Glutathione reductase Antikörper

Glutathione reductase, also designated Glutathione reductase mitochondrial precursor, GRase, GSR or GR, belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The main function of the protein is to maintain high levels of reduced glutathione in the cytosol. With the concomitant oxidation of NADPH, Glutathione reductase transforms oxidized glutathione to the reduced form. Glutathione reductase, which can localize to mitochondria or to the cytoplasm, can form a disulfide-linked homodimer. The active site of the protein is a redox-active disulfide bond. Nethyl maleimide (NEM) and also KLH, a copper containing oxygen carrier generally used in molecular immunology as a carrier protein, are conjugated to low molecular weight molecules, such as Glutathione.   This yields an entire Glutathione compound that is much more immunogenic due to the sheer size of the conjugate complex.