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A8354

Sigma-Aldrich

Anti-β-Amyloid antibody, Mouse monoclonal

clone NAB 228, purified from hybridoma cell culture

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Synonym(s):
Anti-Aβ
MDL number:
NACRES:
NA.41

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)

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This Item
A3981A8978A5213
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

ascites fluid

clone

NAB 228, monoclonal

clone

BAM-10, monoclonal

clone

BAM90.1, monoclonal

clone

BAM-10, monoclonal

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

-

mol wt

antigen ~110 kDa

mol wt

-

mol wt

-

mol wt

-

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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)
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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Shen-Qing Zhang et al.
Frontiers in molecular neuroscience, 13, 613421-613421 (2021-02-02)
Clinical studies have found that some Alzheimer's disease (AD) patients suffer from Cushing's syndrome (CS). CS is caused by the long-term release of excess glucocorticoids (GCs) from the adrenal gland, which in turn, impair brain function and induce dementia. Thus
Detection of plasma biomarkers using immunomagnetic reduction: a promising method for the early diagnosis of Alzheimer?s disease
Yang S Y, et al.
Neurology and therapy, 6(1), 37-56 (2017)
Joana Poejo et al.
International journal of molecular sciences, 22(4) (2021-03-07)
Lipid rafts are a primary target in studies of amyloid β (Aβ) cytotoxicity in neurons. Exogenous Aβ peptides bind to lipid rafts, which in turn play a key role in Aβ uptake, leading to the formation of neurotoxic intracellular Aβ

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