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Key Documents

AB2286

Sigma-Aldrich

Anti-Amyloid Fibrils OC Antibody

serum, Chemicon®

Synonym(s):

Amyloid Fibrils, Amyloid Fibrils OC

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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

species reactivity (predicted by homology)

rat, mouse

manufacturer/tradename

Chemicon®

technique(s)

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

isotype

IgG

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

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

General description

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.

Specificity

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.

Immunogen

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

Quality

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.

Physical form

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

Storage and Stability

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.

Analysis Note

Control
Alzheimer′s Brain tissue

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models.
Sontag, EM; Lotz, GP; Agrawal, N; Tran, A; Aron, R; Yang, G; Necula, M; Lau et al.
The Journal of Neuroscience null
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
TGFbeta1 activates c-Jun and Erk1 via alphaVbeta6 integrin.
Luettich, K; Schmidt, C
Molecular Cancer null

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