A8842
Anti-Amyloid Precursor Protein, KPI Domain antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-APP
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About This Item
MDL number:
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
mouse, rat, human
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200 using formic acid-treated sections of human Alzheimer′s disease (AD) brain
microarray: suitable
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[1][2][3].
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
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Immunohistochemistry (1 paper)
Rabbit Anti-Amyloid Precursor Protein, KPI Domain antibody has been used for immunohistochemistry assays at 1:500[4]. The product can also be used for microarrays.
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.
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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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