Phospho-Stathmin 1 (Ser25) antibody is a specialized tool used to detect the phosphorylation of Stathmin 1 at serine residue 25. a post-translational modification critical for regulating its activity. Stathmin 1. also known as oncoprotein 18 (OP18), is a cytosolic phosphoprotein involved in microtubule dynamics by promoting depolymerization or preventing polymerization of tubulin heterodimers. Its function is tightly regulated by phosphorylation, particularly during cell cycle progression, differentiation, and stress responses. Phosphorylation at Ser25. along with other residues (e.g., Ser16. Ser38. and Ser63), modulates Stathmin 1’s microtubule-destabilizing activity, influencing mitotic spindle formation and cell division.
The Ser25 phosphorylation site is primarily targeted by cyclin-dependent kinases (CDKs) and mitogen-activated protein kinases (MAPKs), linking its activity to cell cycle checkpoints (e.g., G2/M transition) and signaling pathways responsive to extracellular stimuli. Dysregulation of Stathmin 1 phosphorylation is associated with cancer progression, neurodegenerative disorders, and developmental defects, as abnormal microtubule dynamics can impair mitotic fidelity, intracellular transport, or neuronal morphogenesis.
Phospho-Stathmin 1 (Ser25) antibodies enable researchers to study the spatiotemporal activation of Stathmin 1 in various contexts, such as drug-induced mitotic arrest, neuronal development, or cancer cell migration. These antibodies are validated for techniques like Western blotting, immunofluorescence, and immunoprecipitation, aiding in the exploration of Stathmin 1’s role in health and disease. Specificity for the phosphorylated Ser25 epitope ensures accurate detection of the active regulatory state, making it essential for mechanistic studies of microtubule-related processes.