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QED Bioscience
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Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. Many degenerative diseases are known to be related to the accumulation of misfolded proteins as amyloid fibres. These include the amyloid-beta peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimer's symptomology, the deposition of alpha-synuclein in the Lewy bodies of Parkinson's disease, and accumulation of polyglutamine-containing aggregates in Huntington's disease.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: A11; ABPP; AD; AG; Alzheimer disease amyloid A4 protein homolog; Alzheimer disease amyloid protein; amyloid A4; amyloid beta (A4) precursor protein; amyloid beta A4 protein; Amyloid precursor protein; Amyloid-beta (A4) precursor protein; Amyloid-beta A4 protein; Amyloid-beta precursor protein; Amyloidogenic glycoprotein; APP; APPI; appican; beta-amyloid peptide; beta-amyloid peptide(1-40); beta-amyloid peptide(1-42); beta-amyloid precursor protein; Cerebral vascular amyloid peptide; CVAP; Fibrils; OC; peptidase nexin-II; PN-II; PreA4; protease nexin II; Protease nexin-II; testicular tissue protein Li 2
Gene Aliases: A4; AAA; ABETA; ABPP; AD1; Adap; Ag; APP; APPI; betaApp; CTFgamma; CVAP; E030013M08Rik; PN-II; PN2
UniProt ID: (Human) P05067, (Rat) P08592, (Mouse) P12023
Entrez Gene ID: (Human) 351, (Rat) 54226, (Mouse) 11820
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