| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Mitochondrial-derived peptide MOTS-c|Mitochondrial open reading frame of the 12S rRNA-c|MT-RNR1 |
| Assay Time | |
| Detection Method | |
| Detection Range | |
| Product Type | |
| Reactivity | |
| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
| Sensitivity | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Background
human MOTS-c (Mitochondrial-derived peptide MOTS-c) is a molecular target commonly studied in biomedical research. Many proteins are studied as molecular readouts that can change with cellular state, tissue remodeling, or stress responses.
Biological role and mechanism
The biological role of MOTS-c is typically understood in terms of its molecular category and interaction network. Depending on the model system, it may participate in cell–cell communication, intracellular signaling, enzymatic processing, or regulation of gene expression programs. Mechanistic interpretation is often strengthened by considering upstream regulators and downstream readouts rather than relying on a single marker.
Expression and abundance of MOTS-c can vary by tissue, cell type, and physiological state. In many systems, levels are influenced by factors such as developmental stage, immune activation, metabolic status, and cellular stress. Because sample matrix and pre-analytical handling can affect measured concentrations, interpretation is typically strongest when experiments keep collection and processing consistent across groups.
Nomenclature and related terms
MOTS-c (Mitochondrial-derived peptide MOTS-c) may also be referenced as Mitochondrial-derived peptide MOTS-c, Mitochondrial open reading frame of the 12S rRNA-c, and MT-RNR1 in the literature or in databases. When comparing results across studies, confirm that the reported analyte refers to the same molecule, species context, and molecular form (e.g., precursor vs mature protein, or soluble vs membrane-associated forms).
Why it matters in research
- Understanding how MOTS-c relates to signal transduction, tissue homeostasis, stress responses, and disease-model biology in biomedical research.
- Interpreting shifts in MOTS-c levels alongside other pathway components or complementary markers.
- Connecting molecular changes to phenotypes such as inflammation, remodeling, metabolism shifts, or cell-state transitions (context-dependent).
Molecular forms and interpretation
For some targets, isoforms, proteolytic processing, or post-translational modifications (such as phosphorylation or glycosylation) can influence function and apparent abundance. If multiple molecular forms are expected in your model, align interpretation with the form most relevant to the biological question.
Disease and translational relevance
MOTS-c has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with biomedical studies. These associations are interpreted as research findings rather than diagnostic or therapeutic claims, and they should be evaluated alongside model-specific covariates and study design.
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Effects of empagliflozin and dapagliflozin on serum humanin, MOTS-c levels, nitrosative stress, and ferroptosis parameters in diabetic patients with heart failure
IF: 4.2 Journal: European Journal of Pharmacology Author: Faculty of Medicine, Gaziantep University, Gaziantep, Turkey. Cited Date: 2024-08-30
MOTS-c relieves hepatocellular carcinoma resistance to TRAIL-induced apoptosis under hypoxic conditions by activating MEF2A
IF: 3.3 Journal: Experimental Cell Research Author: Department of pathophysiology, Jilin Medical University, Jilin 132013, Jilin Province, P.R. China. Cited Date: 2024-11-29
Nitrosative Stress, Mitochondrial Peptides, and Ferroptosis Markers in Corneal Epithelial Cells from Keratoconus Patients
IF: 2 Journal: Current Eye Research Author: Department of Medical Pharmacology, Faculty of Medicine, Gaziantep University, Gaziantep, Turkey. Cited Date: 2025-11-07