PSEN1 (Presenilin 1) is a critical component of the γ-secretase complex, which plays a key role in the proteolytic processing of amyloid precursor protein (APP) to generate amyloid-β (Aβ) peptides, including the pathogenic Aβ42 species implicated in Alzheimer’s disease (AD). Mutations in the PSEN1 gene are the most common cause of early-onset familial AD, leading to altered γ-secretase activity and increased Aβ42 production. PSEN1 antibodies are essential tools for studying the expression, localization, and function of PSEN1 in both physiological and pathological contexts.
These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to detect PSEN1 in cell lines, animal models, and human tissues. They help investigate PSEN1’s role in Aβ generation, synaptic function, and cellular signaling pathways. However, studies using PSEN1 antibodies occasionally report discrepancies, possibly due to variations in antibody specificity, isoform detection (e.g., full-length vs. cleaved forms), or tissue-processing methods. Some antibodies target specific regions, such as the N-terminal or C-terminal domains, influencing their applicability in different experimental setups.
Research with PSEN1 antibodies has also highlighted its involvement beyond AD, including roles in calcium homeostasis, autophagy, and cancer. However, challenges remain in distinguishing PSEN1 from its homolog PSEN2 and other γ-secretase components. Validating antibody specificity using knockout controls remains crucial. Overall, PSEN1 antibodies continue to advance our understanding of AD mechanisms and potential therapeutic targets.