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EK000143-EK0658: Human APP ELISA Kit
Range 312pg/ml-20,000pg/ml
Sensitivity < 10pg/ml
Specificity: no detectable cross-reactivity with any other cytokine.
Application: for quantitative detection of human APP in sera, plasma or tissue lysates
Expiration: four months at 4°C and eight months at -20°C.
Background
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
Principle
The human APP ELISA Kit was based on standard sandwich enzyme-linked immune-sorbent assay technology. Human APP specific-specific polyclonal antibodies were precoated onto 96-well plates. The human specific detection polyclonal antibodies were biotinylated. The test samples and biotinylated detection antibodies were added to the wells subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with PBS or TBS buffer. HRP substrate TMB was used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the human APP amount of sample captured in plate.
Reference
1.PDB 1RW6; Wang Y, Ha Y (August 2004). "The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain". Mol. Cell 15 (3): 343?3.
2.Priller C, Bauer T, Mitteregger G, Krebs B, Kretzschmar HA, Herms J (July 2006). "Synapse formation and function is modulated by the amyloid precursor protein". J. Neurosci. 26 (27): 7212?1.
3.Turner PR, O'Connor K, Tate WP, Abraham WC (May 2003). "Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory". Prog. Neurobiol. 70 (1): 1?2.
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