Description
Amyloid precursor protein (APP) is an integral membrane protein expressed in many tissues and is concentrated in the synapses of neurons. Its primary function is not known, though it has been implicated as a regulator of synapse formation, neural plasticity and iron export. APP is best known and most commonly studied as the precursor molecule whose proteolysis generates β-amyloid (Aβ), a 39- to 42-amino acid peptide whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients. APP undergoes post-translational proteolytic processing by α-, β-, and γ-secretases. α-secretase generates soluble amyloid protein, while β- and γ-secretases generate APP components with amyloidogenic features. These 2 processing pathways are mutually exclusive. ScienCell's human APP ELISA kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. Human APP-specific polyclonal antibodies are pre-coated onto 8 x 12 divisible strips. The human-specific detection polyclonal antibodies are biotinylated. The test samples and biotinylated detection antibodies are subsequently added to the wells and then washed with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changes to yellow after adding acidic stop solution. The intensity of yellow is proportional to the amount of human APP in the sample that is captured on the strips