The Phospho-PML (Ser518) antibody is a specialized tool used to detect the phosphorylated form of the Promyelocytic Leukemia (PML) protein at serine residue 518. PML is a key component of PML nuclear bodies (PML-NBs), dynamic subnuclear structures involved in diverse cellular processes, including transcriptional regulation, apoptosis, DNA damage response, and antiviral defense. Phosphorylation at Ser518 is a critical post-translational modification that modulates PML's functional interactions and structural organization within PML-NBs. This modification is often induced by cellular stress, DNA damage, or specific kinase signaling pathways (e.g., CK2. ATM/ATR), influencing PML's role in tumor suppression, cell cycle control, and antiviral responses.
The antibody is widely used in research to study PML's involvement in diseases such as acute promyelocytic leukemia (APL), where PML fusion proteins disrupt normal nuclear body function, as well as viral infections (e.g., herpesviruses) that target PML-NBs for immune evasion. By specifically recognizing the phosphorylated Ser518 epitope, this antibody helps elucidate dynamic changes in PML activity under pathological or experimental conditions, aiding in the understanding of PML-NB regulation, stress signaling, and therapeutic targeting. Its applications span Western blotting, immunofluorescence, and immunohistochemistry, providing insights into PML's context-dependent roles in health and disease.