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

whole antiserum

MDL number:

biological source


Quality Level

antibody form

whole antiserum

antibody product type

primary antibodies






15 mM sodium azide

species reactivity



dot blot: 1:6000 using β-amyloid (1-40) conjugated to KLH by dot blot immunoassay
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using human Alzheimer’s disease (AD) brain tissue



UniProt accession no.

shipped in

dry ice

storage temp.


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.


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


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.


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.


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
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)
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)
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...
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...
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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