c-Jun, a key component of the AP-1 transcription factor complex, is a proto-oncoprotein involved in regulating cell proliferation, differentiation, apoptosis, and stress responses. It dimerizes with other Jun/Fos family members (e.g., c-Fos) to bind DNA and modulate gene expression. c-Jun is activated via phosphorylation (e.g., at Ser63/Ser73 by JNK kinases) in response to growth factors, cytokines, or cellular stress, making it a critical mediator in MAPK signaling pathways.
c-Jun antibodies are essential tools for studying its expression, localization, and activation status in biomedical research. These antibodies are widely used in techniques like Western blotting (WB), immunohistochemistry (IHC), and immunofluorescence (IF) to detect endogenous c-Jun or its phosphorylated forms. Specific clones (e.g., recognizing total c-Jun or phospho-Ser63/73) enable differentiation between inactive and activated states, providing insights into cellular signaling dynamics. Validated c-Jun antibodies are critical for investigating its role in cancer (e.g., tumor progression, drug resistance), neurodegenerative diseases, and inflammatory conditions. Many antibodies are raised against epitopes in the N-terminal transactivation domain or C-terminal DNA-binding domain, with host species (rabbit, mouse) and clonal specificity (monoclonal/polyclonal) varying by application. Knockout-validated antibodies ensure reliability in distinguishing c-Jun from homologous proteins. Their applications extend to drug development, as c-Jun is a potential therapeutic target in diseases driven by dysregulated AP-1 activity.