A8717
Anti-Amyloid Precursor Protein, C-Terminal antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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Synonym(s):
APP antibody, Anti-APP
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biological source
rabbit
Quality Level
conjugate
unconjugated
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
mouse, human, rat
packaging
antibody small pack of 25 μL
enhanced validation
recombinant expression
Learn more about Antibody Enhanced Validation
technique(s)
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.
−20°C
target post-translational modification
unmodified
Gene Information
human ... APP(351)
mouse ... App(11820)
rat ... App(54226)
Related Categories
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.
Immunogen
Synthetic peptide corresponding to the C-terminal of human APP695 conjugated to KLH.
Application
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.
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
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.
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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Description
Pricing
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Certificates of Analysis (COA)
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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
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)
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
Timo Sarajärvi et al.
The Journal of biological chemistry, 284(49), 34433-34443 (2009-10-10)
Seladin-1 is a neuroprotective protein selectively down-regulated in brain regions affected in Alzheimer disease (AD). Seladin-1 protects cells against beta-amyloid (Abeta) peptide 42- and oxidative stress-induced apoptosis activated by caspase-3, a key mediator of apoptosis. Here, we have employed RNA
Yvonne S Eisele et al.
Molecular biology of the cell, 18(9), 3591-3600 (2007-07-13)
Amyloid-beta (Abeta) deposition is a major pathological hallmark of Alzheimer's disease. Gleevec, a known tyrosine kinase inhibitor, has been shown to lower Abeta secretion, and it is considered a potential basis for novel therapies for Alzheimer's disease. Here, we show
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