Anti-Amyloid Precursor Protein, C-Terminal antibody produced in rabbit

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Anti-APP, APP antibody
MDL number:

biological source


Quality Level

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen 95-100 kDa

species reactivity

human, mouse, rat


antibody small pack of 25 μL

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation


immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:1000 using formic acid-treated sections of human Alzheimer′s disease (AD) brain
microarray: suitable
western blot: 1:4,000 using rat brain extract



UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

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

General description

Amyloid precursor proteins (APPs) are transmembrane glycoproteins that are found in a wide range of tissues. APP is expressed in the brain. It is located on human chromosome 21. APPs have 3 main isoforms, namely, APP695, APP751 and APP770 that are derived from alternative splicing events in cells. Accumulation of the cleavage products of APP, such as the β-amyloid peptide, can cause Alzheimer′s disease.
The immunogen sequence is identical to rat and mouse APP695 and in the APP isoforms APP751 and APP770. The antibody recognizes APP695, APP751 and APP770.


Synthetic peptide corresponding to the C-terminal of human APP695 conjugated to KLH.


SH-SY5Y cell lysates were analyzed by western blot using rabbit anti-Amyloid Precursor Protein, C-Terminal as the primary antibody at a 1:500 dilution.
Rabbit Anti-Amyloid Precursor Protein, C-Terminal antibody has been used for immunoprecipitation, immunohistochemical analysis, immunohistochemical staining and western blot applications. The product can also be used for IHC (1:1,000) and microarray studies.

Biochem/physiol Actions

In transiently transfected cell lines, APP (amyloid precursor protein) regulates cell growth, motility, neurite outgrowth and cell survival. The intracellular C-terminus of APP acts as a transcriptional regulator and its amino acid domain serves as a regulator of its own intracellular sorting. Mutation of the gene leads to cerebral amyloid angiopathy. Accumulation of the cleavage products of APP, such as the β-amyloid peptide can cause Alzheimer′s disease.

Physical form

Supplied in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as a preservative.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage freeze in working aliquots. Repeated freezing and thawing, or storage in "frostfree" freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.


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.


12 - Non Combustible Liquids

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Fang Cheng et al.
The Journal of biological chemistry, 286(31), 27559-27572 (2011-06-07)
Amyloid β (Aβ) is generated from the copper- and heparan sulfate (HS)-binding amyloid precursor protein (APP) by proteolytic processing. APP supports S-nitrosylation of the HS proteoglycan glypican-1 (Gpc-1). In the presence of ascorbate, there is NO-catalyzed release of anhydromannose (anMan)-containing...
Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
Grabowski TJ, et al.
Annals of Neurology, 49(6), 697-705 (2001)
Amyloid Precursor Protein Processing and Alzheimer?s Disease.
Richard J O, et al.
Annual Review of Neuroscience, 34, 185-204 (2001)
Henri J Huttunen et al.
FEBS letters, 581(8), 1688-1692 (2007-04-07)
Previous studies have shown that acyl-coenzyme A:cholesterol acyl transferase (ACAT), an enzyme that controls cellular equilibrium between free cholesterol and cholesteryl esters, modulates proteolytic processing of APP in cell-based and animal models of Alzheimer's disease. Here we report that ACAT-1...
Mikiko Ohno et al.
Neurobiology of aging, 35(1), 213-222 (2013-08-21)
Amyloid beta (Aβ) peptide, the main component of senile plaques in patients with Alzheimer's disease (AD), is derived from proteolytic cleavage of amyloid precursor protein (APP) by β- and γ-secretases. Alpha-cleavage of APP by α-secretase has a potential to preclude...

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