A8354
Anti-β-Amyloid antibody, Mouse monoclonal
clone NAB 228, purified from hybridoma cell culture
Synonym(s):
Anti-Aβ
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
NAB 228, monoclonal
form
buffered aqueous solution
mol wt
antigen ~110 kDa
species reactivity
human
packaging
antibody small pack of 25 μL
concentration
~2 mg/mL
technique(s)
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 2-4 μg/mL using cell extract of the human embryonal carcinoma NTERA-2 (NT2/D1) cells, treated for 2-3 weeks with 10 μM retinoic acid
isotype
IgG2a
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... APP(351)
Related Categories
General description
Amyloid β-peptide (Aβ), a 38 to 43 amino acid peptide is obtained from the β-amyloid precursor protein (APP). β-amyloid gene is located on human chromosome 21q21. APP is a type I transmembrane protein. It is produced in the endoplasmic reticulum (ER) and then migrated with the help of Golgi apparatus to the trans-Golgi-network (TGN).
The β-amyloid precursor protein (APP) is cleaved sequentially by the proteolytic enzymes β-secretase (BACE1) and γ-secretase to produce β-amyloid (Aβ) peptides with the Aβ1-42 and the Aβ1-40 forms being the most prevalent. Secreted Aβ peptides are degraded either via a re-uptake mechanism followed by endosomal degradation, or by an extracellular insulin degrading enzyme. Extracellular accumulation of Aβ leads to the formation of aggregates, fibrils and eventually amyloid deposits called neuritic plaques, which is the hallmark of Alzheimer′s disease (AD).
The antibody recognizes human β-amyloid peptide, full-length amyloid precursor protein (APP), soluble-APP (sAPPβ′ and sAPPα), C99 cleavage form, and Aβ (1-40/42), but not soluble-APP form sAPPβ.
Immunogen
synthetic peptide corresponding to amino acids 1-11 of human β-amyloid protein.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Monoclonal Anti-β-Amyloid antibody has been used in the titration of IgG1 and IgG2a isotype antibodies. It has also been used in the synthesis of antibody-functionalized magnetic nanoparticles.
Mouse Monoclonal Anti-β-Amyloid antibody has been used for western blot assays. The product can also be used for immunohistochemistry, immunoprecipitation, indirect ELISA and microarray studies.
Biochem/physiol Actions
β-amyloid gene acts as the substrate of insulin-degrading enzyme (IDE). It plays a major role in the pathogenesis of Alzheimer′s disease (AD) and type 2 diabetes mellitus (DM2).
Target description
Amyloids are insoluble protein aggregates consisting of misfolded proteins and peptides. Amyloid deposition are associated with multiple neurodegenerative disorders.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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.
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Product No.
Description
Pricing
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Edward B Lee et al.
The Journal of biological chemistry, 278(7), 4458-4466 (2002-12-14)
Insoluble pools of the amyloid-beta peptide (Abeta) in brains of Alzheimer's disease patients exhibit considerable N- and C-terminal heterogeneity. Mounting evidence suggests that both C-terminal extensions and N-terminal truncations help precipitate amyloid plaque formation. Although mechanisms underlying the increased generation
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