AB2287
Anti-Beta (β)-Amyloid antibody
CHEMICON®, rabbit polyclonal
Synonim(y):
Amyloid Fibrils, Amyloid Fibrils LOC
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About This Item
Kod UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Polecane produkty
Nazwa produktu
Anti-Amyloid Fibrils LOC Antibody, serum, Chemicon®
pochodzenie biologiczne
rabbit
Poziom jakości
forma przeciwciała
serum
rodzaj przeciwciała
primary antibodies
klon
polyclonal
reaktywność gatunkowa
human
reaktywność gatunkowa (przewidywana na podstawie homologii)
mouse, rat
producent / nazwa handlowa
Chemicon®
metody
ELISA: suitable
dot blot: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
Opis ogólny
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.
Specyficzność
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.
Zastosowanie
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.
Jakość
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.
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.
Przechowywanie i stabilność
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.
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.
Informacje prawne
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Kod klasy składowania
10 - Combustible liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Certyfikaty analizy (CoA)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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
Deanna Price et al.
Biochemistry, 59(21), 1981-2002 (2020-05-10)
It is known that the humanin (HN) peptide binding to amyloid-β (Aβ) protects against its cytotoxic effects, while acetylcholinesterase (AChE) binding to Aβ increases its aggregation and cytotoxicity. HN is also known to bind the insulin-like growth factor binding protein-3
Rakez Kayed et al.
Molecular neurodegeneration, 2, 18-18 (2007-09-28)
Amyloid-related degenerative diseases are associated with the accumulation of misfolded proteins as amyloid fibrils in tissue. In Alzheimer disease (AD), amyloid accumulates in several distinct types of insoluble plaque deposits, intracellular Abeta and as soluble oligomers and the relationships between
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