Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor and has been implicated as a regulator of synapse formation, neural plasticity, antimicrobial activity, and iron export. It is coded for by the gene APP and regulated by substrate presentation. APP is best known as the precursor molecule whose proteolysis generates amyloid beta (Aβ), a polypeptide containing 37 to 49 amino acid residues, whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients.
Background References
1. Ono K et al. Aggregation and structure of amyloid beta-protein. Neurochem Int. 2021 Dec
2. Yagi-Utsumi M et al. Conformational Variability of Amyloid-beta and the Morphological Diversity of Its Aggregates. Molecules. 2022 Jul
Dot blot analysis of beta Amyloid on different proteins with Rabbit anti-beta Amyloid antibody (HA722961) at 1/2,000 dilution. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution for 1 hour at room temperature.
Lane 1: Human Aβ37 full length peptide Lane 2: Human Aβ38 full length peptide Lane 3: Human Aβ39 full length peptide Lane 4: Human Aβ40 full length peptide Lane 5: Human Aβ41 full length peptide Lane 6: Human Aβ42 full length peptide Lane 7: Human Aβ43 full length peptide Lane 8: Mouse Aβ42 full length peptide
Proteins loading: 100ng, 50ng;
Blocking and dilution buffer: 5% NFDM/TBST;
Exposure time: 3 minutes; ECL: K1801.
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