Buy NAD+ 2026 — Redox Cofactor for Sirtuin, PARP, and Mitochondrial Research (EU)
NAD+ at a glance
| Designation | NAD+ (β-nicotinamide adenine dinucleotide, free acid) |
|---|---|
| Identity | Dinucleotide coenzyme, No peptide – no amino acid sequence |
| Molecular formula | C₂₁H₂₇N₇O₁₄P₂ |
| Molar mass | approx. 663.43 g/mol (free acid) |
| Synonyms | β-NAD, NAD⁺, Coenzyme I, Diphosphopyridine Nucleotide (DPN), Cozymase |
| Class | Pyridine dinucleotide coenzyme, redox cofactor NAD⁺/NADH |
| Research context | Redox biochemistry, energy metabolism, mitochondrial research, NAD-consuming enzymes (Sirtuins, PARPs, CD38) |
| CAS number | 53-84-9 (free acid; salt forms have different CAS numbers – the batch-specific COA is authoritative) |
| Form | Lyophilised powder (freeze-dried), sealed vial |
| Amount | 500 mg per vial |
| Purity | ≥99% (HPLC), identity confirmed by LC-MS |
| Analysis | External third-party laboratory, batch-specific COA |
| Intended use | For Research Use Only (RUO) |
| Price | €79.90 · Shipping from Germany |
What is NAD+?
NAD+ stands for nicotinamide adenine dinucleotide in its oxidised form and is among the longest-known coenzymes in biochemistry. At the beginning of the 20th century, a heat-stable component required for fermentation was described in yeast extracts – later identified as "cozymase" or coenzyme I.
Important for positioning within the product range: NAD+ is No peptide. It is not composed of amino acids and has no sequence, but is a dinucleotide. Therefore, different analytical and storage considerations apply compared to the peptides in the catalogue.
Molecular profile & target structure
The free acid has the molecular formula C₂₁H₂₇N₇O₁₄P₂ with a molar mass of approximately 663.43 g/mol. The molecule consists of a nicotinamide ribonucleotide and an adenosine monophosphate, linked by a diphosphate bridge.
Chemically, the pyridine ring is crucial: it accepts a hydride ion at position C4, converting into the reduced form NADH. This reversible two-electron transfer makes NAD⁺/NADH a textbook example of a redox cofactor. Furthermore, it is characteristic that NADH absorbs at approximately 340 nm, whereas NAD⁺ does not – this is the basis for many photometric enzyme assays.
In addition, the literature describes enzymes that do not use NAD⁺ as a redox partner but consume it as a substrate: sirtuins, poly(ADP-ribose) polymerases (PARPs), and the NAD glycohydrolase CD38.
What in-vitro and animal model studies document
The following summary reflects only what is described in the publicly accessible preclinical literature – it is not a statement about an effect or suitability in humans.
- Redox Metabolism Academic literature and in-vitro studies describe NAD⁺ as a cofactor for numerous dehydrogenases in glycolysis, the citric acid cycle, and β-oxidation; NADH is investigated in the context of the respiratory chain.
- Sirtuins Published in vitro and animal model studies investigate the NAD⁺ dependence of sirtuins in relation to protein deacetylation.
- PARPs: Several studies document observations of NAD⁺ consumption by PARP enzymes following DNA damage in cell models.
- CD38 Preclinical work describes CD38 as an NAD⁺-consuming glycohydrolase and investigates its links to NAD⁺ tissue levels in rodent models.
- Mitochondria Work on isolated mitochondria documents measurements of the NAD⁺/NADH ratio as an indicator of redox state.
These observations stem from in vitro and animal models. They justify research interest in NAD⁺, but provide no information on safety, efficacy, or application outside of laboratory research.
Purity, COA & Analytical Testing
At BlitzLab, NAD+ is specified as ≥ 99 % (HPLC), with its identity confirmed by LC-MS. As NAD⁺ is sensitive to hydrolysis and oxidation, it is worth taking a closer look at two aspects of the document: the proportion of free nicotinamide and other degradation products, and whether the purity is stated as a percentage by area or as a content. You should also check whether the COA describes the free acid or a salt form.
Each batch is analysed by an external third-party laboratory; the COA with batch number, analysis date and chromatograms is attached to the product page. How to read the document: Understanding and reading a Certificate of Analysis (COA). Among the methods: Peptide Purity: HPLC and LC-MS Explained.
Storage & Handling
As a lyophilised product in a sealed, light-protected vial, NAD+ is significantly more stable than in dissolved form. Critical factors are moisture, heat, and alkaline environments: hydrolysis in aqueous solution is described in the literature as pH- and temperature-dependent, which is why prepared solutions are treated as short-lived in the lab. Further principles: Storing and Handling Research Peptides.
Buying NAD+ in the EU – what matters
NAD+ is widely marketed, and the offers vary accordingly. For procurement as a laboratory chemical, these points can be checked:
- Batch-specific COA instead of a template document: Batch number, date and chromatograms must match the delivery.
- Clear indication of substance: free acid or salt form with appropriate CAS number – NAD⁺, NADH, NMN and NR are different substances.
- Purity with Method "≥99%" without HPLC conditions is not a meaningful specification.
- Clear RUO Labelling Anyone communicating dosages or health claims leaves the RUO framework.
What else to look out for with a reputable provider: 7-point checklist.
Frequently asked questions about buying NAD+
Note on Sources & RUO
The technical information is based on publicly available substance databases (including PubChem) and published scientific literature on NAD⁺ and NAD-dependent enzymes. All observations originate from in-vitro systems, enzyme assays, or animal models; they describe the state of the literature, not product properties.
NAD+ is offered exclusively as a laboratory chemical for research purposes (RUO). It is not a medicinal product, not a dietary supplement, and not a cosmetic. Application to humans or animals, as well as any use outside the laboratory, is excluded.
Certificate of Analysis, specification, and availability directly on the product page.