Research Purposes Only

NAD+ 500mg (NAD) research compound vial — UK lab-tested, for research use only

Cellular & Metabolic Compounds

NAD+

500mg

C₂₁H₂₇N₇O₁₄P₂

Key Research Findings

  • Established role as an electron-carrier coenzyme in mitochondrial oxidative phosphorylation.
  • Published sirtuin-enzyme assay data on SIRT1–SIRT7 cofactor activity.
  • PARP-enzyme studies — characterisation as a required substrate in DNA-strand-break assays.

Overview

NAD+ is nicotinamide adenine dinucleotide, a redox coenzyme present in every living cell and one of the most studied molecules in biochemistry. It is not a peptide, and we group it under cellular and metabolic compounds for that reason. It cycles between an oxidised form, NAD+, and a reduced form, NADH, carrying electrons between the reactions of glycolysis, the citric acid cycle and oxidative phosphorylation. Beyond that classical role it is consumed as a substrate by three families of enzymes, which is what has driven the recent research interest. We supply it as a powder at 500mg per vial with an independent certificate of analysis.

Mechanism of Action

The distinction that matters for assay design is between NAD+ as a cofactor and NAD+ as a substrate. In redox reactions it is recycled and its total pool is unchanged. In contrast the sirtuins, the poly-ADP-ribose polymerases and CD38 cleave NAD+ and consume it, releasing nicotinamide, so their activity is directly limited by how much NAD+ is available. Imai and Guarente set out the sirtuin dependence [3], Canto and colleagues review the balance between the mitochondrial and nuclear pools [2], and Verdin covers the wider picture in ageing and metabolism [1]. NAD+ is hygroscopic and degrades in solution faster than most peptides, so it should be reconstituted immediately before use rather than stored dissolved. Not for human or veterinary use.

Research Effects

Electron-Transport Chemistry

Extensive Research

Characterised in classical biochemistry as an electron-carrier coenzyme in NADH-dependent reactions.

Sirtuin Enzyme Assays

Extensive Research

Reported in published enzyme assays as a co-substrate for the SIRT1–SIRT7 deacetylase family.

PARP Enzyme Assays

Extensive Research

Required substrate for poly(ADP-ribose) polymerase activity in DNA-strand-break repair assays.

References

  1. [1]Verdin E. NAD+ in aging, metabolism, and neurodegeneration. Science. 2015. PMID 26785480 · doi:10.1126/science.aac4854
  2. [2]Canto C, Menzies KJ, Auwerx J. NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus. Cell Metab. 2015. PMID 26118927 · doi:10.1016/j.cmet.2015.05.023
  3. [3]Imai S, Guarente L. NAD+ and sirtuins in aging and disease. Trends Cell Biol. 2014. PMID 24786309 · doi:10.1016/j.tcb.2014.04.002

Cited for the molecular pathways described above. Listing a study is not a claim about any outcome in humans.

Laboratory Research Only — All information on this page is provided for scientific research purposes only. This is a certified reference material sample sold and distributed for laboratory research only.

Quick Facts

Molecular FormulaC₂₁H₂₇N₇O₁₄P₂
Molecular Weight663.43 g/mol
CAS Number53-84-9
Half-LifeVariable by tissue (in-vitro pharmacokinetic data)
SolubilityWater (highly soluble)
Storage−20 °C, protect from light
More in Cellular & Metabolic Compounds

Research Status Key

Extensive Research
Moderate Research
Preliminary Research

Featured in Bundles

NAD+ is included in the following Zenterex research peptide bundles.

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