MOTS-c 10mg

MOTS-c 10mg

$82.95
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MOTS-c 10mg :

Unit Size 10 mg/vial
Unit Quantity 1 vial
Purity (Mass Spectrometry and UV) 99.38%
Sequence Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg
Molecular Formula C101H152N28O22S2
Appearance Lyophilized White Powder
Source Chemical Synthesis
Storage
Lyophilized Mots-C 10mg is stable at room
Temperature for 90 days, however it is best to storer
in a freeze below - 8c for any extended period of time.
Terms The products we offer are intended for laboratory
research use only. Please familiarize yourself with
our terms of service prior to ordering.

MOTS-c 10mg

All content and product information provided on this website are for informational and educational research purposes only. This product is not intended for human consumption, diagnostic use, or therapeutic use.
View Research Overview & References

MOTS-c—short for Mitochondrial ORF of the 12S rRNA Type C—is a 16-amino acid peptide originating from the mitochondrial genome's 12S rRNA region. As part of the class of mitochondrial-derived peptides (MDPs), it is studied in vitro for its role in cellular stress-response signaling.

Nuclear Translocation Research in Human Cells

In vitro studies using human cells found that MOTS-c dynamically translocates from the cytoplasm to the nucleus in response to metabolic stress, where it regulates nuclear gene expression in an AMPK-dependent manner.

Substituting the hydrophobic core residues of MOTS-c with alanines prevented this nuclear translocation, indicating that the process depends on the peptide's specific sequence rather than concentration alone.1

Peptide Origin: A Mitochondrially-Encoded Research Peptide

MOTS-c is structurally unusual among research peptides in that its sequence is encoded within a short open reading frame inside the mitochondrial 12S ribosomal RNA gene rather than by a conventional nuclear protein-coding gene.

Researchers studying its biology have noted that this mitochondrial origin required the discovery of an unconventional translation event, since the 12S rRNA region was not previously recognized as protein-coding. This distinguishes MOTS-c from the broader category of nuclear-DNA-derived signaling peptides.

Analytical Purity Verification

Purity verification for MOTS-c typically combines HPLC with mass spectrometry to confirm the intact 16-residue sequence, with particular attention to the two methionine residues present in the sequence, which are susceptible to oxidation during synthesis and storage.

Storage and Handling in the Laboratory Setting

Given the oxidation-prone methionine residues in its sequence, MOTS-c is best preserved in lyophilized form under sub-zero freezer conditions, away from light and oxidative exposure, since methionine oxidation could alter the peptide's structural and signaling properties in downstream cell-based assays.

Comparative Research Context Among Mitochondrial-Derived Peptides

MOTS-c is studied alongside other mitochondrial-derived peptides, including humanin and the small humanin-like peptides (SHLPs), all of which originate from short open reading frames within mitochondrial DNA rather than the nuclear genome.

Researchers comparing these peptides have focused on their distinct tissue distributions and signaling targets, using MOTS-c's documented AMPK-pathway activation and nuclear translocation under metabolic stress as a point of contrast with humanin's separately characterized cytoprotective signaling profile.

Important Compliance Notice

This product is intended strictly for in vitro laboratory research. It is not for human consumption, nor is it approved for diagnostic or therapeutic applications. These findings do not establish safety, efficacy, or suitability for any human application.

References

1. Kim KH, Son JM, Benayoun BA, Lee C. The mitochondrial-encoded peptide MOTS-c translocates to the nucleus to regulate nuclear gene expression in response to metabolic stress. Cell Metab. 2018;28(3):516-524.e7.

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