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 alpha-, beta-, and gamma-secretases in two alternative processing pathways. In the non-amyloidogenic pathway, APP is first cleaved by the plasma membrane-localized alpha-secretase to generate an N-terminal extracellular sAPPalpha fragment (a.a. 18-687) and a membrane-bound C-terminal fragment C83 (CTFalpha), which can be further cleaved by gamma-secretase to produce a non-toxic small peptide p3 and a cytoplasmic APP intracellular domain (AICD). In the amyloidogenic pathway, APP undergoes beta-cleavage in BACE-1 (beta-site APP-cleaving enzyme)-enriched endosomes to generate an N-terminal extracellular sAPPbeta fragment (a.a. 18-671) and a membrane-bound C-terminal fragment C99 (CTFbeta). Subsequent cleavage of C99 by gamma-secretase releases the amyloid beta peptides, Abeta1-42 (672-713) & Abeta1-40 (672-711), and AICD. Abeta 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 Abeta oligomers are able to induce other aggregation-prone proteins, including alpha-synuclein (alpha-syn), prion protein (PrP), and TDP-43, to assume oligomeric conformations. These proteins can then seed tau aggregation, resulting in neurodegeneration.
Synonyms: Abeta-42 oligomer, Abeta-42 oligomer, Oligomeric Abeta-42, Oligomeric Abeta-42
Application: Dot Blot Analysis: A representative lot detected recombinant Abeta-42, but not Abeta-40, oligomers (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).Neutralizing Analysis: A representative lot neutralized Abeta-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 Abeta-42, but not monomeric Abeta-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.
Other Notes: Concentration: Please refer to lot specific datasheet.