No significant cross-reactivity to beta-Amyloid 42 has been observed. Previous lots of this antibody recognized the sequence of beta-Amyloid [1-40] in the region from amino acids 15-30. No blocking activity was observed with beta-Amyloid [1-12] whereas the peptides beta-Amyloid [14-35], beta-Amyloid [15-28], beta-Amyloid [17-30] and Beta-Amyloid [1-40] were all able to block antibody activity.
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; Abeta40; Abeta42; ABPP; AD1; AICD-50; AICD-57; AICD-59; Alpha-CTF; Alpha-secretase C-terminal fragment; Alzheimer disease amyloid protein; amyloid beta (A4) precursor protein; Amyloid beta A4 protein; Amyloid intracellular domain 50; Amyloid intracellular domain 57; Amyloid intracellular domain 59; Amyloid precursor protein; Amyloid-beta A4 protein; Amyloid-beta precursor protein; Amyloid-beta protein 40; Amyloid-beta protein 42; Amyloidogenic glycoprotein AG; APP; APPI; beta-amyloid peptide; beta-amyloid peptide(1-40); beta-amyloid peptide(1-42); beta-amyloid precursor protein; Beta-APP40; Beta-APP42; Beta-CTF; Beta-secretase C-terminal fragment; C31; C80; C83; C99; Cerebral vascular amyloid peptide; CTFgamma; CVAP; Gamma-CTF(50); Gamma-CTF(57); Gamma-CTF(59); Gamma-secretase C-terminal fragment 50; Gamma-secretase C-terminal fragment 57; Gamma-secretase C-terminal fragment 59; N-APP; P3(40); P3(42); Peptidase nexin-II; PN-II; PN2; PreA4; Protease nexin-II; S-APP-alpha; S-APP-beta; Soluble APP-alpha; Soluble APP-beta; testicular tissue protein Li 2
Gene Aliases: A4; AAA; ABETA; ABPP; AD1; APP; APPI; CTFgamma; CVAP; PN-II; PN2
UniProt ID: (Human) P05067
Entrez Gene ID: (Human) 351
Molecular Function: signaling molecule