This antibody can be used to specifically detect the beta-amyloid precursor protein. The antibody reacts with full-length (APP695, 751, 770) and N-terminal truncated forms of beta-APP. The antibody can also be used to detect the C-terminal membrane-anchored fragment of beta-APP that remains after alpha- or beta-secretase cleavage. This antibody does not detect the beta-APP product N-terminal to the gamma-secretase cleavage site.
Reactivity with this antibody has been confirmed for human, mouse, pig, and rat. Based on sequence homology, reactivity with other species, including monkey, guinea pig, and chicken beta-APP, is highly likely. The CT695 antibody has demonstrated superiority in detecting axonal damage.
This antibody has been tested in western blotting with FRTL-5 (rat thyroid) cells and rat brain lysates. For immunohistochemistry FFPE tissues will require epitope retrieval pretreatment.
Amyloid beta peptide (Abeta/Beta-amyloid) is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimer's disease. Abeta peptide is 40-43 amino acids long and generated from the beta-amyloid precursor protein (beta APP) in a two-step process. The first step involves cleavage of the extracellular, amino-terminal domain of beta APP. Protein cleavage is performed by an aspartyl protease, beta-secretase (BACE) which is synthesized as a propeptide and must be modified to the mature and active form by the prohormone convertase, furin. Beta APP cleavage by the mature form of BACE results in the cellular secretion of a segment of beta APP, and a membrane-bound remnant. The remnant protein is processed by another protease, gamma-secretase. Gamma-secretase cleaves an intra-membrane site in the carboxyl-terminal domain of beta APP, thus generating the amyloid beta peptide. Gamma-secretase is believed to be a multi-subunit complex containing presenilin-1 and 2 as central components. The transmembrane glycoprotein, nicastrin, is associated with presinilins and has been found to bind to the carboxyl-terminus of beta APP and helps to modulate the production of the amyloid beta peptide. Abeta is an extracellular filamentous protein component of amyloid cores, neuritic plaques and is also found as a deposit in neurofibrillary tangles. Alzheimer's disease, the most common cause of senile dementia, is characterized by abnormal filamentous protein deposits in the brain. Beta amyloid deposits are also detected in Lewy body dementia, Down's syndrome, amyloidosis (Dutch type), cerebroarterial amyloidosis (cerebral amyloid angiopathy) and in the Guam Parkinson-Dementia complex.
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Protein Aliases: AAA; ABETA; ABPP; AD1; AG; Alzheimer disease amyloid A4 protein homolog; Alzheimer disease amyloid protein; amyloid A4; amyloid beta (A4) precursor protein; amyloid beta (A4) precursor protein (peptidase nexin-II, Alzheimer disease); Amyloid beta A4 protein; Amyloid precursor protein; Amyloid-beta A4 protein; Amyloid-beta precursor protein; Amyloidogenic glycoprotein; Amyloidogenic glycoprotein AG; APP; APPI; appican; beta-amyloid peptide; beta-amyloid peptide(1-40); beta-amyloid peptide(1-42); beta-amyloid precursor protein; Cerebral vascular amyloid peptide; CTFgamma; CVAP; Peptidase nexin-II; PN-II; PN2; 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
Molecular Function: signaling molecule