MOTS-c is a natural 16-amino-acid mitochondria-derived peptide (MDP), first discovered in 2015 by research team from the University of Southern California. Unlike most conventional peptides encoded by nuclear DNA, MOTS-c is translated from a short open reading frame within mitochondrial 12S rRNA gene. As a critical mitochondrial signaling messenger, it can translocate from mitochondria into cytoplasm and cell nucleus to mediate cross-compartment gene regulation under metabolic stress.

In preclinical laboratory research, MOTS-c functions mainly by activating the AMPK cellular energy pathway and modulating the folate-methionine metabolism cycle. It is widely investigated for its roles in regulating systemic glucose homeostasis, enhancing insulin sensitivity in skeletal muscle cells, promoting glucose uptake and improving cellular bioenergetics. Preclinical studies also explore its anti-inflammatory properties, adaptive response to exercise stress, fat metabolism modulation and its potential correlation with ageing progression. Endogenous MOTS-c levels rise with physical exercise and metabolic challenge, while naturally declining with advancing age.

This synthetic MOTS-c is produced via solid-phase peptide synthesis, followed by multi-step purification and lyophilization. The lyophilized form greatly improves long-term chemical stability. Each production batch undergoes strict quality control procedures, including HPLC purity detection, MS molecular identity verification, moisture content test, and endotoxin inspection to guarantee consistency for in vitro and animal model research. The peptide contains two methionine residues which are susceptible to oxidation, so light exposure and vigorous agitation shall be minimized during laboratory handling.