5-Amino-1MQ 50mg

5-Amino-1MQ 50 mg is a synthetic small-molecule research compound investigated in laboratory studies involving nicotinamide N-methyltransferase (NNMT), cellular methylation, nicotinamide metabolism and enzyme-associated biochemical pathways.

Supplied by Grail Formula as a nominal 50 mg laboratory research preparation, 5-Amino-1MQ is supported by independent batch-specific analytical documentation from Liquilabs s.r.o., Czechia.

For research use only — not for human or veterinary use.

 

Product Overview

5-Amino-1MQ, also known as 5-amino-1-methylquinolinium, is a synthetic quinolinium-based compound studied as an experimental inhibitor of nicotinamide N-methyltransferase (NNMT). This enzyme participates in the methylation of nicotinamide and is associated with biochemical pathways involving methyl-group transfer, cellular metabolite regulation and nicotinamide-associated metabolism.

Unlike peptide-based research compounds, 5-Amino-1MQ is a small organic molecule. Its molecular structure and investigated interaction with NNMT make it relevant to experimental enzymology, molecular biochemistry and laboratory studies involving metabolic regulatory mechanisms.

Grail Formula supplies 5-Amino-1MQ 50 mg as a nominal 50 mg research preparation intended exclusively for controlled laboratory investigations and in vitro scientific experimentation.

Independent third-party testing was performed by Liquilabs s.r.o., Czechia. The Certificate of Analysis was published on 11 October 2026 and identifies production batch GF-5AM50-B243, laboratory sample LYO-1011.

The analytical report documents a measured compound assay content of 51.2 mg ± 0.3 mg and chromatographic purity of greater than 99.8 %.

The measured quantity exceeds the nominal 50 mg designation by 1.2 mg, representing a positive difference of 2.4 %. This difference is disclosed separately from the chromatographic purity result.

The Certificate of Analysis also reports molecular identity-related measurements, bacterial endotoxin concentration, microbiological counts and screening results for seven elemental impurities.

These measurements provide batch-specific analytical information about the tested material. They do not establish biological activity, enzyme inhibition potency, sterility or suitability for administration.

 

Compound Overview

5-Amino-1MQ belongs to the family of substituted quinolinium compounds and is investigated in biochemical research involving NNMT-associated enzymatic activity.

Its chemical designation, 5-amino-1-methylquinolinium, describes a quinolinium structure containing an amino substituent and a methyl group associated with the nitrogen-containing aromatic system.

This defined molecular framework distinguishes 5-Amino-1MQ from peptide hormones, protein fragments and amino acid-based regulatory peptides.

The compound is of scientific interest because of its investigated interaction with nicotinamide N-methyltransferase, a cytosolic enzyme that catalyses methyl-group transfer reactions involving nicotinamide.

In the NNMT-catalysed reaction, nicotinamide acts as a methyl acceptor while S-adenosyl-L-methionine (SAM) serves as the methyl donor. The reaction produces 1-methylnicotinamide and S-adenosyl-L-homocysteine (SAH).

This biochemical process connects nicotinamide metabolism with cellular methyl-donor utilisation and the formation of methylated metabolites.

Researchers investigate NNMT to better understand how enzymatic methylation reactions contribute to intracellular biochemical networks and metabolic regulation.

5-Amino-1MQ provides a compound of interest for experimental studies examining NNMT inhibition, enzyme-substrate interactions and the biochemical consequences of altered methyltransferase activity.

Its small-molecule characteristics also make it relevant to analytical chemistry investigations involving chromatographic separation, molecular ion identification and quantitative compound analysis.

The supplied Liquilabs report identifies a molecular ion mass of 159 Da ± 1 Da. This value is reported as an analytical identity measurement and must not be confused with the measured assay quantity of 51.2 mg.

The specific chemical form, including any associated counterion, is not separately established in the COA summary and should not be inferred solely from the reported molecular ion mass.

 

Historical Background and Scientific Context

Scientific investigation of nicotinamide metabolism developed alongside advances in enzymology, vitamin-associated biochemistry and the understanding of intracellular metabolic regulation.

Nicotinamide, a form of vitamin B3, participates in biochemical pathways associated with nicotinamide adenine dinucleotide (NAD+) metabolism and cellular cofactor regulation.

As researchers characterised nicotinamide-associated reactions, increasing attention was directed toward enzymes responsible for converting nicotinamide into other metabolites.

Nicotinamide N-methyltransferase became an important subject of biochemical investigation because of its role in transferring methyl groups from SAM to nicotinamide.

