MOTS-c 40mg

MOTS-C 40 mg is a synthetic mitochondria-derived peptide research compound supplied by Grail Formula for scientific investigation and controlled laboratory experimentation involving mitochondrial signalling, cellular metabolism, metabolic stress responses and peptide-associated biochemical regulatory pathways.

Supplied as a nominal 40 mg research preparation, MOTS-C is accompanied by independent batch-specific analytical documentation from Liquilabs s.r.o., Czechia.

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

 

Product Overview

MOTS-C, also known as mitochondrial open reading frame of the 12S rRNA-c peptide, is a mitochondria-derived peptide investigated in molecular biology, mitochondrial biochemistry and experimental cellular metabolism research.

Its mitochondrial genetic origin distinguishes MOTS-C from many conventional peptide research compounds encoded by nuclear DNA. This characteristic has attracted scientific interest in mitochondrial genome biology and the relationship between mitochondrial gene expression and intracellular regulatory processes.

Grail Formula supplies MOTS-C 40 mg as a nominal 40 mg peptide research preparation intended exclusively for controlled laboratory investigations and in vitro scientific experimentation.

Independent third-party analytical testing was conducted by Liquilabs s.r.o., Czechia. The Certificate of Analysis, published on 11 October 2026, identifies production batch GF-MOTSC40-B243 and laboratory sample LYO-1001.

The analytical report documents a measured MOTS-C assay content of 43.3 mg ± 0.2 mg and chromatographic purity of 99.6 % ± 0.5 percentage points.

The measured assay content exceeds the nominal 40 mg designation by 3.3 mg, representing a positive difference of 8.25 %. This result is disclosed separately from the chromatographic purity measurement.

The Certificate of Analysis also includes FTIR spectrum identification, retention time assessment, molecular ion mass identification, bacterial endotoxin determination, microbiological counts and elemental impurity screening.

These measurements provide batch-specific analytical information about the tested peptide preparation. They do not independently establish biological activity, experimental potency or particular cellular responses.

 

Peptide Overview

MOTS-C is a 16-amino-acid mitochondria-derived peptide associated with a short open reading frame within the mitochondrial 12S ribosomal RNA region.

Its discovery contributed to the expanding field of mitochondrial-derived peptide research, which investigates molecular sequences associated with mitochondrial genetic material and their potential involvement in cellular regulatory processes.

Mitochondria are essential organelles involved in cellular energy metabolism, oxidative phosphorylation, ATP production and numerous biochemical reactions.

Beyond energy production, mitochondria participate in intracellular communication and are investigated as components of complex cellular signalling networks.

MOTS-C has attracted scientific interest because its mitochondrial genetic origin provides a model for studying relationships between mitochondrial gene expression and broader cellular metabolic regulation.

Experimental investigations have examined MOTS-C-associated processes involving cellular energy sensing, metabolic stress responses and communication between mitochondrial and nuclear regulatory systems.

Research has also explored associations between MOTS-C and pathways involving AMP-activated protein kinase (AMPK), nucleotide metabolism and intracellular biochemical adaptation.

These investigations contribute to understanding how mitochondria-associated molecular signals may participate in cellular regulatory processes under defined experimental conditions.

However, the biological behaviour of MOTS-C depends on the research model, experimental environment and analytical endpoints employed.

Findings from published experimental research should not be interpreted as independently demonstrated biological properties of the Grail Formula MOTS-C 40 mg preparation.

The Liquilabs Certificate of Analysis identifies a molecular ion mass of 2174 Da ± 1 Da, providing an identity-related analytical measurement for the tested peptide.

This result is distinct from both the measured peptide quantity of 43.3 mg and the chromatographic purity of 99.6 %.

 

Historical Background and Scientific Context

Scientific investigation of mitochondrial biology originally concentrated on cellular respiration, oxidative phosphorylation and the biochemical mechanisms involved in energy production.

As molecular biology developed, researchers established that mitochondria contain their own genetic material, separate from nuclear DNA.

Early mitochondrial genetic research focused primarily on genes encoding respiratory-chain proteins, ribosomal RNAs and transfer RNAs.

Advances in molecular genetics subsequently encouraged investigations into additional open reading frames and previously uncharacterised molecular sequences within mitochondrial genetic material.

The identification of mitochondrial-derived peptides expanded scientific interest in the mitochondrial genome as a potential source of short molecular sequences associated with cellular regulation.

MOTS-C was described in scientific research published in 2015 and became an important subject within this developing area of mitochondrial peptide biology.

Initial experimental investigations examined its mitochondrial genetic origin and explored relationships with metabolic regulatory pathways in cellular and preclinical research systems.

These studies contributed to broader scientific interest in mitochondrial-to-nuclear communication and the possibility that mitochondrial-associated peptides participate in intracellular regulatory networks.

