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HSP40/Hdj1, mAb (2E1) antibody

RRID:AB_10621843

Antibody ID

AB_10621843

Target Antigen

HSP40/Hdj1 mAb (2E1) mouse, human, works, human, mouse and rat (hdj1) detects a band of ~40kda by western blot

Proper Citation

(Enzo Life Sciences Cat# ADI-SPA-450, RRID:AB_10621843)

Clonality

monoclonal antibody

Comments

manufacturer recommendations: IgG2a Western Blot; Immunoprecipitation; Immunoprecipitation (2-5µg/200µl from 5x10, 6, cells), Western Blot (1-2µg/ml, ECL), Optimal conditions must be determined individually for each application.

Host Organism

mouse

Vendor

Enzo Life Sciences

Cat Num

ADI-SPA-450

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:


Abstract:

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.