Phospho-Filamin A/B (Ser2152/Ser2107) antibodies are immunological tools designed to detect the phosphorylated forms of Filamin A (FLNA) and Filamin B (FLNB) at specific serine residues (Ser2152 in FLNA and Ser2107 in FLNB). Filamins are actin-binding proteins that crosslink actin filaments into dynamic networks, playing critical roles in cell mechanics, adhesion, migration, and signaling. Phosphorylation at these conserved serine residues modulates Filamin’s interactions with binding partners, such as integrins, transmembrane receptors, and signaling molecules, thereby influencing cytoskeletal remodeling and cellular responses to mechanical or biochemical stimuli.
These antibodies are widely used in research to investigate Filamin’s regulatory mechanisms in physiological processes (e.g., cell motility, wound healing) and pathological conditions (e.g., cancer metastasis, cardiovascular disorders). The phosphorylation events at Ser2152/Ser2107 are associated with kinase pathways, including PAK1 (p21-activated kinase 1) and AMPK (AMP-activated protein kinase), which are activated under stress or growth signals. Detection via Western blotting, immunofluorescence, or immunohistochemistry helps correlate Filamin phosphorylation with cellular states, such as epithelial-mesenchymal transition or mechanotransduction.
Understanding Filamin phosphorylation dynamics provides insights into diseases linked to cytoskeletal dysfunction, making these antibodies valuable for studying molecular pathways in cancer, vascular biology, and developmental disorders. Proper validation (e.g., knockout controls, phosphatase treatment) is essential to ensure specificity due to potential cross-reactivity between FLNA and FLNB isoforms.