RESEARCH PEPTIDE

Glutathione | Laboratory Research Grade

Reduced Glutathione (GSH) Tripeptide — Research Reference
$59.00
Reduced L-glutathione (GSH; γ-Glu-Cys-Gly) supplied as a laboratory research material for analytical and cellular redox studies. Research use only. Not for human or veterinary use.
✓ Scientific Identity Established
⏳ Laboratory Testing In Progress
⏳ Batch Documentation Pending
✓ Research Use Only
✓ U.S. Fulfillment
In Laboratory Testing
Lot Verification Variant-specific documentation
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Primary Literature Peer-reviewed sources
Research Use Only Laboratory research materials

Scientific Specifications

Reference characteristics for laboratory research materials.

CAS Number
70-18-8
Purity
≥98%
Molecular Formula
C10H17N3O6S
Molecular Weight
307.32
Appearance
White lyophilized powder
Storage
-20°C
Research Classification
Research Use Only (RUO). Not for human or veterinary use.

SCIENTIFIC OVERVIEW

Scientific background and research classification for this laboratory reference material.

Glutathione (reduced; GSH) is the defined tripeptide L-γ-glutamyl-L-cysteinyl-glycine (γ-Glu-Cys-Gly). CAS 70-18-8; molecular formula C10H17N3O6S. It is characterized by a γ-glutamyl isopeptide bond (through the glutamate side-chain carboxyl) and a free cysteine thiol, which is the redox-active group. It is supplied as a reduced-glutathione reference material for laboratory research use only.

The governed material is the reduced form (GSH), distinct from oxidized glutathione (GSSG); it is provided as a single defined synthetic compound rather than a mixture.

Primary Research Category
Longevity & Cellular Health
Material Type
Lyophilized Peptide
Intended Use
Laboratory Research
Research Categories
Oxidative Stress

Mechanism of Action

Molecular interaction profile describing how this research material engages receptor systems and influences downstream biological signaling pathways.

Glutathione is the principal low-molecular-weight thiol antioxidant and redox buffer in cells. Its free cysteine thiol participates in redox chemistry, and it serves as a cofactor/substrate for enzymes such as glutathione peroxidases and glutathione S-transferases in oxidative-stress and detoxification biochemistry (Meister & Anderson, 1983; Forman et al., 2009). Glutathione is not a receptor ligand and has no defined governed-vocabulary molecular target; the transcription factor Nrf2 regulates glutathione biosynthesis upstream and is not a target of glutathione. The governed molecular-target and pathway fields are therefore left empty by design.

Biological Pathways
  • Oxidative Stress Response

Research Documentation

Laboratory documentation is presented when available for the selected product specification and current lot.

In Laboratory Testing
Laboratory Documentation In Progress

Laboratory documentation for the current lot is being completed.

Scientific References
Peer-Reviewed Literature

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Laboratory Resources
Technical Guidance

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Related Research
Companion Materials

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Research Center

Scientific literature, laboratory resources, and related materials curated to support research involving this research material.

Scientific References
Peer-Reviewed Literature

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Scientific Dossier
Deeper Technical Treatment

Comprehensive scientific documentation including literature review, mechanism, pharmacology, and study data for this research material.

Laboratory Resources
Technical Guidance

Storage guidance, handling information, analytical standards, research policies, and laboratory support documentation.

Research Library

Curated peer-reviewed literature selected to provide scientific context for this research material.

Review ArticleAnnual Review of Biochemistry 1983

Glutathione

The foundational comprehensive review of glutathione biochemistry — its structure, biosynthesis, metabolism (the γ-glutamyl cycle), and redox/detoxification roles — establishing the molecule's core biochemistry.
Velora Research Insight
Definitive foundational reference for glutathione identity and biochemistry (Meister, Cornell). Anchors the γ-glutamyl-tripeptide identity and redox-cofactor role; independent authoritative source.
Review ArticleMolecular Aspects of Medicine 2009

Regulation of glutathione synthesis

Authoritative review of glutathione biosynthesis and its regulation, including the enzymes and control points of the γ-glutamyl cycle.
Velora Research Insight
Biosynthesis/regulation synthesis (Lu, USC) — independent of the Meister lineage; supports the biosynthesis-and-metabolism research context.
Review ArticleMolecular Aspects of Medicine 2009

Glutathione: overview of its protective roles, measurement, and biosynthesis

Overview of glutathione's protective (antioxidant/redox) roles, methods for its measurement, and its biosynthesis — a widely cited reference on glutathione status and function.
Velora Research Insight
Protective-role/measurement/biosynthesis synthesis (Forman) — independent; supports oxidative-stress and analytical-measurement research context. Antioxidant/redox roles retained at evidence level, not as product efficacy.
Review ArticleThe Journal of Nutrition 2004

Glutathione metabolism and its implications for health

Review of glutathione metabolism and the γ-glutamyl cycle, summarizing its biochemical roles and research implications for cellular and organismal biology.
Velora Research Insight
Metabolism/biochemistry synthesis (Wu, Texas A&M) — independent; the 'implications for health' framing is retained strictly as research context, not as a health/efficacy claim for this research material.