STK17A (serine/threonine kinase 17A) is a member of the death-associated protein kinase (DAPK) family, involved in regulating apoptosis, autophagy, and cellular stress responses. It phosphorylates substrates to modulate programmed cell death and may play dual roles in cancer, acting as either a tumor suppressor or promoter depending on context. STK17A antibodies are essential tools for studying its expression, localization, and function in biological systems. These antibodies are commonly used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to detect STK17A in tissues or cell lines.
Research links STK17A to DNA damage response, cell cycle control, and interactions with p53 or Bcl-2 family proteins. Dysregulation of STK17A has been implicated in cancers (e.g., colorectal, liver, and gliomas), neurodegenerative diseases, and metabolic disorders. However, its mechanisms remain partially controversial; some studies suggest pro-apoptotic activity, while others associate it with chemoresistance. Antibodies targeting specific epitopes (e.g., N-terminal or catalytic domains) help clarify these roles by enabling precise protein detection or functional inhibition. Validation of STK17A antibodies includes testing knockout models to confirm specificity. Their application advances understanding of disease pathways and potential therapeutic targeting, though variability in tissue-specific expression requires careful experimental design.