Research into NNMT contributed to understanding the relationship between methyltransferase activity, methyl-donor availability and intracellular metabolic pathways.

Advances in molecular biology subsequently enabled researchers to investigate NNMT expression and enzymatic activity in different experimental systems.

Studies examined associations between NNMT and biochemical processes involving adipose tissue, cellular metabolism, metabolic adaptation and methylation-associated regulatory mechanisms.

These investigations generated scientific interest in compounds capable of modifying NNMT-associated enzymatic activity under controlled experimental conditions.

The development of small-molecule NNMT inhibitors provided researchers with additional experimental tools for studying the contribution of this enzyme to biochemical networks.

5-Amino-1MQ emerged within this research field as a quinolinium-based compound investigated for its inhibitory interaction with NNMT.

Preclinical investigations have examined NNMT inhibition in biochemical assays, cellular systems and experimental models involving metabolic regulation.

Such research is valuable for exploring relationships between enzyme activity and experimentally measured metabolic responses. However, findings depend on the individual experimental system, compound characteristics and selected analytical endpoints.

Modern analytical techniques, including liquid chromatography and mass spectrometry, have further improved the ability to characterise small-molecule NNMT research compounds.

These methods help distinguish compound identity, chromatographic purity and measured assay content as separate analytical characteristics.

Contemporary research continues to investigate NNMT as part of broader biochemical networks involving nicotinamide utilisation, methyl-group metabolism and intracellular metabolic regulation.

Although 5-Amino-1MQ is associated with this scientific literature, the supplied Grail Formula Certificate of Analysis does not contain biological activity testing and therefore does not independently establish NNMT inhibitory potency for the tested batch.

 

Mechanistic Focus in Research

The principal mechanistic research interest surrounding 5-Amino-1MQ concerns its investigated interaction with nicotinamide N-methyltransferase and the biochemical pathways associated with NNMT-mediated methylation.

Nicotinamide N-methyltransferase inhibition

NNMT is a methyltransferase enzyme involved in the conversion of nicotinamide to 1-methylnicotinamide through a SAM-dependent methylation reaction.

Experimental NNMT inhibition provides researchers with a method for examining how changes in enzymatic activity influence substrate utilisation and methylated metabolite formation.

Laboratory investigations may involve purified enzyme systems, biochemical activity assays and analytical measurements of reaction products.

Researchers can use these experimental approaches to investigate enzyme-associated reaction kinetics, inhibitor interactions and the biochemical characteristics of NNMT-mediated methyl transfer.

Cellular methylation and methyl-donor metabolism

Methylation reactions are fundamental biochemical processes involving the transfer of methyl groups between molecular substrates.

Because NNMT uses SAM as a methyl donor, its enzymatic activity is relevant to investigations involving methyl-group utilisation and the relationship between SAM and SAH metabolism.

Laboratory studies may examine how experimental changes in NNMT activity are associated with alterations in methylated metabolite concentrations and related biochemical measurements.

These investigations contribute to understanding the interactions between individual methyltransferase reactions and broader intracellular metabolic networks.

Nicotinamide-associated biochemical pathways

Nicotinamide is connected to pathways involving NAD+, an essential cofactor participating in numerous cellular biochemical reactions.

NNMT-mediated methylation represents one route of nicotinamide metabolism, making the enzyme relevant to research involving nicotinamide utilisation and metabolite distribution.

Experimental investigations may examine the relationship between NNMT-associated reactions and nicotinamide-dependent metabolic pathways.

However, NNMT inhibition does not automatically establish a predictable change in NAD+ concentrations. Such outcomes require direct experimental measurement and interpretation within the relevant biological model.

Experimental cellular metabolism

NNMT has been investigated in research models involving cellular metabolic regulation and changes in enzyme-associated biochemical activity.

These studies may involve cultured cells, controlled biochemical systems and analytical profiling of metabolites associated with methylation and nicotinamide metabolism.

Researchers examine these models to distinguish direct enzyme-related changes from broader metabolic responses.

The observed effects may depend on inhibitor concentration, enzyme expression, cellular environment, experimental duration and the analytical methods employed.

Small-molecule structure and enzyme interactions

The quinolinium structure of 5-Amino-1MQ makes it relevant to studies examining how molecular characteristics influence interactions with enzyme-associated binding environments.

Structure-activity relationship research investigates how modifications to molecular structures may alter experimentally measured biochemical interactions.

Such studies can contribute to the understanding of compound selectivity, molecular recognition and enzyme inhibition mechanisms.

Analytical limitations of the supplied batch

The Liquilabs Certificate of Analysis provides chemical characterisation and selected impurity measurements for the tested 5-Amino-1MQ sample.

