MSRB E.Coli

Methionine Sulfoxide Reductase B (MsrB) is an enzyme that plays a crucial role in the reduction of methionine-R-sulfoxide back to methionine. This process is essential for protecting cells from oxidative damage and maintaining protein function. The recombinant form of this enzyme, expressed in Escherichia coli (E. coli), is widely used in research to study its structure, function, and potential therapeutic applications.

MsrB belongs to the methionine sulfoxide reductase family and is characterized by its ability to reduce methionine-R-sulfoxide to methionine. This enzyme contains a metal-binding site composed of two CXXC motifs, which can bind zinc or iron. The bound metal ions help stabilize the enzyme’s conformation, ensuring its proper function .

The recombinant MsrB protein from E. coli is typically fused to a His-tag at the N-terminus, which facilitates its purification using conventional chromatography techniques . The protein has a molecular weight of approximately 17.6 kDa and consists of 137 amino acids .

The recombinant MsrB protein is expressed in E. coli and purified using proprietary chromatographic techniques. The expression system in E. coli allows for high-yield production of the protein, making it suitable for various research applications . The purified protein is often used in studies involving protein structure, enzyme kinetics, and oxidative stress response.

Recombinant MsrB protein is used in a wide range of research applications, including:

• Protein Structure Studies: Understanding the three-dimensional structure of MsrB helps researchers gain insights into its catalytic mechanism and interaction with other molecules.
• Enzyme Kinetics: Studying the kinetics of MsrB provides valuable information about its catalytic efficiency and substrate specificity.
• Oxidative Stress Response: MsrB plays a vital role in protecting cells from oxidative damage. Research on this enzyme helps elucidate its role in cellular defense mechanisms and its potential therapeutic applications.