Human. Predicted to react with mouse, rat, rabbit, porcine, bovine based on 100% sequence homology. Immunogen sequence has 91% homology to Zebrafish.

Glutaredoxins (GRXs) are one of thioredoxin superfamily members of thiol/disulfide exchange catalysts, and hence known as thioltransferases serving as reductants of protein SG mixed disulfides providing reducing equivalents to ribonucleotide reductase. Among two mammalian GRXs, GRX1 (Glutaredoxin 1) localizes in the cytosol primarily to mitochondria and to lesser extent in nucleus, whereas GRX2 has nuclear as well as mitochondrial isoforms. GRX1 is a relatively abundant, small ~12 kD cytosolic enzyme that regulates protein mixed disulfides through their reduction by GSH (S-glutathiolated proteins; R-SSG) and its functions depends upon GSH presence. When GRX1 deglutathionylates an S-glutathionylated substrate, a GRX1-SSG intermediate complex is formed, and the free GSH/glutathione reductase (GR) reduces the intermediate complex with NADPH to NADP+ and “reload” GRX1 to continue the catalysis. Unlike thioredoxin 1, GRX1 does not catalyze the reduction of sulfenic acid or intra-/inter-molecular disulfides, thereby efficiently catalyzing the reduction of R-SSG in the presence of NADPH and GR. Glrx1 is upregulated by several cytokines including IL-4, IL-6, IL-13 etc. and its expression is decreased by TGF-beta1.