NAD+ 500mg

NAD+ is a dinucleotide, not a peptide: it consists of a nicotinamide riboside and an adenosine ribonucleoside joined through a pyrophosphate bridge. The nicotinamide ring is quaternised at the ring nitrogen, giving the oxidized form its formal positive charge, which is balanced in the free acid by the diphosphate. The molecule contains two ribose rings, an adenine base and a nicotinamide base, and is supplied as the beta anomer at both glycosidic linkages.

NAD+ is the oxidized member of a redox cofactor pair and serves as substrate or cosubstrate for defined enzyme classes rather than binding a cell-surface receptor. Sirtuin deacylase activity across SIRT1 to SIRT7, poly(ADP-ribose) polymerase activity and CD38 glycohydrolase activity are quantified in cell-free assays using this material as the supplied substrate, with nicotinamide or ADP-ribose release measured by LC-MS or coupled fluorescence. Oxidoreductase turnover is followed spectrophotometrically at 340 nm by tracking NADH absorbance. Readouts terminate at enzyme rate constants and cofactor-conversion values.

Primary literature on this molecule covers its structural chemistry, redox couple thermodynamics, hydrolytic and pH-dependent stability, and the enzymology of sirtuin, PARP and glycohydrolase families that use it as a substrate. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.