What Is MOTS-c and Its Research Applications
MOTS-c (mitochondrial open reading frame of the 12S rRNA type-c) is a mitochondrial-derived peptide encoded by a short open reading frame within the mitochondrial genome. This 16-amino-acid peptide (sequence: Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg) has attracted significant attention in cellular metabolism research. As a mitochondrial-derived peptide (MDP), it represents a unique class of signaling molecules that originate from the mitochondrial DNA and participate in retrograde communication between mitochondria and the nucleus.
Mechanistically, MOTS-c has been shown in laboratory studies to influence key metabolic pathways, including AMP-activated protein kinase (AMPK) signaling and glucose utilization in cellular models. Research groups investigate its role in modulating mitochondrial respiration, oxidative stress responses, and cellular energy homeostasis. Preclinical investigations, conducted exclusively in vitro, have explored the peptide’s interaction with folate-dependent purine biosynthesis and its effects on nuclear gene expression—findings that expand understanding of mitonuclear crosstalk.
Because MOTS-c is a purely research-grade compound, all materials supplied are intended strictly for biochemical and cell-based assays, analytical studies, and other laboratory applications. No statements in this article or accompanying documentation should be interpreted as suggesting suitability for any diagnostic, preventive, or clinical purpose in humans or animals. Every shipment is labeled and documented accordingly to ensure institutional compliance.
Importance of a Certificate of Analysis (COA) for Research Peptides
For a professional MOTS-c supplier with COA, the Certificate of Analysis is the cornerstone of quality transparency. A comprehensive COA documents the exact purity level, molecular identity, and other critical batch-specific parameters, allowing researchers to verify that the peptide meets the required specifications before initiating experiments. This documentation directly supports reproducibility—a fundamental principle of rigorous scientific inquiry—by ensuring that different batches perform consistently across time and between laboratories.
Our COAs are designed to meet the expectations of academic institutions, pharmaceutical research organizations, and contract testing facilities. Each document includes a high-performance liquid chromatography (HPLC) chromatogram with peak integration data, a mass spectrometry (MS) spectrum confirming the observed molecular weight against the theoretical value, and a quantitative statement of peptide content. In addition, the COA records the appearance of the lyophilized powder, storage recommendations, and the date of release testing. By correlating every vial with a unique batch number and retaining full analytical records, we provide a traceable quality chain that facilitates troubleshooting and audit readiness.
Relying on a supplier that supplies a complete, unredacted COA with each order eliminates guesswork from the procurement process and helps research teams align their internal validation protocols with recognized good laboratory practices. This level of transparency is particularly important for projects that require data integrity for peer-reviewed publication, grant reporting, or regulatory dossier preparation.
Our MOTS-c Product Specifications
The MOTS-c we supply is manufactured as a trifluoroacetate salt, presented as a white to off-white lyophilized powder. At release, every batch is tested to confirm purity of at least 95% as measured by reversed-phase HPLC, with the area normalization method applied. The observed molecular weight, verified by electrospray ionization mass spectrometry (ESI-MS), must fall within the accepted tolerance of the theoretical monoisotopic mass. Additionally, peptide content determination—using amino acid analysis or nitrogen content analysis—is documented to allow accurate preparation of stock solutions for laboratory protocols.
Standard packaging consists of sealed, glass vials under an inert argon atmosphere to protect the peptide from moisture and oxidation during transit and storage. Each shipment includes a batch-specific COA that details the analytical results, lot number, production date, and recommended storage conditions.
Analytical Methods Used
All release testing is performed using instruments and protocols calibrated to industry-recognized standards. The following analytical techniques form the core of our quality control platform:
- Reversed-phase high-performance liquid chromatography (RP-HPLC): Purity is assessed on a C18 column with a water/acetonitrile gradient containing 0.1% trifluoroacetic acid. Detection at 214–220 nm allows quantification of the target peptide and related impurities. System suitability and gradient reproducibility are monitored in accordance with principles adapted from pharmacopeial general chapters, such as USP <621>.
