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MOTS-C 10mg

MOTS-C (Mitochondrial Open Reading Frame of the 12S rRNA-c) is a 16-amino-acid peptide encoded within the mitochondrial genome's 12S rRNA region and is classified as a mitochondria-derived peptide (MDP).

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MOTS-C (Mitochondrial Open Reading Frame of the 12S rRNA-c) is a 16-amino-acid peptide encoded within the mitochondrial genome's 12S rRNA region and is classified as a mitochondria-derived peptide (MDP).

Experimental investigations have examined its role in mitochondrial-to-nuclear signaling pathways, intracellular regulatory networks, and adaptive signaling mechanisms associated with mitochondrial communication systems.

Research has also explored interactions with AMP-activated protein kinase (AMPK), FOXO-associated signaling pathways, transcriptional regulatory processes, and downstream signal transduction networks.

Research applications include mitochondrial signaling pathway investigation, AMPK pathway characterization, FOXO signaling studies, mitochondrial communication research, and mechanistic evaluation of mitochondria-derived peptide biology.

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3D Molecular Structure

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Chemical Formula C101H152N28O22S2
Synonyms Mitochondria-derived peptide, mots-c, EX-A626, Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg
Molar Mass 2,174.62 g/mol
CAS Number 1627580-64-6
PubChem CID 146675088
Total Compound Content 10 mg per vial
Shelf Life 36 months
MOTS-C is a 16-amino-acid peptide (Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg; MRWQEMGYIFYPRKLR) encoded within the 12S rRNA region of the mitochondrial genome, making it one of a limited number of peptides derived from mitochondrial DNA. Experimental investigations have examined its role in mitochondrial-to-nuclear communication pathways, intracellular regulatory networks, and signaling mechanisms associated with mitochondrial function. Research has reported interactions with AMP-activated protein kinase (AMPK), FOXO-associated signaling pathways, transcriptional regulatory processes, and downstream signal transduction networks involved in cellular adaptation mechanisms. Additional studies have explored the relationship between MOTS-C and nuclear localization pathways, antioxidant response element (ARE)-associated signaling, and molecular processes governing mitochondrial communication systems. These characteristics have established MOTS-C as a valuable research tool for investigating mitochondria-derived peptide biology, mitochondrial signaling networks, transcriptional regulation, and mechanistic aspects of mitochondrial-nuclear signaling crosstalk. Supplied as a lyophilized preparation. Independently third-party HPLC-tested; COA available per batch.

Results refer to the tested sample. Check the batch and date in the report.

MOTS-C (HPLC)
April 25, 2026
What distinguishes MOTS-C from most other research peptides?

MOTS-C is a 16-amino-acid peptide encoded within the mitochondrial genome, making it part of a relatively small group of mitochondria-derived peptides (MDPs). This unique genetic origin has made MOTS-C a valuable research tool for investigating mitochondrial-to-nuclear communication pathways, intracellular signaling networks, transcriptional regulation mechanisms, and the molecular processes governing mitochondrial signaling systems.

Which signaling pathways have been associated with MOTS-C in experimental investigations?

Research involving MOTS-C has reported interactions with AMP-activated protein kinase (AMPK), FOXO-associated signaling pathways, antioxidant response element (ARE)-associated regulatory networks, and downstream transcriptional processes. These characteristics have established MOTS-C as a useful compound for studying signal transduction mechanisms, pathway-specific regulatory systems, mitochondrial communication networks, and adaptive signaling processes.

How does MOTS-C differ from other mitochondria-derived peptides such as Humanin?

Although both MOTS-C and Humanin are classified as mitochondria-derived peptides, they differ in amino acid sequence, molecular structure, signaling interactions, and pharmacological characteristics. Comparative investigations utilize these peptides to examine distinct aspects of mitochondrial signaling, peptide-mediated regulatory mechanisms, mitochondrial-to-nuclear communication pathways, and structure-function relationships within the broader class of mitochondria-derived peptides.

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