产品名称
Anti-APP (N-terminal region) antibody produced in rabbit, IgG fraction of antiserum
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 ~130 kDa
species reactivity
rat, human, mouse
technique(s)
indirect immunofluorescence: 1:250-1:500 using SH-SY5Y cells., western blot: 1:1,000 using lysates of rat and mouse brain (S1 fraction)
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)
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General description
Amyloid precursor protein (APP) is encoded by the gene mapped to human chromosome 21. It is a transmembrane glycoprotein widely distributed in many tissues. APP exists as multiple isoforms (100-140 kDa) including APP695, APP751 and APP770 that are derived from alternative mRNA splicing.
Immunogen
synthetic peptide corresponding to an N-terminal region of human Amyloid Precursor Protein (APP), conjugated to KLH. The corresponding sequence is highly conserved (single amino acid substitution) in rat and mouse APP.
Application
Anti-APP (N-terminal region) antibody produced in rabbit has been used in:
- immunoblotting
- immunofluorescence
- immunohistochemistry
Biochem/physiol Actions
The amyloid precursor protein (APP) undergoes extensive post-translational modifications including phosphorylation, glycosylation, tyrosine sulfation and nitration. APP has been reported to be phosphorylated at several sites that may affect its processing and secretion. Phosphorylation of APP at Thr688 by cyclin-dependent kinase 5 (Cdk5) has been shown to play a critical role in the proteolytic cleavage of APP. APP Thr688, phosphorylated form is found in the adult brain and it correlates with neuronal differentiation. Mutations in the APP gene are linked with rare forms of autosomal dominant familial Alzheimer′s disease (FAD). These mutations result in increased production of Aβ indicating a central role of Aβ peptide in the neuropathology of AD.
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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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
低风险生物材料
常规特殊物品
此项目有
Neuron-specific phosphorylation of Alzheimer's beta-amyloid precursor protein by cyclin-dependent kinase 5
Iijima K, et al.
Journal of Neurochemistry, 75(3), 1085-1091 (2000)
Thyroid hormones regulate $\beta$-amyloid gene splicing and protein secretion in neuroblastoma cells
Latasa M, et al.
Endocrinology, 139(6), 2692-2698 (1998)
Zhi-Hao Wang et al.
Progress in neurobiology, 202, 102032-102032 (2021-03-16)
ApoE4, an apolipoprotein implicated in cholesterol transport and amyloid-β (Aβ) metabolism, is a major genetic risk determinant for Alzheimer's Disease (AD) and drives its pathogenesis via Aβ-dependent and -independent pathways. C/EBPβ, a proinflammatory cytokines-activated transcription factor, is upregulated in AD
Svetlana Sharifulina et al.
Biomedicines, 10(10) (2022-10-28)
Our studies reveal changes in the expression of the main participants in the processing of amyloid precursor protein (APP) in neurons and astrocytes after photothrombotic stroke (PTS). Here we show the increase in the level of N- and C-terminal fragments
相关内容
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