NAD+
NAD+
Crypto
Restock in progress. Add your email and we will tell you the moment this compound is back in stock.
One email when this is back in stock. No spam, unsubscribe anytime.
Product details
NAD+ is nicotinamide adenine dinucleotide, a dinucleotide cofactor present in every living cell. It is a coenzyme, not a peptide: two nucleotides, one carrying nicotinamide and one carrying adenine, joined through a pair of phosphate groups. It belongs to the pyridine-nucleotide coenzyme class.
In the published preclinical literature, NAD+ has been characterised at the molecular level as the cofactor and substrate of the enzymes that read and consume it. Cell-free structural and enzymology work has resolved how a Sir2-family NAD+-dependent deacetylase couples hydrolysis of the dinucleotide to removal of an acetyl group, forming nicotinamide and O-acetyl-ADP-ribose, and how a CD38 glycohydrolase cleaves the nicotinamide-ribose bond of NAD+ through trapped catalytic intermediates. It is supplied as a research compound and is not intended for human or veterinary use.
Full specifications
Complete your order
supplied for laboratory research only
Recently viewed
picks up where you left off
Research
NAD+ has been characterised in preclinical laboratory models as the cofactor and substrate of the enzymes that process it. The primary studies below, in cell-free structural and enzymology assays, measured how a Sir2-family NAD+-dependent deacetylase couples hydrolysis of the dinucleotide to substrate deacetylation, and how a CD38 glycohydrolase cleaves NAD+ through trapped catalytic intermediates. The literature is preclinical; it describes the compound, not any outcome in humans.
3 preclinical studies indexed · nad+ consumption by a sirtuin deacetylase and nad+ cleavage by a glycohydrolase · links open on PubMed
NAD+ consumption by a sirtuin deacetylase 2 studies
In vitro
Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone and protein deacetylases
In cell-free assays with purified yeast Sir2, yeast HST2, and SIRT2 against acetylated histone peptides, the study measured the kinetic mechanism that couples NAD+ hydrolysis to deacetylation and resolved the individual chemical steps forming nicotinamide and O-acetyl-ADP-ribose as the measured endpoint.
Read the study ↗
In vitro
Structural insights into intermediate steps in the Sir2 deacetylation reaction
By X-ray crystallography of the bacterial sirtuin Sir2Tm captured with substrate analogues, the study resolved intermediate chemical steps of the NAD+-dependent deacetylation reaction, mapping how the dinucleotide is positioned and processed in the catalytic pocket as a structural endpoint.
Read the study ↗
Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
Reviews
Verified-order reviews on service, shipping, and product quality appear here once the first order is reviewed.