Alzheimer's disease, the most common cause of dementia in the elderly, exists in both familial and sporadic forms. Genetic studies have identified three genes; beta-amyloid precursor protein (APP), Presenilin 1 and Presenilin 2 which, when mutated, can cause familial forms of Alzheimer's disease. APP and APP-like proteins are transmembrane glycoproteins with a similar modular domain structure.
APP-228 has been raised to the extracellular portion of APP between the Kunitz protease inhibitor domain and the beta amyloid region. This region shows the least homology with the APP-like proteins. APP-228 and does not cross-react with APP-like proteins. APP reacts with large pyramidal cells as well as smaller neurons, astrocytes and microglia. APP 228 reacts with late-stage neurofibrillary tangle-bearing neurons, neuritic processes surrounding senile plaques and neuropil threads in gray matter of Alzheimer's disease brain. Unmasking in 1mM EDTA (pH8.0) in a pressure cooker may be required for up to 5 minutes in order for this APP-228 to work optimally.
A-Beta proteolysis by TTR is KPI-sensitive.
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