Buy Glutathione 500mg | Reduced L-Glutathione Research Peptide
Glutathione 500mg is a research-grade preparation of L-glutathione, a naturally occurring tripeptide made from three amino acids: glutamic acid, cysteine, and glycine. Glutathione is found in nearly every living cell. It plays an important role in maintaining cellular redox balance and supporting biochemical reactions involving oxidative stress, detoxification, and cellular metabolism. The reduced form, known as GSH, is widely studied because of its involvement in antioxidant enzyme systems and the regulation of reactive oxygen species (ROS). At
Orion Peptides, Glutathione 500mg is available as a lyophilized research compound for controlled laboratory investigations. The nominal 500mg quantity is suitable for projects involving biochemical assays, compound characterization, and redox-related experiments. This compound is intended strictly for laboratory research. It is not approved for human or veterinary administration or therapeutic use.
What Is Glutathione 500mg?
Glutathione is a small sulfur-containing molecule naturally produced by cells. It is made from three amino acids joined together in a specific arrangement. Unlike many common peptides, glutathione contains a gamma-glutamyl bond between glutamic acid and cysteine. This unusual bond is an important part of its chemical structure. Glutathione exists mainly in two forms:
- Reduced glutathione (GSH): Contains a free sulfhydryl (-SH) group that participates in redox reactions.
- Oxidized glutathione (GSSG): Consists of two glutathione molecules joined by a disulfide bond.
Both forms are important in cellular research. Under many normal cellular conditions, reduced glutathione is present at higher levels than oxidized glutathione. Scientists study changes in the GSH/GSSG balance to understand how cells respond to oxidative stress. Glutathione is also involved in enzyme-dependent reactions that process reactive compounds and help maintain cellular chemical balance.
Research reference: Wu G, et al. (2004). Glutathione metabolism and its implications for health.
Glutathione 500mg Molecular Formula and Chemical Properties
Glutathione is classified as a tripeptide because it contains three amino acid residues. Its chemical structure includes a cysteine thiol group, which plays an important role in redox reactions.
| Property | Details |
| Compound name | Glutathione 500mg |
| Chemical name | L-Glutathione, reduced |
| Alternative names | GSH, Reduced Glutathione |
| Peptide type | Naturally occurring tripeptide |
| Amino acid sequence | γ-Glu-Cys-Gly |
| Full sequence | γ-L-Glutamyl-L-cysteinyl-glycine |
| Number of amino acids | 3 |
| Molecular formula | C₁₀H₁₇N₃O₆S |
| Molecular weight | 307.33 g/mol |
| CAS number | 70-18-8 |
| PubChem CID | 124886 |
| Redox forms | GSH and GSSG |
| Nominal vial content | 500mg |
| Physical form | Lyophilized powder |
| Research focus | Redox signaling, oxidative stress, glutathione metabolism |
| Intended use | Laboratory research only |
The molecular formula and weight refer to reduced L-glutathione.
Chemical reference: PubChem: Glutathione, CID 124886.
How Does Glutathione Work?
Glutathione is involved in several biochemical processes that help regulate the balance between oxidation and reduction inside cells. Its activity is closely linked to the cysteine residue, which contains a reactive thiol group. This group allows glutathione to take part in chemical reactions that transfer electrons and influence cellular redox conditions.
Glutathione and Oxidative Stress
Cells produce reactive oxygen species during normal metabolic processes. These molecules are involved in signaling, but excessive accumulation can damage proteins, lipids, and other cellular components. Glutathione participates in systems that regulate reactive oxygen species. One important pathway involves glutathione peroxidase. In this enzyme-catalyzed reaction, reduced glutathione supplies reducing equivalents that help convert certain peroxides into less reactive compounds. As part of the process, GSH is converted into oxidized glutathione (GSSG). Glutathione reductase can then regenerate GSH using NADPH. This cycle helps maintain the cellular supply of reduced glutathione.
Research reference: Forman HJ, Zhang H, Rinna A. (2009). Glutathione: Overview of its protective roles, measurement, and biosynthesis.
Glutathione and Cellular Detoxification
Glutathione is also involved in reactions that process electrophilic compounds. Certain glutathione S-transferase enzymes catalyze the conjugation of glutathione with suitable chemical substrates. These reactions can change the chemical behavior of the compounds and contribute to their metabolism and elimination. Researchers study these pathways to understand cellular responses to reactive chemicals and metabolic stress.
