A8967

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):
Anti-APP
MDL number:
NACRES:
NA.41
Pricing and availability is not currently available.

biological source

rabbit

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 95-100 kDa

species reactivity

human, mouse, rat

application(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200 using formic acid-treated sections of human Alzheimer′s disease (AD) brain
microarray: suitable
western blot: 1:1,000 using rat brain extract or supernatant of 293T cells secreting APP.

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

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. APPs have 3 main isoforms, namely, APP695, APP751 and APP770 that are derived from alternative splicing events in cells. It is expressed at high levels in the brain. APP gene is mapped to human chromosome 21q11.2-q21. It is a 695 amino acid protein which possesses a large ectodomain and comparatively short intracellular region.
The immunogen sequence is identical to the APP isoforms APP751 and APP770 and is highly conserved (single amino acid substitution) in rat and mouse APP695. The antibody recognizes APP695, APP751 and APP770.

Immunogen

synthetic peptide corresponding to the N-terminal of human APP695 (amino acids 46-60) conjugated to KLH.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Anti-Amyloid Precursor Protein, N-Terminal antibody produced in rabbit has been used in:
  • western blotting
  • immunostaining
  • immunofluorescence

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.

Biochem/physiol Actions

Amyloid precursor proteins (APPs) regulates cell growth, motility, neurite outgrowth and cell survival. The intracellular C-terminus of APP serves as a transcriptional regulator and as a receptor for kinesin-1-mediated axonal transport. Alzheimer′s disease is characterized by deposition of amyloid in the central nervous system, in neurite plaques and on cerebral vasculature. Mutations in the APP gene are linked with rare forms of autosomal dominant familial Alzheimer′s Disease (FAD). APPs undergo post-translational processing including N- and O-glycosylation, phosphorylation and sulfation.

Physical form

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

Hazard Codes

Xn

Risk Statement

21/22

Safety Statement

36/37-60

RIDADR

NONH for all modes of transport

WGK Germany

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Homo-and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design
Advances in Protein Chemistry and Structural Biology, 111, 1-59 (2018)
Migration of blood cells to beta-amyloid plaques in Alzheimer's disease
Hohsfield LA, et al.
Experimental Gerontology, 65, 8-15 (2015)
The Alzheimer amyloid precursor protein maps to human chromosome 21 bands q21. 105-q21. 05
Korenberg JR, et al.
Genomics, 5(1), 124-127 (1989)
Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents
Canu N, et al.
Frontiers in Molecular Neuroscience, 10 (2017)
Neuropathological Alterations in Alzheimer Disease
Serrano-Pozo A, et al.
Cold Spring Harbor Perspectives in Medicine, 1(1) (2011)

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