DsbE E.Coli
Description
DsbE is purified by conventional chromatography techniques.
Product Specs
Product Science Overview
Thiol Disulfide Interchange Protein DsbE, also known as CcmG, is a crucial protein in the periplasm of Escherichia coli (E. coli). It plays a significant role in the formation and maintenance of disulfide bonds in proteins, which are essential for their proper folding and stability. The recombinant form of DsbE is produced using genetic engineering techniques to express the protein in E. coli.
DsbE is a periplasmic thioredoxin-like protein that is involved in the maturation of cytochrome c, a component of the electron transport chain. The protein has a thioredoxin fold and contains a CXXC motif, which is critical for its redox activity. The primary function of DsbE is to reduce disulfide bonds in apocytochrome c, facilitating the correct formation of disulfide bonds before the attachment of heme groups by other proteins such as CcmF and CcmH .
Cytochrome c maturation in E. coli involves a complex pathway requiring multiple proteins, including DsbE. DsbE is one of the 12 proteins necessary for the assembly of cytochrome c in the periplasm. It acts as a reducing agent, ensuring that the cysteine residues in apocytochrome c are in the correct redox state for heme attachment. This process is vital for the proper functioning of the electron transport chain and cellular respiration .
The recombinant form of DsbE is produced by cloning the gene encoding DsbE into an expression vector, which is then introduced into E. coli cells. The cells are cultured, and the protein is expressed and purified using conventional chromatography techniques. The recombinant DsbE protein is typically purified to a high degree of purity (>95%) and validated using SDS-PAGE .
Recombinant DsbE is used in various research applications, including studies on protein folding, redox biology, and cytochrome c maturation. It serves as a model protein for understanding the mechanisms of disulfide bond formation and is also used in the development of biotechnological applications that require the correct folding of disulfide-bonded proteins .
