ADH5 Protein, Human (GST)

The ADH5 protein catalyzes the oxidation of long-chain primary alcohols and S-(hydroxymethyl) glutathione. It also oxidizes long-chain omega-hydroxy fatty acids, producing intermediate aldehydes and end products. However, it is ineffective in oxidizing ethanol. ADH5 is crucial for clearing cytotoxic formaldehyde, which causes DNA damage. ADH5 Protein, Human (GST) is the recombinant human-derived ADH5 protein, expressed by E. coli , with N-GST labeled tag. The total length of ADH5 Protein, Human (GST) is 374 a.a., .

ADH5, a Class-III alcohol dehydrogenase, plays a pivotal role in cellular detoxification processes by catalyzing the oxidation of long-chain primary alcohols and S-(hydroxymethyl) glutathione. Additionally, ADH5 is involved in the oxidation of long-chain omega-hydroxy fatty acids, such as 20-hydroxyeicosatetraenoic acid (20-HETE), yielding both the intermediate aldehyde, 20-oxoarachidonate, and the final product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Despite its classification as an alcohol dehydrogenase, ADH5 exhibits low efficiency in oxidizing ethanol. Notably, ADH5 is crucial for cellular defense against formaldehyde, a cytotoxic and carcinogenic metabolite, contributing to the clearance of this substance and preventing potential DNA damage.

Human

E. coli

N-GST

P11766 (M1-I374)

128

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.