MOTS‑c 10mg

MOTS-C 10 mg is a synthetic mitochondrial-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 regulatory pathways.

Supplied as a nominal 10 mg peptide 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.

Unlike many peptides encoded by nuclear DNA, MOTS-C is associated with a short open reading frame within the mitochondrial 12S ribosomal RNA region. This distinctive molecular origin has attracted scientific interest in mitochondrial genome biology and communication between mitochondria and cellular regulatory systems.

Grail Formula supplies MOTS-C 10 mg as a nominal 10 mg 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-MOTSC10-B242 and laboratory sample LYO-1000.

The analytical report documents a measured MOTS-C assay content of 8.88 mg ± 0.04 mg and chromatographic purity of 99.3 % ± 0.5 percentage points.

The measured assay content is 1.12 mg below the nominal 10 mg designation, representing an 11.2 % shortfall. This difference is reported separately from chromatographic purity.

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

These results describe the analytical characteristics of the tested sample and do not independently establish biological activity, experimental potency or specific cellular responses.

 

Peptide Overview

MOTS-C is a 16-amino-acid mitochondria-derived peptide investigated in experimental research involving metabolic signalling, mitochondrial communication and intracellular biochemical regulation.

Its identification contributed to the expanding field of mitochondrial-derived peptides, a group of molecules associated with short open reading frames within mitochondrial genetic material.

Mitochondria are central components of cellular energy metabolism and participate in biochemical processes involving ATP production, metabolic substrate utilisation and intracellular signalling.

Beyond their established role in energy metabolism, mitochondria are investigated as signalling organelles capable of participating in communication with other cellular compartments.

MOTS-C has attracted scientific attention because its mitochondrial genetic origin provides a research model for examining relationships between mitochondrial gene expression and broader cellular regulatory pathways.

Experimental studies have investigated MOTS-C-associated responses involving metabolic stress signalling, cellular energy sensing and interactions between mitochondrial and nuclear regulatory systems.

These investigations include research into pathways associated with AMP-activated protein kinase (AMPK), intracellular metabolic adaptation and cellular responses to experimentally induced changes in energy availability.

MOTS-C has also been studied in experimental models involving nucleotide metabolism and biochemical pathways associated with cellular metabolic regulation.

However, these mechanisms are dependent on the biological model, experimental conditions and analytical endpoints used. They should not be interpreted as independently demonstrated properties of the Grail Formula research preparation.

The Liquilabs Certificate of Analysis identifies a molecular ion mass of 2174 Da ± 1 Da, supporting the reported mass spectrometric characterisation of the tested peptide.

This molecular identity-related measurement is separate from the chromatographic purity result and the measured peptide assay quantity.

 

Historical Background and Scientific Context

Scientific investigation of mitochondrial biology originally focused 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, distinct from nuclear DNA, and contribute to the production of essential components of the mitochondrial protein synthesis system.

For many years, mitochondrial genetic research concentrated primarily on genes encoding respiratory-chain proteins, ribosomal RNAs and transfer RNAs.

Advances in molecular genetics subsequently encouraged investigations into additional mitochondrial open reading frames and their potential contribution to cellular regulatory processes.

The identification of mitochondrial-derived peptides expanded scientific understanding of the mitochondrial genome as a possible source of short biologically relevant molecular sequences.

MOTS-C was described in scientific research published in 2015 and became an important subject of investigation within this developing field.

Researchers examined its mitochondrial genetic origin and investigated its relationship with metabolic regulatory pathways in experimental cellular and preclinical systems.

These studies contributed to broader scientific interest in communication between mitochondrial processes and nuclear-associated cellular regulation.

Subsequent investigations explored MOTS-C in connection with metabolic stress responses, intracellular signalling and experimentally measured changes in cellular biochemical activity.

Scientific attention also expanded toward the relationship between mitochondrial-derived peptides and cellular adaptation to different experimental environments.

Research involving MOTS-C has contributed to the study of how mitochondrial-associated molecular signals may interact with broader metabolic networks.

At the same time, advances in peptide synthesis, chromatography and mass spectrometry have enabled laboratories to characterise synthetic peptide preparations through independent analytical testing.

