GRADE & PURITYBioactive?Bioactive grade — verified to retain biological activity in functional assays. Use when the molecule must be functionally active, not just pure.ActiBioPure™?ActiBioPure™ — Aladdin's premier line for bioactive and recombinant products. Use when both high purity and preserved biological activity are required.Native?Native grade — protein/biomolecule in its natural (non-recombinant, non-denatured) form. Use when native structure and activity are required.High Performance?High-performance grade with optimized purity and performance characteristics. Use for sensitive analyses where ordinary grades fall short.EnzymoPure™?EnzymoPure™ — Aladdin's line of high-quality enzymatic solutions. Use when enzyme purity and defined activity drive assay or process performance.>120 U/mg protein; 1000 U/mL solution
ActiBioPure™, Bioactive, High Performance, EnzymoPure™, Native, >120 U/mg protein; 1000 U/mL solution ActiBioPure™,Bioactive,High Performance,Native,EnzymoPure™ for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Storage & shipping
Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
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Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
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Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Overview
Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP⁺. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, Citrate synthase, EF hands, hemoglobins, lipecalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems. Reaction Equation NADPH+Oxidized glutathione = NADP⁺+2 Glutathione
Assay Procedure
I. Spectrophotometric Method
Wavelength: 340 nm, Light path length: 1 cm Temperature: 25℃ Pipette the following reagents into a cuvette: 2.75 mL Triethanolamine-HCI-NaOH buffer (0.1 mol/L, pH7.5) containing EDTA-2Na(1 mmol/L) 0.15ml GSSG (0.1mol/L) 0.05 mL NADPH (10 mmol/L) dissoluted in Tris (10 mmol/L) 0.02ml GR (about 3 IU/mL)
II. Calculation
ΔA/min = The change in absorbance at 340 nm/minute V = Total volume of reaction mixture (2.97 mL) D = Enzyme dilution factor 6.2 = mM extinction coefficient of NADPH (L⋅mmol
−1⋅cm−1
) d = Light path length (1 cm) v = Volume of enzyme sample (0.02 mL)
Reference Data
Specifications
Product Name
Glutathione Reductase from Yeast, CAS No.9001-48-3
Catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH). Constitutes the major mechanism to maintain a high GSH:GSSG ratio in the cytosol.
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