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L-GLUTATHIONE

CAS#: 70-18-8

L-GLUTATHIONE

Research Use Only

All products are intended solely for laboratory research and are not for human or animal consumption. By purchasing, the buyer agrees to use these products in compliance with all applicable laws.

L-Glutathione Overview

L-Glutathione is a ubiquitous tripeptide present in virtually all living organisms, serving as a primary intracellular antioxidant and redox regulator. In its reduced form (GSH), it participates in neutralizing reactive oxygen species (ROS), maintaining redox homeostasis, and supporting the integrity of proteins, lipids, and DNA against oxidative stress. Through its sulfhydryl group on the cysteine residue, glutathione acts as a substrate for peroxidase enzymes that reduce hydrogen peroxide and lipid peroxides. Research models examine its role in phase II conjugation pathways, molecular proliferation and signaling, mitochondrial function, and protein folding regulation in laboratory settings.

Forman et al. (2009). Lu (2013).

History

Glutathione was first discovered in 1888 by J. de Rey-Pailhade as a sulfur-containing compound in yeast and animal tissues, initially termed “philothion.” The complete chemical structure as a γ-glutamylcysteinylglycine tripeptide was elucidated in 1935 by Frederick Gowland Hopkins, who received the Nobel Prize for his contributions to vitamin discovery. Since then, glutathione has been recognized as a fundamental molecule in cellular biochemistry and redox biology.

Meister & Anderson (1983).

L-Glutathione Structure

CAS#: 70-18-8

Molecular Formula: C₁₀H₁₇N₃O₆S

Molecular Weight: 307.32 g/mol

PubChem ID: 124886

Research Findings

L-Glutathione has been extensively studied in redox biology research, with investigations focusing on antioxidant mechanisms, conjugation pathways, signaling modulation, and molecular integrity in various experimental models. Studies examine glutathione’s role in enzymatic reactions, protein modification, and molecular signaling cascades.

Key Areas of Research:

  • Antioxidant: ROS neutralization, oxidative stress dynamics, lipid peroxidation

  • Conjugation: Phase II reactions, xenobiotic pathways, heavy metal chelation

  • Signaling: Lymphocyte dynamics, cytokine pathway regulation

  • Molecular: Mitochondrial function, protein folding, apoptosis regulation, genomic signaling

Together, these investigations demonstrate glutathione’s central role in redox homeostasis and molecular integrity. As a multifunctional tripeptide, GSH serves as a research tool for examining oxidative stress responses, conjugation capacity, signaling dynamics, and molecular resilience in diverse experimental systems.

Forman et al., Molecular Aspects of Medicine, 2009

Our Process

STEP 1

Precision Lyophilization

Manufactured in a controlled U.S. facility under strict compounding standards.

STEP 2

Verified Purity

Every batch third-party tested with HPLC and mass spectrometry.

STEP 3

Same-Day Fulfillment

Orders dispatched same-day from our U.S. facility.
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Frequently Asked Questions

Orders dispatched same-day from our U.S. facility.

Each vial contains exactly what’s shown on the label. For example, a 10mg vial has exactly 10mg of lyophilized peptide. Researchers can divide it into smaller portions—like four 2.5mg measurements—but the total amount remains 10mg.

Peptides are supplied as lyophilized powder. They do not come reconstituted, and any extra supplies must be sourced separately for research applications.
In lyophilized powder form, peptides stay stable for up to 2 years. After reconstitution, it should be refrigerated and is generally stable for up to 2 months.

Products from Raw Peptides do not include usage instructions, as they are strictly for in vitro research and prohibited by law for human or animal use. Misuse or unlawful application will result in permanent denial of service.

Lyophilized peptides should be stored away from heat and light. Once reconstituted, they must be refrigerated to maintain stability and efficacy.