DsbA
(b) Analysis by SDS-PAGE.
Description
The DsbA is purified by proprietary chromatographic techniques.
Product Specs
was determined and was found to be Met-Ly-Lys-Ala-Trp.
Product Science Overview
Disulfide oxidoreductases are enzymes that play a crucial role in the formation and rearrangement of disulfide bonds in proteins. These bonds are essential for the stability and functionality of many proteins, particularly those that are secreted or located in oxidizing environments. Recombinant disulfide oxidoreductases are produced through genetic engineering techniques, allowing for their expression in various host organisms, such as bacteria, yeast, and mammalian cells.
Disulfide bonds are covalent linkages formed between the sulfur atoms of two cysteine residues within a protein. These bonds contribute to the protein’s tertiary and quaternary structures, enhancing its stability and resistance to denaturation. In eukaryotic cells, disulfide bonds are typically formed in the endoplasmic reticulum, an oxidizing environment that facilitates the formation of these bonds during protein folding and maturation .
Producing recombinant proteins with disulfide bonds can be challenging, especially in prokaryotic hosts like Escherichia coli. The cytoplasm of E. coli is a reducing environment, which impedes the formation of disulfide bonds. To overcome this, researchers have developed strategies to promote disulfide bond formation in the periplasm, an oxidizing compartment of the bacterial cell .
Several strategies have been employed to enhance the recombinant expression of disulfide bond-dependent proteins:
- Targeting to the Periplasm: By directing the recombinant protein to the periplasm, where an oxidizing environment exists, disulfide bond formation can occur more efficiently.
- Co-expression with Chaperones: Co-expressing molecular chaperones and foldases can assist in the proper folding and stabilization of the recombinant protein.
- Optimizing Culture Conditions: Adjusting the growth conditions, such as temperature and induction levels, can improve the yield and quality of the recombinant protein .
Recombinant disulfide oxidoreductases have a wide range of applications in biotechnology and medicine. They are used in the production of therapeutic proteins, including antibodies and hormones, which require correct disulfide bond formation for their activity. Additionally, these enzymes are employed in industrial processes, such as the production of biofuels and bioplastics, where they facilitate the folding and stability of key enzymes .
