Recombinant E.coli secB eiwit

SecB, a remarkable chaperone involved in protein export, binds diverse ligands rapidly with high affinity and low specificity. It plays a crucial role during protein export via the general secretory pathway by modulating the partitioning of precursors between folding or aggregation and delivery to the membrane-bound translocation apparatus. SecB has the potential to participate in functions outside of export acting as a general nonspecific chaperone to provide buffering capacity of the nonnative state of proteins in the cytosolic pool. Recombinant E. coli SecB protein was expressed in E. coli and purified by using conventional chromatography.

Protein export chaperone, SecB, Protein export protein secB, Chaperone SecB

E.coli

E.coli

Non-Tagged

SDS-PAGE

1 mg/mL (determined by Absorbance at 280 nm)

> 95% by SDS-PAGE

17.2 kDa (155aa) confirmed by MALDI-TOF

SecB, Protein export chaperone, SecB, Protein export protein secB, ATGP0318-10 µg, ATGP0318-20 µg, ATGP0318-50 µg, ATGP0318-100 µg, ATGP0318-250 µg, ATGP0318-500 µg, ATGP0318-1 mg, ATGP0318-10, ATGP0318-20, ATGP0318-50, ATGP0318-100, ATGP0318-250, ATGP0318-500, ATGP0318-1

Driessen AJ., et al. (2008), Annu Rev Biochem. 77:643-67.; ; Bechtluft P., et al. (2007) . Science. 318 (5855) :1458-61.;

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 10% glycerol

Heat Shock Proteins

NP_418066

P0AG86

E.coli

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA