5-Amino-1MQ / MOTS-c / NAD+ Blend

This vial contains three chemically distinct materials co-lyophilized into a single cake: a quaternised quinolinium salt, a 16-residue synthetic peptide, and a pyridine dinucleotide. 5-Amino- 1MQ is a quinoline ring system methylated at the ring nitrogen with a primary amino group at the 5- position. MOTS-c is a linear cationic peptide encoded by a short open reading frame in the mitochondrial 12S rRNA gene, carrying two methionines and no cysteine. NAD+ is a nicotinamide riboside and an adenosine ribonucleoside joined through a pyrophosphate bridge, with the nicotinamide ring nitrogen quaternised.

Each component is assayed against its own molecular target and the components are not characterised as a single pharmacological entity. 5-Amino-1MQ inhibition of nicotinamide N-methyltransferase is quantified in cell-free enzyme assays with IC50 and Ki derived by LC-MS/MS product quantitation. MOTS-c binding to MTHFD1 is measured by surface plasmon resonance and pull-down, and AMPK Thr172 phosphorylation signal is quantified by immunoblot in cultured cell lysates. NAD+ serves as the supplied substrate in cell-free sirtuin, PARP and CD38 assays, with turnover followed by LC-MS or at 340 nm. Readouts terminate at enzyme kinetic constants, binding constants and phosphorylation-site signal.

Primary literature relevant to this listing is component-specific: quinolinium salt synthesis and NNMT enzymology for 5-Amino-1MQ, open-reading-frame identification and enzyme-binding chemistry for MOTS-c, and redox couple and cofactor enzymology for NAD+. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.