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GLUTATHIONE 1500mg - Wholesale
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$75.00
Regular price
$150.00
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GLUTATHIONE 1500mg - Wholesale
Overview
Glutathione (GSH) is a naturally occurring tripeptide composed of glutamine, glycine, and cysteine. It is synthesized endogenously in the liver and is present in virtually every cell of the human body. Glutathione is the primary intracellular antioxidant and serves as the foundation of the body's broader antioxidant network. Endogenous levels decline with age by approximately 30–50% between young adulthood and older age, and are further depleted by oxidative stress, chronic illness, toxin exposure, and poor nutrition.
Mechanism of Action
Glutathione neutralizes free radicals and reactive oxygen species (ROS) by donating electrons via its sulfhydryl group. It regenerates oxidized vitamins C and E back to their active forms through the glutathione-ascorbate cycle, maintains the intracellular GSH/GSSG redox ratio, supports phase-II hepatic detoxification pathways, and modulates immune signaling. It also inhibits tyrosinase activity, which influences melanin synthesis.
Research and Off-Label Applications
Cellular antioxidant defense and oxidative stress reduction, hepatic detoxification and liver support, skin brightening and pigmentation modulation, immune function enhancement, neuroprotection and potential role in neurodegenerative conditions, post-chemotherapy recovery support, and general anti-aging and longevity protocols.
Administration
Oral bioavailability is poor due to gastrointestinal degradation of the tripeptide. Clinically meaningful systemic elevation is most reliably achieved via intravenous (IV) infusion, intramuscular (IM), or subcutaneous injection. Plasma half-life of reduced GSH is approximately 14 minutes; cellular effects accumulate with consistent administration over 4–8 week cycles. Liposomal oral formulations offer improved but still variable bioavailability.
Potential Adverse Effects
Generally well tolerated when administered appropriately. Serious adverse events include rare anaphylaxis and potential hepatotoxicity, particularly with intravenous use at non-standardized doses. Long-term use may reduce zinc levels. May worsen asthma in susceptible individuals if inhaled. Should not be used concurrently with chemotherapy without oncologist approval, as it may interfere with treatment efficacy. Quality and sterility of the source compound are critical safety considerations.
Properties
1. Basic Information
2. Structural Properties Peptide Nature: Tripeptide with an atypical isopeptide bond between the gamma-carboxyl group of glutamate and the alpha-amine of cysteine; this gamma-glutamyl linkage is not recognized by standard aminopeptidases, conferring resistance to conventional exopeptidase degradation; the glycine C-terminal residue is linked via a standard alpha-peptide bond
Secondary Structure: No defined secondary structure due to tripeptide length; the cysteine thiol group (pKa ~8.7) is the chemically active site; in reduced form (GSH) the thiol is free; in oxidized form (GSSG) two GSH molecules are covalently linked via a disulfide bond between their cysteine residues
Hydrophobicity: Predominantly hydrophilic; all three residues contribute polar character; the thiol group of cysteine adds minor hydrophobic contribution but the overall molecule is highly water-soluble
Charge: Net negative charge at physiological pH; the gamma-glutamyl alpha-carboxyl (pKa ~2.1), the cysteine thiol (pKa ~8.7), the glycine carboxyl (pKa ~3.5), and the glutamate amino terminus (pKa ~9.1) contribute to an overall charge of approximately −1 at pH 7.4
3. Solubility
4. Stability Thermal Stability: Sensitive to elevated temperatures in solution; lyophilized powder is considerably more stable; aqueous solutions should be prepared fresh or stored at −80°C for extended periods
Oxidative Stability: The free thiol group is readily oxidized to the disulfide (GSSG) upon air exposure, metal ion catalysis, or contact with oxidizing agents; GSSG formation is reversible enzymatically (glutathione reductase/NADPH) but not spontaneously under physiological conditions; protect aqueous solutions from air and light
Proteolytic Stability: The gamma-glutamyl isopeptide bond at the N-terminus confers resistance to standard aminopeptidase degradation; degradation proceeds primarily via gamma-glutamyl transpeptidase (GGT) at cell surfaces, releasing cysteinylglycine and glutamate in the first step of the gamma-glutamyl cycle
Storage: Store lyophilized at −20°C or −80°C under inert atmosphere (argon or nitrogen) if possible; protect from moisture and light; aqueous solutions in sealed vials stable at −80°C for up to 6 months; avoid repeated freeze-thaw cycles; add EDTA (0.1 mM) to aqueous solutions to chelate metal ions and retard oxidation
