Description
L Glutathione Reduced (GSH) – Lyophilized Reagent 1500 mg
Product Specification of L Glutathione
- Product Name : L Glutathione Reduced (GSH)
- Sequence : H-Glu-Cys-Gly-OH (Tripeptide)
- CAS Number : 70-18-8 (Distinct from Oxidized 27025-41-8)
- Molecular Formula : C10H17N3O6S
- Molecular Weight : 307.32 g/mol
- Purity : ≥99% (HPLC Verified)
- State : Lyophilized White Powder
- Solubility : Water Soluble (Highly Hygroscopic)
Disclaimer : For Research Use Only (RUO). Not for human use.
Technical Note: Beware of vendors citing MW ~612 g/mol. That is Oxidized Glutathione (GSSG), the byproduct of oxidative stress. For antioxidant and therapeutic modeling, Reduced (MW 307) is the required substrate.
Product Format : 1500mg Net Content (Lyophilized Vial)
Grade : Reference Material (≥99% HPLC)
CAS : 70-18-8
L Glutathione (Reduced) is the bioactive tripeptide substrate (γ-L-glutamyl-L-cysteinyl-glycine) required for defining redox potential in cellular assays.
Unlike Oxidized (GSSG) or low-purity industrial grades that compromise data integrity, this Lyophilized Reagent is processed to maintain the active sulfhydryl (-SH) moiety. The 1500mg unit size is configured for the preparation of fresh, high-molarity stock solutions in multi-well enzymatic or metabolic workflows (e.g., GST/GPx kinetics).
Chemical Identity & Mechanism
What GSH Does in Research Systems
Master Redox Buffer : The ratio of Reduced Glutathione (GSH) to Oxidized Glutathione (GSSG) is the primary quantifiable metric for cellular oxidative stress. In healthy physiology, this ratio exceeds 100:1; in pathological models (e.g., MASLD, Neurodegeneration), it collapses, driving apoptosis.
Enzymatic Substrate : GSH is the obligatory cofactor for Glutathione Peroxidase (GPx) (neutralizing peroxides) and Glutathione S-Transferases (GSTs) (phase II detoxification).
Pheomelanin Switch : In dermatological research, GSH is investigated for its ability to inhibit tyrosinase and redirect melanogenesis from dark eumelanin to lighter pheomelanin.
Structure of Reduced L Glutathione
2D Chemical Structure of Reduced L Glutathione (GSH) tripeptide showing the gamma-glutamyl-cysteinyl-glycine sequence with the active sulfhydryl (-SH) group highlighted.
Molecular Identity. Chemical structure of L Glutathione (Reduced Form). Verified CAS 70-18-8. Molecular Weight: 307.32 g/mol. This monomeric form contains the free thiol (-SH) required for electron donation in redox assays, distinct from the oxidized dimer (GSSG).
Comparative Research Context
Direct GSH vs. Precursors vs. Incretin-Class Tools
| Feature | L Glutathione (Direct) | GlyNAC (Precursors) | Reta / Tirz / Sema |
|---|---|---|---|
| Molecule Type | Intact Tripeptide | Amino Acid Blend | Receptor Agonist (GLP-1/GIP) |
| Mechanism | Direct Redox Buffer | Rate-Limiting Substrate | Receptor-Mediated Signaling |
| Primary Utility | Acute Restoration (Viral, Hepatic) | Chronic Maintenance (Geriatric) | Metabolic Regulation |
| Assay Target | Cytosolic GSH/GSSG Ratio | De Novo Synthesis Capacity | Insulin/Glucagon Pathways |
| Research Focus | MASLD, Long-COVID, T2DM | Aging “Deficit” Correction | Weight/Glucose Control |
Practical Interpretation for Researchers
- Select Direct GSH when the experimental design requires immediate elevation of cytosolic antioxidant capacity or when studying acute oxidative insults (e.g., viral load models, acute toxicity).
- Select GlyNAC when studying age-related downregulation of synthesis enzymes.
- Select Reta/Tirz when the focus is on hormonal/receptor pharmacology.
Research context and market status
1 – The “Delivery Revolution” (Liposomal & Micellar)
Historically, oral GSH research was dismissed due to rapid hydrolysis in the GI tract.
2025 Update : New Liposomal and LipoMicel delivery systems have fundamentally changed this landscape. Research confirms these vectors protect the peptide bond, allowing intact GSH to bypass hepatic hydrolysis and elevate systemic levels effectively.
Lab Implication : Researchers are now utilizing these advanced vectors to test GSH efficacy in systemic immunity (e.g., restoring Th1 cytokine responses in TB/HIV models).
2 – Metabolic Utility : The Liver-Pancreas Axis
MASLD (Fatty Liver) : Recent systematic reviews (2014–2024) identify GSH as a “fire extinguisher” for hepatic inflammation, significantly reducing ALT and oxidative DNA damage (8-OHdG) in MASH subtypes.
T2DM (Diabetes) : High-dose protocols have been shown to protect Insulin Receptor Substrate (IRS) proteins from stress kinase phosphorylation, directly improving whole-body insulin sensitivity in obese models.
3 – Critical Safety Warning :
Data Integrity & Usage Classification The Issue : FDA guidance and pharmacopeial standards strictly differentiate between Sterile APIs (for compounding) and Research Reagents.
Our Classification : Profound Aminos supplies this material strictly as a Chemical Reference Standard. It is not manufactured under the sterile conditions required for in vivo application.
The Protocol : We guarantee physicochemical stability and <1.0 EU/mg endotoxin levels solely to ensure reproducibility in in vitro cellular environments. This material is for laboratory analysis only.
Our Stance : 10peptides supplies GSH strictly as a Certified Reference Material (CRM) for analytical and in vitro applications. We guarantee thermodynamic stability and <1.0 EU/mg endotoxin levels solely to ensure reproducibility in sensitive cell culture environments.
Usage Definition : This material is chemically classified as a Laboratory Reagent. It is not designated for formulation, manufacturing, or any in vivo application.
- Handling & Stability
Storage : Store lyophilized powder at -20°C. Desiccate to prevent moisture absorption.
Reconstitution : Use bacteriostatic water or sterile buffer (PBS).
Stability Warning : Once reconstituted, GSH oxidizes rapidly to GSSG in the presence of air. Use immediately or freeze in single-use aliquots. Do not store dissolved GSH at room temperature.
Frequently Asked Questions
Q1: Is this product suitable for cosmetic formulation or personal use?
No. This material is a lyophilized Chemical Reference Standard designed strictly for in vitro laboratory analysis. It is not a sterile pharmaceutical ingredient (API) and does not meet the necessary pharmacopeial monographs (USP/EP) for cosmetic, therapeutic, or in vivo application. It lacks the buffer systems and sterility required for any biological administration.
Q2: Why use “Reduced” Glutathione?
Reduced” (GSH) is the active antioxidant form that donates electrons. “Oxidized” (GSSG) is the spent form. For research into redox capacity, you must start with the reduced form to measure the system’s ability to neutralize ROS.
Q3: How does this differ from NAC (N-Acetylcysteine)?
NAC is a precursor that provides cysteine. GSH is the final molecule. Using GSH directly in
assays bypasses the rate-limiting enzymatic steps required to convert NAC, providing immediate redox control in your model.
Q4: Can I use this for “Anti-Aging” research?
Yes, in the context of cellular senescence models. GSH depletion is a hallmark of aging (the “GSH Gap”). Researchers use this peptide to test if restoring cytosolic levels can reverse mitochondrial dysfunction in senescent cell lines.
