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AB5352

Sigma-Aldrich

Anti-Amyloid Precursor Protein Antibody, CT

serum, Chemicon®

Synonyme(s) :

APP

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About This Item

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

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

serum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

human, monkey

Fabricant/nom de marque

Chemicon®

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... APP(351)

Spécificité

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.

Immunogène

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

Forme physique

Serum. Liquid in PBS with 0.02% azide.
Unpurified

Stockage et stabilité

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.

Remarque sur l'analyse

Control
Brain

Autres remarques

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

Informations légales

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

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 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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