The Kelch-like ECH-associated protein 1 (KEAP1) is a critical regulator of the cellular response to oxidative stress, primarily through its interaction with nuclear factor erythroid 2-related factor 2 (NRF2). KEAP1 acts as a substrate adaptor for a Cullin3-based ubiquitin ligase complex, targeting NRF2 for proteasomal degradation under normal conditions. During oxidative stress, KEAP1 undergoes conformational changes, releasing NRF2 to accumulate in the nucleus and activate cytoprotective genes involved in detoxification, antioxidant defense, and metabolism. Dysregulation of the KEAP1-NRF2 pathway, often due to KEAP1 mutations, epigenetic silencing, or protein overexpression, is implicated in various diseases, including cancer, neurodegeneration, and chronic inflammatory disorders. In cancer, KEAP1 inactivation leads to constitutive NRF2 activation, promoting tumor progression, chemoresistance, and radiation resistance. KEAP1 antibodies are essential tools for studying its expression, localization, and interactions in research and diagnostics. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to assess KEAP1 status in tissues or cell lines, aiding in the identification of biomarkers and therapeutic targets. KEAP1-targeted therapies, including NRF2 inhibitors and KEAP1 stabilizers, are under investigation to counteract pathway dysregulation in disease.