A9103

Sigma-Aldrich

Anti-phospho-APP (pThr668) antibody produced in rabbit

affinity isolated antibody, aqueous glycerol solution, 10 blots

MDL number:
Pricing and availability is not currently available.

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

aqueous glycerol solution

usage

10 blots

mol wt

antigen 100-140 kDa

species reactivity

human

application(s)

western blot: 1:1000 using CAD cells transfected with wild type vs. T668A mutant APP.

conjugate

unconjugated

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... APP(351)
mouse ... App(11820)
rat ... App(54226)

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. 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.

Immunogen

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.

Physical form

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.

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.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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...
Bin Peng et al.
Diving and hyperbaric medicine, 49(4), 276-282 (2019-12-13)
When humans breathe compressed air or N2-O2 mixtures at three to four atmospheres pressure, they will experience nitrogen narcosis that may possibly lead to a diving accident, but the underlying mechanisms remain unclear. Mice were exposed to 1.6 MPa breathing...
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...
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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