This product is an active protein and may elicit a biological response in vivo, handle with caution.
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.
Recombinant E. coli DnaJ protein images
SDS-PAGE - DnaJ protein (Active) (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 - DnaJ protein (Active) (ab91598)
All lanes : DnaJ Polyclonal
Lane 1 : Molecular weight markers Lane 2 : ab91598 at 0.1 µg
References for Recombinant E. coli DnaJ protein (ab91598)
has not yet been referenced specifically in any publications.
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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
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