Oxidized dinucleotide cofactor for in vitro redox, sirtuin, and PARP research. Lyophilized NAD+ (nicotinamide adenine dinucleotide) for cellular bioenergetics and longevity model studies.
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Central coenzyme across redox metabolism, sirtuin signaling, and DNA damage response pathways
NAD+ cycles between oxidized (NAD+) and reduced (NADH) states across glycolysis, TCA cycle, fatty acid oxidation, and oxidative phosphorylation. It accepts a hydride at the C4 position of the nicotinamide ring, transferring electrons to the mitochondrial electron transport chain.
NAD+ is a cleaved cosubstrate for the seven mammalian sirtuins (SIRT1-7), which remove acetyl, succinyl, malonyl, and other acyl modifications from histones and metabolic enzymes. Each catalytic turnover consumes one NAD+ and releases nicotinamide plus O-acetyl-ADP-ribose.
PARPs (especially PARP1) use NAD+ as a substrate to synthesize poly(ADP-ribose) chains at DNA strand breaks, recruiting repair machinery. CD38 and SARM1 are additional major NAD+-consuming enzymes whose hydrolase activity strongly modulates intracellular NAD+ pools, particularly in aging and inflammation models.
Reported findings across NAD+ biology and aging research models
Primary areas of NAD+ investigation
NAD+ levels decline in multiple tissues across mammalian aging. Models examine NAD+ pool dynamics, precursor (NMN, NR) supplementation, CD38 upregulation, and links to senescence-associated secretory phenotype (SASP). Reviewed by Covarrubias et al. 2021.
Covarrubias et al. 2021 ↗Used as cofactor in biochemical and cell-based assays of SIRT1-7 activity on histone (H3K9ac, H3K14ac) and non-histone substrates. Imai & Guarente articulated the NAD+-sirtuin axis as central to metabolic and aging regulation.
Imai & Guarente 2014 ↗NAD+/NADH ratio governs mitochondrial respiration, ETC Complex I flux, and TCA cycle activity. Used to interrogate mitochondrial dysfunction models, SIRT3 deacetylation of metabolic enzymes, and metabolic adaptation in disease models. See Verdin 2015 in Science.
Verdin 2015 ↗Substrate for PARP1/PARP2 in poly(ADP-ribosyl)ation at DNA single- and double-strand breaks. Used in studies of base excision repair, replication stress, and the PARP-NAD+-SIRT1 crosstalk relevant to genome maintenance. See Rajman et al. 2018.
Rajman et al. 2018 ↗Technical specifications and analytical profile
Common questions about NAD+ research parameters
Peer-reviewed publications from PubMed