Buy NAD+ 2026 — Redox Cofactor for Sirtuin, PARP, and Mitochondrial Research (EU)

Coenzyme Research · 9 July 2026 · 10 min read · Research Use Only

In short: NAD+ (Nicotinamide Adenine Dinucleotide) is No peptide, but a pyridine dinucleotide coenzyme – the only non-peptide in the range. At BlitzLab as 500-mg Vial with batch-related Certificate of Analysis (COA), HPLC ≥ 99 %, EU delivery. Price: 79.90. For research use only (RUO).

NAD+ at a glance

DesignationNAD+ (β-nicotinamide adenine dinucleotide, free acid)
IdentityDinucleotide coenzyme, No peptide – no amino acid sequence
Molecular formulaC₂₁H₂₇N₇O₁₄P₂
Molar massapprox. 663.43 g/mol (free acid)
Synonymsβ-NAD, NAD⁺, Coenzyme I, Diphosphopyridine Nucleotide (DPN), Cozymase
ClassPyridine dinucleotide coenzyme, redox cofactor NAD⁺/NADH
Research contextRedox biochemistry, energy metabolism, mitochondrial research, NAD-consuming enzymes (Sirtuins, PARPs, CD38)
CAS number53-84-9 (free acid; salt forms have different CAS numbers – the batch-specific COA is authoritative)
FormLyophilised powder (freeze-dried), sealed vial
Amount500 mg per vial
Purity≥99% (HPLC), identity confirmed by LC-MS
AnalysisExternal third-party laboratory, batch-specific COA
Intended useFor Research Use Only (RUO)
Price79.90 · 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.

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:

What else to look out for with a reputable provider: 7-point checklist.

Frequently asked questions about buying NAD+

No. NAD+ is a dinucleotide coenzyme without amino acids. It is the only non-peptide in the BlitzLab catalogue and is listed without a sequence.
The free acid has CAS number 53-84-9. Salt forms have different CAS numbers; the batch-specific COA is authoritative for the goods supplied.
NAD⁺ is the oxidised, NADH the reduced form of the same dinucleotide. NMN and NR are smaller precursor molecules. Four substances with their own CAS numbers.
No. NAD+ is supplied exclusively as a laboratory chemical; we do not publish dosages or application protocols.

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.

NAD+ 500 mg – View batch with COA

Certificate of Analysis, specification, and availability directly on the product page.

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