Rabbit Polyclonal HSP9(Acetyl-Lys435) Antibody

The HSP90 (Acetyl-Lys435) antibody is a specialized tool used to study post-translational modifications of heat shock protein 90 (HSP90), a molecular chaperone critical for protein folding, cellular stress response, and signaling pathways. HSP90 function is tightly regulated by acetylation, a reversible modification that modulates its ATPase activity and interactions with client proteins. Acetylation at lysine 435 (K435) in HSP90 has been implicated in altering chaperone activity, potentially affecting cancer progression, neurodegenerative diseases, and stress adaptation. This antibody specifically recognizes the acetylated form of K435. enabling researchers to investigate the dynamic regulation of HSP90 in physiological and pathological contexts. Its applications include Western blotting, immunoprecipitation, and immunofluorescence to map acetylation-dependent HSP90 interactions, assess drug efficacy (e.g., HDAC inhibitors), and explore disease mechanisms. As HSP90 is a therapeutic target in oncology, understanding site-specific acetylation via this antibody contributes to developing precision therapies targeting chaperone networks. Validation typically involves knockout/knockdown controls or acetyltransferase-deficient models to confirm specificity for the modified epitope.