DsbG E.Coli
Thiol Disulfide Interchange Protein E.Coli Recombinant DsbG
Cat. No.
BT15787
Source
Escherichia Coli.
Synonyms
Thiol:disulfide interchange protein dsbG, dsbG, ybdP, b0604, JW0597.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
Recombinant DsbG produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids and having a molecular mass of 25.8 kDa.
DsbG is purified by conventional chromatography techniques.
DsbG is purified by conventional chromatography techniques.
Product Specs
Introduction
Dsb proteins are responsible for forming and rearranging disulfide bonds, which are crucial for the proper folding of secreted and membrane proteins in bacteria. DsbG, in particular, exhibits both disulfide bond isomerase and chaperone activity. It interacts with intermediates formed during the refolding of chemically denatured citrate synthase, effectively preventing their aggregation in vitro. Interestingly, DsbG shares sequence homology with DsbC. Structurally, DsbG exists as a stable dimer in the periplasm and displays an equilibrium constant with glutathione that is comparable to both DsbA and DsbC. Notably, the expression level of DsbG is approximately 25% that of DsbC.
Description
Recombinant DsbG, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 232 amino acids, resulting in a molecular mass of 25.8 kDa. The purification of DsbG is achieved through standard chromatography techniques.
Physical Appearance
A clear and sterile solution.
Formulation
The DsbG protein solution is formulated in a buffer containing 20mM Tris-HCl at pH 8, 2mM EDTA, and 10% Glycerol.
Stability
For short-term storage (2-4 weeks), the DsbG protein solution should be kept at 4°C. For longer storage durations, it is recommended to store the solution in a frozen state at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. It is important to minimize exposure to repeated freeze-thaw cycles.
Purity
The purity of the DsbG protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Thiol:disulfide interchange protein dsbG, dsbG, ybdP, b0604, JW0597.
Source
Escherichia Coli.
Amino Acid Sequence
MEELPAPVKA IEKQGITIIK TFDAPGGMKG YLGKYQDMGV TIYLTPDGKH AISGYMYNEK GENLSNTLIE KEIYAPAGRE MWQRMEQSHW LLDGKKDAPV IVYVFADPFC PYCKQFWQQA RPWVDSGKVQ LRTLLVGVIK PESPATAAAI LASKDPAKTW QQYEASGGKL KLNVPANVST EQMKVLSDNE KLMDDLGANV TPAIYYMSKE NTLQQAVGLP DQKTLNIIMG NK.
Product Science Overview
Structure and Function
DsbG is known for its dual functionality: it has both disulfide bond isomerase and chaperone activities . The disulfide bond isomerase activity allows DsbG to catalyze the rearrangement of incorrect disulfide bonds in substrate proteins, ensuring proper protein folding. The chaperone activity helps in preventing the aggregation of unfolded or misfolded proteins, thereby assisting in their correct folding .
Expression and Purification
Applications
DsbG is widely used in research to study protein folding and disulfide bond formation. Its ability to interact with refolding intermediates of chemically denatured proteins makes it a valuable tool in biochemical and structural studies . Additionally, it is used in various applications such as SDS-PAGE to analyze protein purity and structure .
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