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anti-DNAK antibody


Antibody ID


Target Antigen

DNAK e coli

Proper Citation

(Matthias P. Mayer, Centre for Molecular Biology (ZMBH), University of Heidelberg Cat# anti-DNAK, RRID:AB_2650528)


polyclonal antibody



Host Organism



Matthias P. Mayer, Centre for Molecular Biology (ZMBH), University of Heidelberg

Cat Num


Publications that use this research resource

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.

  • Nillegoda NB
  • Elife
  • 2017 May 15

Literature context:


Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain folding to protein disaggregation. This versatility in function is achieved through a diverse family of J-protein cochaperones that select substrates for Hsp70. Substrate selection is further tuned by transient complexation between different classes of J-proteins, which expands the range of protein aggregates targeted by metazoan Hsp70 for disaggregation. We assessed the prevalence and evolutionary conservation of J-protein complexation and cooperation in disaggregation. We find the emergence of a eukaryote-specific signature for interclass complexation of canonical J-proteins. Consistently, complexes exist in yeast and human cells, but not in bacteria, and correlate with cooperative action in disaggregation in vitro. Signature alterations exclude some J-proteins from networking, which ensures correct J-protein pairing, functional network integrity and J-protein specialization. This fundamental change in J-protein biology during the prokaryote-to-eukaryote transition allows for increased fine-tuning and broadening of Hsp70 function in eukaryotes.