Abcam, ab126468, Anti-Amyloid Fibril antibody

Size: 100µL
Rabbit Polyclonal Amyloid-beta precursor protein antibody. Suitable for IHC, IP, Dot, ICC/IF, WB, ELISA and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Synthetic Peptide within Human APP.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:IP, Dot, ICC/IF, WB, ELISA, IHCSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human APP. The exact immunogen used to generate this antibody is proprietary information.P05067,
Specificity:Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. Expected to detect in Mouse and Rat based on species homology.

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

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Amyloid fibrils alternatively named fibrillar amyloid are insoluble fibrous protein aggregates resulting from the abnormal folding of proteins. They compose primarily of beta-sheet structures which promote stability and rigidity. Amyloid fibrils are frequently associated with proteins like Aβ and tau known for their high molecular mass. Researchers observe these structures in various tissues where they exhibit significant resilience to both chemical and enzymatic degradation.
Biological function summary
The misfolding and accumulation of proteins into amyloid fibrils prove disruptive within cells. These aggregates often form as part of complex protein assemblies and interfere with normal cellular functions. This disruption further leads to cellular dysfunction and death. While commonly observed in neuronal cells where they are linked to neurodegenerative conditions amyloid fibrils can also appear in other tissues and organs suggesting multi-systemic implications.
Pathways
Scientists recognize amyloid fibrils for their involvement in the amyloidogenic pathways. These pathways often lead to the generation and accumulation of misfolded proteins. The amyloid precursor protein (APP) and presenilins play important roles in pathway processes associated with amyloid fibrils. In addition the fibrillar structures can influence calcium dysregulation and oxidative stress contributing to altered cellular homeostasis.
Amyloid fibrils are strongly associated with Alzheimer's disease and systemic amyloidosis. Within Alzheimer's disease amyloid fibrils formed by Aβ peptides contribute to plaque formation a hallmark of the condition. Furthermore interactions with tau protein exacerbate neurofibrillary tangles compounding neurodegenerative effects. In systemic amyloidosis different precursor proteins undergo fibrillogenesis resulting in widespread organ dysfunction and highlighting the pathogenic potential of amyloid fibrils beyond neurological tissues.