Heat Shock Protein 70 (HSPA1A/1B) Recombinant Protein

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

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: 6p21.3

Cellular Component: signalosome; focal adhesion; mitochondrion; endoplasmic reticulum; inclusion body; cytosol; ribonucleoprotein complex; centriole; nucleoplasm; perinuclear region of cytoplasm; cytoplasm; nuclear speck; nucleus; ubiquitin ligase complex; vesicle

Molecular Function: viral receptor activity; protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; ATPase activity; double-stranded RNA binding; unfolded protein binding; protein N-terminus binding; ATPase activity, coupled; ATP binding

Biological Process: negative regulation of cell proliferation; entry of virus into host cell; protein stabilization; positive regulation of erythrocyte differentiation; mRNA catabolic process; negative regulation of protein ubiquitination; protein refolding; gene expression; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis