PX1 Research supplies analytical-grade 5-Amino-1MQ synthesized specifically for non-clinical laboratory evaluation. As a targeted small-molecule inhibitor of nicotinamide N-methyltransferase (NNMT), 5-Amino-1MQ provides researchers with a precise tool for investigating cellular NAD+ dynamics, mitochondrial respiration, and adipocyte metabolic signaling.
PX1 Research supplies analytical-grade 5-Amino-1MQ synthesized specifically for non-clinical laboratory evaluation. As a targeted small-molecule inhibitor of nicotinamide N-methyltransferase (NNMT), 5-Amino-1MQ provides researchers with a precise tool for investigating cellular NAD+ dynamics, mitochondrial respiration, and adipocyte metabolic signaling.
When purchasing 5-Amino-1MQ for specialized in vitro or animal models, investigators require confirmed analytical identity, high chromatographic purity, and complete freedom from cytotoxic impurities. 5-Amino-1MQ (5-amino-1-methylquinolinium) is a membrane-permeable small molecule developed to selectively block the enzyme nicotinamide N-methyltransferase. Investigators seeking to buy 5-Amino-1MQ for laboratory research rely on PX1 Research for fully verified, USA-manufactured reference material accompanied by lot-specific documentation.
To maintain rigorous experimental consistency, PX1 Researchsubjects every production lot of 5-Amino-1MQ to rigorous quality assays. Our protocols integrate high-performance liquid chromatography (HPLC) to verify chemical purity alongside mass spectrometry (MS) to confirm molecular mass. This ensures that research laboratories receive unadulterated compounds capable of yielding reproducible data across enzymatic assays, transcriptomic profiling, and metabolic flux analyses.
5-Amino-1MQ belongs to the methylquinolinium class of small-molecule compounds. Its systematic chemical name is 5-amino-1-methylquinolin-1-ium, typically prepared as an iodide or chloride salt to ensure chemical stability and solubility in polar solvent systems. Unlike peptide molecules composed of amino acid chains linked by peptide bonds, 5-Amino-1MQ is a stable, non-peptidic synthetic salt with a molecular weight of approximately 159.21 g/mol (free cation basis).
The molecular architecture of 5-Amino-1MQ features a quinolinium core with a methyl substitution at the nitrogen atom and an amino moiety at the 5-position. This structural conformation enables competitive binding within the catalytic pocket of the target enzyme, structurally mimicking substrate dynamics while preventing methyl group transfer. Researchers examining our broader catalog of research peptides and metabolic probes will note that 5-Amino-1MQ's distinct chemical class offers high chemical stability under standard laboratory storage protocols.
The primary mechanism of 5-Amino-1MQ centers on its selective inhibition of nicotinamide N-methyltransferase (NNMT), a cytosolic enzyme predominantly expressed in adipose tissue, liver, and specific cancer cell lines. NNMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (MNA) and S-adenosylhomocysteine (SAH). Because MNA is cleared or excreted, elevated NNMT activity effectively depletes the cellular pool of nicotinamide available for NAD+ salvage synthesis.
By competitively binding to the active site of NNMT, 5-Amino-1MQ prevents the methylation of nicotinamide. Preclinical models indicate that inhibiting this enzymatic sink yields two distinct biochemical consequences: it preserves intracellular nicotinamide levels for conversion into nicotinamide adenine dinucleotide (NAD+) via the salvage pathway, and it prevents the excessive consumption of SAM, thereby modulating cellular methylation potential. For a deeper breakdown of enzymatic pathways, explore our research library.
In vitro data demonstrate that incubation of cultured adipocytes and myocytes with 5-Amino-1MQ leads to a measurable increase in intracellular NAD+ levels. NAD+ serves as a vital co-enzyme for hydride transfer reactions in glycolysis, the tricarboxylic acid (TCA) cycle, and oxidative phosphorylation. Furthermore, NAD+ acts as an essential substrate for sirtuins (such as SIRT1 and SIRT3) and poly(ADP-ribose) polymerases (PARPs), enzymes that regulate mitochondrial biogenesis, oxidative stress responses, and genomic integrity.
In animal studies using diet-induced obesity (DIO) mouse models, administration of NNMT inhibitors resulted in elevated tissue NAD+ concentrations without requiring exogenous NAD+ precursor supplementation. Researchers investigating cellular senescence, metabolic decay, and energy expenditure utilize 5-Amino-1MQ to map how preserving endogenous NAD+ pools influences downstream sirtuin activation and metabolic homeostasis.
Mitochondrial dysfunction and impaired fatty acid oxidation are central hallmarks of metabolic decline. Preclinical studies suggest that NNMT inhibition via 5-Amino-1MQ increases mitochondrial mass and oxygen consumption rate (OCR) in mature adipocytes. When NNMT is active at high levels, the resulting depletion of NAD+ suppresses SIRT1 activity, downregulating peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), a master regulator of mitochondrial biogenesis.
In high-fat diet rodent models, treatment with 5-Amino-1MQ was shown to stimulate basal metabolic rate, enhance fatty acid oxidation, and reduce white adipose tissue (WAT) accumulation without modifying food intake. Research protocols evaluating lipolysis, mitochondrial respiration, and adipocyte differentiation frequently employ 5-Amino-1MQ to dissect the signaling axis connecting methyl-donor availability, sirtuin activation, and lipid turnover.
