Anti-HSP90AB1 (phospho S254) Antibody

The HSP90AB1 (HSP90β) protein belongs to the heat shock protein 90 family and functions as an ATP-dependent molecular chaperone that stabilizes client proteins involved in signal transduction, protein folding, and stress response. Phosphorylation at serine 254 is a post-translational modification located in the charged linker region of HSP90β, modulates chaperone activity and substrate binding kinetics, and has been examined in studies of cancer cell proliferation, heat shock recovery, and kinase signaling cascades involving casein kinase 2.

This rabbit polyclonal IgG antibody from Antibodies.com is raised against the phosphorylated S254 epitope and is validated for Western blot detection across human, mouse, and rat samples. Provided as 100 µl of unconjugated antiserum, it supports researchers investigating chaperone regulation, client protein maturation, and phosphorylation-dependent signaling events. Lysates from heat-shocked or chemically stressed cell lines such as HeLa, HEK293, and NIH/3T3 are commonly used as positive controls to confirm phospho-specific recognition.

Applications include Western blot analysis of immunoprecipitated HSP90 complexes or whole-cell lysates, with the unconjugated format allowing flexibility in secondary antibody choice and detection chemistry. Recommended handling includes brief centrifugation of the vial prior to opening, refrigerated storage for short-term use, and aliquoting for long-term storage below -20 °C to preserve phospho-specific reactivity across multiple freeze-thaw cycles.