Order MOTS-C Online
To order MOTS-c online for laboratory research, investigators must source from verified suppliers providing lot-specific analytical documentation. PX1 Research supplies high-purity, USA-manufactured MOTS-c validated via RP-HPLC, mass spectrometry, and endotoxin assays to ensure reliable data across in vitro and animal models.
Quick answer
To order MOTS-c online for laboratory research, investigators must source from verified suppliers providing lot-specific analytical documentation. PX1 Research supplies high-purity, USA-manufactured MOTS-c validated via RP-HPLC, mass spectrometry, and endotoxin assays to ensure reliable data across in vitro and animal models.
Key takeaways
- [MOTS-c](/research-peptides/mots-c) (Mitochondrial Open Reading Frame of the 12S rRNA Type-c) represents a distinct class of signaling molecules encoded directly within the mitochondrial genome rather than the nuclear genome.
- At the structural level, [MOTS-c](/research-peptides/mots-c) is composed of the sequence Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg.
- A substantial body of preclinical evidence highlights the role of [MOTS-c](/research-peptides/mots-c) in systemic metabolic regulation and physical performance assays.
- When designing mitochondrial target experiments, investigators frequently compare [MOTS-c](/research-peptides/mots-c) against other well-studied mitochondrial-targeted peptides, specifically [SS-31](/product/ss-31) and [Humanin](/product/humanin).
Overview of MOTS-c: A Mitochondrial-Derived Peptide
MOTS-c (Mitochondrial Open Reading Frame of the 12S rRNA Type-c) represents a distinct class of signaling molecules encoded directly within the mitochondrial genome rather than the nuclear genome. Discovered during investigations into mitochondrial-derived peptides (MDPs), MOTS-c consists of a 16-amino acid sequence that plays a pivotal role in cellular communication and metabolic homeostasis. Researchers frequently explore mitochondrial research peptides to analyze how mitochondrial signals regulate systemic physiology outside the organelle itself.
Unlike classic nuclear-encoded regulatory factors, MOTS-c is synthesized in the mitochondrial matrix and translocates to the cytoplasm and nucleus under conditions of metabolic stress. In vitro studies demonstrate that this peptide participates in retrograde signaling—a mechanism by which mitochondria communicate their functional status to the cell nucleus to alter gene transcription. Because of these unique properties, investigators seeking to examine mitochondrial-nuclear cross-talk routinely require access to verified reference materials when they order MOTS-c for controlled laboratory studies.
Molecular Structure and Primary Mechanism of Action
At the structural level, MOTS-c is composed of the sequence Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg. The primary biological mechanism identified in preclinical literature involves the modulation of the folate-methionine cycle and the subsequent activation of 5'-AMP-activated protein kinase (AMPK). In rodent models, cellular stress or metabolic strain triggers MOTS-c to interact with the purine biosynthesis pathway, leading to an accumulation of 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), a known endogenous activator of AMPK.
Through AMPK pathway modulation, MOTS-c influences glucose uptake, fatty acid oxidation, and cellular energy balance without requiring direct ligand binding to classical cell-surface receptor tyrosine kinases. Preclinical studies suggest that nuclear translocation of MOTS-c is further enhanced under oxidative stress, where it interacts with transcription factors such as NRF2 (nuclear factor erythroid 2-related factor 2) to alter the expression of stress-responsive genes. Understanding these precise biochemical interactions relies heavily on using standardized, highly purified material sourced through our complete catalog of research peptides.
Preclinical Literature: Metabolic Regulation and Exercise Capacity
A substantial body of preclinical evidence highlights the role of MOTS-c in systemic metabolic regulation and physical performance assays. In high-fat diet rodent models, administration of MOTS-c prevented diet-induced insulin resistance and attenuated systemic body weight gain. The mechanistic data indicate that MOTS-c enhances skeletal muscle glucose clearance and restores insulin sensitivity independently of food intake, rendering it a target of significant interest within metabolic research peptides.
