0.2ml of distilled water will yield a concentration of 500µg/ml.
Buffer
Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4
Preservative
Thimerosal (Merthiolate), Sodium azide
Storage
-20 °C
Duce, Tsatsanis, Cater, James, Robb, Wikhe, Leong, Perez, Johanssen, Greenough, Cho, Galatis, Moir, Masters, McLean, Tanzi, Cappai, Barnham, Ciccotosto, Rogers, Bush: "Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease." in: Cell, Vol. 142, Issue 6, pp. 857-67, (2010) (PubMed).
Priller, Bauer, Mitteregger, Krebs, Kretzschmar, Herms: "Synapse formation and function is modulated by the amyloid precursor protein." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 26, Issue 27, pp. 7212-21, (2006) (PubMed).
Wang, Ha: "The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain." in: Molecular cell, Vol. 15, Issue 3, pp. 343-53, (2004) (PubMed).
Turner, OConnor, Tate, Abraham: "Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory." in: Progress in neurobiology, Vol. 70, Issue 1, pp. 1-32, (2003) (PubMed).
Amyloid precursor protein (APP) is an integral membrane protein expressed in many tissues and 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 beta amyloid (A), 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 posttranslational proteolytic processing by alpha-, beta-, and gamma-secretases. Alpha-secretase generates soluble amyloid protein, while beta- and gamma-secretases generate APP components with amyloidogenic features. These 2 processing pathways are mutually exclusive.