TPX E.coli

The recombinant form of thiol peroxidase is typically produced in Escherichia coli (E. coli) and is often tagged with a His-tag at the N-terminus to facilitate purification. The amino acid sequence of the recombinant E. coli thiol peroxidase includes a series of histidine residues (His-tag) followed by the sequence corresponding to the native enzyme .

Thiol peroxidase is essential for maintaining cellular redox balance. It catalyzes the reduction of peroxides, which are harmful by-products of cellular metabolism. By doing so, it helps in protecting cellular components from oxidative damage. This activity is particularly important in environments where oxidative stress is prevalent .

Recombinant thiol peroxidase from E. coli is widely used in research to study oxidative stress and redox biology. It serves as a model to understand the mechanisms of peroxiredoxin enzymes and their role in cellular protection. Additionally, it is used in various biochemical assays to investigate its activity and interaction with other cellular components .

The production of recombinant thiol peroxidase involves cloning the gene encoding the enzyme into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the enzyme is expressed and subsequently purified using affinity chromatography techniques, leveraging the His-tag for efficient purification .

Recombinant thiol peroxidase is typically stored in a buffer containing Tris-HCl, glycerol, DTT, and NaCl to maintain its stability. It is recommended to store the enzyme at 4°C for short-term use and at -20°C for long-term storage, avoiding freeze-thaw cycles to preserve its activity .