The Phospho-XIAP (Ser87) antibody is designed to detect XIAP (X-linked inhibitor of apoptosis protein) when phosphorylated at serine residue 87. XIAP, a member of the inhibitor of apoptosis protein (IAP) family, suppresses apoptosis by inhibiting caspases through its BIR domains. Post-translational modifications, including phosphorylation, regulate XIAP’s stability, localization, and anti-apoptotic activity. Phosphorylation at Ser87 has been implicated in modulating XIAP’s interaction with other proteins and its ubiquitination-dependent degradation. Studies suggest this modification may occur in response to cellular stress or survival signals, potentially influencing cell fate decisions in cancer or neurodegenerative diseases.
The Phospho-XIAP (Ser87) antibody is commonly used in research to investigate XIAP regulation in apoptosis, autophagy, and signaling pathways (e.g., NF-κB). It enables detection of this phosphorylation event via techniques like western blotting, immunofluorescence, or immunohistochemistry. Validation often includes testing in cell lines treated with kinase activators/inhibitors or under stress conditions. Researchers utilize this tool to explore XIAP’s role in therapeutic resistance, as dysregulated XIAP phosphorylation may correlate with disease progression or treatment outcomes. Proper controls (e.g., non-phosphorylated XIAP antibodies) are recommended to ensure specificity in experimental settings.