||Recombinant E.coli SecB protein was expressed in E.coli and purified by using conventional chromatography, 17.2 kDa (155aa).
||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.
||Liquid. In 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol.
||> 95% by SDS - PAGE
||1 mg/ml (determined by Bradford assa
|Sequences of amino acids:
||MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA
||Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.