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Chaperone Hsp40 co chaperone with DnaK
Chaperone protein dnaJ
Heat shock protein J
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 - Recombinant E. coli DnaJ protein (ab91598)
Lane 1: Molecular weight markers
Lane 2: 0.5 µg ab91598
Lane 3: 1 µg ab91598
Lane 4: 2 µg ab91598
Lane 5: 5 µg ab91598
Western blot - Recombinant E. coli DnaJ protein (ab91598)
All lanes : DnaJ Polyclonal Antibody
Lane 1 : Molecular weight markers Lane 2 : ab91598 at 0.1 µg
has not yet been referenced specifically in any publications.
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