The extracellular signal-regulated kinase 5 (ERK5), also known as mitogen-activated protein kinase 7 (MAPK7), is a member of the MAPK family that regulates critical cellular processes, including proliferation, differentiation, survival, and stress responses. Unlike other ERK isoforms (e.g., ERK1/2), ERK5 contains a unique C-terminal domain that influences its activation and substrate specificity. It is activated by dual phosphorylation (Thr218/Tyr220) via upstream kinases like MEK5 in response to growth factors, cytokines, or cellular stress. ERK5 signaling is implicated in development, angiogenesis, and tissue homeostasis, with dysregulation linked to cancer, cardiovascular diseases, and neurodegenerative disorders.
ERK5 antibodies are essential tools for studying its expression, localization, and activation in cells and tissues. These antibodies are designed to target specific regions of ERK5. such as the N-terminal kinase domain or phosphorylated residues, enabling detection in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF). High-quality ERK5 antibodies exhibit specificity to distinguish ERK5 from other MAPKs (e.g., ERK1/2) and detect phosphorylated (active) versus total ERK5. Researchers use these antibodies to explore ERK5's role in disease mechanisms, drug response, and signaling crosstalk. Validation across applications and species is critical to ensure reliability, with monoclonal antibodies offering consistency and polyclonal antibodies providing broader epitope recognition. Commercial ERK5 antibodies are widely available, often accompanied by knockout-validated data to confirm target specificity.