Overview
MOTS-c is a short peptide encoded by the mitochondrial genome and is classified in scientific literature as a mitochondrial-derived peptide (MDP). MDPs are discussed in research contexts as signaling molecules associated with mitochondrial communication and intracellular regulatory networks within experimental systems.
Published research describes MOTS-c as being detected in multiple cellular compartments, including mitochondria and, under specific laboratory conditions, the nucleus. Observations regarding localization, interactions, and molecular associations are derived exclusively from controlled in-vitro experiments and animal model studies. These findings are descriptive in nature and are confined to non-clinical research environments.
All references to MOTS-c pertain strictly to mechanistic and observational investigations conducted in laboratory settings and do not extend beyond experimental research use.
Biochemical Characteristics
Reference Source: Public biochemical databases and research literature
Amino Acid Sequence:
Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg
Molecular Formula: C₁₀₁H₁₅₂N₂₈O₂₂S₂
Molecular Weight: 2,174.64 g/mol
PubChem SID: 255386757
CAS Registry Number: 1627580-64-6
Reported Identifiers / Synonyms:
Mitochondrial open reading frame of the 12S rRNA-c (MT-RNR1)
MOTS-c is composed of 16 amino acids. Its primary structure and molecular composition have been documented in biochemical reference sources based on non-clinical analytical characterization. Structural descriptions are limited to physicochemical properties and reported sequence data.
Research Applications
Within the scientific literature, MOTS-c has been referenced in laboratory research involving cellular assays and animal-based experimental models. These studies describe measured molecular markers, signaling components, and pathway-associated readouts observed under defined experimental conditions.
Reported areas of investigation include:
- Mitochondria-associated signaling components
- Nuclear localization phenomena under controlled experimental parameters
- AMPK-linked signaling elements
- Molecular markers associated with metabolic pathways
- Gene expression profiles assessed in cell and animal models
All reported uses are restricted to exploratory and descriptive research conducted in controlled laboratory environments.
Pathway & Mechanistic Context
Preclinical publications discuss MOTS-c in relation to intracellular signaling frameworks associated with energy sensing and cellular stress responses, including components commonly associated with AMPK-related pathways.
Additional research reports describe experimental observations of MOTS-c localization within the nucleus under specific laboratory conditions, alongside correlations with transcription-related molecular markers of nuclear-encoded genes. These descriptions are limited to biochemical and molecular observations and do not imply functional or clinical outcomes.
All pathway-related discussions are confined strictly to non-clinical research contexts.
Summary of Preclinical Research Observations
Preclinical literature documents experimental observations involving MOTS-c across cellular and animal model systems. Reported findings include measurements of signaling proteins, metabolite-associated profiles, and gene expression indicators collected under defined experimental designs.
Additional studies describe associations between MOTS-c and molecular features observed in experimental models of metabolic stress and mitochondrial perturbation. All observations remain specific to the experimental systems and methodologies employed.
Form & Analytical Considerations
MOTS-c is supplied as a research-grade peptide material intended for laboratory investigation. Molecular identity and composition have been described in scientific literature using analytical techniques commonly applied to peptide research, including chromatographic separation methods and mass spectrometric analysis.
Handling, storage conditions, and analytical verification procedures are established by individual laboratories in accordance with internal research protocols and regulatory guidance applicable to research materials.
Scientific Attribution & Literature Context
The scientific concepts summarized above are derived from published research conducted by multiple investigators studying mitochondrial-derived peptides. References to individual researchers and institutions are provided solely for academic acknowledgment of their contributions to the scientific literature.
Any mention of researchers, authors, or institutions does not imply endorsement, affiliation, or authorization of this product for any purpose. Such references are included strictly to recognize published scientific work related to mitochondrial peptides and their characterization in experimental research.
Research Use Only (RUO) Notice
All products available on this website are provided exclusively for in-vitro laboratory research purposes. In-vitro studies are performed outside of living organisms under controlled experimental conditions.
These materials are not drugs, medicines, or therapeutic agents and have not been reviewed or approved by the U.S. Food and Drug Administration (FDA) for the diagnosis, treatment, prevention, or cure of any disease or medical condition.
Any form of administration or introduction into humans or animals is strictly prohibited by law.