Recombinant GSTA1 protein (His tag)

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Recombinant Human Glutathione S-transferase A1 (GSTA1) Fragment (residues 1-222) is a highly purified protein designed for studying glutathione conjugation, isomerization, and peroxidase activities. This fragment fully encompasses the GST N-terminal and C-terminal functional domains, making it an ideal tool for investigating phase II detoxification, hormone biosynthesis, and lipid peroxide metabolism in experimental models.

Glutathione S-transferase A1 (GSTA1) is a cytoplasmic enzyme that catalyzes the conjugation of glutathione to diverse electrophilic compounds, facilitating detoxification and cellular protection. It plays a critical role in metabolizing prostaglandins (PGA2 and PGJ2), isomerizing androst-5-ene-3,17-dione to support hormone biosynthesis, and exhibits glutathione-dependent peroxidase activity toward fatty acid hydroperoxides like 13-HPODE, contributing to oxidized linoleic acid metabolism. Located in the cytoplasm, GSTA1 is essential for endogenous and xenobiotic compound metabolism, oxidative stress response, and regulatory pathways in human physiology.