Thermo Fisher Scientific Amyloid Fibrils Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:1,000

-

Immunohistochemistry (PFA fixed) (IHC (PFA))

1:100

-

Immunocytochemistry (ICC/IF)

Assay-Dependent

View 2 publications 2 publications

ELISA (ELISA)

Assay-Dependent

-

Immunoprecipitation (IP)

Assay-Dependent

-

Dot blot (DB)

1:1,000

-

Product Specifications

Species Reactivity

Human

Published species

Human

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Fibrils prepared from human amyloid beta 42 peptide if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:Amyloid Fibrils,uniProtId:P05067-1,ncbiNodeId:9606,antigenRange:1-770,antigenLength:770,antigenImageFileName:PA5-77843_Amyloid_Fibrils_P05067-1_Rabbit.svg,antigenImageFileNamePDP:PA5-77843_Amyloid_Fibrils_P05067-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

0.5 mg/mL

Purification

Protein A

Storage buffer

PBS, pH 7.4, with 50% glycerol

Contains

0.09% sodium azide

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Wet ice

RRID

AB_2735453

Product Specific Information

Specificity: recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrilllar oligomers or natively folded proteins. Expected to detect Mouse and Rat based on species homology.

A 1:1,000 dilution of PA5-77843 was sufficient for detection of amyloid fibrils on PVDF membranes using transferred fibrils by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.|Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. Expected to detect in Mouse and Rat based on species homology.

Target Information

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. Many degenerative diseases are known to be related to the accumulation of misfolded proteins as amyloid fibres. These include the amyloid-beta peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimers symptomology, the deposition of alpha-synuclein in the Lewy bodies of Parkinsons disease, and accumulation of polyglutamine-containing aggregates in Huntington`s disease.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.