Amyloid beta (Aß) plaques exhibit diverse conformations resulting in structural variants with distinct pathologies.
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Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts. Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
A4, AD1, APP, Amyloid-beta precursor protein, ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta (A4) precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II, CVAP, PN-II
Amyloid beta (Aß) plaques exhibit diverse conformations resulting in structural variants with distinct pathologies.
Amyloid 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.
The antibodies in this panel have been validated using both Dot blot and immunohistochemistry staining on paraffin-embedded human and mouse model samples.
Explore our range of antibody sample panels designed to provide you with a variety of trial-size antibodies in a convenient and cost-effective format.
Carrier-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.
Beta 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.
Beta 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.
Beta 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.
Beta 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.
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IHC image of beta Amyloid staining in Human Brain Alzheimer formalin fixed paraffin embedded tissue section*, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with Anti-beta Amyloid antibody [mOC23] - Conformation-Specific ab205340, 0.1μg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.
For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.
*Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre
IHC image of Amyloid Fibrillin staining in Human Brain Alzheimer formalin fixed paraffin embedded tissue section*, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with Anti-Amyloid Fibril antibody [mOC78] - Conformation-Specific ab205341, 1μg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.
For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.
*Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre
Immunohistochemical staining of human brain tissue from a patient with a diagnosis of Alzheimers disease, male, 81 years, 5 hour post mortem index, tangle stage 5, plaque stage B, mini mental status exam score 12. Sections were cut using a vibratome. No antigen retrieval was performed. Free floating sections were stained using using Anti-vascular Amyloid 1-42 antibody [mOC31] - Conformation-Specific ab201059 at a dilution of 50 ng/mL. The secondary antibody used was a biotinylated goat anti-rabbit at a dilution of 1/225, which was blocked with normal goat serum. The sample was visualized using ABC solution (1 hour incubation) followed by 1-4 minutes of DAB. The sample was mounted and allowed to dry overnight, followed by dehydration in increasingly concentrated ethanol solutions.
IHC image of Amyloid Fibril staining in Human Brain Alzheimer formalin fixed paraffin embedded tissue section*, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific ab205339, 0.1μg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.
For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.
*Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre
IHC image Amyloid Fibrillin staining in Human Brain Alzheimer formalin fixed paraffin embedded tissue section*, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with Anti-Amyloid Fibril antibody [mOC116] - Conformation-Specific ab205342, 0.1μg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.
For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.
*Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre
Immunohistochemical staining of human brain tissue from a patient with a diagnosis of Alzheimers disease, male, 81 years, 5 hour post mortem index, tangle stage 5, plaque stage B, mini mental status exam score 12. Sections were cut using a vibratome. No antigen retrieval was performed. Free floating sections were stained using Anti-Amyloid Fibril antibody [mOC87] - Conformation-Specific ab201062 at a dilution of 50 ng/mL. The secondary antibody used was a biotinylated goat anti-rabbit at a dilution of 1/225, which was blocked with normal goat serum. The sample was visualized using ABC solution (1 hour incubation) followed by 1-4 minutes of DAB. The sample was mounted and allowed to dry overnight, followed by dehydration in increasingly concentrated ethanol solutions.
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