产品名称
Anti-Amyloid Precursor Protein, N-Terminal antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
biological source
rabbit
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
human, rat, mouse
technique(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.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... APP(351)
mouse ... App(11820)
rat ... App(54226)
Application
Anti-Amyloid Precursor Protein, N-Terminal antibody produced in rabbit has been used in:
- western blotting
- immunostaining
- immunofluorescence
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunofluorescence (1 paper)
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.
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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)
Homo-and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design
Advances in Protein Chemistry and Structural Biology, 111, 1-59 (2018)
Dopamine induces apoptosis in APPswe-expressing Neuro2A cells following Pepstatin-sensitive proteolysis of APP in acid compartments
Cagnin M, et al.
Brain Research, 1471, 102-117 (2012)
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)
相关内容
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