Glutathione reductase, also known as GSR, is a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein and 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, GSR maintains the ratio of [GSH] / [GSSG], and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis. Source: Recombinant protein corresponding to aa43-522 from human GSR, used to His-tag at N-terminal, expressed in E. coli. Molecular Weight: ~54.3kD (504aa) Specific Activity: >45units/mg Unit Definition: The unit definition for glutathione reductase activity may be expressed in terms of the oxidation of NADPH or the reduction of GSSG since their molar ratio is 1:1. One unit of glutathione reductase oxidizes 1umol of NADPH/minute at 37C, pH 7.5. AA Sequence: GSSHHHHHH SSGLVPRGSH MGSMAMACRQ EPQPQGPPPA AGAVASYDYL VIGGGSGGLA SARRAAELGA RAAVVESHKL GGTCVNVGCV PKKVMWNTAV HSEFMHDHAD YGFPSCEGKF NWRVIKEKRD AYVSRLNAIY QNNLTKSHIE IIRGHAAFTS DPKPTIEVSG KKYTAPHILI ATGGMPSTPH ESQIPGASLG ITSDGFFQLE ELPGRSVIVG AGYIAVEMAG ILSALGSKTS LMIRHDKVLR SFDSMISTNC TEELENAGVE VLKFSQVKEV KKTLSGLEVS MVTAVPGRLP VMTMIPDVDC LLWAIGRVPN TKDLSLNKLG IQTDDKGHII VDEFQNTNVK GIYAVGDVCG KALLTPVAIA AGRKLAHRLF EYKEDSKLDY NNIPTVVFSH PPIGTVGLTE DEAIHKYGIE NVKTYSTSFT PMYHAVTKRK TKCVMKMVCA NKEEKVVGIH MQGLGCDEML QGFAVAVKMG ATKADFDNTV AIHPTSSEEL VTLR Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
