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Merck

A8354

Sigma-Aldrich

Anti-β-Amyloid antibody, Mouse monoclonal

clone NAB 228, purified from hybridoma cell culture

Szinonimák:

Anti-Aβ

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41
konjugátum:
unconjugated
application:
ARR
ELISA (i)
IHC
IP
WB
klón:
NAB 228, monoclonal
faj reaktivitás:
human
citations:
27
technika/technikák:
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

biológiai forrás

mouse

Minőségi szint

konjugátum

unconjugated

antitest forma

purified immunoglobulin

antitest terméktípus

primary antibodies

klón

NAB 228, monoclonal

Forma

buffered aqueous solution

molekulatömeg

antigen ~110 kDa

faj reaktivitás

human

kiszerelés

antibody small pack of 25 μL

koncentráció

~2 mg/mL

technika/technikák

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

izotípus

IgG2a

UniProt elérési szám

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... APP(351)

Általános leírás

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.

Immunogén

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

Alkalmazás

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.

Biokémiai/fiziológiai hatások

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).

Cél megnevezése

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

Fizikai forma

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

Jogi nyilatkozat

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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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

APP processing in Alzheimer's disease
Zhang Y W, et al.
Molecular Brain, 4(1), 3-3 (2011)
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
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
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

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