Glutathione reductase (GR) is a member of pyridine nucleotide-disulfide oxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG) (1):
GSSG + NADPH + H+  2GSH + NADP+
In most eukaryotic cells, GR maintains the ratio of [GSH]/[GSSG] elevated, and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis (2).

Immunoprecipitation: 1-2 ?l; Immunocytochemistry: 1:100;

Type: Primary
Antigen: GSR (glutathione reductase)
Clonality: Monoclonal
Clone: 1A7
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG2a Kappa
Reactivity: Human