| Customization: | Available |
|---|---|
| Function: | Medicine;Food Ingredient;Cosmetics |
| Certification: | ISO, HACCP, KOSHER, FDA; Halal |
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To fulfill the customers' over-expected satisfaction , we have now our strong crew to provide our greatest general assistance which incorporates promoting, gross sales, planning, creation, top quality controlling, packing, warehousing and logistics for Anti Oxidant L-Glutathione Oxidized Powder , Health Food Ingredient Raw Material Oxidized Glutathione , GSSG , As a key enterprise of this industry, our company makes efforts to become a leading supplier, based on the faith of professional quality & worldwide service.
| Model NO. | GSSG01 |
| CAS No. | 27025-41-8 |
| Formula | C10h17n3o6s |
| Type | Pharmaceutical Intermediates |
| Appearance | Powder |
| Quality | Industrial |
| Colour | White |
| Transport Package | 25kg/Drum |
| Specification | 98% |
| Trademark | GSH World |
| Origin | China |
| HS Code | 2930909099 |
| Production Capacity | 2000 Kg/Month |
|
Product name |
L-Glutathione Oxidized |
| CAS No. | 27025-41-8 |
|
Appearance |
White or almost white powder |
|
Purity ( HPLC ) |
98.0% to100.0% |
|
Heavy metals |
Not more than 10 ppm |
|
Loss on drying |
Not more than 0.5% |
|
Shelf life |
24 months |
| Packing | 25kg/drum or customized |
|
Storage condition |
Store in cool place and keep containeraway from sunlight |
L-Glutathione Oxidized often denoted as GSSG, represents the altered form of glutathione resulting from its exposure to oxidative stress. In this state, glutathione undergoes a chemical transformation, losing electrons and its antioxidant capacity. This oxidized state is a natural part of the cellular redox cycle, where reduced glutathione (GSH) converts to oxidized glutathione (GSSG) during the process of neutralizing free radicals. The balance between these two forms is crucial for cellular health, emphasizing the significance of glutathione in managing oxidative damage and maintaining the delicate equilibrium essential for various physiological functions in the body.
1. Oxidized glutathione is a molecule that is formed when glutathione, an antioxidant, loses an electron. It is also known as glutathione disulfide. The primary function of oxidized glutathione is to be reduced back to glutathione by the enzyme glutathione reductase. This process is essential for maintaining the balance of oxidized and reduced glutathione in cells, which is important for protecting cells from oxidative stress.
2. GSSG, although commonly considered the "spent" or oxidized state of glutathione, serves a crucial purpose. It acts as a reservoir of oxidizing equivalents and participates in enzymatic reactions that eliminate toxins from the body. Moreover, GSSG is involved in signaling pathways that regulate cellular functions, contributing to processes such as cell proliferation and apoptosis. The interplay between reduced and oxidized glutathione underscores the dynamic nature of cellular defense mechanisms, emphasizing the significance of both forms in maintaining overall cellular health and resilience against oxidative challenges.
3. Oxidized glutathione (GSSG) plays a pivotal role in cellular redox homeostasis and detoxification processes within the body. Its primary function lies in its involvement in the glutathione redox cycle, an essential mechanism for mitigating oxidative stress. As cells combat environmental stressors or encounter free radicals generated during metabolic processes, reduced glutathione (GSH) transforms into its oxidized form (GSSG) while neutralizing these harmful entities.
1. Redox Homeostasis: GSSG is an integral part of the cellular redox balance. The dynamic equilibrium between GSH and GSSG ensures that cells can respond to oxidative stress and maintain optimal functioning.
2. Detoxification: GSSG participates in detoxification processes within cells. It serves as a substrate for the enzyme glutathione peroxidase, which neutralizes harmful peroxides and facilitates the removal of toxins from the body.
3. Glutathione Redox Cycle: The glutathione redox cycle involves the continuous interconversion of GSH and GSSG. This cycle is crucial for scavenging free radicals, protecting cellular structures, and sustaining the cellular antioxidant defense system.
4. Enzymatic Reactions: GSSG is involved in various enzymatic reactions within cells. It acts as a co-factor for certain enzymes, contributing to metabolic processes and cellular functions.
5. Cell Signaling: Beyond its role in redox reactions, GSSG is implicated in cell signaling pathways. It modulates the activity of proteins involved in cellular processes such as proliferation, apoptosis, and gene expression.
6. Immune Function: GSSG has immunomodulatory effects. It influences the activity of immune cells, contributing to the body's defense against pathogens and foreign invaders.
7. Antioxidant Recycling: GSSG can be recycled back to GSH through enzymatic reactions catalyzed by glutathione reductase. This recycling mechanism enhances the overall antioxidant capacity of the cell.
8. Protein S-Glutathionylation: S-Glutathionylation, a reversible post-translational modification, involves the addition of a glutathione moiety to cysteine residues in proteins. This modification can regulate protein function and cellular responses to oxidative stress.
9. Cellular Function and Viability: The balance between GSH and GSSG is critical for maintaining cellular function and viability. Disruptions in this balance, leading to an increase in GSSG levels, can be indicative of oxidative stress and cellular dysfunction.
10. Neuronal Health: GSSG has implications for neuronal health. Oxidative stress is a factor in neurodegenerative diseases, and maintaining the redox balance through the glutathione system, including GSSG, is crucial for neuronal protection.
11. Antiproliferative Effects: GSSG has been associated with antiproliferative effects on certain types of cancer cells. Understanding its role in regulating cell growth may offer insights into potential therapeutic strategies.
12. Reduction of Disulfide Bonds: GSSG participates in the reduction of disulfide bonds in proteins, contributing to the maintenance of proper protein structure and function.
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