Buy MOTS-c (40mg Vials) – Peptide Partners

Product Overview & Specifications

MOTS-c (mitochondrial open reading frame of the 12S rRNA-c) is a mitochondrial genome-encoded peptide investigated for its role in metabolic regulation, muscle differentiation, and mitochondrial-nuclear crosstalk. Peptide Partners supplies this research-grade material for in-vitro testing, laboratory experimentation, receptor pharmacology, structural biology, and preclinical metabolic research.

Published studies have examined MOTS-c using myoblast cell lines (LHCN-M2, C2C12), hepatocyte models, protein-protein interaction assays, metabolomic profiling, kinase activation studies, and transcription factor binding analyses. Research areas include myotube formation, STAT3 signaling modulation, Bcl-2 interactions, CK2 kinase activation, mitochondrial metabolic reprogramming, and inflammatory pathway regulation.

The product name supplied for this listing is “MOTS-c (40mg Vials).” Researchers should verify the exact identity, sequence, formulation, and batch-specific certificate of analysis before beginning any experiment. Findings from published MOTS-c studies should not be assumed to apply to every commercial batch or formulation.

Product Specifications

Specification	Details
Product name	MOTS-c (40mg Vials)
Compound type	Mitochondrial genome-encoded peptide (16 amino acids)
Primary molecular targets	STAT3 transcription factor, Bcl-2 protein, protein kinase CK2
Primary research areas	Metabolic regulation, muscle differentiation, mitochondrial-nuclear crosstalk, Bcl-2 interactions, CK2 kinase activation, and inflammatory signaling
Product format	40 mg vials
Vial size	40 mg
Vial capacity	3 mL
Available box combinations	80 mg, 200 mg, and 400 mg
Multi-vial purity	99.41%
Independent testing	Yes
Endotoxin screening	Passed
Heavy-metals screening	Passed
Purity screening	Passed
Manufacturer ID	WF03
Batch ID	MC202602
Cost per milligram	$2.00–$3.15

The stated 99.41% purity is based on multi-vial testing. Researchers should review the batch-specific certificate of analysis before beginning any experiment.

Primary Research Studies & Findings

MOTS-c Promotes Muscle Differentiation In Vitro

Authors: Sandra García-Benlloch, Francisco Revert-Ros, Jose Rafael Blesa, and Rafael Alis

Publication: Peptides (ScienceDirect), 2022

DOI: 10.1016/j.peptides.2022.170891

Reference: View publication

This study investigated the effect of MOTS-c on myogenesis in human (LHCN-M2) and murine (C2C12) myoblasts. The findings indicate that wild-type MOTS-c peptide enhances myotube formation, whereas a variant with a substitution at tyrosine 8 (Y8F) does not. Furthermore, wild-type MOTS-c, but not the Y8F peptide, was shown to counteract the interleukin-6 (IL-6)-induced reduction of nuclear myogenin.

The proposed mechanism is that MOTS-c interacts with the STAT3 transcription factor via its putative SH2 binding motif (YIFY region), thereby reducing STAT3’s transcriptional activity and promoting myotube formation. The researchers demonstrated that the YIFY motif is critical for MOTS-c’s biological activity in muscle cell differentiation models.

The study provides mechanistic insights into how mitochondrial-derived peptides can influence nuclear gene expression and cellular differentiation programs. The findings suggest MOTS-c as a valuable research tool for studying mitochondrial-nuclear crosstalk and muscle development pathways.

Plain-English Research Summary

This research explored how a naturally occurring peptide called MOTS-c affects muscle cell development. Using muscle cells from both humans and mice, the scientists found that MOTS-c helps these cells to mature and form muscle fibers. They also discovered that a specific part of the MOTS-c molecule is crucial for this process. When this part was altered, the beneficial effect was lost. The study suggests that MOTS-c works by influencing a key protein (STAT3) involved in cell growth, which in turn enhances the formation of new muscle tissue.

