5-Amino-1MQ for research is a small-molecule, membrane-permeable inhibitor of nicotinamide N-methyltransferase (NNMT) utilized in preclinical laboratory investigations. By selectively inhibiting NNMT activity, this compound prevents the irreversible methylation of nicotinamide, thereby preserving intracellular NAD+ availability, enhancing mitochondrial respiration, and providing critical insights into fat-metabolism regulation in cellular and animal models.
5-Amino-1MQ for research is a small-molecule, membrane-permeable inhibitor of nicotinamide N-methyltransferase (NNMT) utilized in preclinical laboratory investigations. By selectively inhibiting NNMT activity, this compound prevents the irreversible methylation of nicotinamide, thereby preserving intracellular NAD+ availability, enhancing mitochondrial respiration, and providing critical insights into fat-metabolism regulation in cellular and animal models.
5-Amino-1-methylquinolinium (5-amino-1MQ) is a quinolinium derivative engineered specifically to act as a potent, selective, membrane-permeable small-molecule inhibitor of the cytosolic enzyme nicotinamide N-methyltransferase (NNMT). In biochemistry and preclinical molecular biology, the deployment of 5-amino-1MQ for research has enabled researchers to dissect the complex metabolic crosstalk between SAM (S-adenosylmethionine) utilization, methyl donor kinetics, and cellular energy homeostasis.
Unlike peptide-based metabolic modulators that act predominantly through membrane-bound G-protein coupled receptors, 5-amino-1MQ operates intracellularly. Its primary chemical structure allows efficient passive transport across biological membranes, permitting direct binding to the active site of NNMT without requiring complex drug delivery vectors. As a research chemical, it serves as a precise probe for interrogating how enzymatic methylation of nicotinamide impacts downstream metabolic pathways, mitochondrial efficiency, and intracellular cofactor availability.
Nicotinamide N-methyltransferase (NNMT) is a cytosolic enzyme responsible for catalyzing the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide (NAM), forming 1-methylnicotinamide (MNA) and S-adenosylhomocysteine (SAH). Because MNA is rapidly excreted by cells, this reaction acts as a terminal sink for nicotinamide, permanently removing it from the NAD+ salvage pathway. Elevated NNMT expression has been consistently observed in white adipose tissue, hepatic tissue, and select hyper-proliferative cell lines in preclinical models.
By competing with nicotinamide at the active site of NNMT, 5-amino-1MQ blocks the methylation cascade. Preclinical studies suggest that high-affinity inhibition of NNMT effectively halts the depletion of the cellular NAM pool. Consequently, nicotinamide remains available for salvage synthesis into nicotinamide mononucleotide (NMN) and subsequently nicotinamide adenine dinucleotide (NAD+). In laboratory settings, this fundamental mechanism makes 5-amino-1MQ a primary reagent for investigating NAD+ pathway research and cellular redox signaling.
NAD+ serves as a non-replaceable coenzyme in cellular oxidation-reduction reactions, serving as an electron acceptor in glycolysis, the tricarboxylic acid (TCA) cycle, and mitochondrial beta-oxidation. Furthermore, NAD+ acts as an essential substrate for sirtuins (SIRT1–SIRT7) and poly(ADP-ribose) polymerases (PARPs). In vitro assays demonstrate that inhibiting NNMT with 5-amino-1MQ results in a measurable, dose-dependent rise in intracellular NAD+ levels within adipocytes and myocytes.
This preservation of the intracellular NAD+ pool stimulates sirtuin-1 (SIRT1) catalytic activity. Activated SIRT1 promotes the deacetylation of key transcription factors, including peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α). In rodent literature, PGC-1α upregulation leads to enhanced mitochondrial biogenesis, increased basal oxygen consumption rates (OCR), and elevated expression of electron transport chain complexes. Researchers studying energy expenditure frequently employ 5-amino-1MQ for research to quantify changes in basal metabolic rates and mitochondrial mass without altering extracellular nutrient concentrations.
In animal models of diet-induced obesity, NNMT activity is markedly upregulated in white adipose tissue, leading to diminished intracellular NAD+ levels and compromised metabolic flexibility. Experimental administration of 5-amino-1MQ in mouse models has provided valuable mechanistic data regarding adipose tissue remodeling. Investigators observed that NNMT inhibition selectively reversed adipocyte hypertrophy and promoted a shift toward a thermogenic, lipid-oxidizing phenotype.
Furthermore, preclinical research indicates that 5-amino-1MQ exposure in isolated cell culture models alters lipid droplet dynamics. By reducing intracellular lipid accumulation and elevating basal oxygen consumption without inducing cytotoxicity, the compound facilitates the study of adipogenesis pathways, lipid clearance, and insulin-sensing intracellular cascades. These empirical findings have positioned NNMT inhibition as a central area of inquiry in metabolic disease research, cellular senescence studies, and energy metabolism assays accessible through the PX1 Research catalog.
When designing metabolic and energy expenditure experiments, researchers often evaluate 5-amino-1MQ alongside other laboratory agents that target mitochondrial function, lipid metabolism, or energy sensing. Understanding the mechanistic differences between these reference compounds is critical for selecting the appropriate assay controls.
While 5-amino-1MQ acts specifically as an intracellular enzyme inhibitor of NNMT to spare nicotinamide, mitochondrial-derived peptides like MOTS-c function primarily via activation of the AMPK pathway to regulate metabolic homeostasis. Similarly, fragments such as AOD-9604 act through distinct lipolytic signaling pathways without directly altering intracellular NAD+ synthesis cascades. Comparing 5-amino-1MQ to other metabolic research compounds in concurrent assay panels allows laboratories to differentiate between direct substrate-sparing mechanisms and downstream transcriptional activations.
