AB2286
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
Recommended Products
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
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... APP(351)
mouse ... App(11820)
Related Categories
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
Neuroscience
Research Sub Category
Neurodegenerative Diseases
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.
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.
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
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
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
Pei-Yu Kao et al.
Journal of functional foods, 12, 450-457 (2016-02-20)
The aggregation of the 37-amino acid polypeptide islet amyloid polypeptide (IAPP, amylin), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of pancreatic β-islet cells in type 2 diabetes. It is believed
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
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
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