Abcam, ab205339, Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific

Size: 20µL / 100µL / 1mL
Rabbit Recombinant Monoclonal Amyloid-beta precursor protein antibody. Suitable for Dot, IHC-P and reacts with Synthetic peptide, Human samples. Cited in 6 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:mOC22,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:Dot, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

Product details:
This antibody was developed as part of a collaboration between Abcam and Professor Charles Glabe, UC Irvine.
ab205339 (mOC22) recognizes a conformation-dependent and aggregation-specific generic fibril epitope that is independent of the peptide sequence. Although it maps to a linear segment of Aß (residues 3-7, EFRHD) it also reacts with alpha synuclein and islet amyloid polypeptide (IAPP) fibrils but not monomers (Hatami et al 2014, PMID: 25281743). mOC22 preferentially stains the central core of cored plaques. mOC22 also stains misfolded or aggregated intraneuronal amyloid deposits (Hatami et al 2014, PMID: 25281743). Immunoreactivity on western blots is enhanced by boiling the membrane.
For further information on the immunogen, please refer to Hatami et al 2014, PMID: 25281743 and Kayed et al. 2007, PMID: 17897471.
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb
patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

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.