WH0000351M1

Sigma-Aldrich

Monoclonal Anti-APP antibody produced in mouse

clone 2C12, purified immunoglobulin, buffered aqueous solution

Synonym(s):
Anti-APPI, Anti-AD1, Anti-ABETA, Anti-ABPP, Anti-CVAP, Anti-Amyloid β (A4) precursor protein (protease nexin-II, Alzheimer disease), Anti-CTFγ, Anti-AAA
MDL number:
NACRES:
NA.41

Quality Level

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

2C12, monoclonal

form

buffered aqueous solution

species reactivity

human

application(s)

indirect ELISA: suitable
proximity ligation assay: suitable
western blot: 1-5 μg/mL

isotype

IgG1κ

conjugate

unconjugated

GenBank® accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... APP(351)

General description

This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. (provided by RefSeq)

Immunogen

APP (AAH04369.1, 19 a.a. ~ 305 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
EVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREKWYKEVHSGQARWLML

Biochem/physiol Actions

Amyloid β precursor protein (APP) plays a crucial role in regulation of global gene expression and overexpression of this protein hinders cell proliferation. APP is involved in various physiological functions including, spine density, morphology and plasticity. Mutation of the gene leads to familial Alzheimer′s disease (FAD) and cerebral amyloid angiopathy. APP facilitates production of β-amyloid peptide (Aβ). Increased expression of neuronal APP leads to synaptic dysfunction.

Features and Benefits

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Physical form

Solution in phosphate buffered saline, pH 7.4

Legal Information

GenBank is a registered trademark of United States Department of Health and Human Services

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.

Certificate of Analysis

Certificate of Origin

Mickael Audrain et al.
Molecular neurodegeneration, 11, 5-5 (2016-01-14)
Alzheimer's disease (AD) is the most frequent form of dementia in the elderly and no effective treatment is currently available. The mechanisms triggering AD onset and progression are still imperfectly dissected. We aimed at deciphering the modifications occurring in vivo...
Ya-Ping Tang et al.
Dialogues in clinical neuroscience, 5(1), 17-26 (2003-03-01)
Alzheimer's disease (AD), the most common cause of dementia in aged populations, is believed to be caused by both environmental factors and genetic variations. Extensive linkage and association studies have established that a broad range of loci are associated with...
T J Grabowski et al.
Annals of neurology, 49(6), 697-705 (2001-06-21)
Several mutations in the amyloid precursor protein (APP) gene have been found to associate with pathologic deposition of the beta-amyloid peptide (Abeta) in neuritic plaques or in the walls of cerebral vessels. We report a mutation at a novel site...
Marta Del Campo et al.
Neurobiology of aging, 35(7), 1596-1604 (2014-02-15)
BRI2 protein binds amyloid precursor protein to halt amyloid-β production and inhibits amyloid-β aggregation via its BRICHOS-domain suggesting a link between BRI2 and Alzheimer's disease (AD). Here, we investigate the possible involvement of BRI2 in human AD pathogenesis. BRI2 containing...
Yili Wu et al.
Scientific reports, 6, 22460-22460 (2016-03-05)
Down syndrome (DS), caused by trisomy of chromosome 21, is one of the most common genetic disorders. Patients with DS display growth retardation and inevitably develop characteristic Alzheimer's disease (AD) neuropathology, including neurofibrillary tangles and neuritic plaques. The expression of...

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