Proper handling and solubilization protocols are vital to maintain the structural stability and targeted biochemical reactivity of 5-amino-1MQ in laboratory applications. 5-Amino-1MQ is typically supplied as a lyophilized or crystalline powder. For in vitro and biological assays, appropriate solvent selection depends on the experimental protocol and cell culture conditions.
Common reconstitution guidelines for research include: - **Dimethyl Sulfoxide (DMSO):** Readily soluble up to 20–50 mg/mL, making DMSO the primary stock solvent for high-concentration in vitro screening. - **Aqueous Buffers / Saline:** Limited direct solubility in pure water or PBS; stock solutions prepared in DMSO should be diluted into aqueous media (such as cell culture media or physiological saline) immediately prior to treatment, keeping final DMSO concentrations below 0.1–0.5% v/v to avoid cellular toxicity. - **Storage:** Solid powder should be stored tightly desiccated at -20°C. Aliquoted DMSO stock solutions should be kept at -80°C, protected from light and moisture, and subjected to minimal freeze-thaw cycles.
For research findings to be reproducible, small-molecule inhibitors must meet strict analytical chemistry metrics. Low-purity compounds or residual heavy metals can alter cell viability and introduce confounding variables into enzymatic assays. PX1 Research mandates rigorous batch-level analytical testing for every lot of 5-amino-1MQ distributed to scientific institutions.
Essential quality controls include: - **Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC):** Verifies chemical purity to ensure a minimum of 98% major peak area, eliminating unwanted reaction byproducts or precursor contaminants. - **Mass Spectrometry (ESI-MS):** Confirms exact molecular mass (C10H11N2+) matching the theoretical chemical structure of 5-amino-1-methylquinolinium. - **Endotoxin Testing (LAL Assay):** Ensures endotoxin levels remain strictly below < 0.05 EU/mg, preventing premature inflammatory cytokine responses in primary cell culture or animal tissue models.
All analytical certificates of analysis (COAs) are verified through independent, ISO 17025-accredited testing laboratories, ensuring full lot-to-lot consistency for researchers acquiring high-purity reference materials.
PX1 Research operates as an authoritative USA-based supplier of analytical-grade research compounds, serving academic laboratories, biotechnology firms, and contract research organizations (CROs). We maintain strict quality management systems across GMP-compliant manufacturing protocols and domestic distribution channels.
Key organizational advantages include: - **100% USA-Manufactured Compounds:** Synthesized and processed under strict domestic regulatory and quality control standards. - **Comprehensive Certificate of Analysis:** Every batch is accompanied by an unedited, lot-specific COA detailing HPLC chromatograms and mass spectra. - **Rapid Fulfillment:** Orders ship same-day (Monday–Friday) directly from our centralized warehouses in California and Arizona, preserving cold-chain integrity when temperature-sensitive handling is required.
Whether purchasing standard reagent quantities or setting up custom supply agreements through our bulk research portal, researchers can depend on PX1 Research for absolute product authenticity and operational compliance.
What is 5-amino-1MQ used for in laboratory research?
5-Amino-1MQ is an analytical tool used in preclinical research to inhibit nicotinamide N-methyltransferase (NNMT). Researchers utilize it to investigate intracellular NAD+ salvage pathways, mitochondrial biogenesis, sirtuin activation, and lipid metabolism in adipocyte and muscle cell models.
How does 5-amino-1MQ inhibit the NNMT enzyme?
5-amino-1MQ acts as a direct, membrane-permeable competitive inhibitor of NNMT. By occupying the active site of the enzyme, it prevents the methylation of nicotinamide into 1-methylnicotinamide, preserving intracellular nicotinamide for conversion into NAD+.
What is the purity standard of 5-amino-1MQ from PX1 Research?
PX1 Research provides 5-amino-1MQ tested to a minimum purity threshold of ≥98% as verified by RP-HPLC and mass spectrometry. Each lot undergoes independent ISO 17025 laboratory verification and endotoxin testing prior to release.
How should 5-amino-1MQ be reconstituted for in vitro cell culture assays?
5-Amino-1MQ is generally dissolved in high-purity DMSO to create a concentrated stock solution. This stock is subsequently diluted into sterile culture medium to reach working experimental concentrations, ensuring final DMSO levels remain well below toxic thresholds (<0.1% v/v).
What are the recommended storage conditions for 5-amino-1MQ powder?
Lyophilized or crystalline 5-amino-1MQ powder should be stored desiccated at -20°C, protected from ambient light and moisture. Liquid stock aliquots in DMSO should be stored at -80°C to maintain chemical stability.
Is 5-amino-1MQ approved for human clinical use or consumption?
No. 5-Amino-1MQ is strictly designated for laboratory research, in vitro assays, and preclinical animal investigations. It is not approved for human consumption, therapeutic use, or clinical administration.
How does 5-amino-1MQ differ from peptide metabolic regulators like MOTS-c?
5-Amino-1MQ is a small-molecule enzymatic inhibitor targeting NNMT within the cytosol. Compounds like MOTS-c are mitochondrial-derived peptides that function primarily through cell-surface signaling and AMPK activation cascades. Both compounds modulate cell energetics through distinct biological targets.
Where are PX1 Research products manufactured and shipped from?
All PX1 Research compounds are manufactured in the United States and shipped directly from state-of-the-art logistics facilities located in California and Arizona, featuring same-day fulfillment on business days.
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.