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MOTS-c | CAS: 1627580-64-6

CAS Number:
1627580-64-6
Chemical Classification:
Research peptide

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MOTS-c (CAS 1627580-64-6) is a mitochondria-encoded peptide that has drawn interest for its reported role in metabolic stress adaptation and exercise-mimetic signaling pathways. Because mitochondrial peptide biology spans organelle bioenergetics and systemic glucose handling, experimental readouts range from OCR measurements in myotubes to whole-body glucose-tolerance shifts in active versus sedentary rodent cohorts. Typical bench scenarios include AMPK phosphorylation time courses in C2C12 cultures, palmitate-challenge survival assays, and acute intraperitoneal dosing before treadmill exhaustion testing. Research-grade characterization follows COA, LC-MS, HPLC, and NMR standards.

CAS
1627580-64-6
Molecular Formula
C101H152N28O22S2
Molecular Weight
2174.6 g/mol
Purity
≥98%
Appearance
White lyophilized powder
Storage
Store at -20°C

Analytical Documentation

COA✓ Available
LC-MS✓ Available
HPLC✓ Available
NMR✓ Available

Research Inquiry

Overview

MOTS-c is a mitochondrial-derived peptide encoded within the 12S rRNA gene of the mitochondrial genome, consisting of 16 amino acids that translocate to the nucleus under metabolic stress in research models. Discovered as an exercise-mimetic signaling molecule, MOTS-c regulates glucose and fatty acid metabolism through AMPK activation and nuclear translocation affecting transcriptional programs. Synthetic MOTS-c enables controlled laboratory investigation of mitochondrial-nuclear communication, insulin sensitivity pathways, and aging-associated metabolic decline in cell culture and rodent research. The peptide represents a distinct class of mitokines studied alongside other mitochondrial-encoded factors in metabolic and longevity science without clinical application. Supplied at ≥98% purity (C101H152N28O22S2; 2174.6 g/mol), this material supports controlled laboratory investigation under research-use-only conditions.

Mechanism of Action

MOTS-c activates AMPK by inhibiting the folate cycle enzyme AICAR transformylase/inosine monophosphate cyclohydrolase (ATIC), elevating ZMP levels and mimicking energy stress signaling in research cells. Nuclear translocation allows interaction with transcription factors regulating antioxidant response and glucose metabolism genes. In skeletal muscle research models, MOTS-c enhances glucose uptake independent of insulin receptor phosphorylation at some concentrations. The peptide improves mitochondrial biogenesis markers PGC-1alpha and NRF1 in exercise-mimetic study designs. MOTS-c does not require mitochondrial import for synthetic exogenous activity when added to culture media in research protocols.

Receptor Binding & Signaling

MOTS-c mechanism is primarily enzymatic and transcriptional rather than classical GPCR binding. ATIC inhibition links to AMPK activation pathway. Insulin receptor remains indirectly modulated through downstream metabolic flux rather than direct MOTS-c binding. Off-target GPCR activation is negligible in standard screening at research doses.

Research Applications

AMPK and energy stress signaling

Myotube and hepatocyte cultures use MOTS-c to measure AMPK phosphorylation, ACC inhibition, and glucose uptake with compound C controls. ATIC knockdown validates proposed mechanism. These biochemical platforms advance mitokine signaling research in metabolic laboratories.

Exercise-mimetic metabolic phenotyping

Sedentary rodent models receive MOTS-c in research protocols examining insulin tolerance, muscle glycogen, and fatty acid oxidation rates via indirect calorimetry. Pairing with exercise training arms separates additive effects. Studies model mitochondrial peptide roles in metabolic flexibility research.

Aging and sarcopenia research models

Aged rodent muscle exhibits reduced MOTS-c levels in some reports; exogenous peptide supplementation in research studies measures grip strength, muscle fiber type markers, and mitochondrial respiration in permeabilized fibers. Endpoints remain preclinical physiology metrics.

Nuclear translocation and transcriptomics

Fluorescently tagged MOTS-c tracks nuclear entry in stress conditions while RNA-seq identifies regulated gene sets. Researchers map mitokine-dependent transcriptional networks in cell lines. Bioinformatics supports mitochondrial-nuclear crosstalk hypotheses.

Molecular Information

Sequence & Chain Summary

MRWQEMGYIFYPRK (16-amino-acid mitochondrial open reading frame peptide).

Modification Type

Unmodified synthetic mitokine sequence.

Structural Notes

MOTS-c is a 2174.6 g/mol peptide amenable to SPPS with HPLC purification. Amphipathic character supports membrane interaction preceding nuclear translocation in cell studies. Mass spectrometry confirms identity; oxidation of methionine residues monitored during storage. Batch-specific molecular characterization—including mass confirmation and purity profiling—is available through COA, LC-MS, HPLC, and NMR documentation supplied with MOTS-c.

Molecular Formula
C101H152N28O22S2
Molecular Weight
2174.6 g/mol
Purity Specification
≥98%

Experimental Notes

Stability

Lyophilized MOTS-c stable at −20°C desiccated. Methionine oxidation increases with light and repeated freeze-thaw; store protected from light. Reconstituted aliquots frozen at −80°C for extended use. Lyophilized MOTS-c should be protected from repeated freeze-thaw cycles, moisture, and prolonged exposure to ambient light where applicable. Analytical integrity is best preserved when material is stored under the conditions specified on the certificate of analysis.

Storage Conditions

Store at -20°C. MOTS-c is supplied as white lyophilized powder. For long-term archival storage in research inventories, maintain sealed containers with desiccant where recommended and document lot numbers for traceability across experimental runs.

Laboratory Handling

Reconstitute in sterile water or PBS. Avoid prolonged ambient exposure for oxidizable residues. Use AMPK pathway controls in parallel wells. Document nmol dosing per cell culture well. Reconstitute only with appropriate research-grade solvents compatible with your assay format. Allow vials to reach equilibrium before opening, work under clean bench conditions, and label all working solutions with concentration, date, and researcher ID per institutional SOPs.

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Frequently Asked Questions

Research-focused answers about MOTS-c. For laboratory use only — not medical advice.

What is MOTS-c used for in research?
MOTS-c is for mitochondrial-derived peptide and metabolic research in cell and animal models. Not for human consumption, exercise enhancement products, or clinical metabolic intervention.
How does MOTS-c work biologically?
MOTS-c activates AMPK through ATIC inhibition and regulates nuclear gene programs affecting glucose and lipid metabolism in research models, functioning as a mitokine signal between mitochondria and nucleus.
What receptors does MOTS-c interact with?
Primary mechanism involves ATIC enzyme interaction and AMPK pathway activation rather than a cell surface receptor. Insulin receptor is modulated indirectly through metabolic flux changes in research systems.
Is MOTS-c stable at room temperature?
Lyophilized MOTS-c stable at −20°C desiccated. Methionine oxidation increases with light and repeated freeze-thaw; store protected from light. Reconstituted aliquots frozen at −80°C for extended use. For short-term laboratory workflows, minimize time at room temperature and return unused material to recommended storage promptly. MOTS-c is not formulated for ambient long-term storage.
What is the recommended storage condition for MOTS-c?
Store at -20°C. Store lyophilized material in a dedicated −20°C freezer, protect from moisture ingress, and avoid repeated temperature cycling. Reconstituted solutions should be aliquoted and frozen if not used within the validated window of your internal stability study.