Cell experiment:

SH-SY5Y cells are treated with biotinylated Amyloid β-Peptide (1-42) human peptide 1 μM. Cells are fixed and permeabilized with 3.3% formaldehyde containing 0.5% Triton X-100 followed by 125 mM glycine in PBS containing magnesium and calcium. Cells are blocked with 5% fetal bovine calf serum followed by the primary antibody. Biotin-Amyloid β-Peptide (1-42) human peptide is detected with the monoclonal antibody AB or alternatively with Avidin Fluor488. Nuclei are stained with DAPI. Images are obtained using an LSM 510 meta confocal microscope[2].

Amyloid β-Peptide (1-42) human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

Amyloid β-Peptide (1-42) human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease. Application of Amyloid β-Peptide (1-42) human (1 to 10 μM) in the bathing solution does not change delayed rectifier K+-current and leakage current, but enhances inactivation of Са2+-current and blocks Са2+-dependent К+-current[1]. At 2.5 μM concentration, Amyloid β-Peptide (1-42) human reduces viability of SH-SY5Y cells to 65%. Results show that Amyloid β-Peptide (1-42) human localizes in both the cytoplasm and nucleus of SH-SY5Y cells after 30 min of incubation and after 8 h. In the latter, large accumulations of Amyloid β-Peptide (1-42) human are seen in the cytoplasm and in the nucleus. Increased APP mRNA levels are also detected upon Amyloid β-Peptide (1-42) human treatment[2].

References:
[1]. Solntseva EI, et al. Impact of amyloid-β peptide (1-42) on voltage-gated ion currents in molluscan neurons. Bull Exp Biol Med. 2011 Oct;151(6):671-4.
[2]. Barucker C, et al. Nuclear translocation uncovers the amyloid peptide Aβ42 as a regulator of gene transcription. J Biol Chem. 2014 Jul 18;289(29):20182-91.