MOTS-c (Mitochondrial Open Reading Frame of the 12S rRNA Type-c) is a unique 16-amino acid mitochondrial-derived peptide actively investigated for its role in cellular energy balance and metabolic homeostasis. PX1 Research provides reference-grade MOTS-c synthetically produced under strict quality control standards for preclinical and in vitro research applications.
MOTS-c (Mitochondrial Open Reading Frame of the 12S rRNA Type-c) is a unique 16-amino acid mitochondrial-derived peptide actively investigated for its role in cellular energy balance and metabolic homeostasis. PX1 Research provides reference-grade MOTS-c synthetically produced under strict quality control standards for preclinical and in vitro research applications.
When qualified investigators seek to buy MOTS-c research compound for laboratory experimentation, securing sequence-verified, high-purity material is essential. MOTS-c is a 16-amino acid mitochondrial-derived peptide evaluated in preclinical models for metabolic regulation, mitochondrial bioenergetics, and exercise adaptation. PX1 Research supplies analytical-grade MOTS-c research compound (>98% purity verified via RP-HPLC and mass spectrometry) strictly for in vitro and animal research use.
To ensure precise experimental reproducibility, researchers must rely on vendors that issue lot-specific Certificates of Analysis (COAs) detailing chemical purity, molecular weight verification, and endotoxin levels. All reference peptides offered by PX1 Research are manufactured in US facilities operating under strict quality protocols, shipped directly from distribution hubs in California and Arizona.
MOTS-c belongs to an emerging class of signaling molecules known as mitochondrial-derived peptides (MDPs). Unlike classic nuclear-encoded peptides, MOTS-c is encoded within the mitochondrial genome—specifically within the 12S ribosomal RNA (rRNA) gene locus. First identified in 2015, this 16-amino acid peptide (sequence: Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg) demonstrates how the mitochondrial genome actively communicates with the nuclear genome to orchestrate metabolic adaptation.
In cell culture assays and structural evaluations, MOTS-c displays unique amphipathic characteristics that enable cellular signaling under bioenergetic stress. When cellular homeostasis is perturbed, MOTS-c translocates from the mitochondrion to the nucleus, acting as a transcriptional repressor or co-regulator. Researchers interested in broader nuclear-mitochondrial cross-talk frequently consult our mitochondrial-derived peptides guide for comparative structural analysis across the MDP family.
Preclinical investigations demonstrate that MOTS-c plays a central role in maintaining mitochondrial health, organelle respiration, and oxidative phosphorylation efficiency. In rodent models of metabolic challenge, exogenous administration of synthetic MOTS-c has been observed to modulate mitochondrial dynamics, preserving mitochondrial membrane potential and reducing the accumulation of damaging reactive oxygen species (ROS).
In vitro data indicate that MOTS-c interacts directly with the folate-methionine cycle, inhibiting de novo purine synthesis. This accumulation of 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) leads to the downstream activation of AMP-activated protein kinase (AMPK)—a primary master regulator of cellular energy expenditure. Researchers examining cellular energy pathways often pair MOTS-c inquiries with studies on other energy-sensing molecules cataloged in the PX1 Research library.
Metabolic research represents one of the primary domains for MOTS-c evaluation. Preclinical trials using high-fat diet (HFD) rodent models indicate that MOTS-c supplementation enhances systemic insulin sensitivity and blunts diet-induced weight gain without altering calorie intake. The proposed mechanism involves AMPK-mediated translocation of glucose transporter 4 (GLUT4) to plasma membranes in skeletal muscle tissue.
Furthermore, in vitro studies using murine myoblasts suggest that MOTS-c increases fatty acid oxidation while suppressing lipogenesis. By remodeling substrate utilization toward lipid oxidation, the peptide helps reverse intracellular lipid accumulation in skeletal muscle and hepatic cell assays. For laboratories conducting high-throughput screening on metabolic signaling, exploring our wider range of metabolic research peptides provides valuable context for comparative experimental design.
MOTS-c is often described in preclinical literature as an 'exercise mimetic' due to its ability to induce cellular adaptations similar to physical exertion. In treadmill running models using aged rodents, systemic MOTS-c treatment significantly improved physical performance, running distance, and grip strength. These physiological changes correlated with upregulation of heat shock response pathways and enhanced antioxidant enzyme expression.
Crucially, exercise itself transiently increases endogenous MOTS-c expression in skeletal muscle and systemic circulation in animal models, suggesting a physiological feedback loop. Laboratory models evaluating physical resilience, age-related decline, and muscle physiology utilize synthetic MOTS-c to dissect these stress-response pathways. Investigators can cross-reference these experimental frameworks across our entire full peptide catalog.
When designing mitochondrial target assays, researchers frequently select between several distinct mitochondrial-targeted peptides. While MOTS-c functions primarily via nuclear translocation and AMPK activation to regulate systemic metabolism, SS-31 peptide acts directly at the inner mitochondrial membrane by binding cardiolipin, preventing electron leakage, and reducing ROS directly at Complex I and III. In contrast, Humanin research studies focus largely on cytoprotective and anti-apoptotic signaling pathways through interactions with Bax proteins and cell-surface receptors.
