SEPTIN1 is a member of the septin family, a group of GTP-binding proteins involved in diverse cellular processes, including cytokinesis, cell polarity, membrane remodeling, and cytoskeletal organization. SEPTIN1 plays critical roles in neuronal development, synaptic plasticity, and tumorigenesis. It forms heteromeric complexes with other septins to create dynamic filaments that regulate cellular architecture and signaling pathways.
Antibodies targeting SEPTIN1 are essential tools for studying its expression, localization, and function in both normal and pathological contexts. These antibodies are widely used in techniques such as Western blotting, immunofluorescence, and immunohistochemistry to detect SEPTIN1 in tissues and cultured cells. Research has linked SEPTIN1 dysregulation to neurodegenerative disorders (e.g., Alzheimer’s disease) and cancers (e.g., leukemia, prostate cancer), where altered expression patterns correlate with disease progression.
Most commercial SEPTIN1 antibodies are raised against specific epitopes within its N-terminal or C-terminal domains, often validated using knockout/knockdown controls to ensure specificity. Species reactivity typically includes human and mouse models. Recent studies also explore SEPTIN1's interaction partners and post-translational modifications, facilitated by antibody-based pull-down assays. However, researchers must verify antibody performance across experimental setups due to potential cross-reactivity with other septin family members.