{"product_id":"abcam-ab218719","title":"Abcam, ab218719, Conformation-Specific Amyloid beta Antibody Sampler Panel","description":"\u003cp\u003eSize: 1Pack\u003cbr\u003e\nAmyloid beta (Aß) plaques exhibit diverse conformations resulting in structural variants with distinct pathologies.\u003cbr\u003e\nKey facts\u003cbr\u003e\nTarget:APPSee target data\u003c\/p\u003e\n\n\u003cp\u003eProduct details:\u003cbr\u003e\nAmyloid beta (Aß) plaques exhibit diverse conformations resulting in structural variants with distinct pathologies. Conformation-specific Aß antibody sampler panel (ab218719), includes recombinant rabbit monoclonal antibodies against fibrils of Aß 1-42 that can distinguish conformation variation in amyloid structures. It also contains a goat anti-rabbit (HRP) secondary antibody.\u003cbr\u003e\nThe antibodies in this panel have been validated using both Dot blot and immunohistochemistry staining on paraffin-embedded human and mouse model samples.\u003cbr\u003e\nExplore our range of antibody sample panels designed to provide you with a variety of trial-size antibodies in a convenient and cost-effective format.\u003cbr\u003e\nCarrier-free formulations of our recombinant antibodies are also available for easy conjugation to labels of your choice and for multiplex applications. Use our intuitive search and select carrier-free or your label of choice. For bespoke conjugations or large volumes email bespoke@abcam.com.\u003c\/p\u003e\n\n\u003cp\u003eProperties and Storage Information:\u003cbr\u003e\nShipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°C\u003c\/p\u003e\n\n\u003cp\u003eSupplementary Information:\u003cbr\u003e\nThis supplementary information is collated from multiple sources and compiled automatically.\u003cbr\u003e\nBeta Amyloid (β-amyloid) also known as Amyloid-beta (Aβ) is a peptide with a mass of approximately 4 kDa. It originates from the amyloid precursor protein (APP) through enzymatic cleavage. Common fragments include Aβ1-40 and Aβ1-42 which differ in their amyloid fibril formation tendencies. Aβ is expressed in various tissues but predominantly in the brain where it accumulates extracellularly. The peptide can aggregate to form plaques a process that disrupts neuronal function.\u003cbr\u003e\nBiological function summary\u003cbr\u003e\nBeta amyloid aggregates into amyloid fibrils impacting cellular processes by disrupting membrane integrity and impairing neuronal communication. Aβ1-42 possesses greater aggregation propensity than Aβ1-40 leading to its frequent association with neurodegenerative diseases. These peptides are not standalone but interact as part of larger amyloid complexes. Aggregation involves beta-sheet-rich structures often referred to as beta conformations that disrupt cell membranes and synaptic function.\u003cbr\u003e\nPathways\u003cbr\u003e\nBeta amyloid integrates into key pathways related to neuronal development and maintenance. The amyloidogenic pathway involves proteins like beta-secretase (BACE1) and gamma-secretase responsible for its production from APP. The non-amyloidogenic pathway involving alpha-secretase bypasses Aβ formation. Both pathways are integral to cellular homeostasis and synaptic health where imbalances can influence pathogenesis.\u003cbr\u003e\nBeta amyloid strongly associates with Alzheimer's disease (AD) and cerebral amyloid angiopathy (CAA). In AD its accumulation forms senile plaques contributing to neuroinflammation and neuronal loss. Familial Alzheimer's is connected to mutations in APP and related presenilin proteins that favor Aβ42 production. In CAA beta amyloid deposits in cerebral blood vessels impair vascular function. Understanding these interactions clarifies how beta amyloid contributes to neurodegeneration.\u003c\/p\u003e","brand":"Abcam","offers":[{"title":"Default Title","offer_id":46847585091753,"sku":"ab218719","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/ar\/products\/abcam-ab218719","provider":"Iright","version":"1.0","type":"link"}