MOTS-c

$50

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MOTS-c is a naturally occurring mitochondrial-derived peptide involved in cellular energy regulation, metabolic signaling, and mitochondrial communication pathways. It is widely studied for its role in metabolic adaptation, AMPK-related signaling, glucose utilization, and longevity-focused research applications.

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Third-Party Tested

Independent analytical testing performed on supported batches.

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Accessible Verification

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Retatrutide

MOTS-c

Synonym: Mitochondrial Open Reading Frame of the 12S rRNA-c

CAS Number: N/A

Molecular Formula: C₁₀₁H₁₅₂N₂₈O₂₂S₂

Molecular Weight: ~2174.7 g/mol

Structure: Mitochondrial-derived peptide consisting of 16 amino acids


Overview

MOTS-c is a naturally occurring mitochondrial-derived peptide (MDP) encoded within the mitochondrial 12S ribosomal RNA region. Unlike most peptides encoded by nuclear DNA, MOTS-c originates from the mitochondrial genome and functions as a signaling molecule involved in the regulation of cellular metabolism and energy homeostasis.

The peptide has attracted significant research interest due to its role in metabolic adaptation, mitochondrial signaling, and cellular responses to energetic stress.


Mechanism of Action

MOTS-c functions as a metabolic signaling peptide influencing several cellular pathways:

  • Metabolic Regulation
    • Modulates pathways involved in glucose utilization and energy balance
    • Influences cellular adaptation to nutrient availability
  • AMPK-Related Signaling
    • Associated with activation of pathways linked to AMP-activated protein kinase (AMPK)
    • Supports cellular responses to energetic stress
  • Mitochondrial-Nuclear Communication
    • Functions as a signaling molecule between mitochondria and the nucleus
    • Influences expression of genes involved in metabolism and cellular maintenance
  • Cellular Stress Response
    • Participates in adaptive responses to metabolic and environmental stressors
    • Contributes to maintenance of metabolic homeostasis

The peptide is considered an important component of mitochondrial signaling networks that coordinate cellular energy management.


Pharmacokinetic Characteristics

  • Naturally produced within mammalian tissues
  • Small peptide structure enables systemic signaling activity
  • Participates in endogenous mitochondrial communication pathways
  • Metabolized through normal peptide degradation mechanisms

Structural Characteristics

MOTS-c is a 16-amino acid peptide encoded by mitochondrial DNA.

Key features include:

  • Mitochondrial genomic origin
  • Conserved sequence among mammalian species
  • Functions as a bioactive signaling peptide
  • Distinct from traditional nuclear-encoded peptide hormones

Research Applications

MOTS-c is commonly studied in research involving:

  • Mitochondrial function
  • Cellular energy metabolism
  • Metabolic signaling pathways
  • AMPK-related biology
  • Glucose utilization mechanisms
  • Longevity and healthy aging research

It is frequently utilized in investigations exploring the relationship between mitochondrial signaling, cellular adaptation, and metabolic homeostasis.


Handling & Stability

  • Typically supplied as a lyophilized powder
  • Requires reconstitution with a suitable sterile solvent prior to use
  • Store at -20°C or below for long-term stability
  • Protect from excessive heat, moisture, and prolonged light exposure
  • Avoid repeated freeze-thaw cycles

Note

This material is intended for laboratory research use only and is not approved for human or veterinary applications.

Every batch undergoes independent third-party analytical testing for purity, identity, and consistency. Relevant documentation is maintained to support verification and traceability.
Yes. Analytical documentation is maintained for supported products and batches. Verification resources are available to help researchers review relevant testing information.
Each production batch is assigned documentation that links materials to associated testing records and verification resources, helping maintain consistency and transparency.
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