STK17A Antibody / Serine/threonine-protein kinase 17A, 100 ug

STK17A antibody detects Serine/threonine-protein kinase 17A, also known as DRAK1, a pro-apoptotic kinase that regulates programmed cell death, cytoskeletal organization, and transcriptional responses to stress. STK17A belongs to the death-associated protein kinase (DAPK) family and is activated by genotoxic and oxidative stress. The STK17A antibody is widely used in apoptosis research, cancer biology, and neurodegeneration studies.

STK17A is encoded by the STK17A gene on human chromosome 7p13. The protein is approximately 42 kilodaltons and consists of an N-terminal catalytic kinase domain and a C-terminal regulatory tail rich in serine residues. STK17A localizes mainly to the nucleus and cytoplasm, where it phosphorylates substrates involved in apoptosis signaling and actin remodeling.

The STK17A antibody detects a 47-53 kilodalton band by western blot and demonstrates nuclear enrichment under apoptotic conditions. STK17A mediates cell death through phosphorylation of transcription factors such as FOXO3 and histone H2B, promoting DNA fragmentation and chromatin condensation. Its expression is upregulated by p53 following DNA damage, placing it downstream of tumor-suppressive signaling pathways.

STK17A also influences cytoskeletal dynamics by modulating RhoA activity and actin filament organization, linking apoptosis regulation to cellular morphology. In neurons, STK17A activation contributes to axon retraction and degeneration during stress. Conversely, suppression of STK17A enhances survival and regenerative capacity in damaged tissues.

Dysregulated STK17A signaling is implicated in multiple diseases. Overexpression promotes apoptosis and tissue atrophy, while reduced activity correlates with tumor survival and resistance to therapy. Pharmacologic targeting of STK17A could restore controlled cell death in cancer or prevent neurodegeneration in stress-related disorders. NSJ Bioreagents provides a validated STK17A antibody optimized for its applications, supporting detailed investigation of apoptotic signaling and stress-response regulation.