TXN1, His
Greater than 95.0% as determined by SDS-PAGE.
Description
Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Thioredoxin exists as a disulfide-linked homodimer and contains a single thioredoxin domain . The protein participates in redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions . This activity is essential for maintaining the redox balance within cells and protecting against oxidative damage.
Recombinant thioredoxin is produced using various expression systems, with E. coli being one of the most common hosts . The recombinant protein is often tagged with a His tag (histidine tag) to facilitate purification. The His tag is a sequence of histidine residues that binds strongly to nickel ions, allowing for easy isolation of the protein using nickel-affinity chromatography .
Recombinant thioredoxin, especially with a His tag, is widely used in research and biotechnology. Some of its applications include:
- Protein Folding: Thioredoxin assists in the correct folding of proteins by catalyzing the formation and isomerization of disulfide bonds.
- Redox Studies: It is used to study redox reactions and signaling pathways within cells.
- Fusion Protein: Thioredoxin can be fused to other proteins to enhance their solubility and stability during expression and purification .
Recombinant thioredoxin is typically provided as a lyophilized powder and should be stored at -20°C to -80°C for long-term stability . Once reconstituted, the protein solution can be stored at 4-8°C for short-term use. Proper storage conditions are crucial to maintain the protein’s activity and prevent degradation .
