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Glutathione-1200mg

Glutathione-1200mg

$50.00
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FOR RESEARCH USE ONLY – NOT FOR HUMAN OR VETERINARY USE
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Form: Powder/solution-ready material (1200mg)

šŸ”¬ Glutathione — Overview

Glutathione is a naturally occurring tripeptide composed of three amino acids — glutamate, cysteine, and glycine — that serves as the primary intracellular antioxidant and a central component of cellular redox homeostasis in animals, plants, and many microorganisms. It exists mainly in a reduced form (GSH) and can be reversibly oxidized (to GSSG) during detoxification and oxidative stress responses. It also participates in detoxification, immune regulation, and metabolic processes.


šŸ“Œ Brief Functional Description

  • Antioxidant & Redox Buffer: Glutathione neutralizes reactive oxygen species (ROS) and reactive nitrogen species, protecting cells from oxidative damage.
  • Detoxification: Acts as a cofactor for glutathione-dependent enzymes (e.g., glutathione peroxidase) and contributes to conjugation reactions that facilitate elimination of toxins.
  • Cellular Roles: Involved in immune function, protein and DNA synthesis, recycling of other antioxidants (like vitamins C and E), and maintenance of thiol status in proteins.
  • Physiological Importance: Produced by the liver and widely present in tissues; levels may decline with aging, stress, or toxin exposure.

🧪 Chemical & Structural Information

šŸ”¢ CAS Number

  • 70-18-8 — the primary CAS registry number for reduced glutathione (GSH).

🧬 Molecular Formula

  • C₁₀H₁₇Nā‚ƒO₆S — the elemental composition of reduced glutathione.

āš–ļø Molecular Weight

  • ā‰ˆ307.32 g/mol (Da) — average molecular weight of GSH.

🧬 Amino Acid Sequence & Structure

  • γ-L-Glutamyl-L-cysteinyl-glycine — unique among peptides because the glutamate–cysteine bond is a γ-peptide linkage (i.e., between the side-chain carboxyl of glutamate and the amino group of cysteine).
  • The thiol (-SH) group on the cysteine residue is the active center for antioxidant and detoxification chemistry.
  • In solution, GSH exists predominantly in the reduced form, and two GSH molecules can form a disulfide (GSSG) upon oxidation.

🧪 Typical SMILES (text structural representation, reduced form):

NC(CCC(=O)NC(CS)C(=O)NCC(=O)O)C(O)=O
(This encodes the backbone with the cysteine thiol.)


🧠 Mechanism & Biological Context

  • Antioxidant defense: GSH directly scavenages radicals and acts as a substrate for glutathione peroxidase, which reduces peroxides to water or alcohols, forming GSSG.
  • Redox cycling: The enzyme glutathione reductase uses NADPH to regenerate GSH from GSSG, maintaining a highly reduced intracellular environment.
  • Detoxification reactions: Through glutathione S-transferases, GSH conjugates electrophiles and facilitates elimination of xenobiotics.
  • Cell signaling & protein modification: GSH participates in reversible protein glutathionylation, impacting protein function and cellular signaling.

āš ļø Safety & Supplement Notes

  • Forms: Supplements and research reagents often refer specifically to the reduced form (GSH).
  • Clinical benefits proposed for supplementation include support for oxidative balance, liver health, and immune function, although evidence varies by context.

🧪 Quick Reference

Property Detail
Name Glutathione (reduced form, GSH)
CAS # 70-18-8
Molecular Formula C₁₀H₁₇Nā‚ƒO₆S
Molecular Weight ~307.32 Da
Type Tripeptide antioxidant
Sequence γ-L-Glutamyl-L-cysteinyl-glycine
Primary Function Antioxidant defense, detoxification, redox homeostasis

Notice: Research use only. Not for human or veterinary use.

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