Subsequent investigations examined MOTS-C-associated processes in relation to metabolic stress signalling, cellular energy sensing and experimentally measured biochemical responses.

Research also expanded toward understanding how mitochondrial-derived molecular signals may interact with pathways involved in cellular adaptation to changing experimental conditions.

Scientific investigations involving MOTS-C have contributed to the study of relationships between mitochondrial genome biology, intracellular signalling and metabolic regulatory mechanisms.

At the same time, advances in synthetic peptide chemistry and analytical instrumentation have improved the ability to characterise peptide research materials.

High-performance liquid chromatography, ultra-high-performance liquid chromatography and mass spectrometry provide methods for examining peptide composition, molecular identity and quantitative assay content.

These analytical techniques allow researchers to distinguish between chromatographic purity, molecular identity and the actual measured quantity of a peptide preparation.

This distinction is particularly relevant for batch-specific research documentation because a high chromatographic purity percentage does not necessarily indicate that the nominal peptide quantity has been recovered.

Contemporary research continues to investigate mitochondrial-derived peptides within the broader fields of mitochondrial signalling, molecular metabolism and experimental cellular regulatory biology.

 

Mechanistic Focus in Research

The principal mechanistic research interest surrounding MOTS-C concerns its association with mitochondrial-derived signalling and the biochemical pathways involved in cellular metabolic regulation.

Mitochondrial-derived peptide signalling

MOTS-C is investigated as part of the broader mitochondrial-derived peptide research field, which examines molecular signals associated with mitochondrial genetic material.

Researchers study these peptides to better understand relationships between mitochondrial gene expression, intracellular communication and cellular regulatory mechanisms.

Experimental investigations may examine molecular signalling markers, metabolic enzyme activity and cellular responses under defined laboratory conditions.

AMPK-associated cellular signalling

AMP-activated protein kinase is an important intracellular energy-sensing enzyme involved in regulating biochemical responses to changes in cellular energy availability.

Experimental research has investigated MOTS-C-associated signalling in relation to AMPK and downstream metabolic regulatory pathways.

These investigations contribute to understanding how mitochondria-derived molecular signals may interact with cellular energy-sensing systems.

The direction and magnitude of experimentally observed responses depend on the biological model, peptide preparation and analytical methods employed.

Cellular metabolic stress research

Cells respond to changes in nutrient availability, energy status and other experimental stress conditions through interconnected biochemical signalling pathways.

MOTS-C has been investigated in research models involving metabolic stress-associated responses and changes in cellular regulatory activity.

Laboratory studies may examine biochemical markers, intracellular signalling intermediates and gene expression to characterise these relationships.

These investigations provide scientific context for studying cellular adaptation and mitochondrial-associated regulatory processes.

Mitochondrial-to-nuclear communication

Mitochondrial-to-nuclear communication is an important area of molecular biology involving regulatory interactions between cellular compartments.

Experimental investigations have explored MOTS-C-associated processes in connection with nuclear regulatory responses under certain metabolic stress conditions.

Researchers examine these mechanisms to better understand how mitochondrial-associated molecular signals may participate in broader cellular regulatory networks.

Such findings remain specific to the experimental models in which they were observed.

Nucleotide and folate-associated metabolic pathways

Scientific investigations have examined MOTS-C in relation to biochemical pathways involving nucleotide metabolism and folate-associated reactions.

These pathways contribute to broader intracellular metabolic networks and provide experimental contexts for studying peptide-associated biochemical regulation.

Researchers may use metabolite profiling, biochemical assays and molecular measurements to investigate changes in these systems.

Peptide structure and molecular characterisation

MOTS-C is also relevant to analytical investigations involving synthetic peptide identity, chromatographic separation and molecular mass determination.

Analytical techniques such as UHPLC and mass spectrometry provide information about the chemical characteristics of peptide research preparations.

The supplied Liquilabs Certificate of Analysis documents chromatographic purity, quantitative assay content and molecular identity-related measurements for the tested MOTS-C sample.

However, the report does not contain AMPK activation assays, mitochondrial functional measurements, cellular metabolic response data or other biological activity testing.

Accordingly, the mechanistic research topics described above represent scientific research areas associated with MOTS-C rather than experimentally confirmed functional properties of batch GF-MOTSC40-B243.

 

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 MOTS-C 40 mg was published on 11 October 2026 and identifies production batch GF-MOTSC40-B243, laboratory sample LYO-1001.

The 14-page report includes peptide assay results, chromatographic purity assessment, FTIR spectrum identification, retention time assessment, mass spectrometry, bacterial endotoxin testing, microbiological counts and elemental impurity screening.

