Compound identity
- Designation
- NAD+ (β-nicotinamide adenine dinucleotide, oxidized)
- Class
- Dinucleotide coenzyme (non-peptide)
- Composition
- Nicotinamide mononucleotide joined to adenosine monophosphate by a pyrophosphate bridge
- Molecular formula
- C21H27N7O14P2
- Molecular weight
- approx. 663.4 g/mol (free acid)
- CAS number
- 53-84-9
Nomenclature and identity
NAD+ is the oxidized member of the NAD+/NADH redox couple. In biochemical literature it is studied both as a hydride carrier in central metabolism and as a consumed substrate for enzyme families including sirtuins, poly(ADP-ribose) polymerases (PARPs), and CD38/CD157 glycohydrolases.
Research material is typically a white to off-white solid that may be supplied as the free acid or as a salt. The phosphorylated form NADP+ and the reduced forms NADH and NADPH are distinct compounds with different identifiers.
What the published literature examines
A 2016 review in Biochimica et Biophysica Acta (Yang et al.) covers NAD+ metabolism across bioenergetics, signaling, and approaches researchers have used to modulate NAD+ levels in experimental systems. A 2024 review in Nature Reviews Molecular Cell Biology (Migaud et al.) examines how NAD+ synthesis, consumption, and compartmentalization are regulated, and the technical and biological challenges in targeting NAD+ metabolism experimentally.
Both reviews emphasize that NAD+ pools differ between cellular compartments and that measuring and interpreting NAD+ changes requires careful methodology.
Analytical and research considerations
NAD+ is susceptible to hydrolysis, particularly under alkaline conditions and elevated temperature, giving degradation products such as nicotinamide and ADP-ribose. NADH, by contrast, is more labile under acidic conditions. Purity is commonly assessed by HPLC with UV detection at 260 nm, and identity by mass spectrometry or enzymatic assay.
Enzymatic cycling assays and LC-MS methods used in published work distinguish NAD+ from NADH. Buffer choice and sample handling time affect measured ratios.
What a Certificate of Analysis can and cannot establish
A lot COA can
- Confirm that the tested lot matches the expected identity by an orthogonal method such as mass spectrometry.
- Report chromatographic purity (typically HPLC area percent) for that specific lot at the stated test date.
- Tie results to a lot or batch number that can be matched against the vial label.
A lot COA cannot
- Describe any lot other than the one tested, or material after the stated test date.
- Establish biological activity, safety, or suitability for any experimental model.
- Substitute for a researcher's own incoming-material verification where a study design requires it.
Current report status for every catalog item is listed in the Certificate of Analysis library. See also how to read a peptide COA.
Selected independent literature
- NAD(+) metabolism: Bioenergetics, signaling and manipulation for therapy.Yang Y et al. Biochim Biophys Acta, 2016. PubMed ID 27374990.Review of NAD+ metabolism, bioenergetics, signaling, and experimental modulation.
- Regulation of and challenges in targeting NAD(+) metabolism.Migaud ME et al. Nat Rev Mol Cell Biol, 2024. PubMed ID 39026037.Review of NAD+ regulation, compartmentalization, and experimental challenges.
Literature is cited for scientific context only. Neon Valley Research did not author these publications, and their findings are not claims about any product.
NAD+ Buffered 500 MG
Nicotinamide Adenine Dinucleotide (oxidized), non-peptide coenzyme. Supplied as 500 mg / vial.
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Related research references
- MOTS-c research referenceA 16-amino-acid peptide encoded within the mitochondrial 12S rRNA gene.
- GHK-Cu research referenceThe copper(II) complex of the tripeptide glycyl-L-histidyl-L-lysine.
RESEARCH USE ONLY – NOT FOR HUMAN OR ANIMAL USE. This reference is provided for laboratory and analytical research context only. It is not guidance for any human or animal use.