---
title: "NAD+ research summary and literature | Sable Peptides"
description: "NAD+: what the published literature covers, how it compares with MOTS-c, key facts (CAS 53-84-9, MW 663.4) and 4 verified PubMed citations."
canonical: https://www.sablepeptides.co.uk/research/nad
dateModified: 2026-10-14
publisher: Sable Peptides Limited (UK company 17488610)
note: Research use only. Not for human or veterinary use.
---

[Research summaries](/research)

# NAD+: research summary

For laboratory research use only. Not for human or veterinary use. This page summarises published literature. It gives no advice on use.

## What the literature covers

NAD+ (nicotinamide adenine dinucleotide, oxidised form) is not a peptide. It is a dinucleotide coenzyme that carries electrons in redox reactions and is consumed as a substrate by sirtuins and PARP enzymes.

Classic biochemistry measured the free NAD+/NADH redox state in the cytoplasm and mitochondria. Later work linked NAD+ availability to SIRT1 deacetylase activity and to AMPK signalling. NAD+ is a standard reagent in enzymology and metabolism research.

Its molecular weight is about 663.4 g/mol (C21H27N7O14P2). It is hygroscopic and light-sensitive, so keep it sealed and protected from moisture.

## Key facts

|  | NAD+ | MOTS-c |
| --- | --- | --- |
| CAS | 53-84-9 | 1627580-64-6 |
| Formula | C21H27N7O14P2 | C101H152N28O22S2 |
| Molecular weight (g/mol) | 663.4 | 2174.6 |

Source: [PubChem CID 5892](https://pubchem.ncbi.nlm.nih.gov/compound/5892).

## NAD+ compared with MOTS-c

NAD+ is often listed next to peptides, but it is a small-molecule coenzyme, whereas MOTS-c is a 16-residue peptide. Both appear in metabolism and mitochondrial research, but the experiments differ: NAD+ is used as an enzyme substrate and cofactor, while MOTS-c is studied as a signalling peptide.

[Full side-by-side: NAD+ vs MOTS-c](/versus/mots-c/nad-plus) · [MOTS-c research summary](/research/mots-c)

## Frequently asked questions

Is NAD+ a peptide?

No. It is a dinucleotide coenzyme made of two nucleotides joined through their phosphate groups.

Which enzymes use NAD+?

Dehydrogenases use it as an electron carrier. Sirtuins (such as SIRT1) and PARPs consume it as a substrate.

How should NAD+ be stored?

Sealed, dry, cold and out of light. It absorbs moisture readily.

## Published literature cited

1.  Cantó C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, Milne JC, Elliott PJ, Puigserver P, Auwerx J. (2009). AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. *Nature*. [PMID 19262508](https://pubmed.ncbi.nlm.nih.gov/19262508/) · [doi:10.1038/nature07813](https://doi.org/10.1038/nature07813)
2.  Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, Pandita TK, Guarente L, Weinberg RA. (2001). hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. *Cell*. [PMID 11672523](https://pubmed.ncbi.nlm.nih.gov/11672523/) · [doi:10.1016/s0092-8674(01)00527-x](https://doi.org/10.1016/s0092-8674\(01\)00527-x)
3.  Williamson DH, Lund P, Krebs HA. (1967). The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. *Biochem J*. [PMID 4291787](https://pubmed.ncbi.nlm.nih.gov/4291787/) · [doi:10.1042/bj1030514](https://doi.org/10.1042/bj1030514)
4.  Cantó C, Menzies KJ, Auwerx J. (2015). NAD(+) Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus. *Cell Metab*. [PMID 26118927](https://pubmed.ncbi.nlm.nih.gov/26118927/) · [doi:10.1016/j.cmet.2015.05.023](https://doi.org/10.1016/j.cmet.2015.05.023)

Every citation was looked up by PMID in Europe PMC (MEDLINE) on 2026-10-14 and its title matched. Citation means the paper exists and is relevant to the compound. It does not mean the paper supports any use.

## On this site

-   [NAD+ vials, sizes and prices](/nad-plus-uk)
-   [NAD+ reference record](/ref/nad)
-   [NAD+ UK price check](/uk-price-check/nad)
-   [Certificates of Analysis](/coa)

NAD+ (nicotinamide adenine dinucleotide, oxidised form) is not a peptide. It is a dinucleotide coenzyme that carries electrons in redox reactions and is consumed as a substrate by sirtuins and PARP enzymes. This page summarises 4 verified PubMed papers and compares NAD+ with MOTS-c. Research use only; no human-use guidance is given.

Updated 2026-10-14