MOTS-c is a short peptide encoded within the mitochondrial genome and is described in the scientific literature as part of the mitochondrial-derived peptide (MDP) class, discussed in the context of mitochondrial signaling and inter-organelle communication in experimental systems. Reports in the research literature describe MOTS-c localization in cellular compartments that can include mitochondria and, under defined laboratory stress conditions, the nucleus; these observations are limited to non-clinical cellular and animal model investigations.

Note: This product is supplied as a lyophilized powder and should be reconstituted with bacteriostatic water for appropriate research handling.

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For laboratory research only. Not for human consumption, medical, or veterinary use.

Sequence: Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg

Molecular Formula: C101H152N28O22S2

Molecular Weight: 2174.64 g/mol

PubChem SID: 255386757

CAS Number: 1627580-64-6

Reported Synonyms: Mitochondrial open reading frame of the 12S rRNA-c, MT-RNR1

In the published scientific literature, MOTS-c is referenced in non-clinical research that includes cellular assays and animal model studies, where molecular interactions, signaling components, and pathway-associated markers are measured under defined experimental conditions.

Reported research contexts include experimental work examining mitochondrial signaling-associated molecular components, nuclear translocation phenomena under laboratory stress conditions, AMPK-associated signaling elements, metabolic pathway-linked molecular markers, and gene expression patterns evaluated in cellular and animal models.

Mechanistic discussions in preclinical publications commonly frame MOTS-c within energy-sensing and stress-responsive molecular networks, including components tied to AMPK signaling.

Additional research describes dynamic nuclear localization following metabolic stress in an AMPK-dependent manner and reports interaction with stress-responsive transcriptional control frameworks, including antioxidant response element (ARE)–related regulation, within the experimental systems studied.

The original characterization of MOTS-c described a mitochondrial 12S rRNA sORF encoding a 16-amino-acid peptide and reported cellular actions linked to folate-cycle–connected metabolism and AMPK activation, alongside observations in mouse models under dietary and age-associated metabolic stress paradigms.

Subsequent Cell Metabolism work described stress-triggered nuclear translocation of MOTS-c and broad nuclear gene-expression changes under glucose restriction and related stress conditions in cell models.

Additional preclinical studies have reported MOTS-c–associated changes in signaling and metabolite profiles in diet-induced obesity models using metabolomics approaches, supporting its use as a laboratory probe for pathway mapping in metabolic-stress settings.

Lee, C., Zeng, J., Drew, B. G., et al. (2015). The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. Cell Metabolism.

Kim, K. H., Son, J. M., Benayoun, B. A., & Lee, C. (2018). The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. Cell Metabolism, 28(3), 516–524.e7. https://doi.org/10.1016/j.cmet.2018.06.008

Kumagai, H., Kim, S.-J., Miller, B., et al. (2024). MOTS-c modulates skeletal muscle function by directly binding and activating CK2. iScience, 27(11), 111212. https://doi.org/10.1016/j.isci.2024.111212

Lee, C., & Cohen, P. (2016). MOTS-c: A novel mitochondrial-derived peptide regulating muscle and fat metabolism. Trends in Endocrinology & Metabolism.

Kim, S.-J., Miller, B., Mehta, H. H., et al. (2019). The mitochondrial-derived peptide MOTS-c is a regulator of plasma metabolites and enhances insulin sensitivity. Physiological Reports, 7(13), e14171. https://doi.org/10.14814/phy2.14171

Kumagai, H., Coelho, A. R., Wan, J., et al. (2021). MOTS-c reduces myostatin and muscle atrophy signaling. American Journal of Physiology – Endocrinology and Metabolism, 320, E680–E690. https://doi.org/10.1152/ajpendo.00275.2020

Mohtashami, Z., Singh, M. K., Salimiaghdam, N., Ozgul, M., & Kenney, M. C. (2022). MOTS-c, the Most Recent Mitochondrial Derived Peptide in Human Aging and Age-Related Diseases. International Journal of Molecular Sciences, 23(19), 11991. https://doi.org/10.3390/ijms231911991

To protect experimental integrity, store peptides cold, dry, and shielded from light to minimize oxidation, contamination, and degradation. For near-term use, keep unopened material refrigerated at ≤4 °C (≤39 °F) and limit time at room temperature during handling. Lyophilized (dry) peptides can tolerate short periods at room temperature, but refrigeration is preferred for best stability and longevity. For longer-term storage, keep unmixed material frozen—−18 °C (0 °F) is acceptable, while −80 °C (−112 °F) is optimal for multi-month to multi-year preservation. Avoid frost-free freezers and repeated freeze–thaw cycles, which can accelerate breakdown. If reconstituted (in solution), use sterile buffer (ideally pH 5–6 when feasible), split into aliquots, and freeze (preferably −80 °C (−112 °F)) to reduce handling-related degradation.

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