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Anti-APP (N-terminal region) antibody produced in rabbit

IgG fraction of antiserum

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Anti-ABETA, Anti-ABPP, Anti-AD1, Anti-APPI, Anti-CTFgamma, Anti-CVAP, Anti-PN-II, Anti-PN2, Anti-amyloid beta A4 protein precursor, AAA

biological source




antibody form

IgG fraction of antiserum

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen ~130 kDa

species reactivity

rat, human, mouse


indirect immunofluorescence: 1:250-1:500 using SH-SY5Y cells.
western blot: 1:1,000 using lysates of rat and mouse brain (S1 fraction)

UniProt accession no.

shipped in

dry ice

storage temp.


target post-translational modification


Gene Information

human ... APP(351)
mouse ... App(11820)
rat ... App(54226)

General description

Amyloid precursor protein (APP) is encoded by the gene mapped to human chromosome 21. It is a transmembrane glycoprotein widely distributed in many tissues. APP exists as multiple isoforms (100-140 kDa) including APP695, APP751 and APP770 that are derived from alternative mRNA splicing.


synthetic peptide corresponding to an N-terminal region of human Amyloid Precursor Protein (APP), conjugated to KLH. The corresponding sequence is highly conserved (single amino acid substitution) in rat and mouse APP.


Anti-APP (N-terminal region) antibody produced in rabbit has been used in:
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry

Biochem/physiol Actions

The amyloid precursor protein (APP) undergoes extensive post-translational modifications including phosphorylation, glycosylation, tyrosine sulfation and nitration. APP has been reported to be phosphorylated at several sites that may affect its processing and secretion. Phosphorylation of APP at Thr688 by cyclin-dependent kinase 5 (Cdk5) has been shown to play a critical role in the proteolytic cleavage of APP. APP Thr688, phosphorylated form is found in the adult brain and it correlates with neuronal differentiation. Mutations in the APP gene are linked with rare forms of autosomal dominant familial Alzheimer′s disease (FAD). These mutations result in increased production of Aβ indicating a central role of Aβ peptide in the neuropathology of AD.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.


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.

Storage Class Code

10 - Combustible liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Neuron-specific phosphorylation of Alzheimer's beta-amyloid precursor protein by cyclin-dependent kinase 5
Iijima K, et al.
Journal of Neurochemistry, 75(3), 1085-1091 (2000)
Thyroid hormones regulate $\beta$-amyloid gene splicing and protein secretion in neuroblastoma cells
Latasa M, et al.
Endocrinology, 139(6), 2692-2698 (1998)
Zhi-Hao Wang et al.
Progress in neurobiology, 202, 102032-102032 (2021-03-16)
ApoE4, an apolipoprotein implicated in cholesterol transport and amyloid-β (Aβ) metabolism, is a major genetic risk determinant for Alzheimer's Disease (AD) and drives its pathogenesis via Aβ-dependent and -independent pathways. C/EBPβ, a proinflammatory cytokines-activated transcription factor, is upregulated in AD
Svetlana Sharifulina et al.
Biomedicines, 10(10) (2022-10-28)
Our studies reveal changes in the expression of the main participants in the processing of amyloid precursor protein (APP) in neurons and astrocytes after photothrombotic stroke (PTS). Here we show the increase in the level of N- and C-terminal fragments

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