protein

GSTA1 Protein, Human (HEK293, C-His)

HY-P75153A

5 μg;10 μg;50 μg;100 μg

45;70;200;340 USD

GSTA1 Protein, Human (HEK293, C-His)

proteins

HEK293

5 μg;10 μg;50 μg;100 μg

45;70;200;340 USD

The GSTA1 protein catalyzes the attack of glutathione on various compounds, forming conjugates of PGA2 and PGJ2. It also converts AD into D4-androstene-3,17-dione, contributing to hormone biosynthesis. Additionally, it participates in the metabolism of oxidized linoleic acid through its peroxidase activity against 13-HPODE. GSTA1 Protein, Human (HEK293, C-His) is the recombinant human-derived GSTA1 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of GSTA1 Protein, Human (HEK293, C-His) is 222 a.a., with molecular weight of ~26 kDa.

Human

The GSTA1 Protein serves as a glutathione S-transferase, catalyzing the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a broad spectrum of both exogenous and endogenous compounds (Probable). This enzymatic activity includes the formation of glutathione conjugates for prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Additionally, GSTA1 plays a role in hormone biosynthesis by catalyzing the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione. Notably, its glutathione-dependent peroxidase activity extends to the metabolism of oxidized linoleic acid, specifically targeting the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE. The diverse enzymatic functions of GSTA1 underscore its involvement in crucial cellular processes, from detoxification reactions to hormone biosynthesis and the metabolism of oxidized lipids.

Glutathione S-transferase A1; GST-epsilon; GSTA1-1; GTH1; GSTA1

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.