| Pcs | Single Vial, 3-Pack, 6-Pack, Pack of 10 |
|---|---|
| Strength | 500mg, 1000mg |
NAD+
Price range: $90.00 through $915.00
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VERIFICATION
How to read this report
NAD+, in structural terms.
- Sequence
- Not applicable. NAD+ is a dinucleotide coenzyme, not a peptide.
- Molecular formula
- C₂₁H₂₇N₇O₁₄P₂
- Molecular weight
- Approximately 663.4 g/mol
- CAS number
- 53-84-9
- Structure type
- Reagent
- Primary molecular target
- NAD+-dependent dehydrogenases (as a redox cofactor); sirtuin deacetylases (SIRT1-SIRT7), poly(ADP-ribose) polymerases (PARPs) and CD38 (as a consumed substrate).
- Physical form
- Lyophilized powder
- PubChem CID
- 5892
NAD+ is a dinucleotide, not a peptide. It consists of nicotinamide mononucleotide and adenosine monophosphate joined through a pyrophosphate bridge. In cells it cycles between the oxidized form (NAD+) and the reduced form (NADH), and it is also consumed as a substrate by enzymes that transfer its ADP-ribose group.
Where NAD+ appears in the literature.
- Published studies have used NAD+ in:
- Enzyme kinetics of NAD+-dependent dehydrogenases
- Sirtuin deacetylase activity assays
- PARP activity and ADP-ribosylation studies
- NAD+/NADH ratio and NAD+ salvage pathway studies
- Mitochondrial and nuclear NAD+ pool studies
- Purified recombinant enzymes
- Yeast models (Sir2 studies)
- Cultured mammalian cell lines
- Isolated mitochondria
- Cell-free coupled enzyme assays
- Spectrophotometric NADH measurement at 340 nm
- Enzymatic cycling assays
- LC-MS/MS quantification of NAD+ metabolites
- Fluorometric sirtuin deacetylase assays
- PARP activity assays
- NAD+ and NADH concentrations and their ratio
- Enzyme turnover and Michaelis constants for NAD+
- Sirtuin deacetylation rate
- ADP-ribose polymer formation
- NAD+ salvage pathway enzyme activity
What has been studied, and in what systems.
NAD+ acts in two distinct ways in experimental systems: as a redox cofactor that cycles between NAD+ and NADH, and as a substrate that enzymes consume. Studies of the yeast protein Sir2 showed that it is an NAD-dependent histone deacetylase, which linked NAD+ availability to enzymatic gene silencing (Imai et al., 2000).
Later work showed that the NAD+ salvage pathway is regulated by the CLOCK-SIRT1 circadian machinery in cell and mouse models (Nakahata et al., 2009).
Reviews have described how NAD+ is distributed between mitochondrial and nuclear pools and how consuming enzymes such as sirtuins, PARPs and CD38 compete for it (Cantó et al., 2015). These studies place NAD+ in enzymology and redox biology research.
These are published research systems. They do not describe approved clinical applications, and they do not establish efficacy or safety in humans.
Imai S et al., 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. PMID 10693811. https://pubmed.ncbi.nlm.nih.gov/10693811/
Nakahata Y et al., 2009. Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1. Science. PMID 19286518. https://pubmed.ncbi.nlm.nih.gov/19286518/
Cantó C et al., 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/
Read our research write-up on this compound:
About this compound and its batch data.
What is NAD+?
NAD+ is nicotinamide adenine dinucleotide, an endogenous redox coenzyme. It is a dinucleotide, not a peptide: nicotinamide mononucleotide joined to adenosine monophosphate through a pyrophosphate linkage. CAS 53-84-9. Astramide supplies it as a lyophilized powder for laboratory research use only. It is not intended for human or animal consumption, clinical use, or therapeutic application.
What has NAD+ been examined for in published research?
In mouse embryo fibroblasts, researchers found that intracellular NAD+ levels oscillate over 24 hours, driven by circadian regulation of NAMPT, the rate-limiting enzyme of the NAD+ salvage pathway (Nakahata et al., 2009, PMID 19286518). Published work is pre-clinical. Astramide makes no claim about outcomes in humans.
What purity does the current NAD+ lot reach?
Lot Brown Cap returned 99.89% chromatographic purity by HPLC-UV/MS, tested by Krause Analytical under Lab No. 200516 and reported 2 March 2026. Identity was confirmed. The laboratory left the Batch/Lot field blank on this certificate, and Astramide identifies the lot by its brown vial cap.
How much NAD+ is in the vial?
Astramide sent a 100 mg vial from lot Brown Cap for testing. The lot is sold in 500 mg and 1000 mg vials. The label claim on the tested vial is 100 mg. The laboratory measured 82.5 mg, which is 82.5% of label. Astramide publishes the measured figure rather than the label figure. Net content is a separate question from purity.
How is Astramide's NAD+ tested?
Testing is performed by Krause Analytical, a DEA-registered, ISO/IEC 17025-certified laboratory in Austin, Texas. This material was analysed by four methods: identity, chromatographic purity by HPLC-UV/MS, net content by HPLC-UV-MS, and endotoxin by USP 85. Heavy metals, microbial and pH were not performed, and the page shows those rows as not reported.
How should NAD+ be stored for research use?
Lyophilized material is stored at -20C and protected from light. Once reconstituted, storage is 2 to 8C with use within 14 to 30 days. Storage conditions affect compound stability, and results from this lot apply to material handled within these conditions.
What is the difference between research-grade and pharmaceutical-grade NAD+?
These are separate classifications. Research-grade material is supplied for laboratory research use only and is not manufactured, tested or released under the regulatory framework that governs drugs for human use. Pharmaceutical-grade is an FDA classification for human-use products. Astramide supplies research-grade material exclusively and does not represent it as pharmaceutical-grade.
Is NAD+ a peptide?
No. NAD+ is a dinucleotide cofactor with no amino acid sequence. Astramide lists it alongside research peptides because it is supplied, stored and tested the same way, as a lyophilized powder with a published certificate.
This product is intended strictly for in-vitro laboratory research conducted by qualified professionals. It is not intended for human or animal consumption, clinical use, or therapeutic application. The statements on this page have not been reviewed by the FDA. These research peptides are not intended to diagnose, treat, cure, or prevent any disease. Research Use Only.






