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UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Clone:
WO2, monoclonal
Species reactivity:
mouse, human
Application:
ELISA, IHC, WB
Citations:
47
Servicio técnico
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Permítanos ayudarleNombre del producto
Anti-Amyloid β Antibody, clone W0-2, clone WO2, from mouse
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
clone
WO2, monoclonal
species reactivity
mouse, human
technique(s)
ELISA: suitable, immunohistochemistry: suitable (paraffin), western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... APP(351)
General description
The cerebral and vascular plaques associated with Alzheimer′s disease (AD) are mainly composed of amyloid beta peptides (Aβ). Aβ is derived from cleavage of the amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. Aβ [1-40], Aβ [1-42], and Aβ [1-43] peptides result from cleavage of APP after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last APP processing step. Aβ [1-40], [1-42] and [1-43] peptides are major constituents of the plaques and tangles that occur in AD. These Amyloid beta antibodies and peptides have been developed as tools for elucidating the biology of AD.
Calculated MW is 4 kDa This antibody can also show 120 and 105 kDa APP proteins, and ~45 kDa oligomers of amyloid proteins on our western blot of human Alzheimer diseased brain lysate.
Immunogen
Epitope: Amino acid residues 4-10
Human Amyloid β peptide
Application
Detect Amyloid β using this Anti-Amyloid β Antibody, clone W0-2 validated for use in WB, IH, ELISA.
Immunohistochemistry Analysis: 1:500 dilution from a previous lot detected Amyloid β in Alzheimer’s diseased hippocampus.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
Biochem/physiol Actions
This antibody recognizes amino acid residues 4-10 of human Amyloid β.
Physical form
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
Human Alzheimer diseased brain tissue lysate
Human Alzheimer diseased brain tissue lysate
Evaluated by Western Blot in human Alzheimer disease brain tissue lysate.
Western Blot Analysis: 0.5 µg/ml of this antibody detected Amyloid β in 10 µg of human Alzheimer diseased brain tissue lysate.
Western Blot Analysis: 0.5 µg/ml of this antibody detected Amyloid β in 10 µg of human Alzheimer diseased brain tissue lysate.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: MAB1561
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.
Clase de almacenamiento
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Contenido relacionado
Alzheimer’s Disease: Amyloid Cascade and Beyond Product Focus
Luisa Diomede et al.
Neurobiology of disease, 62, 521-532 (2013-11-05)
Although Alzheimer's disease (AD) is usually sporadic, in a small proportion of cases it is familial and can be linked to mutations in β-amyloid precursor protein (APP). Unlike the other genetic defects, the mutation [alanine-673→valine-673] (A673V) causes the disease only
Yuhai Zhao et al.
Frontiers in aging neuroscience, 8, 140-140 (2016-07-06)
One prominent and distinguishing feature of progressive, age-related neurological diseases such as Alzheimer's disease (AD) and prion disease (PrD) is the gradual accumulation of amyloids into dense, insoluble end-stage protein aggregates. These polymorphic proteolipid lesions are known to contribute to
Eitan Wong et al.
Proceedings of the National Academy of Sciences of the United States of America, 116(13), 6385-6390 (2019-03-10)
The mechanism by which γ-secretase activating protein (GSAP) regulates γ-secretase activity has not yet been elucidated. Here, we show that knockout of GSAP in cultured cells directly reduces γ-secretase activity for Aβ production, but not for Notch1 cleavage, suggesting that
Número de artículo de comercio global
| SKU | GTIN |
|---|---|
| MABN10 | 04053252668081 |