Abcam, ab252816, Anti-beta Amyloid antibody [2E9]

Size: 20µg / 100µg / 1mg
Knockout Tested Rat Recombinant Monoclonal Amyloid-beta precursor protein antibody. Suitable for IP, WB, IHC-P and reacts with Human samples. Cited in 1 publication.
Key facts
Host species:Rat,
Clonality:Monoclonal,
Clone number:2E9,
Isotype:IgG2a,
Carrier free:No,
Reacts with:Human,
Applications:IP, WB, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
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
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com

Properties and Storage Information:
Form-Liquid, Purification technique-Ion exchange chromatography, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: 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.
Beta amyloid also known as amyloid beta peptide is a small protein fragment composed of 36-43 amino acids. It typically has a mass of approximately 4 kDa. This peptide primarily emerges from the amyloid precursor protein (APP) through enzymatic actions by beta-secretase and gamma-secretase. Beta amyloid is commonly expressed in the brain particularly within the neuronal tissue. It is known for aggregating into insoluble fibrils leading to the formation of beta amyloid plaques. Researchers often study beta amyloid using tools like amyloid beta IHC and with specific antibodies like moab 2 and 2e9 which help in detecting its presence and distribution.
Biological function summary
In the context of neuronal function beta amyloid is significant yet contentious. It is believed to play a role in synaptic transmission and may partake in homeostatic regulation. However the true physiological role still remains not well defined. Beta amyloid often self-assembles into oligomers and further into beta amyloid plaques which are part of a larger complex that includes various cellular and molecular components. The plaques contribute to neural pathway disruptions and may interfere with synaptic connections.
Pathways
Beta amyloid integrates into important cellular processes such as the amyloidogenic and non-amyloidogenic pathways. The amyloidogenic pathway involves the sequential cleavage of APP by beta and gamma secretases leading to beta amyloid release which can aggregate. In contrast the non-amyloidogenic pathway mediated by alpha-secretase precludes beta amyloid formation. Proteins such as presenilin-1 and nicastrin are closely tied to beta amyloid formation due to their roles in the gamma-secretase complex.
Beta amyloid is primarily associated with Alzheimer's disease where its accumulations form characteristic amyloid plaques observed in patients' brains. These plaques are implicated in neuronal damage and cognitive decline. Beyond Alzheimer's beta amyloid may also connect to cerebral amyloid angiopathy a condition marked by amyloid deposits in the blood vessels of the brain leading to increased risk of hemorrhagic stroke. Recent studies suggest other proteins such as tau link closely with beta amyloid pathology in Alzheimer's promoting neurofibrillary tangles and synaptic degeneration.