Anti-Hsp70

Anti-Hsp70 Antibody was prepared from monospecific antiserum by delipidation and defibrination. A BLAST analysis was used to suggest cross-reactivity with Hsp70 from Human, mouse, rat, beluga, cow, dog, fish (carp), guinea pig, hamster, monkey, pig, sheep, coral, tomato, tobacco, spiny dogfish shark (Squalus acanthias), and Atlantic Hagfish (Myxine glutinosa) based on 100% homology with the immunizing sequence. Cross-reactivity with Hsp70 from other sources has not been determined. Heat Shock research. Protein function: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. [The UniProt Consortium]