Glutathione and Mitochondrial Function
Mitochondria are involved in cellular energy production and are also a source of reactive oxygen species. Glutathione participates in mitochondrial redox regulation. Researchers examine mitochondrial GSH availability, changes in oxidative stress markers, and the activity of glutathione-dependent enzymes. These investigations are relevant to understanding how mitochondrial redox conditions influence cellular function.
Reduced Glutathione (GSH) vs Oxidized Glutathione (GSSG)
Reduced and oxidized glutathione are closely related but chemically different.
| Feature | Reduced Glutathione (GSH) | Oxidized Glutathione (GSSG) |
| Chemical form | Reduced | Oxidized |
| Structure | Single tripeptide | Two glutathione units linked by a disulfide bond |
| Free thiol group | Present | Absent at the linked cysteine residues |
| Molecular weight | 307.33 g/mol | Approximately 612.63 g/mol |
| Main research interest | Reducing activity and redox regulation | Oxidation state and redox balance |
| Relationship | Can be oxidized to GSSG | Can be reduced back to GSH |
Researchers often measure both forms when investigating cellular redox balance. A change in the relationship between GSH and GSSG can provide useful information about oxidation and reduction processes. However, interpretation depends on the experimental model, cellular compartment, and analytical method.
Glutathione 500mg Research Applications
Glutathione is used in many areas of biochemical and cellular research.
1. Oxidative Stress Research
Glutathione is involved in the regulation of reactive oxygen species. Researchers investigate GSH concentrations, oxidation rates, and antioxidant enzyme activity to better understand cellular responses to oxidative stress. These studies may also examine how experimental conditions influence the balance between GSH and GSSG.
2. Glutathione Metabolism Research
Cells synthesize glutathione through a two-step enzyme-dependent pathway involving glutamate, cysteine, and glycine. The main enzymes involved are glutamate-cysteine ligase and glutathione synthetase. Researchers study these processes to understand how glutathione production is regulated and how precursor availability influences intracellular concentrations.
Research reference: Lu SC. (2013). Glutathione synthesis.
3. Liver Cell Research
Glutathione plays an important role in liver metabolism. Researchers investigate the relationship between glutathione availability, reactive metabolites, and cellular responses to chemical exposure. Experimental studies often examine glutathione-dependent enzyme systems and the consequences of glutathione depletion. These investigations help explain how the liver processes certain reactive compounds.
4. Mitochondrial Research
Mitochondrial function depends partly on maintaining suitable redox conditions. Scientists study glutathione-related pathways to better understand mitochondrial oxidation, cellular stress responses, and changes in metabolic activity.
5. Protein Redox Regulation
The oxidation and reduction of protein thiol groups can influence protein activity. Glutathione participates in reactions involving protein glutathionylation and deglutathionylation. These processes are relevant to studies of enzyme regulation, protein structure, and cellular signaling.
6. Glutathione-Dependent Enzyme Studies
Glutathione is involved in several enzyme systems, including:
- Glutathione peroxidases
- Glutathione reductase
- Glutathione S-transferases
- Glutaredoxins
These enzymes are investigated for their roles in oxidative stress, cellular metabolism, and chemical regulation.
Research reference: Deponte M. (2013). Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Glutathione 500mg and 600mg Research Vials
Orion Peptides lists two glutathione research quantities.
Both compound sizes should be compared using their batch-specific specifications. The primary difference is the nominal quantity listed for each vial. Researchers should also verify whether the compounds have the same chemical form, formulation, and analytical standards.
Glutathione 500mg Purity and COA Testing
Accurate analytical documentation is important in glutathione research because the compound can undergo oxidation. Researchers should confirm not only the identity and purity of the material but also its chemical form.
High-Performance Liquid Chromatography
HPLC separates chemical components under defined laboratory conditions. For glutathione, chromatography can help measure purity and detect certain related substances. A reported purity percentage should be supported by the actual chromatographic method and batch results.
Mass Spectrometry
Mass spectrometry helps verify the molecular identity of the tested compound. Reduced glutathione has a molecular weight of approximately 307.33 g/mol. The expected molecular mass differs from that of oxidized glutathione.
Certificate of Analysis
A useful glutathione COA should include:
- Compound identification
- Batch or lot number
- Analytical testing date
- Testing laboratory
- Chemical identity results
- Purity results
- Actual content or assay results, when available
- Relevant oxidation-related impurity information
Where possible, researchers should also review whether the analytical method can distinguish reduced glutathione from oxidized forms. A high purity percentage alone does not establish sterility, endotoxin content, or suitability for biological administration.
