MAPK14 (mitogen-activated protein kinase 14), also known as p38α, is a serine/threonine kinase belonging to the p38 MAPK family. It plays a central role in cellular responses to stress signals (e.g., cytokines, UV irradiation, osmotic shock) and regulates processes like inflammation, apoptosis, cell differentiation, and cell cycle progression. Activated via phosphorylation by upstream kinases (MKK3/MKK6), MAPK14 phosphorylates downstream targets, including transcription factors (e.g., ATF2. MEF2) and kinases (e.g., MSK1/2), to modulate gene expression and signaling cascades. Its dysregulation is linked to cancer, autoimmune diseases, and neurodegenerative disorders.
MAPK14 antibodies are essential tools for studying its expression, activation, and localization in various biological contexts. They are widely used in techniques such as Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and flow cytometry. Specific antibodies detect either total MAPK14 or its phosphorylated (active) form (e.g., phosphorylated at Thr180/Tyr182). Researchers must validate antibody specificity using knockout controls or siRNA knockdown to avoid cross-reactivity with other p38 isoforms (p38β, p38γ, p38δ). Commercial MAPK14 antibodies are often raised against synthetic peptides corresponding to conserved or unique regions of the human protein, with reactivity tested across species (human, mouse, rat). Proper selection ensures accurate interpretation of MAPK14's role in disease mechanisms and therapeutic targeting.