||Recombinant human GSR protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
||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.
||Liquid. In 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT, 10% glycerol, 0.1 M NaCl.
||54.3 kDa (504 aa) confirmed by MALDI-TOF
||> 95 % by SDS-PAGE
||1 mg/ml (determined by Bradford assay)
|Sequences of amino acids:
||MGSSHHHHHH 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
||Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.
||Glutathione metabolism; Metabolism of nucleotides; Oxidative Stress; Selenium Pathway; Synthesis and interconversion of nucleotide di- and triphosphates; ascorbate glutathione cycle; glutathione redox reactions I;glutathione redox reactions II