γ secretase are proteases that cleave substrates such as the amyloid precursor protein (APP) and the Notch proteins. Abnormal proteolysis of APP is involved in the pathogenesis of Alzheimer's Disease (AD) and overactive Notch signaling plays an oncogenic role in a variety of cancers. γ Secretase have emerged as promising targets for drug development in the treatment of AD and cancer.
Fluofarma’s proprietary γ secretase biosensor is a chimeric construct based on a GFP-like reporter linked to C99 protein (β amyloid precursor) specifically cleaved by γ secretase. Our specific biosensor allows the assessment of γ secretase activity as it induces relocation of the fluorescence signal from the inner plasma membrane into the cytoplasm.
When γ secretase is not active, the fluorescent biosensor is located to the inner plasma membranes and its fluorescence remains in the cell after plasma membrane permeabilization. In contrast, when γ secretase is active, the biosensor is cleaved; the GFP-like protein relocates to the cytoplasm and the fluorescence is lost after the permeabilization of the plasma membrane. The number of fluorescent cells in a given condition provides a quantitative measure of γ secretase activity.