Abcam, ab126892, Anti-Amyloid Oligomers antibody

Size: 100µL
Rabbit Polyclonal Amyloid-beta precursor protein antibody. Suitable for IP, ELISA, Dot, WB, IHC-P, IHC-Fr and reacts with Mouse, Rat, Human samples. Cited in 11 publications.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human, Rat,
Applications:WB, IHC-P, ELISA, IHC-Fr, IP, DotSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Specificity:Recognizes all types of amyloid oligomers. Appears to recognize a peptide backbone epitope that is common to amyloid oligomers, but is not found in native proteins, amyloidogenic monomer or mature amyloid fibrils.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-Preservative: 0.09% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Storage information-Stable for 12 months at -20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Amyloid oligomers also known as beta amyloid oligomers or oligomeric amyloid beta are protein aggregates that play a significant role in various neurodegenerative processes. These oligomeric formations consist of small soluble assemblies of amyloid beta typically ranging from dimers to dodecamers and often measure approximately 4 to 10 kDa in mass. Amyloid oligomers are usually expressed in the brain particularly in regions associated with memory and cognition such as the hippocampus and cortex.
Biological function summary
Amyloid oligomers interfere with synaptic function leading to a cascade of neuronal dysfunction and cell death. Unlike their fibrillar counterparts these oligomers are not part of larger insoluble plaques and they exhibit more harmful properties to neurons. They may form part of a complex with other proteins such as tau which can exacerbate their toxic effects. Amyloid beta oligomers disrupt cellular function primarily through interaction with synaptic receptors influencing calcium homeostasis and promoting oxidative stress.
Pathways
Amyloid oligomers are integral components of amyloidogenic pathways that influence neuronal communication and survival. The amyloid beta pathway involves the cleavage of amyloid precursor protein (APP) by enzymes such as beta-secretase and gamma-secretase leading to the formation of these toxic oligomers. Related proteins include APP the enzymes mentioned and tau which can further disrupt microtubule stability when amyloid oligomers are present. The accumulation of amyloid oligomers is interlinked with pathways that regulate synaptic plasticity and inflammatory responses.
Amyloid oligomers have strong associations with Alzheimer's disease and mild cognitive impairment. These oligomers are directly linked to synaptic loss and dysfunction which contributes heavily to the progression of Alzheimer's disease. Connections with proteins such as tau and APP highlight their role in forming toxic complexes that lead to neurofibrillary tangles and plaque buildup. Additionally amyloid oligomers may relate to other neurodegenerative disorders where protein aggregation and cognitive deficits are apparent.