HSP70 Mouse Monoclonal Antibody [3G10]

Function

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.

Background References

1. Radons J. The human HSP70 family of chaperones: where do we stand? Cell Stress Chaperones 21:379-404(2016).

2. Hasson S.A. et al. High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy. Nature 504:291-295(2013).

Subcellular Location

Cytosol, Mitochondrion, Nucleus.

UNIPROT

SwissProt: P0DMV8 Human

SwissProt: P0DMV9 Human

Synonyms