Anti-MDM2 (phospho S166) Antibody

Phosphorylation at serine 166 is a key regulatory switch on the E3 ubiquitin ligase MDM2, controlling its subcellular localization, protein stability, and ability to ubiquitylate p53 during DNA damage responses and PI3K/AKT signaling. This unconjugated rabbit polyclonal IgG reagent from Antibodies.com is raised against the phospho-S166 epitope and selectively detects the modified form of MDM2 in human samples across Western blot, immunohistochemistry, and immunofluorescence workflows.

Supplied as 50 µl of ready-to-use reagent, the antibody is validated for WB, IHC, and IF applications on human tissue and cell lines. Investigators studying p53 pathway dysregulation in cancer biology, genotoxic stress responses, and AKT-driven signaling routinely probe phospho-S166 MDM2 as a readout of pathway activation status. Store the vial frozen at -20°C in working aliquots to limit freeze-thaw cycles and protect from light.

Because S166 phosphorylation is dynamically regulated and phosphatase-labile, lysate preparation with freshly added phosphatase inhibitors is recommended to preserve epitope integrity. The unconjugated format allows flexible pairing with custom fluorophore or enzyme conjugates depending on the detection platform, and the polyclonal backbone tolerates minor sequence variation around the phospho-epitope, supporting broad recognition of the modified target.