It does not report NNMT inhibition potency, IC50 values, enzyme selectivity, cellular metabolite responses or other functional biological activity measurements.

Accordingly, the mechanistic research topics described above represent established areas of scientific investigation associated with 5-Amino-1MQ and NNMT biology, rather than experimentally confirmed functional properties of this particular Grail Formula batch.

 

Analytical Verification (COA)

Grail Formula provides independent batch-specific analytical documentation through testing conducted by Liquilabs s.r.o., Czechia.

The Certificate of Analysis for 5-Amino-1MQ 50 mg was published on 11 October 2026 and identifies batch GF-5AM50-B243, laboratory sample LYO-1011.

The 13-page report includes compound assay results, chromatographic purity assessment, identity-related measurements, mass spectrometry, bacterial endotoxin testing, microbiological counts and elemental impurity screening.

Compound assay and chromatographic purity

• Nominal product quantity: 50 mg
• Measured 5-amino-1-methylquinolinium assay content: 51.2 mg ± 0.3 mg
• Reported chromatographic purity: greater than 99.8 %
• Measured difference from nominal quantity: 1.2 mg above the labelled 50 mg
• Measured assay as a proportion of nominal quantity: 102.4 %
• Analytical screening designation: Peptide Screening 0.1% TFA, as reported by Liquilabs

The measured assay content exceeds the nominal quantity by 2.4 %. This positive difference is a batch-specific analytical finding and is reported separately from the chromatographic purity measurement.

The reported purity greater than 99.8 % describes the chromatographic composition under the applied analytical conditions. It does not mean that 99.8 % of the nominal 50 mg quantity was recovered.

Although the COA uses the designation Peptide Screening 0.1% TFA, 5-Amino-1MQ is chemically a small-molecule compound rather than a peptide.

The report also includes supporting UHPLC analytical documentation, calibration information and chromatographic records relating to compound content and purity assessment.

Compound identity assessment

• FTIR spectrum identification result: 991 ± 5, as reported
• Retention time identification result: 0.992 ± 0.005, as reported
• Molecular ion mass identification: 159 Da ± 1 Da
• Mass spectrometry identity assessment: MS deconvolution

The Certificate of Analysis includes chromatographic and mass spectrometric documentation supporting the analytical characterisation of the tested compound.

The FTIR and retention time values are reproduced as reported. The summary does not provide separate explicit pass/fail interpretations for these identification measurements.

The molecular ion mass of 159 Da is an identity-related analytical result and is distinct from the measured compound assay content expressed in milligrams.

Bacterial endotoxin assessment

• Bacterial endotoxin: 0.350 EU/mg
• Reported uncertainty: ± 0.007 EU/mg
• Laboratory acceptable range: 0–0.5 EU/mg
• Analytical reference: USP <85> / European Pharmacopoeia 2.6.14
• Method: Chromogenic bacterial endotoxin testing

The bacterial endotoxin concentration of 0.350 EU/mg represents 70 % of the laboratory’s stated upper acceptable limit of 0.5 EU/mg.

This is a measurable endotoxin result and should not be represented as an absence of bacterial endotoxins.

Although the result falls within the stated laboratory range, it does not establish sterility, biological safety or suitability for administration.

Microbiological assessment

• Total aerobic microbial count: 0 CFU/g
• Total yeast and mould count: 0 CFU/g
• Reported aerobic microbial count range: 0–1000 CFU/g
• Reported yeast and mould count range: 0–100 CFU/g
• Analytical reference: USP <61> / European Pharmacopoeia 2.6.12
• Method: Plate-count testing

Both microbiological counts were reported as zero under the applied laboratory testing conditions.

The accompanying analytical documentation describes the microbiological methodology, including sample preparation, culture conditions and evaluation of colony-forming units.

These results describe the tested sample and do not demonstrate the absence of every possible microorganism.

Elemental impurity screening

Seven elemental impurities were evaluated using procedures referenced to USP <232> and European Pharmacopoeia 5.20 / 2.4.20.

• Arsenic: below 0.001 ppm
• Cadmium: below 0.001 ppm
• Mercury (listed as quicksilver): below 0.001 ppm
• Lead: below 0.001 ppm
• Nickel: below 0.001 ppm
• Vanadium: below 0.001 ppm
• Cobalt: below 0.001 ppm

All seven reported elemental impurity concentrations were below 0.001 ppm and within their respective laboratory acceptable ranges.

Values below the analytical reporting threshold indicate concentrations below that threshold rather than confirmation of absolute absence.

