NAD+

Third-Party Tested

Independent lab verified

Batch-Specific CoA

Publicly accessible

YPB.223

Reference number

500mg

Lyophilized vial

Origin

NAD+ was first identified by Arthur Harden and William John Young in 1906 as a factor in yeast fermentation. Its complete structure was determined by Hans von Euler-Chelpin in the 1930s, work that contributed to his Nobel Prize in Chemistry. NAD+ is a coenzyme present in every living cell, essential for over 500 enzymatic reactions.

Research Lineage

Modern NAD+ research was revitalized by Guarente and Sinclair's work on sirtuins beginning in the late 1990s. Imai, Yoshino, and colleagues at Washington University have characterized the NAD+ biosynthetic salvage pathway and its decline with age. Brenner's identification of nicotinamide riboside as an NAD+ precursor opened the supplementation research field. Over 40,000 PubMed entries reference NAD+.

Mechanism of Action

NAD+ serves as an electron carrier in mitochondrial oxidative phosphorylation (Complexes I and III) and as a substrate for NAD+-consuming enzymes including sirtuins (SIRT1-7), PARPs, and CD38. Sirtuins use NAD+ as a co-substrate for protein deacetylation, linking cellular energy status to epigenetic regulation. NAD+ levels have been observed to decline with age, correlating with reduced sirtuin activity.

Structural Notes

Dinucleotide coenzyme. Composed of nicotinamide mononucleotide (NMN) and adenosine monophosphate (AMP) linked by pyrophosphate bond. Molecular weight: 663.43 Da. Exists in oxidized (NAD+) and reduced (NADH) forms.