Glutathione
Price range: $150.00 through $160.00
Description
A single-component research material supplied for controlled research environments. Glutathione (600 mg) is a tripeptide (γ-L-glutamyl-L-cysteinylglycine) widely studied for its role in redox regulation, detoxification pathways, and cellular defense mechanisms. This preparation is intended for research use in biochemical and pharmacological model systems.Not for human use.
Documentation & Quality Assurance
Each lot is sourced through our verified global supply chain with emphasis on traceability and quality control.These documents are reviewed internally and displayed as they become available. Independent third-party testing is also performed on select lots to confirm identity, purity, and alignment with our internal specifications.
Important Notice
This product is intended for laboratory research use only. It is not intended for human or veterinary use, and must not be used for diagnostic, therapeutic, or clinical purposes.
This material is not a drug, medical device, or dietary supplement, and has not been evaluated by the U.S. Food and Drug Administration.
Quality & Manufacturing
All materials are sourced from carefully vetted domestic and international manufacturing partners who follow quality systems consistent with ISO and cGMP principles. Each supplier is reviewed for reliability, documentation integrity, and transparency in testing.
We require a verified purity of 99% or higher and perform independent third-party spot testing to confirm that select lots meet our internal standards for identity, purity, and composition. Where available, endotoxin testing results are included on Certificates of Analysis to verify laboratory purity; their inclusion is for research quality assessment only and does not imply suitability for human or veterinary use.
All research materials are sealed for integrity and packaged for stability during storage and transport from manufacturing through final delivery.
Additional information
| Weight | 0.0625 lbs |
|---|---|
| Dosage | 600mg, 1500mg |
Published Scientific Research
Explore the full library of peer-reviewed studies, clinical data, mechanism breakdowns, and molecular specifications for Glutathione.
All research is sourced from PubMed-indexed journals for informational and educational purposes only. For Research Use Only (RUO). Not for human use.
View Full Research Library →Certificate of Analysis
Every batch undergoes independent third-party laboratory analysis to verify identity, potency, and safety. Testing includes quantitative assay verification, heavy metals screening, and comprehensive microbial analysis.
All Available COAs
Storage Instructions
All products from Apex Health Performance are manufactured using a lyophilization (freeze-drying) process. This method is designed to maintain product integrity and allows vials to remain stable during shipping for approximately 3–4 months.
Once a vial is reconstituted with bacteriostatic water, it should be stored in the refrigerator to help maintain stability. Under these conditions, reconstituted material is generally considered stable for up to 30 days.
Lyophilization is a dehydration technique in which compounds are frozen and then exposed to low pressure. This causes the water in the vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure. This powder can be kept at room temperature until reconstitution.
Upon receipt, products should be stored away from heat and light. For short-term use, refrigeration at approximately 4°C (39°F) is suitable. For long-term storage (several months to years), vials may be placed in a freezer at approximately -80°C (-112°F). Freezing is the preferred method for preserving product stability over extended periods.
⚠️ Important Notice:
These products are intended for research use only. Not for human consumption.
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Research Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating research peptides
GSTA1 depletes glutathione and exacerbates oxidative stress in α-Amanitin-induced hepatotoxicity.
METHODS: A mouse model of α-AMA-induced liver injury was established. Integrated transcriptomics and metabolomics were employed to identify critical pathways.
View Full Study on PubMedA novel glutathione-conjugates of deoxynivalenol biotransformation in vitro and the cytotoxic properties evaluation.
This interaction leads to the formation of diverse structural products, facilitated by glutathione S-transferase (GST), which plays a pivotal role in supporting plants' innate defense mechanisms. Cell experiments demonstrated that the transformed product exhibited significantly reduced toxicity to HepG2 and Caco-2 cells compared to DON, without compromising the integrity of the integrity of the Caco-2 cell barrier.
View Full Study on PubMedPeptide AEDL and Glutathione Stimulates Root Development .
Glutathione (GSH) plays an important role in the stress resistance and redox homeostasis of plant cells and effectively protects the cell from the stress-induced generation of ROS. A scheme of the mechanism behind the regulation of the redox balance in the stem cell niche and the participation of the AEDL and GSH peptides in the regulation of the fate of stem cells was proposed.
View Full Study on PubMedDetection of Protein-Protein Interactions Using Glutathione-S-Transferase (GST) Pull-Down Assay Technique.
Pull-down assay is a technique to analyze direct protein-protein interaction under in vitro condition. Also, this technique is appropriate for investigating the direct interaction between two purified proteins. Glutathione-s-transferase (GST) protein is a widely used affinity tag for affinity purification. In this chapter, we explain the widely used GST pull-down assay to identify the protein-protein interaction between purified proteins.
View Full Study on PubMedGlutathione S-Transferases Mediate In Vitro and In Vivo Inactivation of Genipin: Implications for an Underlying Detoxification Mechanism.
Genipin (GP), the reactive metabolite of geniposide (GE), is responsible for GE-induced hepatotoxicity. As a potential detoxification pathway, the inactivation of GP by glutathione S-transferases (GSTs) has not yet been characterized.
