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 antibody is stable for at least 1 year from the date of receipt when stored at -20°C to -70°C. Reconstituted antibody can also be aliquotted and stored at 4°C for 1 month or at -20°C to -70°C in a manual defrost freezer for many months without detectable loss activity. Please avoid freeze-thaw cycles.

The antibody can specifically bind to its immunogen, and did not show any cross reactivity with unrelated antigens in ELISA. The specificity for binding to recombinant protein, cellular protein and native antigen is not defined. Cross reactivity with mouse and rat HSP70 has not yet been tested.

Mouse Anti-Mycobacterium tuberculosis Heat Shock Protein-70 (HSP70) (cat# MD-02-0038 ) Mouse Anti-Human Heat Shock Protein-70 (HSP70) (cat# MD-02-0037 )