Anti-Aβ-42 Antibody, oligomeric (VIA)

Amyloid beta A4 protein (UniProt P05067; also known as ABPP, Alzheimer disease amyloid protein, Amyloid precursor protein, APP, APPI, Cerebral vascular amyloid peptide, CVAP, PN-II, PreA4, Protease nexin-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID 351) in human. Amyloid precursor protein (APP) is initially produced with a signal peptide sequence (a.a. 1-17), the removal of which yields the mature protein with a large extracellular portion (a.a. 18-699), followed by a transmembrane segment (a.a. 700-723) and a cytoplasmic (a.a. 724-770) tail. APP can be further processed by the α-, β-, and γ-secretases in two alternative processing pathways. In the non-amyloidogenic pathway, APP is first cleaved by the plasma membrane-localized α-secretase to generate an N-terminal extracellular sAPPα fragment (a.a. 18-687) and a membrane-bound C-terminal fragment C83 (CTFα), which can be further cleaved by γ-secretase to produce a non-toxic small peptide p3 and a cytoplasmic APP intracellular domain (AICD). In the amyloidogenic pathway, APP undergoes β-cleavage in BACE-1 (β-site APP-cleaving enzyme)-enriched endosomes to generate an N-terminal extracellular sAPPβ fragment (a.a. 18-671) and a membrane-bound C-terminal fragment C99 (CTFβ). Subsequent cleavage of C99 by γ-secretase releases the amyloid β peptides, Aβ1-42 (672-713) & Aβ1-40 (672-711), and AICD. Aβ accumulation in the cortical and hippocampal regions of the brain is a major pathological feature of Alzheimer′s disease (AD). Growing evidences implicate soluble oligomers as the more toxic species and the extent of oligomer formation and assembly correlates better with disease progression and cognitive dysfunction. These Aβ oligomers are able to induce other aggregation-prone proteins, including α-synuclein (α-syn), prion protein (PrP), and TDP-43, to assume oligomeric conformations. These proteins can then seed tau aggregation, resulting in neurodegeneration.

Anti-Aβ-42, oligomeric (VIA), Cat. No. ABN1665, is a highly specific rabbit polyclonal antibody that targets Amyloid beta 42 oligomers and has been tested in Dot Blot, Neutralizing, and Western Blotting.

Dot Blot Analysis: A representative lot detected recombinant Aβ-42, but not Aβ-40, oligomers (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Neutralizing Analysis: A representative lot neutralized Aβ-42 toxicity to cultured SH-SY5Y cells (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Western Blotting Analysis: A representative lot detected oligomeric Aβ-42, but not monomeric Aβ-42, monomeric or oligomeric A -40 (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Note: Both purified antibody (Cat. No. ABN1665) and unpurified antiserum (Cat. No. ABN1650) are suitable for Dot blot, immunofluorescence, immunohistochemistry, and Western blotting applications. However, we recommend using only the purified antibody for neutralization studies.

Evaluated by Dot Bot analysis of A proteins.

Dot Blot Analysis: 6.67 µg/mL of this antibody detected recombinant Aβ-42, but not Aβ-40, oligomer.

Variable depending on the sizes of the Aβ-42 oligmers.

Format: Purified

Purified rabbit polyclonal antibody in PBS without preservatives.

Concentration: Please refer to lot specific datasheet.