Mitogen-activated protein kinase 13 (MAPK13), also known as p38δ, belongs to the p38 MAPK family, which regulates cellular responses to stress, inflammation, and apoptosis. It is activated by dual phosphorylation on Thr-Gly-Tyr motifs in response to cytokines, environmental stressors, or growth factors. MAPK13 interacts with downstream substrates to modulate transcription factors, cytoskeletal dynamics, and signaling cascades. Antibodies targeting MAPK13 are critical tools for studying its expression, activation, and localization in various biological contexts. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to investigate MAPK13's role in diseases such as cancer, neurodegenerative disorders, and autoimmune conditions. Specific MAPK13 antibodies can distinguish between phosphorylated (active) and non-phosphorylated forms, enabling research into pathway activation under experimental or pathological conditions. Validation of antibody specificity often involves knockout cell lines or peptide competition assays. Commercial MAPK13 antibodies are typically raised against unique epitopes within the kinase domain or C-terminal region. Research has linked MAPK13 to tumor progression, immune regulation, and tissue fibrosis, highlighting its potential as a therapeutic target. Reliable antibodies are essential for elucidating its complex roles in cellular signaling and disease mechanisms.