APP Antibody Summary
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Amyloid Precursor Protein by Western Blot. Western blot of rat hippocampal lysate showing specific immunolabeling of the approximately 120 kDa APP protein.
Preparation and Storage
APP, or amyloid precursor protein, is a heparin-binding, 120 kDa type I transmembrane glycoprotein that belongs to the APP family of proteins. It is highly conserved across species, showing at least 97% amino acid (aa) identity between human, monkey, rat, mouse and dog. There are almost a dozen potential alternate splice forms for human APP. The neuronal (or standard) form is referred to as APP695. The 695 includes a 17 aa signal peptide and 678 aa mature region. This form contains a multidomain, 610 aa extracellular region (ECD), a 24 aa transmembrane segment (aa 625 - 648), and a short 47 aa cytoplasmic tail. Longer forms of APP, APP751 and APP770 are characterized by the presence of a 57 aa KPI, or Kunitz protease inhibitor domain in the ECD. This has protease-inhibition activity and may be involved in memory. Membrane-bound APP695 undergoes two-stage proteolytic processing. There is an initial cleavage by either an alpha - or beta -secretase, followed by cleavage by a gamma -secretase. The choice of alpha - or beta -secretase may depend upon the APP glycosylation pattern or phosphorylation events. alpha -Secretase cleavage occurs between K612 and L613. This releases a soluble APPa piece that shows proliferative activity with EGF family members on neural progenitor cells and keratinocytes. beta -secretase cleaves between M596 and D597. When followed by gamma -secretase cleavage following position V637, or A639, small 40 or 42 aa A beta peptides are released that may contribute to the formation of amyloid plaques.
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- Kang, J. et al. (1987) Nature 325:733.
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