Fri, 09/20/2013 - 12:34

70-kDa Heat Shock Protein (Hsp70) is an abundant protein cofactor commonly known as a molecular chaperone. Found in most eukaryotes, Hsp genes are members of a heat-inducible multigene family. These proteins are found in most cellular compartments of eukaryotes - everything from nuclei, mitochondria, chloroplasts, to endoplasmic reticulum and cytosol. A review on chaperone-mediated protein folding and the distinction between the different chaperone families highlights the abundant use of Hsp70 antibody (1). Bork’s group employed the Hsp70 antibody to demonstrate that not only does Hsp70 bind to ATP with high affinity, but interestingly, it also possesses a weak ATPase activity that can be stimulated through binding to unfolded proteins and synthetic peptides, suggesting a common evolutionary origin for these different enzymes (2). Studies examining the mechanisms behind the uncoating of clathrin-coated vesicles used the Hsp70 antibody and a truncated form of Hsp70 to show that the clathrin light chain A is more important that the clathrin light chain B n guiding reversible conformational changes that occur in response to ion concentration fluxes (3).

Western Blot: Hsp70 Antibody Western Blot: Hsp70 Antibody

Results with the Hsp70 antibody in Choi’s lab found that ERBB3 (HER3) is a key sensor in EGF downstream-signaling by driving ERBB3/HER3 and EGFR/ERBB3 dimerization, opening up the potential for ERBB3 as an antibody therapeutic target for cancer (4). Pharmacological studies with Hsp70 antibody in endothelial cells have found novel four candidates of endogenous modulators of soluble guanylyl cyclase (sGC) (5). One of them was identified as hsp70 through co-immunoprecipitation and mass spectrometry analysis.

  1. PMID: 10221986
  2. PMID: 1323828
  3. PMID: 1975516
  4. PMID: 23342251
  5. PMID: 15509556

Novus Biologicals offers various Hsp70 reagents for your research needs including:

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