NAD+ Kit — Nicotinamide Adenine Dinucleotide | 1000mg

NAD+ (nicotinamide adenine dinucleotide) is a pyridine-nucleotide coenzyme found in every living cell: the electron carrier at the centre of glycolysis, the citric-acid cycle and oxidative phosphorylation, and the substrate that sirtuins, PARPs and CD38 consume. It is searched for as the "NAD+ peptide" or "NAD peptide" so often that the phrase has stuck, but strictly it is not a peptide — it is built from two nucleotides, not from amino acids. It is listed here because the laboratories that work with research peptides are the same ones that work with NAD+, and it is supplied the same way: pre-mixed, as a solution in a sealed 3 ml vial, research grade, HPLC-verified, with a batch Certificate of Analysis, from our UK facility. The NAD+ guide covers the naming question in full.

Research use only. The NAD+ kit is supplied strictly for in-vitro laboratory research. This page describes chemistry, format, quality and handling. It does not describe dosing, administration or use in humans or animals, and makes no therapeutic claims. It is not an infusion or injection product, and we do not supply NAD+ for that purpose.

The NAD+ kit at a glance

What NAD+ is, chemically

NAD+ is nicotinamide mononucleotide joined to adenosine monophosphate through a pyrophosphate bridge. Its chemistry runs on two separate tracks, and research on it splits the same way.

Redox. The nicotinamide ring accepts a hydride to give NADH and gives it back on oxidation. That single NAD+/NADH couple carries most of the electron flow from fuel oxidation into complex I of the respiratory chain, which is why metabolic work reports the free NAD+/NADH ratio rather than the absolute NAD+ concentration.

Consumption. Sirtuins, poly(ADP-ribose) polymerases and the CD38/CD157 ectoenzymes cleave the glycosidic bond and release nicotinamide, so in these reactions NAD+ is destroyed rather than recycled and has to be resynthesised. The NAMPT-dependent salvage pathway that rebuilds it from nicotinamide is rate-limiting in most cell types, and much of the current literature on NAD+ decline concerns the balance between that consumption and resynthesis.

NAD+ vs NMN vs NR

Three molecules are routinely confused in this space, and they are not interchangeable in an experiment.

Precursor studies exist largely because how extracellular NAD+ crosses an intact cell membrane is still an open research question, so cell-based work on NAD+ availability often supplies a precursor and measures the resulting NAD+ pool. Cell-free and enzyme work uses the coenzyme itself, which is what this kit supplies.

How NAD+ is used in the laboratory

• As the substrate or cofactor in enzymology — dehydrogenase assays, sirtuin and PARP activity assays, and NAD+/NADH cycling assays in which it is the reference standard.
• In redox and mitochondrial-function models, where the NAD+/NADH ratio is the readout for metabolic state.
• In studies of NAD+-dependent signalling — sirtuins in chromatin regulation, PARPs in DNA-repair signalling, and cyclic ADP-ribose-generating enzymes in calcium signalling.
• Alongside MOTS-c, because the AMPK energy-sensing pathway most examined in MOTS-c research and the NAD+/sirtuin axis are interconnected systems.

Experimental outcomes depend on intracellular NAD+/NADH ratios, compartmentalisation and the metabolic state of the model, which is why NAD+ is used as a reference compound rather than treated as a single-answer reagent. These are in-vitro observations only and are not established effects in humans or animals.

Stability: why NAD+ is less forgiving than a peptide

NAD+ does not behave like a peptide in solution, and the differences decide what you actually have on the bench.

• pH dominates. NAD+ is labile under alkaline conditions while NADH degrades under acid catalysis, so the two forms have opposite sensitivities and the practical optimum for a buffered solution sits near pH 8.5. A buffer chosen for a peptide protocol is not automatically right here, and Tris holds that window where phosphate does not. Our solution-stability guide uses NAD+ as the worked example.
• Time and temperature matter. Aqueous NAD+ loses activity measurably over time, faster when warm, and freeze–thaw cycling accelerates it — which is why the vial ships cold-chain, is stored at 2–8 °C and should be used within the window on its label rather than kept as shelf stock.
• Degradation is invisible. A degraded NAD+ solution usually looks unchanged, so the batch date on the certificate matters more than appearance.
• Light. Keep the vial in its box or otherwise protected from light.

Quality: HPLC purity and the Certificate of Analysis

Every NAD+ batch is verified by HPLC at 99%+ purity, and the certificate records the value measured for that batch. A batch-specific COA ships with every order, sample certificates are viewable in the COA library before you buy, and given the stability profile above the batch date on that certificate deserves more attention than it would for a lyophilised peptide.

Buying NAD+ in the UK: what to check

1. Content in milligrams, stated per vial or per kit, and the batch date.
2. A batch-specific Certificate of Analysis viewable before ordering, naming the method.
3. Format and handling. Most UK suppliers ship NAD+ as a lyophilised powder to reconstitute; ours is a pre-mixed solution, which removes the reconstitution step but needs cold-chain delivery, 2–8 °C storage, light protection, and a buffer plan if you will be diluting it.
4. What it is for. Research-grade NAD+ is a laboratory reagent. It is not the clinic-administered IV NAD+ that most of the results for "NAD injections" describe; a regulated clinical provider is the right source for that, and we do not supply it.
5. Legal status. NAD+ is lawful to buy and possess in the UK for laboratory research. It is not a licensed medicine, and every kit is supplied and labelled for in-vitro research use only.