
Recombinant E.coli dsbG eiwit
Kwaliteit
ISO Gecertificeerd
Levering
24-48 uur
Technische Specificaties
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.
Thiol:disulfide interchange protein dsbG, ybdP, Thiol:disulfide interchange protein dsbG ECK0598, JW0597, Periplasmic disulfide isomerase/thiol disulphide oxidase
E.coli
E.coli
Non-Tagged
SDS-PAGE
1 mg/mL (determined by Bradford assay)
> 95% by SDS-PAGE
25.8 kDa (232aa) confirmed by MALDI-TOF
DsbG, Thiol:disulfide interchange protein dsbG, ybdP, Thiol:disulfide interchange protein dsbG ECK0598, JW0597, Periplasmic disulfide isomerase/thiol disulphide oxidase, ATGP0281-10 µg, ATGP0281-20 µg, ATGP0281-50 µg, ATGP0281-100 µg, ATGP0281-250 µg, ATGP0281-500 µg, ATGP0281-1 mg, ATGP0281-10, ATGP0281-20, ATGP0281-50, ATGP0281-100, ATGP0281-250, ATGP0281-500, ATGP0281-1
Riley M., et al (2006) Nucleic Acids Res. 34 (1) :1-9.; ; Andersen CL., et al (1997) Mol Microbiol. 26 (1) :121-32;
Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 2mM EDTA, 10% glycerol
Heat Shock Proteins
NP_415137
P77202
E.coli
MEELPAPVKA IEKQGITIIK TFDAPGGMKG YLGKYQDMGV TIYLTPDGKH AISGYMYNEK GENLSNTLIE KEIYAPAGRE MWQRMEQSHW LLDGKKDAPV IVYVFADPFC PYCKQFWQQA RPWVDSGKVQ LRTLLVGVIK PESPATAAAI LASKDPAKTW QQYEASGGKL KLNVPANVST EQMKVLSDNE KLMDDLGANV TPAIYYMSKE NTLQQAVGLP DQKTLNIIMG NK
Beschrijving
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
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