Heat Shock Protein 70 (HSP-70) ELISA Kit for Rat

HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70.

Protein type: Chaperone; Heat shock protein; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 20p12

Cellular Component: apical plasma membrane; basolateral plasma membrane; centriole; centrosome; cytoplasm; cytosol; focal adhesion; inclusion body; intracellular; intracellular ribonucleoprotein complex; membrane raft; mitochondrion; nuclear speck; nucleus; perinuclear region of cytoplasm; protein complex; ubiquitin ligase complex; vesicle

Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; cadherin binding; denatured protein binding; enzyme binding; G-protein coupled receptor binding; heat shock protein binding; histone deacetylase binding; NF-kappaB binding; protease binding; protein binding; protein N-terminus binding; receptor binding; RNA binding; ubiquitin protein ligase binding; unfolded protein binding

Biological Process: ATP metabolic process; binding of sperm to zona pellucida; chaperone-mediated protein complex assembly; defense response; mRNA catabolic process; negative regulation of apoptosis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; negative regulation of myeloid cell apoptosis; negative regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of vasoconstriction; positive regulation of interleukin-8 production; positive regulation of NF-kappaB transcription factor activity; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of T cell mediated cytotoxicity; protein refolding; protein stabilization; regulation of protein ubiquitination; response to heat; response to unfolded protein