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Key Documents

AB2286

Sigma-Aldrich

Anti-Amyloid Fibrils OC Antibody

serum, Chemicon®

Synonyme(s) :

Amyloid Fibrils, Amyloid Fibrils OC

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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

Réactivité de l'espèce (prédite par homologie)

rat, mouse

Fabricant/nom de marque

Chemicon®

Technique(s)

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

Isotype

IgG

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. In disease state oligomerization, extensive amyloid oligomerization creates plaques in neural tissue that correlates with Alzheimer’s symptomology.

Spécificité

This antibody recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. It may also show weak reactivity against Aβ monomers while AB2287 does not.

Immunogène

Fibrils prepared from human Aß42 peptide.

Application

Anti-Amyloid Fibrils OC Antibody is an antibody against Amyloid Fibrils OC for use in IP, IC, IH, ELISA, WB, DB.
Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in monomers, oligos, and fibrils.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Qualité

Evaluated by Dot Blot in monomers, oligos, and fibrils.

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in monomers, oligos, and fibrils.

Forme physique

Unpurified
Unpurified rabbit polyclonal antibody serum containing 0.05% sodium azide.

Stockage et stabilité

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Remarque sur l'analyse

Control
Alzheimer′s Brain tissue

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 1


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Consulter la Bibliothèque de documents

Rosa Sánchez et al.
Scientific reports, 6, 32801-32801 (2016-09-07)
Amyloids are polymeric structural states formed from locally or totally unfolded protein chains that permit surface reorganizations, stability enhancements and interaction properties that are absent in the precursor monomers. β-Parvalbumin, the major allergen in fish allergy, forms amyloids that are
Peng Liu et al.
Cell reports, 11(11), 1760-1771 (2015-06-09)
The accumulation of amyloid-β (Aβ) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer's disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects when generated in
Sofia B Carvalho et al.
PloS one, 8(10), e76629-e76629 (2013-10-08)
S100 proteins are small dimeric calcium-binding proteins which control cell cycle, growth and differentiation via interactions with different target proteins. Intrinsic disorder is a hallmark among many signaling proteins and S100 proteins have been proposed to contain disorder-prone regions. Interestingly
Michael H Hayes et al.
Biology open, 5(6), 801-806 (2016-05-25)
A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids
Functional amyloids in the mouse sperm acrosome.
Guyonnet, B; Egge, N; Cornwall, GA
Molecular and cellular biology null

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