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AB5352

Sigma-Aldrich

Anti-Amyloid Precursor Protein Antibody, CT

serum, Chemicon®

Sinónimos:

APP

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, monkey

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... APP(351)

Categorías relacionadas

Specificity

Recognizes Amyloid Precursor Protein (APP), C-terminal. Recognizes full length APP and C-terminal fragments resulting from cleavage by secretase. May react with APLP1 and APLP2.

Immunogen

Epitope: C-terminus
Nine amino acid peptide from the C-terminus of APP (YKFFEQMQN)

Application

Detect Amyloid Precursor Protein using this Anti-Amyloid Precursor Protein Antibody, C-terminus validated for use in IC, IH, IP & WB.
Immunohistochemistry: 1:100-1:400

Immunocytochemistry on NTera2 and COS cell lines: 1:100-1:400

Western blot: 1:500-1:2000: The low abundance of full length APP in untreated cells means that poor response is seen with immunoblotting of whole cell lysates. We recommend that membrane fractions be prepared to increase the loading of APP as well as remove potential interferences from soluable proteins. NTera2, Cos7 and Hela cell membrane preparations are positive by western blots.

Immunoprecipitation: 1:100-1:400.

Optimal working dilutions must be determined by end user.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Physical form

Serum. Liquid in PBS with 0.02% azide.
Unpurified

Storage and Stability

Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Analysis Note

Control
Brain

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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R van Dijk et al.
Journal of neurochemistry, 90(3), 712-723 (2004-07-17)
Frame-shifted amyloid precursor protein (APP(+1)), which has a truncated out-of-frame C-terminus, accumulates in the neuropathological hallmarks of patients with Alzheimer's disease pathology. To study a possible involvement of APP(+1) in the pathogenesis of Alzheimer's disease, we expressed APP695 and APP(+1)
GGA proteins mediate the recycling pathway of memapsin 2 (BACE).
He, X; Li, F; Chang, WP; Tang, J
The Journal of Biological Chemistry null
Virgil Muresan et al.
Neuro-degenerative diseases, 13(2-3), 122-125 (2013-09-07)
The pathology of amyotrophic lateral sclerosis (ALS), a neurodegenerative disorder affecting motor neurons, comprises aberrant accumulations of neurofilaments; mutations in the peripherin subunit of neurofilaments have been identified in some forms of ALS. Recently, the amyloid-β precursor protein (APP), a
Cara L Croft et al.
Cell death & disease, 8(3), e2671-e2671 (2017-03-17)
The spatiotemporal transmission of pathological tau in the brain is characteristic of Alzheimer's disease. Release of both soluble and abnormal tau species from healthy neurons is increased upon stimulation of neuronal activity. It is not yet understood whether the mechanisms
A Kamal et al.
Neuron, 28(2), 449-459 (2001-01-06)
We analyzed the mechanism of axonal transport of the amyloid precursor protein (APP), which plays a major role in the development of Alzheimer's disease. Coimmunoprecipitation, sucrose gradient, and direct in vitro binding demonstrated that APP forms a complex with the

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