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A8326

Sigma-Aldrich

Anti-β-Amyloid Protein (1-40) antibody produced in rabbit

enhanced validation

whole antiserum

Synonyme(s) :

Anti-AAA, Anti-ABETA, Anti-ABPP, Anti-AD1, Anti-APPI, Anti-CTFgamma, Anti-CVAP, Anti-PN-II, Anti-PN2, Anti-alpha-sAPP, Anti-preA4

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About This Item

Numéro MDL:
MFCD00212892
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

whole antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

liquid

Contient

15 mM sodium azide

Espèces réactives

human

Validation améliorée

independent
Learn more about Antibody Enhanced Validation

Technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using human Alzheimer’s disease (AD) brain tissue
indirect ELISA: 1:4000-1:8000

Numéro d'accès UniProt

P05067

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... APP(351)

Description générale

Amyloid precursor proteins (APPs) are members of a large family of 70 kDa transmembrane glycoproteins that are found in a wide range of tissues. APP is expressed in the brain. It is located on human chromosome 21. APPs have three main isoforms, namely, APP695, APP751 and APP770, that are derived from alternative splicing events in cells.

Immunogène

synthetic β-amyloid (1-40) conjugated to BSA.

Application

Anti-β-Amyloid Protein (1-40) antibody produced in rabbit has been used in:
  • immunocytochemical localization of Aβ peptides
  • immunocytochemistry
  • immunoprecipitation
  • focused ultrasound-microbubble enhanced antibody delivery (FUS-MB)

Actions biochimiques/physiologiques

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).
Rabbit Anti-β-Amyloid Protein (1-40) antibody does not stain control sections of normal brain tissues.

Forme physique

Rabbit Anti-β-Amyloid (1-40) is supplied as a liquid containing 0.1% sodium azide as preservative.

Clause de non-responsabilité

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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Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

The metabolism of beta-amyloid converting enzyme and beta-amyloid precursor protein processing
Benjannet S, et al.
Biochemical and Biophysical Research Communications, 325(1), 235-242 (2004)
Jonathan P T Corcoran et al.
The European journal of neuroscience, 20(4), 896-902 (2004-08-13)
We have disrupted the retinoid signalling pathway in adult rats by a dietary deficiency of vitamin A. After 1 year of this dietary deficiency, there was a deposition of amyloid beta in the cerebral blood vessels. There is a downregulation
S Benjannet et al.
The Journal of biological chemistry, 276(14), 10879-10887 (2001-01-22)
Processing of the beta-amyloid precursor protein (betaAPP) by beta- and gamma-secretases generates the amyloidogenic peptide Abeta, a major factor in the etiology of Alzheimer's disease. Following the recent identification of the beta-secretase beta-amyloid-converting enzyme (BACE), we herein investigate its zymogen
Learning performances, brain NGF distribution and NPY levels in transgenic mice expressing TNF-alpha
Fiore M, et al.
Behavioural Brain Research, 112(1), 165-175 (2000)
Yanfang Rui et al.
Molecular brain, 9(1), 79-79 (2016-08-19)
Small oligomeric forms of amyloid-β (Aβ) are believed to be the culprit for declined brain functions in AD in part through their impairment of neuronal trafficking and synaptic functions. However, the precise cellular actions of Aβ oligomers and underlying mechanisms
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