GSH and GSSG Analysis Service


Glutathione is an important  tripeptidethiol (γ-glutamylcysteinyl glycine) antioxidant composted of three  amino acids, cysteine, glycine, and glutamate. As an important tripeptidethiol  antioxidant widely distributed in biological fluids and tissues of plants,  animals, fungi, and some bacteria and archaea, it is associated with many  physiological functions, such as the transportation of amino acids, the  synthesis of proteins and DNA, the stabilization of cell membranes and the  detoxification of xenobiotics.

Glutathione plays an important role  in fighting against toxic effects brought by reactive oxygen species like free  radicals, lipid peroxides, peroxides and heavy metals. The reduced  glutathione/oxidized glutathione ratio (GSH/GSSG) is widely used in clinics for  the evaluation of oxidative stress status in biological systems. The changes of  the ratio are shown existed in medical disorders such as inflammation,  autoimmune disorders, sepsis, apoptosis, aging, cancer, HIV replication, and  cardiovascular diseases.

The reduced form of glutathione GSH  and oxidized form of glutathione GSSG work together with other redox-active  compounds such as NADPH to maintain and regulate cellular redox status. GSH is  quantitatively described as the redox potential, calculated by the Nernst  equation. The synthesis of GSH is catalyzed by L-cysteine –ligase and  glutathione synthase, while the oxidation, conjugation, and hydrolysis  contribute to the consumption of GSH. Conjugation with endogenous and exogenous  electrophiles is responsible for a large portion of cellular GSH consumption.  The balance between its production, consumption, and transportation determine  and strictly regulate the intracellular and extracellular GSH levels. The  activities of the enzymes associated with GSH metabolism are regulated at  transcriptional, translational, and posttranslational levels.

Besides acting as antioxidant,  glutathione has several additional functions. For example, it is a reserve of  cysteine and nitric oxide. It also takes part in the metabolism of estrogens,  leukotrienes, and prostaglandins and the reduction of ribonucleotides to  deoxyribonucleotides. What’s more, it is associated with the operation of  certain transcription and the detoxification of many endogenous compounds.  Because of its significant role in the organism, it is of great interest among  pharmacologists to take GSH system as a possible target for medical  interventions. Buthioninesulfoximine (BSO) has been used as the most popular  approach to depleting GSH. Supplementation with precursors, such as cysteine in  the form of different esters, has been used to enhance GSH levels.

Numerous technologies are available  for the determination of GSH and GSSG, but only few of these are suitable for  direct measurement of GSH and GSSG. HPLC-UV, capillary electrophoresis, HPLC-MS  are among the methods described in the literature. These methodologies have  different sensitivity, selectivity, specificity, and susceptibility to  interferences. HPLC-MS is of the highest sensitivity, selectivity, and specificity.  Creative Proteomics has established a robust, reproducible and highly sensitive  HPLC-MS platform for the simultaneous quantification of GSH and GSSG.



Sample Requirement


Compounds Quantified in This Service

With integrated set of separation,  characterization, identification and quantification systems featured with  excellent robustness & reproducibility, high and ultra-sensitivity,  Creative Proteomics provides reliable, rapid and cost-effective GSH and GSSG targeted metabolomics services.

* For Research Use Only. Not for use in diagnostic procedures.
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