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Key Documents

SAB5200113

Sigma-Aldrich

Anti-APP antibody produced in rabbit

1 mg/mL, affinity isolated antibody

Synonym(s):

Anti-A11, Anti-Amyloid Oligomer αβ, Anti-Amyloid Oligomers (A11)

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

mouse, eukaryotes, rat, human

concentration

1 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
indirect immunofluorescence: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... APP(351)

General description

Amyloid β precursor protein (APP) is a type 1 transmembrane protein. The gene is located on human chromosome 21q21.3.

Specificity

Recognizes all types of amyloid oligomers. Appears to recognize a peptide backbone epitope that is common to amyloid oligomers, but is not found in native proteins, amyloidogenic monomer or mature amyloid fibrils.

Immunogen

Synthetic molecular mimic of soluble oligomers.

Application

Anti-APP antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

Amyloid β precursor protein (APP) regulates cell signaling. Mutation in this gene is associated with Alzheimer′s disease. It is implicated in synaptic plasticity, dendritic morphogenesis and neuroprotection. APP modulates synaptic vesicle proteins and synaptic transmission. It is involved in GABAergic transmission and maintains the excitatory/inhibitory (E/I) balance.
Amyloid precursor protein (APP) plays a key role in Wnt signalling. It helps to increase synaptoxicity, that is facilitated by Dickkopf-1 (Dkk1). Mutations on this gene results in autosomal dominant early-onset Alzheimer disease (ADEOAD)/hereditary dementia with cerebral amyloid angiopathy (CAA).

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

PBS, 50% glycerol, and 0.09% sodium azide

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A role for APP in Wnt signalling links synapse loss with beta-amyloid production
Elliott C, et al.
Translational Psychiatry, 8(1), 179-179 (2018)
Novel derivative of Paeonol, Paeononlsilatie sodium, alleviates behavioral damage and hippocampal dendritic injury in Alzheimer's disease concurrent with cofilin1/phosphorylated-cofilin1 and RAC1/CDC42 alterations in rats
Han F, et al.
PLoS ONE, 12(9), e0185102-e0185102 (2017)
Fei Han et al.
PloS one, 12(9), e0185102-e0185102 (2017-09-22)
Alzheimer's disease (AD) is a typical hippocampal amnesia and the most common senile dementia. Many studies suggest that cognitive impairments are more closely correlated with synaptic loss than the burden of amyloid deposits in AD progression. To date, there is
Human brain-derived Abeta oligomers bind to synapses and disrupt synaptic activity in a manner that requires APP
Wang Z, et al.
The Journal of Neuroscience, 8(1), 11947-11966 (2017)
Human brain-derived Abeta oligomers bind to synapses and disrupt synaptic activity in a manner that requires APP
Wang Z, et al.
The Journal of Neuroscience, 37(49), 11947-11966 (2017)

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