Modern peptide characterisation distinguishes between molecular identity, chromatographic purity and measured peptide content rather than treating these measurements as interchangeable.

For research compounds such as MOTS-C, these distinctions are important because a high chromatographic purity percentage does not necessarily establish that the nominal peptide quantity is present.

Contemporary scientific investigations continue to examine mitochondrial-derived peptides within the broader context of mitochondrial signalling, molecular metabolism and experimental cellular regulation.

 

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 understand potential relationships between mitochondrial gene expression, intracellular communication and cellular regulatory mechanisms.

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

AMPK-associated cellular signalling

AMP-activated protein kinase is an important cellular energy-sensing enzyme involved in regulating biochemical responses to changes in 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 mitochondrial-derived molecular signals may interact with intracellular energy-sensing systems.

The presence, direction and magnitude of experimentally observed responses depend on the model and measurement conditions 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, gene expression and intracellular signalling intermediates to characterise these relationships.

Mitochondrial and nuclear communication

Mitochondrial-to-nuclear communication is an important area of molecular biology research involving the exchange of regulatory information between cellular compartments.

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

These studies contribute to scientific understanding of mitochondrial signalling without establishing that every MOTS-C preparation produces equivalent cellular effects.

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 participate in broader intracellular metabolic networks and provide experimental contexts for investigating peptide-associated metabolic regulation.

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

Peptide structure and molecular characterisation

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

Methods such as high-performance liquid chromatography and mass spectrometry provide information about the chemical characteristics of peptide research materials.

The supplied Liquilabs Certificate of Analysis documents the tested MOTS-C preparation through chromatographic purity assessment, quantitative assay and molecular identity-related measurements.

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-MOTSC10-B242.

 

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 10 mg was published on 11 October 2026 and identifies production batch GF-MOTSC10-B242, laboratory sample LYO-1000.

The 13-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: 10 mg
• Measured MOTS-C assay content: 8.88 mg ± 0.04 mg
• Reported chromatographic purity: 99.3 % ± 0.5 percentage points
• Measured assay difference from nominal quantity: 1.12 mg below the labelled 10 mg
• Measured assay as a proportion of nominal quantity: 88.8 %
• Analytical screening designation: Peptide Screening 0.1% TFA

The measured assay content represents an 11.2 % shortfall relative to the nominal 10 mg quantity. This batch-specific difference is disclosed independently of the chromatographic purity result.

The reported 99.3 % chromatographic purity describes the relative composition measured under the applied chromatographic conditions. It does not indicate that 99.3 % of the nominal 10 mg quantity was recovered.

The supporting analytical documentation includes chromatographic method specifications, calibration information and UHPLC analytical records.

Peptide identity assessment

• FTIR spectrum identification result: 964 ± 5, as reported
• Retention time identification result: 0.996 ± 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 spectrum identification 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 2174 Da is an identity-related analytical measurement and must not be confused with the peptide assay content expressed in milligrams.

Bacterial endotoxin assessment

• Bacterial endotoxin: 0.009 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 0.009 EU/mg falls within the laboratory’s stated acceptable range.

The reported result is measurable and should not be represented as an 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.

This finding 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 results 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 13 pages of analytical findings and supporting documentation, including chromatographic records, mass spectrometric data, endotoxin determination information and microbiological testing methodology.

The reported findings relate 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 10 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 8.88 mg against the nominal 10 mg quantity, chromatographic purity of 99.3 % and bacterial endotoxin concentration of 0.009 EU/mg.

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

The measured assay shortfall 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 10 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 10 mg quantity
• Chromatographic purity: 99.3 % ± 0.5 percentage points
• Assay content measured at 8.88 mg ± 0.04 mg
• Measured assay content 11.2 % below nominal quantity
• Identification evaluated by FTIR spectrum and retention time analysis
• FTIR spectrum identification result: 964 ± 5
• Retention time identification result: 0.996 ± 0.005
• Molecular ion mass identified at 2174 Da ± 1 Da
• Bacterial endotoxin level of 0.009 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-MOTSC10-B242
• Laboratory sample identification: LYO-1000
• COA publication date: 11 October 2026
• Independent 13-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.