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.
SDS-PAGE - DnaJ protein (ab51305)
ab51305 in 13% SDS-PAGE
This product has been referenced in:
Kharenko OA et al. Identification and characterization of interactions between abscisic acid and human heat shock protein 70 family members. J Biochem154:383-91 (2013).
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