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A8326

Sigma-Aldrich

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

enhanced validation

whole antiserum

Synonym(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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

form

liquid

contains

15 mM sodium azide

species reactivity

human

enhanced validation

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... APP(351)

General description

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.

Immunogen

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)

Biochem/physiol Actions

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.

Physical form

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

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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
Scott B Raymond et al.
PloS one, 3(5), e2175-e2175 (2008-05-15)
Alzheimer's disease is a neurodegenerative disorder typified by the accumulation of a small protein, beta-amyloid, which aggregates and is the primary component of amyloid plaques. Many new therapeutic and diagnostic agents for reducing amyloid plaques have limited efficacy in vivo
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
Jhana O Hendrickx et al.
International journal of molecular sciences, 22(13) (2021-07-03)
Increasing epidemiological evidence highlights the association between systemic insulin resistance and Alzheimer's disease (AD). As insulin resistance can be caused by high-stress hormone levels and since hypercortisolism appears to be an important risk factor of AD, we aimed to investigate

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