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A8842

Sigma-Aldrich

Anti-Amyloid Precursor Protein, KPI Domain antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):
Anti-APP
MDL number:
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

species reactivity

mouse, rat, human

application(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200 using formic acid-treated sections of human Alzheimer′s disease (AD) brain
microarray: suitable

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. Accumulation of the cleavage products of APP, such as the β-amyloid peptide, can cause Alzheimer′s disease.
The immunogen sequence is identical in rat and mouse APP770 and in the APP isoform APP751, and is absent in APP695. By immunohistochemistry, the antibody recognizes APP770.

Immunogen

synthetic peptide corresponding to the Kunitz Protease Inhibitor (KPI) domain of human APP770 (amino acids 301-315) conjugated to KLH.

Application

Rabbit Anti-Amyloid Precursor Protein, KPI Domain antibody has been used for immunohistochemistry assays at 1:500. The product can also be used for microarrays.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

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.

WGK Germany

3

Ralf Palmisano et al.
BMC neuroscience, 12, 24-24 (2011-03-10)
The cause of sporadic amyotrophic lateral sclerosis (ALS) is largely unknown but hypotheses about disease mechanisms include oxidative stress, defective axonal transport, mitochondrial dysfunction and disrupted RNA processing. Whereas familial ALS is well represented by transgenic mutant SOD1 mouse models...
Orit Beilin et al.
Neuroreport, 18(6), 581-584 (2007-04-07)
Amyloid precursor protein can be translated from three alternatively spliced mRNAs. We measured levels of amyloid precursor protein isoforms containing the Kunitz protease inhibitor domain (KPIAPP), and amyloid precursor protein without the Kunitz protease inhibitor domain (KPIAPP) in brain homogenates...
R E Tanzi et al.
Science (New York, N.Y.), 235(4791), 880-884 (1987-02-20)
The amyloid beta protein has been identified as an important component of both cerebrovascular amyloid and amyloid plaques of Alzheimer's disease and Down syndrome. A complementary DNA for the beta protein suggests that it derives from a larger protein expressed...
R E Tanzi et al.
Nature, 331(6156), 528-530 (1988-02-11)
Amyloid B-protein/amyloid A4 is a peptide present in the neuritic plaques, neurofibrillary tangles and cerebrovascular deposits in patients with Alzheimer's disease and Down's syndrome (trisomy 21) and may be involved in the pathogenesis of Alzheimer's disease. Recent molecular genetic studies...
D Goldgaber et al.
Science (New York, N.Y.), 235(4791), 877-880 (1987-02-20)
Four clones were isolated from an adult human brain complementary DNA library with an oligonucleotide probe corresponding to the first 20 amino acids of the beta peptide of brain amyloid from Alzheimer's disease. The open reading frame of the sequenced...

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