Epithalon
COA published
A synthetic tetrapeptide studied in telomere-biology and cellular-senescence research.
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NAD+
CAS53-84-9MEASURED PURITY99.55%
A coenzyme studied in cellular-energetics, redox-balance and sirtuin-pathway research.
- Test methods
- HPLC-UV + LC-MS
- Purity target
- 99%+ verified
- Sizes available
- 3
- Availability
- Backordered
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Quantity
1
Total
$40.00
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Batch J_0726-01-NAD1000 · Certificate of Analysis available
For Research Use Only. Not for Human Consumption.
Products supplied by Synthrex Biotech LLC are intended strictly for in-vitro laboratory research and development by qualified professionals. They are not drugs, foods, cosmetics, or dietary supplements, and are not approved by the FDA for human or veterinary use. They are not sold for, and must not be used for, human or animal consumption or administration of any kind. Synthrex Biotech LLC is not a compounding pharmacy or chemical compounding facility as defined under section 503A of the Federal Food, Drug, and Cosmetic Act, and is not an outsourcing facility as defined under section 503B of that Act. By purchasing, you affirm that you are a qualified researcher acquiring these materials for lawful research purposes only. A Safety Data Sheet (SDS/MSDS) is available on request for every compound.
Sold by Synthrex Biotech LLC. A Safety Data Sheet (SDS) is available on request at support@synthrexbiotech.com.
✦ Research Notes
Background & literature
Origin
NAD+ is not a peptide at all — it is nicotinamide adenine dinucleotide, a coenzyme present in every living cell, and one of the oldest molecules in biochemistry. It was first identified by Arthur Harden and William Young in 1906 as a heat-stable fraction required for yeast fermentation. Its structure was determined by Hans von Euler-Chelpin, and Otto Warburg later established its role in hydride transfer. The modern interest in NAD+ dates to the discovery that sirtuins — a family of protein deacetylases — consume NAD+ as a substrate, which linked cellular NAD+ availability to a regulatory system rather than just to metabolism.
What has been characterised
NAD+ functions as an electron carrier in redox reactions and as a consumed substrate for three enzyme families: sirtuins, PARPs, and CD38/cADPR synthases. Because those enzymes cleave rather than recycle it, their activity depletes the cellular pool — the mechanistic basis for the research interest in NAD+ availability. The two review articles cited below, in Trends in Cell Biology and Science, are the standard entry points to that literature. Supplied as a laboratory research material.
Sources
- 1.“NAD+ and sirtuins in aging and disease.” Trends Cell Biol, 2014. PMID 24786309
- 2.“NAD⁺ in aging, metabolism, and neurodegeneration.” Science, 2015. PMID 26785480
These notes are provided for scientific context only. They describe published laboratory and preclinical research and are not a claim of any effect in humans. These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.
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Related Compounds
MOTS-c
A mitochondrial-derived peptide studied in metabolic-signalling and cellular-energetics research.
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These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.