Anti-HSP70 (C-terminus) Antibody

The HSP70 heat shock protein family comprises stress-inducible molecular chaperones of roughly 70 kDa that assist in protein folding, translocation across membranes, and protection from aggregation under proteotoxic stress. This unconjugated mouse monoclonal reagent targets the C-terminal substrate-binding region of HSP70, a domain that engages client polypeptides during refolding cycles and is structurally distinct from the N-terminal ATPase module. Supplied as 100 µl of purified IgG in 0.1 M Tris-glycine (pH 7.4), 150 mM NaCl buffer containing 0.2% sodium azide and 50% glycerol, the preparation remains stable when stored refrigerated and protected from light, with the glycerol cryoprotectant tolerating occasional freeze-thaw cycles for repeated use.

Validated for Western blot and immunoprecipitation on human samples, the antibody supports detection of endogenous HSP70 in whole-cell lysates and tissue homogenates, and enables pull-down experiments that interrogate chaperone-client complexes under basal or heat-shocked conditions. C-terminus-specific recognition is particularly useful when researchers need to discriminate full-length HSP70 activity from truncations or post-translational events affecting the regulatory N-terminus. Laboratories working on cancer cell survival, neurodegeneration, and proteostasis broadly use this reagent in standard immunoblotting and co-immunoprecipitation workflows.

From Antibodies.com, this monoclonal is part of the primary antibody portfolio targeting conserved stress-response proteins and ships as a single-use vial ready for dilution into standard blocking and wash buffers.