Additionally, preclinical investigations into exercise capacity demonstrate that MOTS-c levels increase significantly in response to acute physical exertion. Mouse models subjected to treadmill running protocols exhibited improved exercise endurance and enhanced skeletal muscle fatty acid oxidation following MOTS-c treatment. These findings suggest that MOTS-c acts as an exercise-mimetic signaling peptide at the cellular level. Researchers designing comparative metabolic trials can review published datasets via the PX1 Research Hub to contextualize experimental parameters.
Comparative Analysis: MOTS-c, SS-31, and Humanin
When designing mitochondrial target experiments, investigators frequently compare MOTS-c against other well-studied mitochondrial-targeted peptides, specifically SS-31 and Humanin. While all three target mitochondrial health and cellular bioenergetics, their primary sites of action and biochemical mechanisms differ substantially.
SS-31 (Elamipretide) acts directly within the inner mitochondrial membrane by binding selectively to cardiolipin, preventing electron transport chain uncoupling and reducing reactive oxygen species (ROS) production. Conversely, Humanin—the first identified mitochondrial-derived peptide—primarily functions as a cytoprotective factor that inhibits apoptosis by binding to Pro-apoptotic BAX proteins and interacting with membrane-bound cell surface receptors (such as the FPRL1 receptor). MOTS-c differs from both compounds by primarily targeting metabolic signaling pathways via the folate cycle and AMPK activation, illustrating that each compound serves a distinct role within mitochondrial research.
Critical Criteria When Evaluating Online Vendors for MOTS-c
Because synthetic peptide manufacturing requires high precision, sourcing reference materials online introduces significant variables regarding purity, stability, and batch-to-batch consistency. Laboratories seeking to order MOTS-c online must evaluate suppliers against stringent quality control protocols before introducing peptides into cell culture assays or animal models.
Key evaluation factors include facility certification, analytical validation methodologies, and raw material controls. Substandard peptide batches may contain truncation sequences, residual trifluoroacetic acid (TFA) salts, organic solvents, or heavy metal contamination—all of which introduce confounding variables in bioenergetic assays. PX1 Research mitigates these risks by producing all compounds within USA-based, ISO 17025-accredited and GMP-compliant facilities, ensuring consistent primary sequence integrity and minimal counter-ion interference.
Analytical Validation: RP-HPLC, Mass Spectrometry, and Endotoxin Testing
To guarantee experimental reproducibility, every lot of MOTS-c produced for PX1 Research undergoes rigorous third-party analytical testing. Reversed-Phase High-Performance Liquid Chromatography (RP-HPLC) is performed to confirm purity levels equal to or exceeding 98%. RP-HPLC separates the target sequence from incomplete deletion peptides or chemical synthesis byproducts, establishing exact chemical purity.
Electrospray Ionization Mass Spectrometry (ESI-MS) is subsequently utilized to confirm the precise molecular weight of the 16-amino acid chain, verifying that no amino acid substitutions or modifications occurred during solid-phase peptide synthesis (SPPS). Furthermore, because bacterial endotoxins can activate inflammatory pathways in cell lines and animal models, PX1 Research conducts chromogenic Limulus Amebocyte Lysate (LAL) testing on every lot. Only lots exhibiting endotoxin levels below 0.1 EU/mg are approved for release, ensuring optimal stability for sensitive downstream applications such as AMPK activation peptides research.
Laboratory Reconstitution and Handling Protocols
Proper reconstitution of MOTS-c is vital to maintain peptide stability and prevent physical aggregation in vitro. MOTS-c is supplied as a lyophilized (freeze-dried) powder under inert gas. For most laboratory applications, reconstituting the lyophilized cake in sterile, bacteriostatic water or sterile phosphate-buffered saline (PBS, pH 7.4) is recommended depending on the final assay environment.
