Anti-Hsp70 Antibody

The 70 kDa heat shock protein Hsp70 is an ATP-dependent molecular chaperone that assists nascent polypeptide folding, prevents aggregation of misfolded substrates, and refolds stress-denatured proteins under heat shock, oxidative, and proteotoxic stress. Produced by Antibodies.com as a recombinant rabbit monoclonal reagent, this unconjugated primary antibody recognizes the Hsp70 target and has been validated for western blot, immunocytochemistry, immunofluorescence, immunohistochemistry, and flow cytometry on human, mouse, and rat samples.

Each vial contains 100 µl of antibody in 1x TBS (pH 7.4) supplemented with 1% BSA, 40% glycerol, and 0.05% sodium azide as preservative. The glycerol-rich formulation supports storage at -20 °C and limits freeze-thaw damage across multiple uses. Researchers investigating the heat shock response in tumor cell survival, neurodegeneration models, ischemia-reperfusion injury, and chaperone-mediated autophagy routinely deploy this reagent to probe Hsp70 expression across cell lysates, fixed-cell preparations, and tissue sections.

For western blot, denatured lysates are separated by SDS-PAGE, transferred to nitrocellulose or PVDF, and detected with HRP- or fluorophore-conjugated secondary reagents. In immunocytochemistry and immunofluorescence, the antibody reveals predominantly cytoplasmic staining with redistribution to the nucleus under stress. Immunohistochemistry on formalin-fixed paraffin-embedded sections supports tumor biopsy profiling and rodent tissue studies. The unconjugated format also pairs cleanly with user-selected fluorophore-conjugated secondaries for flow cytometry panels, enabling co-expression analysis with other stress or immune markers.