E. coli DnaJ (aa 1 - 376), recombinant protein from E. coli
Escherichia coli dnaJ (NP_414556, 1 a.a. - 376 a.a.) full-length recombinant protein expressed inEscherichia coli .
In 25 mM Tris-HCl, 100 mM NaCl, pH 7.5 (5 mM DTT, 10% glycerol)
2-8°C short term, -20°C long term
DnaK and DnaJ both bind to the same target peptide, forming a ternary complex. The DnaK system of Escherichia coli is a homolog of the eukaryotic Hsp70 chaperone system.
The E. coli heat-shock protein DnaJ has been implicated in protein folding and protein complex dissociation. DnaJ, Heat shock protein, functions in association with DnaK(Hsp70) molecular chaperone to facilitate protein folding. p70 chaperone. DnaJ plays a key role in the chaperone reaction by stimulating the ATPase activity and activating the substrate binding of Hsp70. DnaJ consists of four domains that are N-terminal 76 amino acid J-domain, G/F domain, zinc-binding cystein rich CR-domain, C-terminal CTD-domain and they are conserved to various degrees among the homologues.