GRXB E.Coli
Description
GRXB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Glutaredoxin-2 (Grx2) is a member of the glutaredoxin family, which are small redox enzymes that play a crucial role in maintaining cellular redox homeostasis. These enzymes utilize glutathione as a cofactor to catalyze the reversible oxidation and reduction of protein thiols. Glutaredoxin-2 is particularly significant due to its involvement in various cellular processes, including electron transport, protein folding, and regulation of transcription factors.
Glutaredoxin-2 is a mitochondrial thiol transferase with a molecular weight of approximately 15 kDa. It contains an N-terminal mitochondrial targeting signal and a CSYC (Cys-Ser-Tyr-Cys) motif, which is essential for its catalytic activity . The enzyme is composed of about 100 amino acid residues and is characterized by its ability to form disulfide bonds and undergo glutathionylation.
Recombinant expression of Glutaredoxin-2 in Escherichia coli is a common method used to produce this enzyme for research and industrial applications. The recombinant protein is typically expressed with an N-terminal His6-ABP (Albumin Binding Protein) tag to facilitate purification. The expression in E. coli allows for high yields of the protein, which can then be purified using techniques such as immobilized metal affinity chromatography (IMAC) .
Glutaredoxin-2 plays a pivotal role in cellular redox regulation. It catalyzes the formation and reduction of disulfide bonds in proteins, thereby maintaining the equilibrium between the mitochondrial glutathione pool and protein thiols. This regulation is crucial for the cellular response to oxidative stress and apoptotic stimuli . Unlike other glutaredoxins, Grx2 is not inhibited by the oxidation of its structural cysteine residues, making it uniquely resilient under oxidative conditions .
The recombinant Glutaredoxin-2 expressed in E. coli is widely used in various biochemical assays and research studies. It is employed to study the mechanisms of redox regulation, protein folding, and the cellular response to oxidative stress. Additionally, it serves as a valuable tool in the development of therapeutic strategies targeting redox-related diseases.
