Compound reference
NAD+
Cellular & Longevity Research · vial. For laboratory research use only. Not for human or veterinary consumption, diagnostic use, therapeutic use, or clinical use.
Chemistry identity
Reference identifiers
COA documentation
Lot record status
COA on file - lab confirmation pendingView Lab ReportsPublished literature
Research context
Peer-reviewed literature referencing this compound, provided for research context.
Sigma-1 receptor promotes glycolysis in neuronal systems by suppressing GRIM192026
Couly S, Yasui Y, Grammatikakis I, Kimura Y, Hinkle JJ, Gomez JL, et al.
iScience
In Sigma-1 receptor (S1R) knockout Neuro2a neuronal cells and cortical neurons, plus S1R-knockout mice, loss of S1R increased the NAD+/NADH ratio and reduced glycolytic activity through a GRIM19-dependent mechanism at mitochondrial complex I; PET imaging showed reduced brain glucose uptake in the knockout mice, linking S1R signaling to neuronal NAD+/glycolysis balance.
A sustained NAD(+) supplementation-biosynthesis nanoplatform for metabolic restoration in aged bone regeneration2026
Xie F, He Z, Xu S, Bai X, Wang X, Zhang F, et al.
Bioactive materials
In senescent bone marrow-derived mesenchymal stromal cells (BMSCs) and an aged-mouse bone-defect model, a nanoparticle platform delivering NAD+ together with an NAD+ biosynthesis activator raised the NAD+/NADH ratio roughly 11-fold and increased ATP production about 3-fold in senescent cells, and increased bone volume fraction in the in vivo model, illustrating NAD+ restoration as a mechanism studied in cellular senescence and bone-regeneration research.
Emerging chemical strategies for CD38 inhibition: restoring NAD(+) metabolism and disease control2026
Zhang Z, Ansari AJ, Fayne ER, Zhang Y
Bioorganic & medicinal chemistry
This medicinal-chemistry review surveys covalent and non-covalent small-molecule inhibitors of CD38, the ectoenzyme that hydrolyzes NAD+ and drives cellular NAD+ depletion during aging, inflammation, and tumor growth in preclinical models, framing CD38 inhibition as a chemical-biology strategy for studying NAD+ homeostasis restoration.
Nicotinamide Mononucleotide Supplementation Improves Mitochondrial Dysfunction and Rescues Cellular Senescence by NAD/Sirt3 Pathway in Mesenchymal Stem Cells2022
Wang H, Sun Y, Pi C, Yu X, Gao X, Zhang C, et al.
International Journal of Molecular Sciences
This in vitro study of mesenchymal stem cells found that nicotinamide mononucleotide (NMN) supplementation raised intracellular NAD+ levels and Sirt3 expression and ameliorated mitochondrial function in replicatively senescent cells; Sirt3 over-expression and inhibition experiments implicated the NAD+/Sirt3 pathway as the mechanism linking NMN to mitochondrial function and cellular-senescence markers.
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase2000
Imai S, Armstrong CM, Kaeberlein M, Guarente L
Nature
Landmark biochemical study showing that yeast and mouse Sir2 proteins are NAD+-dependent histone deacetylases that remove acetyl groups from histone H3 (lysines 9 and 14) and H4 (lysine 16); this NAD+-dependent deacetylase activity was shown to underlie gene silencing, suppression of recombination, and extension of replicative lifespan in yeast.
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