The Phospho-Amyloid Precursor Protein (APP) (Thr743) antibody is a specialized tool used to detect APP phosphorylated at threonine residue 743. a post-translational modification implicated in Alzheimer’s disease (AD) research. APP is a transmembrane protein cleaved by secretases to generate amyloid-beta (Aβ) peptides, which aggregate into plaques—a hallmark of AD. Phosphorylation at Thr743. located near the Aβ domain within the cytoplasmic region, is thought to regulate APP processing and trafficking, influencing Aβ production. Studies suggest this modification may enhance APP interaction with adaptor proteins, altering its cleavage by γ-secretase or promoting lysosomal degradation. The antibody is widely used in Western blotting, immunohistochemistry, and immunofluorescence to investigate APP phosphorylation dynamics in cellular models, transgenic animals, or human brain tissues. Its development has helped elucidate mechanisms linking APP post-translational modifications to AD pathogenesis, including Aβ accumulation, synaptic dysfunction, and neurodegeneration. Researchers also utilize it to explore kinase/phosphatase pathways (e.g., cyclin-dependent kinases) modulating APP metabolism. However, variability in phosphorylation states across experimental conditions or disease stages necessitates careful validation of antibody specificity to avoid cross-reactivity with non-phosphorylated APP or unrelated epitopes. Overall, this antibody remains critical for studying APP biology and its role in neurodegenerative disorders.