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AB5352

Sigma-Aldrich

Anti-Amyloid Precursor Protein Antibody, CT

serum, Chemicon®

Sinónimos:

APP

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About This Item

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

origen biológico

rabbit

Nivel de calidad

forma del anticuerpo

serum

tipo de anticuerpo

primary antibodies

clon

polyclonal

reactividad de especies

human, monkey

fabricante / nombre comercial

Chemicon®

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... APP(351)

Especificidad

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.

Inmunógeno

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

Aplicación

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

Forma física

Serum. Liquid in PBS with 0.02% azide.
Unpurified

Almacenamiento y estabilidad

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.

Nota de análisis

Control
Brain

Otras notas

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

Información legal

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

Cláusula de descargo de responsabilidad

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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Opcional

Referencia del producto
Descripción
Precios

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°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)
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
GGA proteins mediate the recycling pathway of memapsin 2 (BACE).
He, X; Li, F; Chang, WP; Tang, J
The Journal of Biological Chemistry null
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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