DsbA E.Coli
Disulfide oxidoreductase A, dsbA, rpbB, Disulfide oxidoreductase (DsbA) E Coli, DsDNA-binding protein A, Doublestranded DNA-binding protein, Disulfide oxidoreductase A periplasmic protein disulfide isomerase I, Thiol disulfide interchange protein dsbA.
Greater than 95.0% as determined by SDS-PAGE.
Description
DsbA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (20-208) and having a molecular mass of 21.2 kDa. DsbA E.Coli is purified by proprietary chromatographic techniques.
Product Specs
Disulfide oxidoreductase A, dsbA, rpbB, Disulfide oxidoreductase (DsbA) E Coli, DsDNA-binding protein A, Doublestranded DNA-binding protein, Disulfide oxidoreductase A periplasmic protein disulfide isomerase I, Thiol disulfide interchange protein dsbA.
MAQYEDGKQY TTLEKPVAGA PQVLEFFSFF CPHCYQFEEV LHISDNVKKK LPEGVKMTKY HVNFMGGDLG KDLTQAWAVA MALGVEDKVT VPLFEGVQKT QTIRSASDIR DVFINAGIKG EEYDAAWNSF VVKSLVAQQE KAAADVQLRG VPAMFVNGKY QLNPQGMDTS NMDVFVQQYA DTVKYLSEKK.
Product Science Overview
Disulfide oxidoreductases are enzymes that catalyze the formation and isomerization of disulfide bonds in proteins. These bonds are crucial for the structural stability and biological activity of many proteins. In recombinant protein production, especially in bacterial systems like Escherichia coli (E. coli), the formation of correct disulfide bonds is a significant challenge due to the reducing environment of the bacterial cytoplasm.
In eukaryotic cells, disulfide bonds are typically formed in the oxidizing environment of the endoplasmic reticulum. However, E. coli lacks such a specialized compartment, making the formation of disulfide bonds in its cytoplasm difficult . This limitation often necessitates targeting the protein to the periplasm or expressing it as inclusion bodies, which are then solubilized and refolded in vitro .
Several strategies have been developed to overcome these challenges. One such approach is the CyDisCo (Cytoplasmic Disulfide bond formation in E. coli) system, which involves co-expressing the protein of interest with a sulfhydryl oxidase and a disulfide bond isomerase . This system allows the formation of disulfide bonds in the cytoplasm, even in the presence of reducing pathways .
Recent studies have shown that it is possible to achieve high yields of soluble disulfide-bonded proteins in the cytoplasm of E. coli using the CyDisCo system . For example, the production of human single-chain IgA1 antibody fragments and hen avidin has been successfully scaled up to bioreactor cultivations . These advancements demonstrate the feasibility of producing complex disulfide-bonded proteins in E. coli on a large scale.
