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Key Documents

A8354

Sigma-Aldrich

Anti-β-Amyloid antibody, Mouse monoclonal

clone NAB 228, purified from hybridoma cell culture

Sinonimo/i:

Anti-Aβ

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

NAB 228, monoclonal

Forma fisica

buffered aqueous solution

PM

antigen ~110 kDa

Reattività contro le specie

human

Confezionamento

antibody small pack of 25 μL

Concentrazione

~2 mg/mL

tecniche

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

Isotipo

IgG2a

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... APP(351)

Descrizione generale

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.

Immunogeno

synthetic peptide corresponding to amino acids 1-11 of human β-amyloid protein.

Applicazioni

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.

Azioni biochim/fisiol

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).

Descrizione del bersaglio

Amyloids are insoluble protein aggregates consisting of misfolded proteins and peptides. Amyloid deposition are associated with multiple neurodegenerative disorders.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (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
Thai Thao Ly et al.
Biosensors, 11(10) (2021-10-23)
An extraordinary optical transmission fibre-optic surface plasmon resonance biosensing platform was engineered to improve its portability and sensitivity, and was applied to monitor the concentrations of monoclonal antibodies (Mabs). By refining the fabricating procedure and changing the material of the
Jose Gregorio Salazar et al.
Antioxidants (Basel, Switzerland), 10(3) (2021-03-07)
Brain oxidative lipid damage and inflammation are common in neurodegenerative diseases such as Alzheimer's disease (AD). Paraoxonase-1 and -3 (PON1 and PON3) protein expression was demonstrated in tissue with no PON1 or PON3 gene expression. In the present study, we
An overview of APP processing enzymes and products
Chow V W, et al.
Neuromolecular Medicine, 12(1), 1-12 (2010)
APP processing in Alzheimer's disease
Zhang Y W, et al.
Molecular Brain, 4(1), 3-3 (2011)

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