Phospho-FGFR1 (Tyr654) antibody detects the activated form of fibroblast growth factor receptor 1 (FGFR1), a transmembrane tyrosine kinase receptor critical for regulating cell proliferation, differentiation, and survival. FGFR1 signaling is initiated upon binding of FGF ligands, leading to receptor dimerization, autophosphorylation of specific tyrosine residues (including Tyr654), and recruitment of downstream adaptor proteins. Phosphorylation at Tyr654. located in the kinase domain, is a key regulatory event that stabilizes the active conformation of the receptor, enhancing catalytic activity and promoting signal transduction through pathways like MAPK/ERK, PI3K/AKT, and PLCγ. Aberrant FGFR1 activation, often linked to mutations or overexpression, is implicated in cancers, developmental disorders, and metabolic diseases. The Phospho-FGFR1 (Tyr654) antibody specifically recognizes this post-translational modification, enabling researchers to study FGFR1 activation status in cellular models, tissues, or experimental therapies targeting FGFR signaling. Its applications include Western blotting, immunohistochemistry, and functional studies to explore FGFR1's role in disease mechanisms or therapeutic responses. Validating phosphorylation at Tyr654 also aids in assessing the efficacy of FGFR inhibitors in preclinical or clinical research.