GLRX
GLRX (glutaredoxin, also known as GRX or GRX1) is a cytoplasmic member of the glutaredoxin family. It shows glutathione-disulfide oxidoreductase activity and reverses glutathione-protein mixed disulfides, supporting antioxidant defence and redox signalling. Browse Assay Genie's current range of GLRX research reagents below, or read on for the biology behind the target.
GLRX encodes glutaredoxin-1, an enzyme with glutathione-disulfide oxidoreductase activity. In the presence of NADPH and glutathione reductase, it reduces low molecular weight disulfides and proteins. It catalyses the reversible reduction of glutathione-protein mixed disulfides, which makes it a significant contributor to the cell's antioxidant defence system.
Beyond general redox buffering, GLRX is important for several signalling pathways because it controls the S-glutathionylation status of signalling mediators. By adding or removing glutathione from target proteins, this modification acts as a reversible switch, and glutaredoxin activity determines which state is favoured. The protein is a cytoplasmic enzyme and belongs to the glutaredoxin family, which HGNC classifies within the glutaredoxin domain containing gene group.
The GLRX gene has the aliases GRX and GRX1, and was previously named glutaredoxin (thioltransferase). According to the NCBI Gene summary, multiple alternatively spliced transcript variants have been identified, all encoding the same protein. GLRX has also been linked to beta-amyloid toxicity and Alzheimer's disease. Mouse and rat both carry a corresponding ortholog named Glrx, so the protein can be studied in common rodent models. A related family member, GLRX3, is also covered at Assay Genie.
GLRX reduces low molecular weight disulfides and proteins using glutathione, making it a core component for studying thiol-based redox control.
The enzyme contributes strongly to the antioxidant defence system by reversing glutathione-protein mixed disulfides.
GLRX controls the S-glutathionylation status of signalling mediators, so it is central to work on redox-regulated signalling pathways.
GLRX is involved in beta-amyloid toxicity and Alzheimer's disease, linking glutaredoxin function to neurodegenerative mechanisms.
GLRX is a glutathione-disulfide oxidoreductase that, with NADPH and glutathione reductase, reduces low molecular weight disulfides and proteins. It catalyses the reversible reduction of glutathione-protein mixed disulfides, supporting antioxidant defence and controlling S-glutathionylation of signalling mediators.
GLRX is also called GRX and GRX1, and UniProt lists the protein as glutaredoxin-1. Its previous HGNC name was glutaredoxin (thioltransferase). NCBI reports several alternatively spliced transcript variants, but all of them encode the same protein.
Mouse and rat each have a Glrx ortholog, so rodent models are available; check the datasheet of any product for its validated reactivity. NCBI Gene notes that GLRX is involved in beta-amyloid toxicity and Alzheimer's disease.
Other glutaredoxin family members involved in glutathione-dependent redox regulation.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P35754; product specifications from Assay Genie datasheets.