Peptide assay and chromatographic purity

• Nominal product quantity: 40 mg
• Measured MOTS-C assay content: 43.3 mg ± 0.2 mg
• Reported chromatographic purity: 99.6 % ± 0.5 percentage points
• Measured assay difference from nominal quantity: 3.3 mg above the labelled 40 mg
• Measured assay as a proportion of nominal quantity: 108.25 %
• Analytical screening designation: Peptide Screening 0.1% TFA

The measured assay content exceeds the nominal quantity by 8.25 %. This positive difference is a batch-specific analytical finding and is disclosed independently of the chromatographic purity measurement.

The reported purity of 99.6 % describes the chromatographic composition under the applied analytical conditions. It does not mean that 99.6 % of the nominal 40 mg quantity was recovered.

The supporting analytical documentation includes UHPLC method specifications, calibration information and chromatographic records relating to peptide content and purity assessment.

Peptide identity assessment

• FTIR spectrum identification result: 978 ± 5, as reported
• Retention time identification result: 0.999 ± 0.005, as reported
• Molecular ion mass identification: 2174 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 peptide.

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

The molecular ion mass of 2174 Da is an identity-related analytical result and is distinct from the measured peptide assay content expressed in milligrams.

Bacterial endotoxin assessment

• Bacterial endotoxin: 0.002 EU/mg
• Reported uncertainty: ± 0 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 0.002 EU/mg falls within the laboratory’s stated acceptable range.

This is a measurable analytical result and should not be represented as the complete absence of bacterial endotoxins.

The laboratory’s stated uncertainty of ± 0 is reproduced as reported and should not be interpreted as proof of absolute measurement precision.

The endotoxin result 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 supporting documentation describes microbiological sample preparation, culture conditions, incubation and evaluation of colony-forming units.

These findings apply to 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.

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

The complete Certificate of Analysis contains 14 pages of analytical findings and supporting documentation, including chromatographic records, mass spectrometric data, endotoxin determination information and microbiological testing methodology.

The reported findings relate exclusively to the tested sample and should not automatically be applied to unrelated production batches.

 

Research Applications

MOTS-C is investigated in experimental mitochondrial biology, cellular metabolism and peptide-associated molecular signalling research.

Its scientific relevance arises from its mitochondrial genetic origin and its investigated relationship with cellular energy-sensing and metabolic regulatory pathways.

Potential areas of laboratory investigation include:

• Mitochondrial-derived peptide research
• Mitochondrial genome-associated signalling investigations
• Experimental cellular metabolism research
• AMPK-associated intracellular signalling pathways
• Mitochondrial-to-nuclear communication studies
• Cellular metabolic stress response investigations
• Nucleotide and folate-associated metabolic pathway research
• Peptide structure and molecular identity characterisation
• Chromatographic purity and quantitative peptide analysis
• Comparative laboratory studies involving mitochondrial-derived peptides

These applications describe scientific research directions rather than demonstrated biological activity of the tested batch.

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

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

 

Grail Formula Quality

Grail Formula focuses on supplying laboratory research compounds supported by transparent product information and independently documented analytical findings.

For MOTS-C 40 mg, Liquilabs testing provides batch-specific information concerning peptide assay content, chromatographic purity, analytical identity, bacterial endotoxin concentration, microbiological counts and selected elemental impurities.

The report documents a measured assay content of 43.3 mg against the nominal 40 mg quantity, chromatographic purity of 99.6 % and bacterial endotoxin concentration of 0.002 EU/mg.

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

The positive assay difference is disclosed transparently as part of the batch-specific analytical profile.

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

 

When You Choose Grail Formula

Grail Formula provides MOTS-C 40 mg with independent batch-specific analytical documentation from Liquilabs s.r.o., Czechia.

Researchers can review the Certificate of Analysis to examine the reported peptide assay, chromatographic purity, FTIR spectrum identification, retention time assessment, molecular ion mass, 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 peptide descriptions, scientific context and transparent reporting of laboratory findings rather than unsupported biological activity claims.

For laboratory research involving mitochondrial-derived peptides and cellular metabolic signalling, this documentation provides a reference for the measured characteristics of the tested MOTS-C 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
• MOTS-C mitochondrial-derived peptide research compound with nominal 40 mg quantity
• Chromatographic purity: 99.6 % ± 0.5 percentage points
• Assay content measured at 43.3 mg ± 0.2 mg
• Measured assay content 8.25 % above nominal quantity
• Identification evaluated by FTIR spectrum and retention time analysis
• FTIR spectrum identification result: 978 ± 5
• Retention time identification result: 0.999 ± 0.005
• Molecular ion mass identified at 2174 Da ± 1 Da
• Bacterial endotoxin level of 0.002 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-MOTSC40-B243
• Laboratory sample identification: LYO-1001
• COA publication date: 11 October 2026
• Independent 14-page batch-specific Certificate of Analysis
• Investigated in mitochondrial-derived peptide and cellular metabolic signalling research
• Relevant to controlled laboratory studies involving mitochondrial regulatory 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.