The Mitochondrial Genome-Encoded Peptide MOTS-c Interacts with Bcl-2 to Alleviate Nonalcoholic Steatohepatitis Progression

Authors: Huanyu Lu, Linni Fan, Wenli Zhang, Guo Chen, An Xiang, Li Wang, Zifan Lu, and Yue Zhai

Publication: Cell Reports (ScienceDirect), 2023

DOI: 10.1016/j.celrep.2023.113599

Reference: View publication

This study elucidates the molecular mechanism by which MOTS-c ameliorates nonalcoholic steatohepatitis (NASH). The research demonstrates that MOTS-c directly interacts with the BH3 domain of the antiapoptotic protein B-cell lymphoma-2 (Bcl-2). This interaction enhances Bcl-2 protein stability by suppressing its ubiquitination.

In vitro experiments using a Bcl-2 inhibitor and adeno-associated virus (AAV)-mediated Bcl-2 knockdown confirmed that the protective effects of MOTS-c against NASH-induced mitochondrial dysfunction, inflammation, and fibrosis are dependent on Bcl-2 function. Metabolomic analysis further revealed that MOTS-c reverses NASH-induced mitochondrial metabolic deficiencies.

The findings establish a direct molecular interaction between MOTS-c and Bcl-2, linking mitochondrial peptide signaling to apoptotic regulation and metabolic homeostasis. The research provides a mechanistic framework for understanding how mitochondrial-derived peptides can influence liver pathology in experimental models.

Plain-English Research Summary

This research uncovers how a natural peptide called MOTS-c can help protect the liver from a serious condition called nonalcoholic steatohepatitis (NASH), which is a severe form of fatty liver disease. The scientists discovered that MOTS-c works by interacting with a protein called Bcl-2, which is known to prevent cell death. By binding to Bcl-2, MOTS-c makes it more stable and prevents it from being broken down by the cell. This action helps to restore normal function to the mitochondria, the powerhouses of the cells, and reduces the inflammation and scarring associated with NASH.

MOTS-c Modulates Skeletal Muscle Function by Directly Binding and Activating CK2

Authors: Hiroshi Kumagai, Su-Jeong Kim, Brendan Miller, et al.

Publication: iScience (Cell Press), 2024

DOI: 10.1016/j.isci.2024.111237

Reference: View publication

This study identifies protein kinase CK2 as a direct and functional target of MOTS-c. In vitro, cell-free systems demonstrated that MOTS-c directly binds to and activates CK2. This interaction is crucial for the metabolic effects of MOTS-c. The study also investigated a naturally occurring variant, K14Q MOTS-c, which showed reduced binding to CK2 and a concomitant lack of activation.

The researchers used biochemical assays, structural modeling, and functional studies to characterize the MOTS-c–CK2 interaction. The K14Q variant’s reduced binding affinity provided a molecular basis for the observed physiological effects, linking the in vitro findings to in vivo and clinical observations.

The findings establish CK2 as a direct downstream effector of MOTS-c signaling, providing mechanistic insights into how this mitochondrial peptide regulates cellular metabolism. The research demonstrates that single amino acid variations can significantly alter peptide-protein interactions and biological activity.

Plain-English Research Summary

This research discovered that a small protein called MOTS-c works by directly switching on an enzyme called CK2. Using experiments in a test tube, the scientists showed that MOTS-c binds to CK2 and activates it. This is like a key fitting into a lock to turn on a machine. They also found that a common variation of the MOTS-c ‘key’ doesn’t fit the CK2 ‘lock’ as well, and so it can’t turn on the machine. This discovery helps to explain how MOTS-c affects our bodies at a molecular level, and why some people might be more prone to certain health issues.

Standard Research Disclaimer

Research Use Only. Not for use in diagnostic tests.

This product is solely intended for research purposes as a chemical compound. It is designated exclusively for in-vitro testing and laboratory experimentation. All information provided about this product is educational and should be evaluated by appropriately qualified research personnel.

By law, bodily introduction of this product into humans or animals is strictly prohibited. This compound must not be used, administered, or represented as a drug, food, dietary supplement, metabolic treatment, muscle-building compound, liver treatment, diagnostic material, or medical treatment. It is not intended to diagnose, treat, cure, or prevent any disease. It should be handled only by licensed and qualified professionals in an appropriately equipped laboratory and in accordance with applicable laws, institutional procedures, and relevant safety requirements.