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The Human Aggregated Amyloid Beta ELISA quantitates Hu aggregated Aβ in human tissue homogenates, ventricular fluid, CSF, tissue culture supernatant, and buffered solution. The assay will exclusively recognize both natural and recombinant Hu aggregated Aβ.
Principle of the method
The Human aggregated Aβ solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen.
Rigorous validation
Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Gene aliases : A4, AAA, ABETA, ABPP, AD1, APP, APPI, CTFgamma, CVAP, PN-II, PN2
Gene ID : (Human) 351
Gene symbol : APP
Protein Aliases : ABPP, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Alzheimer disease, CTF gamma, CTF-alpha, OTTHUMP00000096096, Pan-Abeta, PreA4 751, Amyloid b, Amyloid beta, Amyloid β, Amyloid, amyloid beta (A4) precursor protein, Amyloid precursor protein, Amyloid-beta (A4) precursor protein, Amyloid-beta A4 protein, Amyloid-beta precursor protein, APP, APPI, beta-amyloid peptide, beta-amyloid peptide(1-40), beta-amyloid peptide(1-42), beta-amyloid precursor protein, Cerebral vascular amyloid peptide, CVAP, peptidase nexin-II, PN-II, PreA4, Protease nexin-II, testicular tissue protein Li 2
UniProt ID (Human) P05067
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