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Research use only

NAD+

β-Nicotinamide adenine dinucleotide

β-Nicotinamide adenine dinucleotide (NAD+), the oxidized form of the redox coenzyme and the substrate consumed by PARPs, sirtuins and CD38. Supplied in a sealed vial for enzymology and cell research.

$49.99

Per 5 mg vial · excl. VAT · volume pricing from 5 units

Ships within 24 hours

Cold-packed from Leiden, tracked across the EU and UK.

Documentation included

HPLC and mass-spec tested. Batch CoAs coming soon.

Lot traceable

Every vial maps to a signed batch release record.

Specification

Compound monograph — NAD+

NAD+ (β-nicotinamide adenine dinucleotide, oxidized form) is a dinucleotide coenzyme that carries electrons in glycolysis, the TCA cycle and mitochondrial respiration. Much NAD+ research studies it as a consumed substrate: ADP-ribosyltransferases such as PARP1, the sirtuin deacetylases and the NADase CD38 all break it down, and in some tissues its half-life is on the order of minutes. Researchers have also studied extracellular NAD+ release, degradation and uptake in rat brain and mouse hypothalamus. Research Market supplies NAD+ with lot data on the certificate of analysis. It is sold strictly for laboratory research use.

Chemical structure and identification

  • Molecular formula: C21H27N7O14P2
  • Molecular weight: 663.4 g/mol
  • CAS number: 53-84-9
  • PubChem CID: 5892
  • Synonyms: β-NAD+, nicotinamide adenine dinucleotide, NAD
  • Form: Supplied in a sealed research vial
  • Analytical methods: Identity and purity data reported on the batch certificate of analysis

Research applications

  • NAD+ turnover: A perspective on NAD(H) as a redox cofactor and as a substrate for non-oxidative reactions in signaling, post-translational modification and RNA capping, noting half-lives of minutes in some tissues [1]
  • PARP1 and sirtuins: Reviewed for how ARTD1 (PARP1) and the sirtuins share NAD+ as a substrate, and for PARP1 activation and energy depletion as a trigger of cell death after DNA damage [2]
  • Extracellular β-NAD+ and CD38: Rat forebrain synaptosomes released β-NAD+ on high-K+ stimulation by a vesicular mechanism, carried the NAD+-metabolizing protein CD38 on their membranes, degraded β-NAD+, and took up a fluorescent analog; local β-NAD+ triggered Ca2+ transients in cortical neurons [3]
  • Cellular uptake: Extracellular NAD was imported into N1 hypothalamic neuronal cells through a connexin 43-dependent, CD73-independent route, and blocking hypothalamic connexin 43 in mice prevented hypothalamic NAD uptake [4]

Reference citations

  1. Chini C.C.S. et al. (2021). Evolving concepts in NAD+ metabolism. Cell Metab, 33(6):1076–1087. PMID 33930322 · DOI
  2. Fouquerel E. et al. (2014). ARTD1 (PARP1) activation and NAD+ in DNA repair and cell death. DNA Repair (Amst), 23:27–32. PMID 25283336 · DOI
  3. Durnin L. et al. (2012). Release, neuronal effects and removal of extracellular β-nicotinamide adenine dinucleotide (β-NAD+) in the rat brain. Eur J Neurosci, 35(3):423–435. PMID 22276961 · DOI
  4. Roh E. et al. (2018). Exogenous nicotinamide adenine dinucleotide regulates energy metabolism via hypothalamic connexin 43. Metabolism, 88:51–60. PMID 30179604 · DOI

Compound data from PubChem CID 5892. Literature summaries describe published preclinical research and are not claims about this product’s effects in humans or animals.

Important regulatory notice

This product is supplied for laboratory research use only. It is not a medicinal product, is not intended for human or veterinary consumption, diagnostic use or any therapeutic application, and has not been evaluated or approved by the EMA, the FDA or any other regulatory authority. Purchase is restricted to qualified research professionals working in appropriately equipped facilities. The purchaser is responsible for ensuring compliance with all applicable national and institutional rules governing the acquisition, handling, storage and disposal of this material.

Research use only — not for human or veterinary consumption, and not a medicinal product.

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