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

IgG fraction of antiserum

Anti-APPI, Anti-AD1, Anti-ABETA, Anti-ABPP, Anti-amyloid beta A4 protein precursor, AAA, Anti-CVAP, Anti-CTFgamma, Anti-PN2, Anti-PN-II
Pricing and availability is not currently available.

biological source


antibody form

IgG fraction of antiserum

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen ~130 kDa

species reactivity

human, rat, 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.


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.


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Thyroid hormones regulate $\beta$-amyloid gene splicing and protein secretion in neuroblastoma cells
Latasa M, et al.
Endocrinology, 139(6), 2692-2698 (1998)
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)

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