|Detection of Mouse Glutaredoxin 1 by Western Blot. Western blot shows lysates of NIH-3T3 mouse embryonic fibroblast cell line and C2C12 mouse myoblast cell line. PVDF membrane was probed with 0.5 µg/mL of Mouse Glutaredoxin 1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3119) followed by HRP‑conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for Glutaredoxin 1 at approximately 12 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 2.|
Glutaredoxin 1s or thioltransferases are a universally distributed family of small molecular weight proteins with thiol-disulfide exchange activity. Glutaredoxin 1 (GLRX1/GRX) is a 12 kDa protein with glutathione-disulfide oxidoreductase activity. Glutaredoxin 1s utilize the reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH and glutathione reductase (the Glutaredoxin 1 system). The amino acid sequence of Glutaredoxin 1 in mouse is highly homologous with that in other mammals (81‑89%), and contains the conserved active sequence motif -Cys-Pro-Try-Cys-. Glutaredoxin 1 also catalyzes the formation of mixed disulfides (glutathionylation), which is an important redox regulatory mechanism, particularly in mammalian cells under oxidative stress conditions, to sense cellular redox potential.
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