Each peptide targets mitochondrial biology through distinct molecular mechanisms: SS-31 offers biophysical membrane stabilization, Humanin prevents stress-induced cell death, and MOTS-c serves as a nuclear-mitochondrial signaling messenger controlling metabolic homeostasis. Combining or comparing these compounds in multi-arm cellular assays provides a comprehensive framework for mitochondrial research.
Because small structural impurities or peptide fragments can alter signaling responses in cell culture, verifying chemical purity is essential prior to buying MOTS-c research compound. PX1 Research enforces strict quality assurance protocols for every batch of custom and catalog peptides manufactured.
Our analytical validation process includes:
• High-Performance Liquid Chromatography (RP-HPLC): Confirms chemical purity equal to or exceeding 98.0%, ensuring the removal of truncated deletion sequences.
• Electrospray Ionization Mass Spectrometry (ESI-MS): Verifies exact theoretical molecular weight (2174.6 g/mol) and identity.
• Endotoxin Testing: Quantifies bacterial endotoxin (LPS) levels using Chromogenic LAL assays to ensure levels remain <0.01 EU/mg, preventing baseline inflammatory interference in cell assays.
• ISO 17025 Accreditation: Analytical testing is validated by independent third-party laboratories. Every order includes a lot-specific Certificate of Analysis available for lab compliance archives.
To preserve peptide integrity and avoid enzymatic or chemical degradation, laboratories must follow standard handling guidelines upon receiving lyophilized MOTS-c:
1. Reconstitution: Reconstitute the lyophilized cake using sterile bacteriostatic water or laboratory-grade phosphate-buffered saline (PBS, pH 7.4). Allow the vial to sit at room temperature for several minutes; gently swirl without vigorous shaking or vortexing to prevent peptide denaturation.
2. Aliquoting: To minimize repeated freeze-thaw cycles—which degrade peptide tertiary structure—solubilized MOTS-c should be divided into single-use working aliquots using sterile, low-protein-binding microcentrifuge tubes.
3. Storage Conditions: Lyophilized powder remains stable at -20°C for up to 24 months, or -80°C for extended storage. Once reconstituted, liquid aliquots should be maintained at -80°C and used promptly upon thawing.
For additional guidelines regarding solvent compatibility and stability parameters across various assay media, researchers can refer to our technical documentation or consult with our bulk lab purchasing team.
PX1 Research provides institutional, academic, and private laboratories with seamless procurement of reference-grade research peptides. Recognizing that experimental timelines require strict supply chain consistency, we maintain dedicated inventory hubs in California and Arizona to support fast, reliable delivery.
Orders placed before 12:00 PM PST Monday through Friday ship the same day. Every container is securely sealed and dispatched with full lot-traceability documentation, guaranteeing that the MOTS-c research compound delivered to your bench matches the exact chemical specifications detailed in our published analytical COAs.
What is the purity level of PX1 Research MOTS-c?
PX1 Research MOTS-c is certified at ≥98% purity as determined by Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Mass Spectrometry (MS) analysis.
How should MOTS-c be reconstituted for in vitro or animal models?
Lyophilized MOTS-c should be reconstituted using sterile bacteriostatic water or sterile PBS (pH 7.4). Swirl gently to dissolve and avoid high-shear vortexing. Reconstituted stock solution should be aliquoted and stored at -80°C.
How does MOTS-c differ from SS-31 in laboratory models?
MOTS-c is a mitochondrial-derived signaling peptide that translocates to the nucleus to regulate metabolic genes via AMPK activation. SS-31 (Elamipretide) is a synthetic tetrapeptide that targets cardiolipin in the inner mitochondrial membrane to directly optimize electron transport chain activity.
What documentation is provided with PX1 Research peptides?
Every lot of MOTS-c includes a downloadable, lot-specific Certificate of Analysis (COA) detailing RP-HPLC purity profiles, mass spec mass verification, and endotoxin assay results.
What are the recommended storage conditions for lyophilized MOTS-c?
Desiccated lyophilized peptide powder should be stored at -20°C or -80°C away from light and moisture. Under these conditions, the dry compound remains stable for up to 24 months.
Is MOTS-c approved for human administration or clinical use?
No. MOTS-c supplied by PX1 Research is strictly sold as a research chemical intended for in vitro cellular assays and non-human animal models. It is not approved for human therapeutic, clinical, or diagnostic use.
What endotoxin limit is verified for PX1 MOTS-c lots?
PX1 Research enforces strict bacterial endotoxin testing on all peptide lots, ensuring endotoxin levels remain below 0.01 EU/mg to prevent immune activation in delicate cell culture models.
Where does PX1 Research manufacture and ship its compounds from?
All PX1 Research compounds are synthesized under strict quality management in the USA and shipped directly from fulfillment centers located in California and Arizona.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.