The mitogen-activated protein kinase 8 (MAPK8), also known as JNK1 (c-Jun N-terminal kinase 1), is a member of the serine/threonine protein kinase family. It plays a critical role in regulating cellular responses to stress, inflammation, and apoptosis. MAPK8 is activated by upstream kinases (MKK4/MKK7) through phosphorylation, triggering its translocation to the nucleus where it modulates transcription factors like c-Jun, ATF2. and p53. This signaling pathway is implicated in diverse biological processes, including cell proliferation, differentiation, and programmed cell death. Dysregulation of MAPK8 has been linked to cancer, neurodegenerative disorders, and immune diseases.
MAPK8 antibodies are essential tools for studying its expression, activation, and localization in experimental models. These antibodies typically target specific epitopes, such as phosphorylated residues (e.g., Thr183/Tyr185) for detecting active MAPK8 or total protein regions. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and flow cytometry. Validation of MAPK8 antibodies often involves knockout cell lines or inhibition studies to confirm specificity. Researchers rely on these antibodies to explore MAPK8's role in disease mechanisms, drug discovery, and signaling crosstalk. Commercial antibodies vary in clonality, host species, and conjugation formats, enabling flexibility in experimental design. Proper controls are critical due to potential cross-reactivity with homologous kinases like JNK2/JNK3.