DsbG protein (30R-1281)
Purified recombinant E.coli DsbG protein
|Synonyms||ybdP protein, Thiol:disulfide interchange protein dsbG ECK0598 protein, Periplasmic disulfide isomerase/thiol disulphide oxidase protein, , JW0597 protein|
Coomassie Blue stained SDS-PAGE of DsbG protein (30R-1281)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||18-248 amino acids: MEELPAPVKA IEKQGITIIK TFDAPGGMKG YLGKYQDMGV TIYLTPDGKH AISGYMYNEK GENLSNTLIE KEIYAPAGRE MWQRMEQSHW LLDGKKDAPV IVYVFADPFC PYCKQFWQQA RPWVDSGKVQ LRTLLVGVIK PESPATAAAI LASKDPAKTW QQYEASGGKL KLNVPANVST EQMKVLSDNE KLMDDLGANV TPAIYYMSKE NTLQQAVGLP DQKTLNIIMG NK|
|Purity||> 95% pure|
|Molecular Weight||25.8 kDa(232 aa), confirmed by MALDI-TOF.|
|Form & Buffer||Supplied as a liquid in 20mM Tris-HCl buffer, pH 8.0, containing 2mM EDTA, and 10% glycerol.|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||Dsb proteins control the formation and rearrangement of disulfide bonds during the folding of secreted and membrane proteins in bacteria. DsbG, a member of this family, has disulfide bond isomerase and chaperone activity. So DsbG was shown to interact with refolding intermediates of chemically denatured citrate synthase and prevents their aggregation in vitro. In addition to sharing sequence homology with the thiol disulfide exchange protein DsbC, DsbG likewise was shown to form a stable periplasmic dimer and it displays an equilibrium constant with glutathione comparable with DsbA and DsbC. DsbG was found to be expressed at approximately 25% the level of DsbC. Recombinant DsbG was expressed in E. coli and purified by conventional chromatography techniques.|
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