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HomeShopMetabolic Research5-Amino-1MQ
5-Amino-1MQ 10 mg - Research Peptide | Pepcore

5-Amino-1MQ

€69.00
In Stock
Strength
1

For in-vitro laboratory research use only. Not intended for human consumption, veterinary, diagnostic, or clinical use.

EU delivery 2–5 days
EU delivery 2–5 days
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≥99% HPLC Purity
≥99% HPLC Purity
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COA on Request
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OrderedToday
Shipped19 Jun
Delivered22 Jun–24 Jun
Product Specifications
Format
Lyophilized powder
Strength
10 mg
Purity
99%
Testing
Third-party HPLC/MS
CAS
685079-15-6
Intended use
Research only

Description

5-Amino-1MQ (5-amino-1-methylquinolinium) is a research-grade small-molecule compound and a selective, membrane-permeable inhibitor of nicotinamide N-methyltransferase (NNMT). It is supplied as an investigational laboratory compound for use in metabolic-pathway research, adipose-biology research, and methyl-donor metabolism research.

Laboratory research studies have positioned 5-Amino-1MQ as a reference tool compound for examining how pharmacological NNMT inhibition reshapes intracellular nicotinamide and S-adenosyl-methionine (SAM) pools. Research models have characterised its binding to the NNMT substrate pocket, the resulting suppression of 1-methylnicotinamide (1-MNA) production, and downstream shifts in NAD⁺ salvage, lipid handling, and energy-metabolism research endpoints (Neelakantan et al., 2018, Biochemical Pharmacology).

Beyond enzyme kinetics, 5-Amino-1MQ is investigated in cellular and animal research models that explore adipocyte differentiation, lipid mobilisation, methyl-donor flux, and inflammatory-pathway signaling within metabolic tissues. Comparative metabolic-pathway research often pairs it with mitochondrial signaling tools and with ERR-targeted metabolic compounds to map overlapping energy-balance endpoints. The small-molecule scaffold, its membrane permeability, and its selectivity over related methyltransferases also make 5-Amino-1MQ a frequent subject of structure-activity research and chemical-biology studies of the NNMT pathway.

The compound is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

See also: SLU-PP-332, NAD⁺, MOTS-c 10 mg

Scientific Background

Nicotinamide N-methyltransferase (NNMT) is a cytosolic enzyme that transfers a methyl group from S-adenosyl-methionine (SAM) to nicotinamide, generating 1-methylnicotinamide (1-MNA) and S-adenosyl-homocysteine (SAH). Through this single reaction, NNMT sits at the intersection of NAD⁺ salvage, methyl-donor balance, and one-carbon metabolism.

Elevated NNMT expression has been reported in adipose tissue under energy-imbalance conditions and in several neoplastic-pathway research models, where it contributes to metabolic reprogramming and altered methylation landscapes. Targeting NNMT has therefore emerged as a focused research strategy for probing the metabolic consequences of nicotinamide depletion in cellular and animal model systems.

5-Amino-1MQ was developed as a selective, membrane-permeable NNMT inhibitor, enabling researchers to dissect NNMT-driven contributions to lipogenesis, adipocyte biology, and methyl-donor cycling in controlled in vitro and in vivo research settings.

Structure

Compound Class:Methylquinolinium small-molecule NNMT inhibitor
IUPAC Name:5-amino-1-methylquinolin-1-ium
Molecular Formula:C₁₀H₁₁N₂⁺
Molecular Weight:159.21 g/mol
CAS Number:685079-15-6
PubChem CID:950107
Synonyms:5-Amino-1MQ, 5A1MQ, NNMTi

Mechanism of Action

1. Selective NNMT Inhibition

5-Amino-1MQ occupies the substrate-binding region of NNMT, competing with nicotinamide and reducing the enzymatic conversion of nicotinamide into 1-methylnicotinamide (1-MNA). This selective binding preserves intracellular nicotinamide pools and shifts methyl-donor flux, providing researchers a clean pharmacological handle on NNMT activity in cellular models.

2. Modulation of NAD⁺ Salvage and Energy Metabolism

By suppressing nicotinamide methylation, 5-Amino-1MQ increases the substrate pool available to nicotinamide phosphoribosyltransferase (NAMPT), supporting NAD⁺ salvage. Research models report associated shifts in NAD⁺-dependent sirtuin signaling, mitochondrial function, and oxidative-metabolism endpoints relevant to energy-metabolism research.

3. Effects on Lipid Handling and Adipocyte Biology

In vitro and in vivo research models indicate that NNMT inhibition by 5-Amino-1MQ is associated with reduced adipocyte differentiation, increased lipolysis, and lower lipid accumulation in adipose tissue. These observations make 5-Amino-1MQ a frequently used probe in metabolic-pathway research focused on energy balance and adipose remodeling.

4. Influence on Methyl-Donor and Inflammatory Signaling

NNMT activity drains the SAM methyl pool and has been linked to inflammatory-pathway signaling in metabolic tissues. By suppressing NNMT, 5-Amino-1MQ rebalances SAM and SAH pools and is reported in research models to modulate cytokine and chemokine signaling in adipose and stromal compartments.

Research Applications

•NNMT enzyme mechanism and selectivity research
•Adipocyte differentiation and lipid-handling studies
•NAD⁺ salvage and sirtuin-pathway research
•Energy-metabolism and metabolic-pathway research models
•Methylation and one-carbon metabolism studies
•Oncology-pathway metabolism research in cellular models

Conclusion

5-Amino-1MQ is a selective NNMT inhibitor with broad relevance across metabolic and chemical-biology research. Through targeted modulation of nicotinamide methylation, methyl-donor flux, and downstream NAD⁺ salvage, it serves as a valuable tool compound for investigating energy-metabolism research, adipose biology, and NNMT-driven pathway research. Its continued use across cellular and animal model systems underscores its position as a reference NNMT-inhibitor scaffold.

References

•Neelakantan H. et al. (2018). Selective and membrane-permeable small molecule inhibitors of nicotinamide N-methyltransferase. Biochemical Pharmacology.
•Kannt A. et al. (2018). Small molecule inhibition of nicotinamide N-methyltransferase for metabolic-pathway research. Scientific Reports.
•Mor-Yossef Moldovan L. et al. (2020). NNMT and adipocyte biomechanical and metabolic regulation in research models. Journal of Cellular Physiology.
•Michalczyk K. et al. (2021). NNMT signaling and adipose tissue metabolic-pathway research. Diagnostics.
•Komatsu M. et al. (2018). NNMT inhibition reverses high-fat-diet metabolic-adaptation in research models. Scientific Reports.
•Roberti A. et al. (2021). Nicotinamide N-methyltransferase: at the intersection of metabolism and chemical biology research. Cell Death Discovery.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.

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