The complete Certificate of Analysis includes 13 pages of analytical findings and supporting documentation. The results apply to the tested sample and should not automatically be interpreted as evidence of identical characteristics across unrelated batches.

 

Research Applications

5-Amino-1MQ is investigated in experimental enzymology, molecular biochemistry and laboratory research involving NNMT-associated metabolic pathways.

Its relevance to scientific research arises from its investigated interaction with nicotinamide N-methyltransferase and the biochemical reactions associated with nicotinamide methylation.

Potential areas of laboratory investigation include:

• Nicotinamide N-methyltransferase (NNMT) inhibition research
• Experimental enzyme activity and inhibition assays
• Nicotinamide-associated metabolic pathway studies
• S-adenosyl-L-methionine and methyl-donor metabolism research
• 1-Methylnicotinamide formation and metabolite analysis
• Cellular methylation-associated biochemical investigations
• Experimental NAD+ pathway research
• Small-molecule inhibitor characterisation
• Quinolinium compound structure-activity relationship studies
• Analytical chromatography and molecular identity assessment
• Comparative biochemical research involving methyltransferase enzymes

These applications describe scientific research directions and do not constitute evidence of demonstrated biological activity for the tested batch.

Experimental investigations require suitable analytical controls, appropriate reference materials and validated methods for evaluating compound-associated biochemical responses.

Batch-specific Certificate of Analysis documentation can support laboratory recordkeeping and provide researchers with information about the reported analytical characteristics of the preparation.

 

Grail Formula Quality

Grail Formula focuses on supplying laboratory research compounds supported by transparent product information and independent analytical documentation.

For 5-Amino-1MQ 50 mg, Liquilabs testing provides batch-specific information concerning measured compound content, chromatographic purity, analytical identity, bacterial endotoxin concentration, microbiological counts and elemental impurity screening.

The report documents a measured assay content of 51.2 mg against the nominal 50 mg quantity, chromatographic purity greater than 99.8 % and bacterial endotoxin concentration of 0.350 EU/mg.

These measurements are presented separately to maintain a clear distinction between compound quantity, chromatographic composition and microbiological characteristics.

Each analytical result should be interpreted within the scope of the tested sample, the applied laboratory methodology and the reported measurement uncertainty.

Transparent presentation of both analytical findings and limitations supports responsible scientific documentation.

 

When You Choose Grail Formula

Grail Formula provides 5-Amino-1MQ 50 mg with independent batch-specific analytical documentation from Liquilabs s.r.o., Czechia.

Researchers can review the Certificate of Analysis to examine the reported compound assay, chromatographic purity, identity assessment, microbiological findings and elemental impurity results.

The report identifies the production batch, laboratory sample and publication date, supporting analytical traceability and research documentation.

Grail Formula emphasises factual compound descriptions, scientific context and transparent reporting of laboratory findings rather than unsupported biological activity claims.

For research involving NNMT-associated biochemical pathways, this documentation provides a reference for the measured characteristics of the tested 5-Amino-1MQ preparation.

Research Use Limitation

Used solely for in vitro experiments and cannot be:

• Used in clinical trials involving humans
• Administered to humans as part of an experiment or investigation
• Supplied to another party for human investigational use.

• Independently analysed by Liquilabs s.r.o. Czechia
• 5-Amino-1MQ research compound with nominal 50 mg quantity
• Chromatographic purity greater than 99.8 % reported by COA
• Assay content measured at 51.2 mg ± 0.3 mg
• Measured assay content 2.4 % above nominal quantity
• Identification evaluated by FTIR spectrum and retention time analysis
• FTIR spectrum identification result: 991 ± 5
• Retention time identification result: 0.992 ± 0.005
• Molecular ion mass identified at 159 Da ± 1 Da
• Bacterial endotoxin level of 0.350 EU/mg ± 0.007 EU/mg
• Total aerobic microbial count: 0 CFU/g
• Total yeast and mould count: 0 CFU/g
• All seven reported elemental impurities below 0.001 ppm
• Batch number: GF-5AM50-B243
• Laboratory sample identification: LYO-1011
• COA publication date: 11 October 2026
• Independent 13-page batch-specific Certificate of Analysis
• Synthetic quinolinium-based small-molecule research compound
• Investigated in NNMT enzyme inhibition and nicotinamide metabolism research
• Relevant to laboratory studies involving methylation-associated biochemical pathways
• For research use only – not for human or veterinary use

For laboratory research only. Not intended for human consumption, injection, or cosmetic use.

This product is for research purposes only. Not for human use or diagnostic/therapeutic applications. Keep out of reach of children.