Glutathione 500mg Storage and Handling
Glutathione storage conditions depend on the formulation and physical state of the material. Reduced glutathione can undergo oxidation under certain environmental conditions. For this reason, researchers should protect the compound from inappropriate exposure to moisture, heat, and other conditions that may affect its chemical stability. Lyophilized material should be stored according to the manufacturer’s validated recommendations. General laboratory handling considerations include:
- Keep containers properly sealed.
- Protect the material from unnecessary moisture and light exposure.
- Follow the specified storage temperature.
- Minimize unnecessary exposure to air during handling when oxidation is a concern.
- Avoid repeated temperature fluctuations.
- Use suitable laboratory protective equipment.
After dissolution, glutathione stability may depend on the solvent, pH, temperature, oxygen exposure, and storage duration. Laboratories should follow validated stability protocols rather than assuming a universal shelf life.
Frequently Asked Questions About Glutathione 500mg
What is Glutathione 500mg?
Glutathione 500mg is a research compound containing a nominal 500mg quantity of glutathione. Reduced L-glutathione is a naturally occurring tripeptide studied for its involvement in cellular redox reactions and metabolism.
Is glutathione a peptide?
Yes. Glutathione is a tripeptide made from glutamic acid, cysteine, and glycine. It contains a gamma-glutamyl bond that distinguishes it from many conventional peptides.
What is the molecular formula of glutathione?
Reduced L-glutathione has the molecular formula C₁₀H₁₇N₃O₆S.
What is the molecular weight of glutathione?
The molecular weight of reduced glutathione is approximately 307.33 g/mol.
What is the CAS number of glutathione?
The CAS number for reduced L-glutathione is 70-18-8.
What is the difference between GSH and GSSG?
GSH is reduced glutathione and contains a free thiol group. GSSG is the oxidized form, consisting of two glutathione units linked by a disulfide bond.
Why do researchers study the GSH/GSSG ratio?
The relationship between reduced and oxidized glutathione provides information about cellular redox conditions. Researchers use it as one measure of oxidative stress and redox regulation.
What is the difference between Glutathione 500mg and 600mg?
Both refer to glutathione research compounds with different nominal quantities. The appropriate selection depends on the research requirements and the verified specifications of each batch.
How can researchers check glutathione purity?
Researchers can review the batch-specific COA, chromatographic purity testing, identity results, and quantitative assay information where available.
Does 99% purity mean exactly 500mg of glutathione is present?
Not necessarily. Chromatographic purity and actual compound content are different measurements. A quantitative assay may be needed to confirm the amount present.
How should glutathione be stored?
Glutathione should be stored according to the supplier’s validated instructions. Protection from conditions that promote oxidation is particularly important for reduced glutathione.
Is Orion Peptides Glutathione 500mg intended for human use?
No. The compound is intended strictly for legitimate laboratory research. It is not approved for human or veterinary administration, cosmetic treatment, or therapeutic use.
Research Use Only Disclaimer
Glutathione 500mg supplied by Orion Peptides is intended exclusively for scientific and laboratory research. It is not marketed as an FDA-approved medication, injectable preparation, dietary supplement, or cosmetic compound. The scientific literature describes the biological functions of naturally occurring glutathione. Those findings do not establish that a research-grade compound is safe or suitable for human administration. All research must follow applicable laws, laboratory safety procedures, and institutional requirements.
Scientific References
- Lu SC. (2013). Glutathione synthesis. Biochimica et Biophysica Acta – General Subjects, 1830(5), 3143–3153. PubMed. DOI: 10.1016/j.bbagen.2012.09.008.
- Wu G, Fang YZ, Yang S, Lupton JR, Turner ND. (2004). Glutathione metabolism and its implications for health. Journal of Nutrition, 134(3), 489–492. PubMed. DOI: 10.1093/jn/134.3.489.
- Forman HJ, Zhang H, Rinna A. (2009). Glutathione: Overview of its protective roles, measurement, and biosynthesis. Molecular Aspects of Medicine, 30(1–2), 1–12. PubMed. DOI: 10.1016/j.mam.2008.08.006.
- Deponte M. (2013). Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes. Biochimica et Biophysica Acta – General Subjects. PubMed.
- Couto N, Wood J, Barber J. (2016). The role of glutathione reductase and related enzymes on cellular redox homeostasis network. Free Radical Biology and Medicine. PubMed. DOI: 10.1016/j.freeradbiomed.2016.02.028.
- National Center for Biotechnology Information. PubChem Compound Summary for Glutathione, CID 124886. PubChem.
