride transfer to C4 giving NADH, with a standard reduction potential near -0.32 V at pH 7. That single couple carries the bulk of catabolic electron flow into complex I of the respiratory chain, which is why bioenergetics research reports the free NAD+/NADH ratio rather than absolute NAD+ concentration. The second half of nicotinamide adenine dinucleotide biology is non-redox and consumptive. Sirtuins, poly(ADP-ribose) polymerases and the CD38/CD157 ectoenzymes cleave the glycosidic bond between the nicotinamide and the ADP-ribosyl moiety, releasing nicotinamide stoichiometrically, so NAD+ is destroyed rather than recycled and must be resynthesised through the NAMPT-limited salvage pathway (Cantó, Menzies and Auwerx, Cell Metabolism, 2015). Camacho-Pereira and colleagues (Cell Metabolism, 2016) reported that CD38 expression and NADase activity rise with age in mice and drive tissue NAD+ decline alongside SIRT3-dependent mitochondrial dysfunction, while Liu and colleagues (Cell Metabolism, 2018) applied stable-isotope tracing to quantify NAD synthesis and breakdown fluxes directly and map tissue-specific turnover rather than inferring it from pool sizes. One mechanistic point matters to anyone designing experiments: intact NAD+ is not efficiently transported across the mammalian plasma membrane. Extracellular NAD+ is processed by surface ectoenzymes instead, with CD73 shown to generate nicotinamide riboside that is subsequently taken up (Grozio et al., Journal of Biological Chemistry, 2013). Laboratories buying NAD+ in the UK typically use it as a defined cofactor in oxidoreductase assays and in sirtuin, PARP and mitochondrial bioenergetics work.

Storage and Reconstitution

Store NAD+ powder at -20°C, away from light and moisture, for up to 24 months. After reconstitution, keep the solution at 2-8°C and use it within 4 weeks. For longer storage, freeze single-use aliquots at -20°C and avoid repeated freeze-thaw cycles.

Vials are sold on their own, without bacteriostatic water for mixing or other supplies.

How to reconstitute and handle

Let the vial and the bacteriostatic water reach room temperature and swab both stoppers with alcohol. Add the water slowly down the inside wall of the vial and swirl gently until dissolved. Do not shake. Avoid alkaline buffers: NAD+ is fairly stable in acid but hydrolyses in base, at both the nicotinamide-ribose bond and the pyrophosphate link.

• NAD+ is comparatively stable in acidic solution and labile in alkaline solution, where both the nicotinamide-ribose glycosidic bond and the pyrophosphate linkage are susceptible to hydrolysis. NADH shows the opposite pH profile, so keep reconstituted NAD+ cold and avoid basic buffers.
• Oxidised NAD+ absorbs at 260 nm, and reduction to NADH adds the characteristic 340 nm band that is the standard spectrophotometric check on redox state and integrity. Prepare single-use aliquots and avoid repeated freeze-thaw cycles.

For the full method, see the peptide reconstitution guide and the reconstitution calculator.

Research References

• NAD+ Metabolism and the Control of Energy Homeostasis (Cantó et al., Cell Metab, 2015)
• CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction (Camacho-Pereira et al., Cell Metab, 2016)
• Quantitative Analysis of NAD Synthesis-Breakdown Fluxes (Liu et al., Cell Metab, 2018)
• CD73 as a source of extracellular precursors for NAD+ biosynthesis (Grozio et al., J Biol Chem, 2013)

Published research on NAD+ is indexed on PubMed. See our full UK buyer's guide for NAD+ 1000mg.