Amyloid Antikörper
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- Target
- Amyloid
- Reaktivität
- Human
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Wirt
- Kaninchen
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Klonalität
- Polyklonal
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Konjugat
- Unkonjugiert
- Applikation
- ELISA, Immunohistochemistry (IHC), Western Blotting (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC), Immunofluorescence (IF), Dot Blot (DB)
- Spezifität
- 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 homology.
- Kreuzreaktivität
- Human
- Aufreinigung
- Protein A Purified
- Immunogen
- Fibrils prepared from human amyloid beta 42 peptide
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- Applikationshinweise
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- WB (1:1000)
- IHC (1:100)
- optimal dilutions for assays should be determined by the user.
- Kommentare
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A 1:1000 dilution of ABIN863211 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.
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Buffer
- PBS, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
- Konservierungsmittel
- Sodium azide
- Vorsichtsmaßnahmen
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Lagerung
- -20 °C
- Informationen zur Lagerung
- -20°C
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MEK guards proteome stability and inhibits tumor-suppressive amyloidogenesis via HSF1." in: Cell, Vol. 160, Issue 4, pp. 729-44, (2015) (PubMed).
: "Acute amnestic encephalopathy in amyloid-β oligomer-injected mice is due to their widespread diffusion in vivo." in: Neurobiology of aging, Vol. 36, Issue 6, pp. 2043-52, (2015) (PubMed).
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MEK guards proteome stability and inhibits tumor-suppressive amyloidogenesis via HSF1." in: Cell, Vol. 160, Issue 4, pp. 729-44, (2015) (PubMed).
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- Target
- Amyloid
- Synonyme
- amyloid beta precursor protein antikoerper, App antikoerper
- Hintergrund
- 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 (1, 2). These include the amyloid-β peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimer's symptomology, the deposition of α-synuclein in the Lewy bodies of Parkinson's disease, and accumulation of polyglutamine-containing aggregates in Huntington's disease (2, 3).
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