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NAD+ in ageing research

Illustration of mitochondria and the NAD+ / NADH cycle

A literature summary. Summarises published literature for educational purposes.

What is NAD+?

Nicotinamide adenine dinucleotide (NAD) is a coenzyme found in all living cells. It exists in an oxidised form (NAD+) and a reduced form (NADH). NAD+ has two broad roles that are central to its place in ageing research [1,2]:

  1. Redox reactions. NAD+/NADH carries electrons in metabolic pathways, including glycolysis, the citric acid cycle and mitochondrial oxidative phosphorylation.
  2. Enzyme substrate. NAD+ is consumed as a substrate by several enzyme families, including the sirtuins (NAD+-dependent deacylases), poly(ADP-ribose) polymerases (PARPs), which are involved in DNA damage responses, and the NAD+-degrading enzyme CD38.
Property Detail
Full name Nicotinamide adenine dinucleotide (oxidised form)
Molecular formula C21H27N7O14P2
Molar mass approx. 663.4 g/mol
Form supplied Lyophilised powder (see product page and COA)

Reported age-related changes in NAD+

Several studies have reported lower NAD+ levels in older tissue samples or older animals:

  • Human tissue samples: in a study of pelvic skin samples from 49 donors aged from newborn to 77, NAD+ levels correlated negatively with age in both males and females. In males, PARP activity increased with age [3]. This was a cross-sectional study in a single tissue.
  • Mice: expression and activity of the NAD+-degrading enzyme CD38 were reported to increase with age, and mice lacking CD38 did not show the same age-related NAD+ decline in the tissues studied [4].
  • Mice: in ageing mouse muscle, lower NAD+ was linked to a disruption of communication between the nucleus and mitochondria involving SIRT1 and HIF-1α, which the authors described as a “pseudohypoxic” state [5].

Reviews of the field note that the size of the reported decline differs between tissues, species and measurement methods, and that measuring NAD+ accurately is technically demanding [2].

Research areas involving NAD+

Research area Why NAD+ is studied Key reference
Sirtuin biology Sirtuins require NAD+ as a co-substrate Verdin 2015 [1]
DNA damage and PARPs PARP activation consumes NAD+ Massudi 2012 [3]; Covarrubias 2021 [2]
NAD+ degradation (CD38) CD38 is a major NAD+-consuming enzyme in ageing tissues Camacho-Pereira 2016 [4]
Mitochondrial function NADH supplies electrons to the respiratory chain Gomes 2013 [5]
NAD+ biosynthesis Salvage, Preiss–Handler and de novo pathways Covarrubias 2021 [2]
Diagram of NAD+ synthesis and NAD+-consuming enzymes

Considerations for laboratory work

  • NAD+ is sensitive to heat, pH and light in solution. Literature methods typically specify fresh preparation and controlled storage.
  • Analytical methods reported for NAD+ quantification include enzymatic cycling assays and LC-MS. The choice of method affects the values reported [2].
  • Results from cell and animal models should be interpreted within the limits of those models.

Research material: NAD+

NAD+

Price: 100mg £14.99 · 500mg £44.99 · 1000mg £74.99

Certificate of Analysis: NAD+ 1000mg, report LDA22161142 (Lingda Laboratory, tested 3 September 2026, HPLC purity >99.77%). View certificates on our Verification page

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Longevity Research Digest

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Research use only. This article summarises published scientific literature for educational purposes. It does not describe the effects of any Corex Vitality™ product. NAD+ supplied by Corex Vitality™ is for laboratory research use only and is not intended for human or veterinary use, or for the diagnosis, treatment, prevention or cure of any disease or medical condition.

References

  1. Verdin E. NAD+ in aging, metabolism, and neurodegeneration. Science. 2015;350(6265):1208-1213. PubMed: https://pubmed.ncbi.nlm.nih.gov/26785480/ · DOI: https://doi.org/10.1126/science.aac4854
  2. Covarrubias AJ, Perrone R, Grozio A, Verdin E. NAD+ metabolism and its roles in cellular processes during ageing. Nat Rev Mol Cell Biol. 2021;22(2):119-141. PubMed: https://pubmed.ncbi.nlm.nih.gov/33353981/ · DOI: https://doi.org/10.1038/s41580-020-00313-x
  3. Massudi H, Grant R, Braidy N, Guest J, Farnsworth B, Guillemin GJ. Age-associated changes in oxidative stress and NAD+ metabolism in human tissue. PLoS One. 2012;7(7):e42357. PubMed: https://pubmed.ncbi.nlm.nih.gov/22848760/ · DOI: https://doi.org/10.1371/journal.pone.0042357
  4. Camacho-Pereira J, Tarragó MG, Chini CCS, et al. CD38 dictates age-related NAD decline and mitochondrial dysfunction through an SIRT3-dependent mechanism. Cell Metab. 2016;23(6):1127-1139. PubMed: https://pubmed.ncbi.nlm.nih.gov/27304511/ · DOI: https://doi.org/10.1016/j.cmet.2016.05.006
  5. Gomes AP, Price NL, Ling AJY, et al. Declining NAD+ induces a pseudohypoxic state disrupting nuclear-mitochondrial communication during aging. Cell. 2013;155(7):1624-1638. PubMed: https://pubmed.ncbi.nlm.nih.gov/24360282/ · DOI: https://doi.org/10.1016/j.cell.2013.11.037

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📚 Peer-Reviewed Literature · PubMed Indexed

Published Research — NAD+ (Nicotinamide Adenine Dinucleotide)

NCBI PubMed Database ↗ Verify Batch COAs →
  1. [1] Ramsey KM et al. · Science (2009)

    Molecular and murine biochemical study demonstrating that nicotinamide phosphoribosyltransferase (NAMPT) and intracellular NAD+ levels oscillate under CLOCK:BMAL1 transcriptional control to regulate SIRT1 deacetylase activity.

    PMID: 19299583 ↗ DOI: 10.1126/science.1171641 ↗
  2. [2] Gomes AP et al. · Cell (2013)

    Cellular and murine bioenergetics study showing that nuclear NAD+ depletion reduces SIRT1 activity and stabilises HIF-1α under normoxic conditions, downregulating mitochondrially encoded oxidative phosphorylation (OXPHOS) subunits.

    PMID: 24360282 ↗ DOI: 10.1016/j.cell.2013.11.037 ↗
  3. [3] Cantó C et al. · Cell Metab (2015)

    Mechanistic review of subcellular NAD+ compartmentalisation, salvage-pathway enzymatic synthesis, sirtuin and PARP cosubstrate consumption, and the mitochondrial unfolded protein response (UPRmt).

    PMID: 26118927 ↗ DOI: 10.1016/j.cmet.2015.05.023 ↗
  4. [4] Camacho-Pereira J et al. · Cell Metab (2016)

    Enzymatic and knockout-mouse study identifying the ectoenzyme NADase CD38 as a primary regulator of cellular NAD+ degradation, mitochondrial oxygen consumption, and SIRT3-dependent protein deacetylation.

    PMID: 27304511 ↗ DOI: 10.1016/j.cmet.2016.05.006 ↗

References are provided for scientific context only. All Corex Vitality™ compounds are supplied strictly for in-vitro laboratory research use (RUO).