Glutaredoxin-1, Thioltransferase-1, TTase-1, Glrx, Glrx1, Grx, Grx1.
GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.
GLRX Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107 a.a) and having a molecular mass of 14.3kDa. GLRX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GLRX protein solution (0.5mg/ml) containing 20mM MES (pH5.0), 20% Glycerol and 0.1M NaCl.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Greater than 95.0% as determined by SDS-PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQEFVN CKIQSGKVVV FIKPTCPYCR KTQEILSQLP FKQGLLEFVD ITATNNTSAI QDYLQQLTGA RTVPRVFIGK DCIGGCSDLI SMQQTGELMT RLKQIGALQL
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