Glutathione Reductase Human,
Mouse Monoclonal Antibody, Clone: 2B3

Introduction to the Molecule

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):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.

Source of Antigen

E.coli

Host

Mouse

Isotype

IgG1, kappa

Preparation

PBS containing 50% glycerol

Species Reactivity

Human (+), Mouse (-), Rat (-)

Storage/Stability

Store for 1 year at –20°C from date of shipment

Applications

ELISA, Immunoprecipitation

By molecule:

• Glutathione reductase