- Electrospray ionization mass spectrometry (ESI-MS): The intact mass is confirmed on a single-quadrupole or time-of-flight instrument operating in positive ion mode. Deconvolution of the multiply charged ion envelope yields the experimental molecular weight, which must agree with the theoretical value within ±1.0 Da.
- Amino acid analysis (AAA): For composition verification, the peptide is hydrolyzed and the liberated amino acids are derivatized for chromatographic separation and UV detection. The molar ratios are compared against the expected sequence to confirm correct assembly and rule out critical deletions or substitutions.
- Residual solvent and counter-ion testing: Where applicable, gas chromatography and ion chromatography are employed to verify that levels of residual solvents and trifluoroacetate are within acceptable limits for research peptides.
These analytical procedures are performed in a controlled laboratory environment, with data reviewed and approved by quality assurance personnel before a batch is released.
Quality Assurance and Supply Chain Integrity
Our MOTS-c is synthesized by solid-phase peptide synthesis (SPPS) using Fmoc chemistry, which allows stepwise assembly of the amino acid chain on a polymeric resin. This well-established method provides precise control over sequence fidelity and minimizes the risk of deletions. Following cleavage from the resin and global deprotection, the crude peptide undergoes purification by preparative HPLC, with pooled fractions analyzed in-process to ensure only cuts meeting the purity target advance to final lyophilization.
Throughout the synthesis and purification workflow, in-process controls include ninhydrin tests for coupling efficiency, analytical HPLC monitoring of intermediate purity, and mass confirmation at critical steps. The final lyophilized powder is conditioned under vacuum and sealed under argon to displace ambient oxygen and moisture. Bulk storage is maintained at −20°C in a temperature-monitored freezer, with continuous data logging and alarm systems. Every step—from resin loading to labeling—is captured in a batch record that remains on file for the full shelf life of the product, supporting complete traceability in the event of a quality inquiry.
Ordering MOTS-c for Your Research Facility
We supply MOTS-c in standard vial sizes covering a range from milligram research quantities to multi-gram amounts suitable for large-scale screening projects. The typical lead time from receipt of a validated purchase order is five to seven business days, provided the product is in stock at the requested scale. Custom synthesis scales can be accommodated through a quotation process.
All shipments are dispatched with temperature-controlled packaging options: insulated containers with validated gel packs for ambient-sensitive peptides, and dry ice for frozen transport when required by the destination. Comprehensive shipping documentation—commercial invoice, packing list, and material safety data sheet—accompanies each consignment. We serve research institutions, pharmaceutical R&D centers, and authorized distributors globally, adhering to all applicable import regulations for research-grade biochemicals. A minimum order value may apply, and dedicated account managers are available to discuss volume requirements, standing order arrangements, or customized refill schedules.
Frequently Asked Questions About MOTS-c and COA
- How should MOTS-c be reconstituted for in vitro experiments? For laboratory handling, the lyophilized powder is typically dissolved in sterile, nuclease-free water or phosphate-buffered saline (PBS) to the concentration required by the protocol. Gentle vortexing or pipetting is recommended to avoid foaming. Any solution not used immediately should be stored in aliquots at −20°C or colder to maintain integrity.
- What is the shelf life? When the lyophilized peptide is stored continuously at −20°C in the original, unopened vial and protected from light, stability data support a shelf life of two years from the date of manufacture. Reconstituted solutions are more labile, and researchers should consult the COA for guidance on working solution stability under their specific experimental conditions.
- Can I request a COA before purchase? Yes. We can provide a representative COA that illustrates the typical format and analytical detail included with each batch. This document helps you evaluate our quality standards and confirm that our documentation will satisfy your institutional requirements before you commit to an order.
- Is MOTS-c for injection? No. The peptide is furnished solely for laboratory research purposes. It is not prepared, tested, or intended for administration to humans or animals in any clinical or veterinary context. Our terms and conditions explicitly limit use to in vitro and ex vivo research.
All products discussed in this article are for research use only and are not intended for human or animal diagnostic, prophylactic, or other in vivo applications. Researchers are responsible for ensuring that their use complies with all applicable laws, regulations, and institutional policies.
Solo para uso en investigación. No apto para uso humano ni veterinario.
