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CJC-1295 (No DAC) vs Glutathione

CJC-1295 (No DAC) and Glutathione 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:Metabolic
ClassGHRH(1-29) tetra-substituted analogue (DAC-free)Endogenous thiol tripeptide (γ-L-glutamyl-L-cysteinyl-glycine), reduced form
Molecular weight3367.9 g/mol307.3 g/mol
CAS numberNot assigned / not specified70-18-8
Purity spec≥99%≥99%
Research areasHormonal & Endocrine, MetabolicCellular Longevity, Metabolic
Primary diluentBacteriostatic water (0.9% benzyl alcohol)Sterile water (USP grade)
Working windowCommonly worked with for 2-3 weeks at 2-8 °C.Commonly worked with for about 1 week at 2-8 °C; frozen aliquots keep longer.
Lead degradation routeDeamidation at Asn/Gln residues over long solution storage.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.
Freeze–thawAliquot on first reconstitution; avoid re-freezing the solution.Tolerates a few freeze-thaw cycles, but each thaw exposes the thiol to dissolved oxygen. Aliquot once and thaw each portion only once.
Light sensitivityNo specific light requirement beyond normal practice.Not strongly light-sensitive, but oxygen-sensitive: minimise headspace and avoid metal spatulas or metal-contaminated buffers.

How they actually differ

Comparing the two: CJC-1295 (No DAC) is ghrh(1-29) tetra-substituted analogue (dac-free), while Glutathione is endogenous thiol tripeptide (γ-l-glutamyl-l-cysteinyl-glycine), reduced form — different molecular classes with different handling consequences; they call for different primary diluents (bacteriostatic water (0.9% benzyl alcohol) versus sterile water (usp grade)); their leading degradation routes differ (deamidation at asn/gln residues over long solution storage. for CJC-1295 (No DAC), 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), 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.

CJC-1295 (No DAC) — origin

CJC-1295 without DAC is the first 29 residues of growth-hormone-releasing hormone carrying four stabilising substitutions (D-Ala2, Gln8, Ala15, Leu27) that resist DPP-4 cleavage. Omitting the Drug Affinity Complex — the albumin-binding element of the DAC version — gives it a short half-life, which is the property researchers study it for.

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.

CJC-1295 (No DAC) research themes

Pulsatile GH release

Studied for prompting growth-hormone release in short, physiological pulses via the GHRH receptor.

DPP-4 resistance

The four substitutions are studied for extending the molecule beyond the minutes-long survival of native GHRH.

Complementary pairing

Frequently studied alongside ghrelin-receptor secretagogues such as Ipamorelin, which recruit a second GH-release pathway.

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.

CJC-1295 (No DAC) handling

  • Reach room temperature before opening.
  • Swirl to dissolve; do not shake or vortex — foam indicates interfacial stress on the helix.
  • Aliquot and refrigerate; never re-freeze reconstituted solution.

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.

Both third-party tested

Every Popular Peptides batch of CJC-1295 (No DAC) and Glutathione 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.

CJC-1295 (No DAC) reference

Glutathione reference

Related comparisons

CJC-1295 (No DAC) and Glutathione 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.