The SEPTIN2 antibody is a crucial tool for studying the septin family of GTP-binding proteins, which play essential roles in cellular processes such as cytokinesis, cytoskeletal organization, and membrane dynamics. SEPTIN2. a member of the septin family, forms heteromeric complexes with other septins to create structural scaffolds that regulate cell division, vesicle trafficking, and apoptosis. Its involvement in these processes links it to various diseases, including cancer, neurodegenerative disorders, and infections. Researchers utilize SEPTIN2 antibodies primarily in techniques like Western blotting, immunofluorescence, and immunohistochemistry to detect protein expression levels, subcellular localization (e.g., filamentous structures near membranes or mitotic spindles), and interactions with binding partners. These antibodies are often validated in knockout (KO) models or siRNA-treated cells to confirm specificity. Commercially available SEPTIN2 antibodies are produced in hosts such as rabbits or mice, with monoclonal and polyclonal variants offering distinct advantages in sensitivity and cross-reactivity. Recent studies highlight its dysregulation in tumors (e.g., breast, prostate cancers) and neurological conditions like Alzheimer's, driving interest in its molecular mechanisms. Proper antibody selection depends on experimental goals, epitope regions, and validation data, emphasizing its importance in both basic research and clinical biomarker investigations.