Skip to content
WELCOME10 — 10% OFF YOUR FIRST ORDERSHOP NOW →

Glutathione vs MOTS-C

Glutathione and MOTS-C are studied in overlapping research areas, which is why they are frequently compared. This is a neutral side-by-side reference drawn from published preclinical literature and laboratory handling data.

Shared research areas:Cellular LongevityMetabolic
ClassEndogenous thiol tripeptide (γ-L-glutamyl-L-cysteinyl-glycine), reduced formMitochondrial-derived peptide, 16 residues
Molecular weight307.3 g/mol2174.5 g/mol
CAS number70-18-8Not assigned / not specified
Purity spec≥99%≥98%
Research areasCellular Longevity, MetabolicMetabolic, Cellular Longevity
Primary diluentSterile water (USP grade)Sterile or bacteriostatic water
Working windowCommonly worked with for about 1 week at 2-8 °C; frozen aliquots keep longer.Commonly worked with for 2–3 weeks at 2–8 °C.
Lead degradation routeOxidation of the cysteine thiol to glutathione disulfide (GSSG, about 612.6 Da), catalysed by trace Cu²⁺/Fe³⁺ and faster at neutral-to-alkaline pH.Methionine oxidation to the sulfoxide (+16 Da), and MOTS-c carries methionine at the N-terminus and internally.
Freeze–thawTolerates a few freeze-thaw cycles, but each thaw exposes the thiol to dissolved oxygen. Aliquot once and thaw each portion only once.Aliquot on reconstitution. Each vial opening introduces oxygen that acts on two susceptible residue types at once.
Light sensitivityNot strongly light-sensitive, but oxygen-sensitive: minimise headspace and avoid metal spatulas or metal-contaminated buffers.Protect from light throughout — tryptophan photo-oxidation applies here as it does to DSIP.

How they actually differ

Comparing the two: Glutathione is endogenous thiol tripeptide (γ-l-glutamyl-l-cysteinyl-glycine), reduced form, while MOTS-C is mitochondrial-derived peptide, 16 residues — different molecular classes with different handling consequences; they call for different primary diluents (sterile water (usp grade) versus sterile or bacteriostatic water); their leading degradation routes differ (oxidation of the cysteine thiol to glutathione disulfide (gssg, about 612.6 da), catalysed by trace cu²⁺/fe³⁺ and faster at neutral-to-alkaline ph. for Glutathione, methionine oxidation to the sulfoxide (+16 da), and mots-c carries methionine at the n-terminus and internally. for MOTS-C), so the storage precautions that matter are not the same; their practical working windows differ once reconstituted. The sections below set out each in full.

Glutathione — origin

Glutathione is the tripeptide γ-glutamyl-cysteinyl-glycine. The glutamate is joined through its side-chain (γ) carboxyl rather than the usual α link, which protects it from most peptidases. It was named by Frederick Gowland Hopkins in 1921, and its role in cellular redox chemistry was mapped out through the 20th century, most influentially in Alton Meister's work on the γ-glutamyl cycle.

MOTS-C — origin

MOTS-c is encoded not in nuclear DNA but within the mitochondrial genome — specifically an open reading frame inside the 12S ribosomal RNA gene. Its discovery helped establish that mitochondria encode short signalling peptides that act on the rest of the cell, a genuinely recent addition to cell biology and the reason the compound attracted rapid research interest.

Glutathione research themes

Cellular redox buffering (GSH/GSSG ratio)

Glutathione is the most abundant low-molecular-weight thiol in most cells, and the ratio of reduced to oxidised glutathione is widely used as a read-out of oxidative stress in cell-culture and tissue studies.

The γ-glutamyl cycle

Meister and Anderson (Annu Rev Biochem 1983) reviewed glutathione synthesis by γ-glutamylcysteine synthetase and glutathione synthetase, and its breakdown by γ-glutamyl transpeptidase — the framework most synthesis and turnover studies still use.

Detoxification by glutathione S-transferases

GSTs conjugate glutathione to electrophilic compounds, and this conjugation step is a standard model in xenobiotic-metabolism research.

The glutathione peroxidase system

Glutathione peroxidases use GSH to reduce hydrogen peroxide and lipid hydroperoxides, with glutathione reductase recycling GSSG back to GSH using NADPH — a common model for studying peroxide handling in vitro.

MOTS-C research themes

Mitochondrial-derived signalling

Part of a novel class demonstrating that mitochondria encode peptides acting systemically.

AMPK pathway

The most-studied signalling interaction, examined in metabolic and exercise models.

Insulin sensitivity

Investigated in glucose-metabolism research models.

Exercise and longevity biology

Studies have examined MOTS-c expression in relation to physical activity and ageing in animal models.

Glutathione handling

  • Let the vial reach room temperature before opening to stop condensation getting in.
  • Use degassed diluent where possible and cap promptly after drawing.
  • Avoid metal tools and buffers with trace copper or iron; plastic or glass only.
  • Label aliquots with reconstitution date and diluent.

MOTS-C handling

  • Use amber vials or wrap in foil; treat light protection as mandatory rather than precautionary.
  • Minimise vial openings — headspace oxygen is the practical driver of oxidation.
  • Use low-bind labware for dilute working solutions.

Both third-party tested

Every Popular Peptides batch of Glutathione and MOTS-C is independently tested by HPLC and LC-MS with a published Certificate of Analysis. Enter a lot number to pull the COA for a specific vial.

Glutathione reference

MOTS-C reference

Related comparisons

Glutathione and MOTS-C are supplied strictly as research chemicals for in-vitro laboratory and research use only. They are not intended for human or animal consumption, diagnostic, or therapeutic use. This comparison summarizes published preclinical literature and laboratory handling data; it is not medical advice, not a claim of efficacy, and not usage guidance.