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Key Documents

AB2287

Sigma-Aldrich

Anti-Amyloid Fibrils LOC Antibody

serum, Chemicon®

Synonym(s):

Amyloid Fibrils, Amyloid Fibrils LOC

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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)

mouse, rat

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 monomers, prefibrillar oligomers or natively folded proteins.

Immunogen

Fibrils prepared from human islet amyloid polypeptide.

Application

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.
This Anti-Amyloid Fibrils LOC Antibody is validated for use in IP, IC, IH, ELISA, WB, DB for the detection of Amyloid Fibrils LOC.

Quality

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

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.

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. After thawing, store at 4°C in 0.02% sodium azide.

Legal Information

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

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Storage Class

10 - Combustible liquids

wgk_germany

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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Neuroinflammation and related neuropathologies in APPSL mice: further value of this in vivo model of Alzheimer's disease.
Loffler, T; Flunkert, S; Havas, D; Schweinzer, C; Uger, M; Windisch, M; Steyrer, E; Hutter-Paier, B
Journal of Neuroinflammation null
Juan Jose Ramos-Rodriguez et al.
Molecular neurobiology, 54(5), 3428-3438 (2016-05-15)
Age remains the main risk factor for developing Alzheimer's disease (AD) although certain metabolic alterations, including prediabetes and type 2 diabetes (T2D), may also increase this risk. In order to understand this relationship, we have studied an AD-prediabetes mouse model
Elin K Esbjörner et al.
Chemistry & biology, 21(6), 732-742 (2014-05-27)
Insight into how amyloid β (Aβ) aggregation occurs in vivo is vital for understanding the molecular pathways that underlie Alzheimer's disease and requires new techniques that provide detailed kinetic and mechanistic information. Using noninvasive fluorescence lifetime recordings, we imaged the formation
Sahil Chandhok et al.
Scientific reports, 13(1), 14471-14471 (2023-09-03)
The formation of protein aggregates is a hallmark of many neurodegenerative diseases and systemic amyloidoses. These disorders are associated with the fibrillation of a variety of proteins/peptides, which ultimately leads to cell toxicity and tissue damage. Understanding how amyloid aggregation
Thomas Filip et al.
Alzheimer's research & therapy, 13(1), 175-175 (2021-10-18)
To better understand the etiology and pathomechanisms of Alzheimer's disease, several transgenic animal models that overexpress human tau or human amyloid-beta (Aβ) have been developed. In the present study, we generated a novel transgenic rat model by cross-breeding amyloid precursor

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