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Rabbit Recombinant Monoclonal Amyloid-beta precursor protein antibody. Suitable for Dot, IHC-P and reacts with Synthetic peptide, Human samples. Cited in 4 publications.


Images

Key facts

Isotype

IgG

Host species

Rabbit

Storage buffer

pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: 59% PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA

Form

Liquid

Clonality

Monoclonal

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Reactivity data

Select an application
Product promiseTestedExpectedPredictedNot recommended
DotIHC-P
Human
Expected
Tested
Synthetic peptide
Tested
Not recommended

Tested
Tested

Species

Synthetic peptide

Dilution info

1/7000

Notes

-

Expected
Expected

Species

Human

Dilution info

Use at an assay dependent concentration.

Notes

-

Tested
Tested

Species

Human

Dilution info

0.1-0.5 µg/mL

Notes

Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.

Not recommended
Not recommended

Species

Synthetic peptide

Dilution info

-

Notes

-

Target data

Function

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 synapes 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.N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).

Alternative names

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Rabbit Recombinant Monoclonal Amyloid-beta precursor protein antibody. Suitable for Dot, IHC-P and reacts with Synthetic peptide, Human samples. Cited in 4 publications.

Alternative names

Key facts

Isotype

IgG

Form

Liquid

Clonality

Monoclonal

Clone number

mOC22

Purification technique

Affinity purification Protein A

Concentration
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Storage

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

Notes

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.

Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

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.

Supplementary info

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.

Activity summary

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.

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.

Associated diseases and disorders

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.

Product promise

We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.

In the unlikely event of one of our products not working as expected, you are covered by our product promise.

Full details and terms and conditions can be found here:
Terms & Conditions.

3 product images

  • Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific (ab205339), expandable thumbnail

    Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific (ab205339)

    IHC image of Amyloid Fibril staining in Human Brain Alzheimer formalin fixed paraffin embedded tissue section*, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with ab205339, 0.1μg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.

    For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.

    *Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre

  • Dot Blot - Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific (ab205339), expandable thumbnail

    Dot Blot - Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific (ab205339)

    Dot blot analysis of beta Amyloid labeled with ab205339 at 1/7000 dilution.

    Lane 1: beta Amyloid (Aβ) 1-40;

    Lane 2: beta Amyloid (Aβ) 1-42.

    Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated (ab97051) at 1/30000 was used as secondary antibody.

    Blocking/Dilution buffer: 5% NFDM/TBST.

    Exposure time: 30 seconds.

    Note: Antibody reactivity was assessed using a dot blot, which is a non-quantitative method that maintains the native conformation of beta Amyloid. beta Amyloid 1-40 and 1-42 peptides underwent the following aggregation conditions before being spotted onto a nitrocellulose membrane and detected using ab205339:

    Monomers: 0.3 mg of beta Amyloid peptide was dissolved in 30 μl 100 mM NaOH and incubated at room temperature for 10 minutes. It was then diluted with 970 μl of 1% SDS and boiled for five minutes.

    Oligomers: 0.3 mg of beta Amyloid peptide was dissolved in 30 μl 100 mM NaOH and incubated at room temperature for 10 minutes. It was then diluted with 970 μl of 10 mM phosphate buffer pH 7.4 containing 0.02% sodium azide and incubated at room temperature for four days.

    Fibrils: 0.3 mg of beta Amyloid peptide was dissolved in 1 ml 50% hexafluoroisopropanol (HFIP) with 0.02% sodium azide. It was then stirred constantly for nine days; the first seven with a cap on and the final two with the cap removed to allow evaporation of the HFIP. Fibrils were then sedimented at 20,000 rpm in a microcentrifuge for 20 minutes and resuspended in 1 ml of PBS + 0.02% sodium azide.

  • Dot Blot - Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific (ab205339), expandable thumbnail

    Dot Blot - Anti-Amyloid Fibril antibody [mOC22] - Conformation-Specific (ab205339)

    Negative control (secondary ab only) Dot blot analysis of beta Amyloid.

    Lane 1: beta Amyloid (Aβ) 1-40;

    Lane 2: beta Amyloid (Aβ) 1-42.

    Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated (ab97051) at 1/30000 was used as secondary antibody.

    Blocking/Dilution buffer: 5% NFDM/TBST.

    Exposure time: 30 seconds.

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Product protocols

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

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

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