To reconstitute, allow the vial to equilibrate to room temperature before removing the stopper to prevent atmospheric moisture condensation inside the vial. Inject the chosen solvent gently along the inner glass wall of the vial rather than directly onto the lyophilized pellet. Allow the peptide to dissolve passively or agitate with gentle swirling; vortexing should be strictly avoided as high shear force can denature peptide secondary structures and promote aggregation. If low concentrations require vehicle carriers, 0.1% Bovine Serum Albumin (BSA) can be incorporated to minimize non-specific adsorption to plastic laboratory consumables.
Storage, Degradation Prevention, and Freeze-Thaw Guidelines
Lyophilized MOTS-c exhibits excellent long-term stability when stored at -20°C or -80°C in a desiccated environment shielded from direct light. Under these conditions, the dry powder remains stable for up to 24 months without significant primary sequence degradation. Upon reconstitution into aqueous solution, the shelf life shortens, necessitating strict storage management.
Reconstituted liquid solutions should be divided into single-use experimental aliquots to eliminate repeated freeze-thaw cycles, which degrade peptide bonds and reduce active concentrations. Reconstituted aliquots stored at 4°C should be used within 7 to 10 days, whereas aliquots frozen at -80°C remain viable for up to 3 to 6 months. Researchers should strictly monitor stock solution degradation using standard UV-Vis spectrophotometry or HPLC aliquot sampling when conducting multi-week study protocols.
Procurement, Wholesale Sourcing, and Supply Chain Integrity
PX1 Research operates dedicated fulfillment hubs in California and Arizona to support fast, reliable distribution across North America. Orders placed Monday through Friday before cut-off times qualify for same-day dispatch, ensuring that temperature-sensitive research compounds arrive swiftly without degradation during transport.
For academic institutions, biotechnology firms, and contract research organizations (CROs) requiring ongoing material for large-scale studies, PX1 Research offers a formal wholesale supply program. Bulk orders undergo identical lot-specific HPLC, MS, and endotoxin verification, accompanied by complete analytical documentation to fulfill internal QA/QC requirements.
Frequently Asked Questions
What is the purity level of MOTS-c supplied by PX1 Research?
PX1 Research supplies MOTS-c with a guaranteed chemical purity of ≥98%, as verified by lot-specific Reversed-Phase High-Performance Liquid Chromatography (RP-HPLC).
How is the molecular identity of MOTS-c verified?
Molecular identity is confirmed via Electrospray Ionization Mass Spectrometry (ESI-MS), which measures the exact mass-to-charge ratio of the 16-amino acid sequence against its theoretical molecular weight.
What are the endotoxin limits for PX1 Research MOTS-c?
Every lot of MOTS-c undergoes chromogenic LAL testing to ensure endotoxin levels remain below 0.1 EU/mg, preventing confounding inflammatory responses in cell culture and animal models.
How should lyophilized MOTS-c be stored upon arrival?
Lyophilized MOTS-c should be stored at -20°C or -80°C in a dry, dark environment. Upon reconstitution, liquid aliquots should be stored at -80°C to prevent freeze-thaw degradation.
Is MOTS-c suitable for human consumption or clinical administration?
No. MOTS-c provided by PX1 Research is strictly designated for laboratory research use only (in vitro and animal models). It is not for human or veterinary diagnostic, therapeutic, or clinical applications.
What solvents are recommended for reconstituting MOTS-c?
Sterile bacteriostatic water or sterile PBS (pH 7.4) are commonly used for reconstitution. Gentle swirling is recommended; avoid vigorous vortexing.
Where are PX1 Research peptides manufactured and shipped from?
All PX1 Research compounds are manufactured in USA-based, ISO 17025-accredited facilities and shipped directly from fulfillment centers in California and Arizona.
Can institutions purchase bulk quantities of MOTS-c?
Yes, PX1 Research offers tiered pricing and bulk procurement options for research laboratories and institutions through our dedicated wholesale program.
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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.