A9103
Anti-phospho-APP (pThr668) antibody produced in rabbit
affinity isolated antibody, aqueous glycerol solution, 10 blots
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About This Item
Prodotti consigliati
Origine biologica
rabbit
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
affinity isolated antibody
Tipo di anticorpo
primary antibodies
Clone
polyclonal
Forma fisica
aqueous glycerol solution
impiego
10 blots
PM
antigen 100-140 kDa
Reattività contro le specie
human
tecniche
western blot: 1:1000 using CAD cells transfected with wild type vs. T668A mutant APP.
N° accesso UniProt
Temperatura di conservazione
−20°C
Informazioni sul gene
human ... APP(351)
mouse ... App(11820)
rat ... App(54226)
Descrizione generale
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.
Rabbit Anti-phospho-APP (pThr668) antibody binds to human APP phosphorylated at Thr668. Mouse, rat and frog APP are 100% homologous.
Rabbit Anti-phospho-APP (pThr668) antibody binds to human APP phosphorylated at Thr668. Mouse, rat and frog APP are 100% homologous.
Immunogeno
synthetic phosphopeptide corresponding to the region of APP containing threonine 688.
Applicazioni
Cultured cortical neurons were immunostained for APP using rabbit anti-phospho-APP (pThr688) antibody.
Rabbit Anti-phospho-APP (pThr668) antibody can be used for western blot applications at a dilution of 1:1,000.
Stato fisico
Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, with 50% glycerol, 1.0 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.
Esclusione di responsabilità
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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Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
Chun-Yan Wang et al.
Antioxidants & redox signaling, 30(11), 1411-1431 (2018-04-11)
Oxidative stress and neuroinflammation play important roles in the pathology of Alzheimer's disease (AD). Thioredoxin-interacting protein (TXNIP), an endogenous inhibitor of antioxidant thioredoxin, is suspected to be an important modulator of oxidative stress and inflammation. However, the underlying mechanism involved
Yoichi Ohshima et al.
The Journal of toxicological sciences, 43(4), 257-266 (2018-04-06)
The increased ratio of longer amyloid-β (Aβ1-42)/shorter amyloid-β (Aβ1-40) peptides, generated from amyloid precursor protein (APP), is known to promote the development of Alzheimer's disease (AD). To investigate the role of smoking in Aβ production, we determined the production of
Roberta Roncarati et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(10), 7102-7107 (2002-05-16)
The beta-amyloid precursor protein (APP) and the Notch receptor undergo intramembranous proteolysis by the Presenilin-dependent gamma-secretase. The cleavage of APP by gamma-secretase releases amyloid-beta peptides, which have been implicated in the pathogenesis of Alzheimer's disease, and the APP intracellular domain
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
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
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