5. Chemical Reactivity The cysteine thiol (−SH) is the primary reactive site; undergoes rapid oxidation to disulfide (GSSG) under aerobic conditions; rate accelerated by metal ions (Fe²⁺, Cu²⁺), alkaline pH, and UV light
GSH participates in S-glutathionylation reactions, forming mixed disulfides with protein cysteine residues; this reversible modification is a key redox regulatory mechanism in biological systems
The thiol group reacts with electrophiles via the glutathione S-transferase (GST) enzyme system as part of phase-II detoxification; non-enzymatic conjugation also occurs with reactive Michael acceptors
Gamma-glutamyl isopeptide bond is chemically stable at physiological pH; resistant to acid hydrolysis under mild conditions; complete hydrolysis requires prolonged strong acid treatment
GSSG (oxidized form) is readily reduced back to two GSH molecules by glutathione reductase using NADPH as the electron donor; this regeneration cycle is the basis of the cellular antioxidant recycling system
6. Other Properties
- Name: Glutathione (GSH; γ-L-glutamyl-L-cysteinyl-glycine)
- Type: Naturally occurring endogenous tripeptide antioxidant
- Length: 3 amino acids
- Sequence: γ-Glu-Cys-Gly (notable: glutamate is linked via its gamma-carboxyl group, not the alpha-carboxyl, forming an atypical peptide bond resistant to standard peptidase cleavage)
- Molecular Weight: ~307.32 Da (reduced form, GSH); ~612.63 Da (oxidized form, GSSG)
- Formula: C₁₀H₁₇N₃O₆S (reduced GSH)
2. Structural Properties Peptide Nature: Tripeptide with an atypical isopeptide bond between the gamma-carboxyl group of glutamate and the alpha-amine of cysteine; this gamma-glutamyl linkage is not recognized by standard aminopeptidases, conferring resistance to conventional exopeptidase degradation; the glycine C-terminal residue is linked via a standard alpha-peptide bond
Secondary Structure: No defined secondary structure due to tripeptide length; the cysteine thiol group (pKa ~8.7) is the chemically active site; in reduced form (GSH) the thiol is free; in oxidized form (GSSG) two GSH molecules are covalently linked via a disulfide bond between their cysteine residues
Hydrophobicity: Predominantly hydrophilic; all three residues contribute polar character; the thiol group of cysteine adds minor hydrophobic contribution but the overall molecule is highly water-soluble
Charge: Net negative charge at physiological pH; the gamma-glutamyl alpha-carboxyl (pKa ~2.1), the cysteine thiol (pKa ~8.7), the glycine carboxyl (pKa ~3.5), and the glutamate amino terminus (pKa ~9.1) contribute to an overall charge of approximately −1 at pH 7.4
3. Solubility
- Highly soluble in water; solubility exceeds 50 mg/mL in sterile water at neutral pH
- Solubility decreases under acidic conditions and in the presence of divalent metal cations which may form complexes with the thiol group
- Supplied as lyophilized white crystalline powder (reduced form); reconstitution in sterile water or phosphate-buffered saline recommended
4. Stability Thermal Stability: Sensitive to elevated temperatures in solution; lyophilized powder is considerably more stable; aqueous solutions should be prepared fresh or stored at −80°C for extended periods
Oxidative Stability: The free thiol group is readily oxidized to the disulfide (GSSG) upon air exposure, metal ion catalysis, or contact with oxidizing agents; GSSG formation is reversible enzymatically (glutathione reductase/NADPH) but not spontaneously under physiological conditions; protect aqueous solutions from air and light
Proteolytic Stability: The gamma-glutamyl isopeptide bond at the N-terminus confers resistance to standard aminopeptidase degradation; degradation proceeds primarily via gamma-glutamyl transpeptidase (GGT) at cell surfaces, releasing cysteinylglycine and glutamate in the first step of the gamma-glutamyl cycle
Storage: Store lyophilized at −20°C or −80°C under inert atmosphere (argon or nitrogen) if possible; protect from moisture and light; aqueous solutions in sealed vials stable at −80°C for up to 6 months; avoid repeated freeze-thaw cycles; add EDTA (0.1 mM) to aqueous solutions to chelate metal ions and retard oxidation
5. Chemical Reactivity The cysteine thiol (−SH) is the primary reactive site; undergoes rapid oxidation to disulfide (GSSG) under aerobic conditions; rate accelerated by metal ions (Fe²⁺, Cu²⁺), alkaline pH, and UV light
GSH participates in S-glutathionylation reactions, forming mixed disulfides with protein cysteine residues; this reversible modification is a key redox regulatory mechanism in biological systems
The thiol group reacts with electrophiles via the glutathione S-transferase (GST) enzyme system as part of phase-II detoxification; non-enzymatic conjugation also occurs with reactive Michael acceptors
Gamma-glutamyl isopeptide bond is chemically stable at physiological pH; resistant to acid hydrolysis under mild conditions; complete hydrolysis requires prolonged strong acid treatment
GSSG (oxidized form) is readily reduced back to two GSH molecules by glutathione reductase using NADPH as the electron donor; this regeneration cycle is the basis of the cellular antioxidant recycling system
