MilliporeSigma™ phospho-Amyloid beta (Ser26), Mouse, Unlabeled, Clone: 5H11C10,

Description

• 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) and 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)
• Aβ serine phosphorylation is shown to promote Aβ aggregation into oligomeric and fibrillar assemblies and to prevent Aβ proteolytic clearance by certain proteases.