View Full Study on PubMedMolecular Docking Studies and the Effect of Fluorophenylthiourea Derivatives on Glutathione-Dependent Enzymes.
1-(2,6-difluorophenyl)thiourea was showed the best inhibition effect for both GST and GR enzymes.
View Full Study on PubMedResearch Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating research peptides
GSTA1 depletes glutathione and exacerbates oxidative stress in α-Amanitin-induced hepatotoxicity.
METHODS: A mouse model of α-AMA-induced liver injury was established. Integrated transcriptomics and metabolomics were employed to identify critical pathways.
View Full Study on PubMedA novel glutathione-conjugates of deoxynivalenol biotransformation in vitro and the cytotoxic properties evaluation.
This interaction leads to the formation of diverse structural products, facilitated by glutathione S-transferase (GST), which plays a pivotal role in supporting plants' innate defense mechanisms. Cell experiments demonstrated that the transformed product exhibited significantly reduced toxicity to HepG2 and Caco-2 cells compared to DON, without compromising the integrity of the integrity of the Caco-2 cell barrier.
View Full Study on PubMedPeptide AEDL and Glutathione Stimulates Root Development .
Glutathione (GSH) plays an important role in the stress resistance and redox homeostasis of plant cells and effectively protects the cell from the stress-induced generation of ROS. A scheme of the mechanism behind the regulation of the redox balance in the stem cell niche and the participation of the AEDL and GSH peptides in the regulation of the fate of stem cells was proposed.
View Full Study on PubMedDetection of Protein-Protein Interactions Using Glutathione-S-Transferase (GST) Pull-Down Assay Technique.
Pull-down assay is a technique to analyze direct protein-protein interaction under in vitro condition. Also, this technique is appropriate for investigating the direct interaction between two purified proteins. Glutathione-s-transferase (GST) protein is a widely used affinity tag for affinity purification. In this chapter, we explain the widely used GST pull-down assay to identify the protein-protein interaction between purified proteins.
View Full Study on PubMedGlutathione S-Transferases Mediate In Vitro and In Vivo Inactivation of Genipin: Implications for an Underlying Detoxification Mechanism.
Genipin (GP), the reactive metabolite of geniposide (GE), is responsible for GE-induced hepatotoxicity. As a potential detoxification pathway, the inactivation of GP by glutathione S-transferases (GSTs) has not yet been characterized.
View Full Study on PubMedMolecular Docking Studies and the Effect of Fluorophenylthiourea Derivatives on Glutathione-Dependent Enzymes.
1-(2,6-difluorophenyl)thiourea was showed the best inhibition effect for both GST and GR enzymes.
View Full Study on PubMedResearch Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating research peptides
GSTA1 depletes glutathione and exacerbates oxidative stress in α-Amanitin-induced hepatotoxicity.
METHODS: A mouse model of α-AMA-induced liver injury was established. Integrated transcriptomics and metabolomics were employed to identify critical pathways.
View Full Study on PubMed →A novel glutathione-conjugates of deoxynivalenol biotransformation in vitro and the cytotoxic properties evaluation.
This interaction leads to the formation of diverse structural products, facilitated by glutathione S-transferase (GST), which plays a pivotal role in supporting plants' innate defense mechanisms. Cell experiments demonstrated that the transformed product exhibited significantly reduced toxicity to HepG2 and Caco-2 cells compared to DON, without compromising the integrity of the integrity of the Caco-2 cell barrier.
View Full Study on PubMed →Peptide AEDL and Glutathione Stimulates Root Development .
Glutathione (GSH) plays an important role in the stress resistance and redox homeostasis of plant cells and effectively protects the cell from the stress-induced generation of ROS. A scheme of the mechanism behind the regulation of the redox balance in the stem cell niche and the participation of the AEDL and GSH peptides in the regulation of the fate of stem cells was proposed.
View Full Study on PubMed →Detection of Protein-Protein Interactions Using Glutathione-S-Transferase (GST) Pull-Down Assay Technique.
Pull-down assay is a technique to analyze direct protein-protein interaction under in vitro condition. Also, this technique is appropriate for investigating the direct interaction between two purified proteins. Glutathione-s-transferase (GST) protein is a widely used affinity tag for affinity purification. In this chapter, we explain the widely used GST pull-down assay to identify the protein-protein interaction between purified proteins.
View Full Study on PubMed →Glutathione S-Transferases Mediate In Vitro and In Vivo Inactivation of Genipin: Implications for an Underlying Detoxification Mechanism.
Genipin (GP), the reactive metabolite of geniposide (GE), is responsible for GE-induced hepatotoxicity. As a potential detoxification pathway, the inactivation of GP by glutathione S-transferases (GSTs) has not yet been characterized.
View Full Study on PubMed →Molecular Docking Studies and the Effect of Fluorophenylthiourea Derivatives on Glutathione-Dependent Enzymes.
1-(2,6-difluorophenyl)thiourea was showed the best inhibition effect for both GST and GR enzymes.
View Full Study on PubMed →Important Research Notice: These products are research chemicals intended exclusively for in vitro laboratory research by qualified professionals. Not for human or animal consumption. Not approved by the FDA for any therapeutic purpose. Sold strictly for scientific research applications only.