6. Other Properties
- Redox couple: The GSH/GSSG ratio is the primary indicator of intracellular redox status; physiological ratio is approximately 100:1 (GSH:GSSG) in healthy cells; ratio decline is a marker of oxidative stress in research models
- Gamma-glutamyl cycle: GSH degradation and resynthesis occur via the gamma-glutamyl cycle involving six enzymatic steps; resynthesis requires glutamate, cysteine, and glycine as precursors and consumes two molecules of ATP
- Oral bioavailability limitation: The intact tripeptide undergoes extensive gastrointestinal degradation via brush border gamma-glutamyl transpeptidase; systemic GSH elevation following oral administration is limited; liposomal encapsulation and precursor supplementation (N-acetylcysteine, glycine) represent alternative research strategies reported in the literature
- Endogenous concentrations: Intracellular GSH concentrations range from 1–10 mM in most mammalian cell types; highest concentrations in hepatocytes (up to 10 mM); plasma GSH concentrations substantially lower (~2–20 µM) due to rapid oxidation and uptake
- Age-related decline: Endogenous GSH synthesis capacity declines with age; published observational studies report 30–50% reduction in circulating GSH levels between young adulthood and older age, discussed in the context of age-associated oxidative stress research
Description
Glutathione (GSH) is a naturally occurring tripeptide and has been described in the scientific literature as the primary intracellular antioxidant, comprising glutamine, glycine, and cysteine residues. Publications referencing Glutathione discuss it in the context of reactive oxygen species (ROS) neutralization, intracellular redox regulation, hepatic detoxification pathway pharmacology, and immune signaling modulation within experimental systems.
Reports involving Glutathione describe its proposed interactions with oxidative stress pathway components and associated downstream signaling properties under defined experimental conditions. Observations of GSH/GSSG redox ratio dynamics, phase-II hepatic detoxification pathway markers, vitamin C and E regeneration cycle components, and tyrosinase activity modulation are limited to non-clinical research settings and are reported as descriptive findings within cellular and animal model studies.
All references to Glutathione in investigational contexts are confined to mechanistic and observational research and do not extend beyond laboratory-based and clinical investigation.
In the scientific literature, Glutathione has been referenced in non-clinical and clinical research involving oxidative stress assays, hepatic metabolism studies, immunological models, and antioxidant pathway investigations. These publications describe experimental contexts in which molecular interactions, redox signaling components, and pathway-associated markers were observed and recorded.
Reported research contexts include examination of:
- Reactive oxygen species (ROS) neutralization dynamics and intracellular GSH/GSSG redox ratio components observed in cellular research settings
- Phase-II hepatic detoxification pathway markers and conjugation reaction components evaluated under experimental conditions
- Glutathione-ascorbate cycle dynamics and oxidized vitamin regeneration signaling assessed in antioxidant pathway research contexts
- Tyrosinase activity modulation and melanin synthesis pathway markers reported in pigmentation-associated experimental models
- Immune signaling pathway components and inflammatory marker modulation evaluated in immunological research settings
All reported applications are confined to descriptive investigation within controlled laboratory and clinical research environments.
Mechanistic discussions in preclinical and clinical publications describe Glutathione as a tripeptide in which the cysteine-derived sulfhydryl group is described as the active electron-donating moiety responsible for free radical neutralization. Age-associated endogenous GSH decline is discussed in the context of increased oxidative burden within the cited literature. Oral bioavailability limitations attributed to gastrointestinal degradation of the intact tripeptide are noted in formulation and pharmacokinetic research contexts. These descriptions are limited to molecular and biochemical observations within experimental systems and do not imply functional outcomes beyond the reported research context.
Glutathione is supplied as a research-grade peptide material. Identity and composition have been reported as characterized using analytical techniques commonly applied to peptide research materials, including chromatographic and mass spectrometric methods. Individual laboratories determine handling, storage, and analytical verification parameters in accordance with internal research protocols.
COA
Storage
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months. Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
