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
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Stability & Storage
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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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Amyloid Precursor Protein
Entrez Gene IDs:
351 (Human); 11820 (Mouse)
amyloid beta (A4) precursor protein-binding, family B, member 2; amyloid beta A4 precursor protein-binding family B member 2; Amyloid beta precursor protein; Amyloid beta; APP; beta Amyloid; Protease Nexin II
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