GSTO1 Human Mutant
Description
GSTO1 Variant Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 241 amino acids fragment (1-241) having a total molecular mass of 36kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The GSTO1 is purified by proprietary chromatographic techniques.
Product Specs
Recombinant human GSTO1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 241 amino acids (fragment 1-241). It has a molecular mass of 36 kDa and includes a 4.5 kDa amino-terminal hexahistidine tag.
Purification of GSTO1 is achieved using proprietary chromatographic techniques.
Product Science Overview
Glutathione S-Transferase Omega 1 (GSTO1) is an enzyme belonging to the omega class of the glutathione S-transferase (GST) family. These enzymes play a crucial role in the detoxification of endogenous and xenobiotic compounds by catalyzing the conjugation of glutathione to various substrates. GSTO1 is particularly notable for its involvement in the reduction of monomethylarsonate, an intermediate in the pathway of arsenic biotransformation .
GSTO1 is a homodimeric protein found in the cytoplasm and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities . The enzyme contains four conserved cysteine residues (C32, C90, C191, C236), which are essential for its catalytic activity . These residues are often mutated in patients with associated diseases, highlighting their importance in the enzyme’s function.
Several polymorphisms in the coding regions of the human GSTO1 gene have been identified. One notable variant is the A140D mutation, which results from an alanine-to-aspartate substitution at amino acid position 140 . This mutation produces a variant with altered enzymatic properties and is often studied in the context of its role in oxidative stress and its potential link to diseases such as Alzheimer’s, vascular dementia, and stroke .
Recombinant human GSTO1 is typically expressed in Escherichia coli (E. coli) systems. The recombinant protein is often fused with an amino-terminal hexahistidine tag to facilitate purification . The recombinant form retains the enzymatic activities of the native protein and is used extensively in research to study its biochemical properties and potential therapeutic applications .
GSTO1 is widely used in research due to its role in detoxification processes and its potential implications in various diseases. Studies have shown that GSTO1 protects cells from oxidative stress, a risk factor for several neurodegenerative diseases . Additionally, its role in arsenic biotransformation makes it a target for studies on arsenic toxicity and detoxification .
