A9103
Anti-phospho-APP (pThr668) antibody produced in rabbit
affinity isolated antibody, aqueous glycerol solution, 10 blots
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About This Item
Produits recommandés
Source biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
aqueous glycerol solution
Utilisation
10 blots
Poids mol.
antigen 100-140 kDa
Espèces réactives
human
Technique(s)
western blot: 1:1000 using CAD cells transfected with wild type vs. T668A mutant APP.
Numéro d'accès UniProt
Température de stockage
−20°C
Informations sur le gène
human ... APP(351)
mouse ... App(11820)
rat ... App(54226)
Description générale
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.
Immunogène
synthetic phosphopeptide corresponding to the region of APP containing threonine 688.
Application
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.
Forme physique
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.
Clause de non-responsabilité
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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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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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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