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AB187908

HRP Anti-beta Amyloid antibody [DE2B4]

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(1 Publication)

Mouse Monoclonal Amyloid-beta precursor protein antibody - conjugated to HRP. Suitable for ELISA, ICC, IP, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human APP aa 1-50.

View Alternative Names

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

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

DE2B4

Isotype

IgG1

Conjugation

HRP

Excitation/Emission
Carrier free

No

Reacts with

Human

Applications

IP, ICC, ELISA, IHC-P

applications

Immunogen

Synthetic Peptide within Human APP aa 1-50. The exact immunogen used to generate this antibody is proprietary information.

P05067

Specificity

This antibody recognises an epitope within amino acids 1- 16 of amyloid beta A4 peptide and recognises the C-terminus of alpha-secretase cleaved amyloid precursor protein.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS
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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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.
See full target information APP

Publications (1)

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American journal of human genetics 112:59-74 PubMed39701103

2024

Bi-allelic variants in DAP3 result in reduced assembly of the mitoribosomal small subunit with altered apoptosis and a Perrault-syndrome-spectrum phenotype.

Applications

Unspecified application

Species

Unspecified reactive species

Thomas B Smith,Robert Kopajtich,Leigh A M Demain,Alessandro Rea,Huw B Thomas,Manuel Schiff,Christian Beetz,Shelagh Joss,Gerard S Conway,Anju Shukla,Mayuri Yeole,Periyasamy Radhakrishnan,Hatem Azzouz,Amel Ben Chehida,Monique Elmaleh-Bergès,Ruth I C Glasgow,Kyle Thompson,Monika Oláhová,Langping He,Emma M Jenkinson,Amir Jahic,Inna A Belyantseva,Melanie Barzik,Jill E Urquhart,James O'Sullivan,Simon G Williams,Sanjeev S Bhaskar,Samantha Carrera,Alexander J M Blakes,Siddharth Banka,Wyatt W Yue,Jamie M Ellingford,Henry Houlden,Kevin J Munro,Thomas B Friedman,Robert W Taylor,Holger Prokisch,Raymond T O'Keefe,William G Newman
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