Laboratory investigations into metabolic regulation often compare 5-Amino-1MQ against alternative small molecules and peptides targeting mitochondrial pathways. While 5-Amino-1MQ operates upstream by inhibiting NNMT to salvage NAD+, compounds like MOTS-c function as mitochondrial-derived peptides that regulate nuclear gene expression and glucose transactivation directly. Similarly, experimental ligands such as SLU-PP-332 act as estrogen-related receptor (ERR) agonists to upregulate oxidative muscle fiber capacity.
Understanding the operational differences between these molecules allows investigators to design robust comparative studies. While SLU-PP-332 targets transcription factors controlling mitochondrial machinery and MOTS-c acts as a metabolic signaling peptide, 5-Amino-1MQ uniquely targets methyl-group kinetics and cofactor salvage. For researchers conducting comparative studies across these classes, details on experimental design can be found in our overview of mitochondrial research compounds.
When purchasing compounds for sensitive bioassays, analytical purity is non-negotiable. Substandard or contaminated reference materials introduce confounding variables that compromise experimental validity. PX1 Research enforces strict quality assurance protocols for every batch of 5-Amino-1MQ, utilizing third-party testing performed in ISO 17025 accredited laboratories.
Our analytical validation process includes Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) to establish chemical purity (consistently target ≥98%), Electrospray Ionization Mass Spectrometry (ESI-MS) to verify exact molecular weight, and chromogenic LAL assays to ensure endotoxin levels remain below stringent research limits. Every order includes access to a lot-specific Certificate of Analysis (COA) matching the exact batch shipped to your facility.
5-Amino-1MQ is supplied as a lyophilized crystalline powder. To maintain structural stability, the solid compound should be stored at -20°C in a dry environment sealed from moisture. Prior to opening, vials should be allowed to equilibrate to room temperature to prevent condensation inside the container.
For in vitro research, 5-Amino-1MQ demonstrates high solubility in dimethyl sulfoxide (DMSO) and sterile water or phosphate-buffered saline (PBS), depending on the specific salt form. A common laboratory stock solution preparation involves dissolving the powder in sterile DMSO to create a 10 mM to 50 mM stock, which can then be aliquoted and frozen at -80°C to avoid repeated freeze-thaw cycles. Dilutions into cell culture media should be prepared immediately prior to experimental assays.
PX1 Research supports university laboratories, private biotechnology firms, and contract research organizations (CROs) requiring dependable supplies of metabolic research compounds. Through our wholesale program, institutional buyers can secure high-volume lots of 5-Amino-1MQ with consistent lot-to-lot purity guarantees and bulk pricing structures.
All PX1 Research products are manufactured in compliance with strict quality standards within USA-based facilities. Orders placed before cutoff times ship same-day from our distribution centers in California and Arizona, ensuring minimal transit delays and reliable supply chain support for ongoing research timelines.
What is 5-Amino-1MQ used for in laboratory research?
5-Amino-1MQ is a selective inhibitor of the enzyme nicotinamide N-methyltransferase (NNMT). In preclinical research, it is used to investigate cellular NAD+ preservation, cellular energy expenditure, sirtuin signaling, mitochondrial biogenesis, and lipid metabolism in cultured cells and animal models.
Is 5-Amino-1MQ a peptide?
No. 5-Amino-1MQ (5-amino-1-methylquinolinium) is a small-molecule quinolinium derivative, not a peptide. It does not consist of amino acid chains linked by peptide bonds, giving it distinct physical properties and high chemical stability.
What purity levels are guaranteed for 5-Amino-1MQ from PX1 Research?
PX1 Research guarantees a chemical purity of ≥98% for 5-Amino-1MQ, verified by Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Mass Spectrometry (MS). Every lot is tested by an independent ISO 17025 accredited laboratory.
How should 5-Amino-1MQ be stored upon receipt?
Lyophilized powder should be stored at -20°C in a desiccated container away from light. Once reconstituted into liquid stock solutions (e.g., in DMSO or buffer), solutions should be divided into single-use aliquots and stored at -80°C to minimize degradation from repeated freeze-thaw cycles.
Does PX1 Research provide Certificates of Analysis (COA)?
Yes. Every batch of 5-Amino-1MQ includes a lot-specific Certificate of Analysis detailing HPLC purity analysis, mass spec identity verification, appearance, and endotoxin levels.
What is the primary target enzyme of 5-Amino-1MQ?
5-Amino-1MQ selectively targets and inhibits nicotinamide N-methyltransferase (NNMT), an enzyme involved in methyl transfer reactions that consumes S-adenosylmethionine (SAM) and depletes nicotinamide available for NAD+ synthesis.
Where does PX1 Research ship from?
All orders ship directly from PX1 Research facilities located in California and Arizona, USA. Orders placed Monday through Friday before our daily shipping cutoff time are dispatched the same day.
Is 5-Amino-1MQ approved for human consumption or therapeutic use?
No. 5-Amino-1MQ is sold strictly as a research chemical for in vitro assays, laboratory experimentation, and preclinical research. It is not for human or animal consumption, medical treatment, or diagnostic use.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.