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Key Documents

A5213

Sigma-Aldrich

Anti-β-Amyloid antibody, Mouse monoclonal

enhanced validation

clone BAM-10, ascites fluid

Synonym(s):

Anti-β-Amyloid antibody, Mouse monoclonal, Anti-A-BETA, Anti-Amyloid β Precursor Protein, Clone BAM91

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About This Item

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

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

BAM-10, monoclonal

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): 1:2,000 using formic acid-treated, formalin-fixed, human Alzheimer′s disease (AD) brain sections.
indirect ELISA: suitable

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... APP(351) , APP(351)

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General description

β-amyloid protein or aβ4 is derived from larger protein that belongs to the family of 70kDa transmembrane glycoproteins (amyloid precursor proteins, APP). These are produced in various isoforms by alternative splicing. APPs are synthesized by many tissues including brain cells. Abnormal β-amyloid protein deposits have been associated with Alzheimer′s disease, Down′s syndrome, Dutch-type amyloidosis and Lewy body dementia.
The antibody reacts specifically with β-amyloid protein. The epitope recognized by the antibody resides within amino acids 1-12 of the β-amyloid protein. It specifically stains amyloid plaques within the cortex and amyloid deposits in blood vessels using formic acid-treated, formalin-fixed, paraffin-embedded, and Methacarn-fixed sections of human Alzheimer′s disease (AD) brain tissue.

Specificity

Monoclonal Anti-β-Amyloid Protein reacts specifically with β-amyloid protein. The epitope recognized by the antibody resides within amino acid residues 1-12 of the β-amyloid protein. The antibody specifically stains amyloid plaques within the cortex, and amyloid deposits in blood vessels, in formic acid-treated, formalin-fixed, paraffin-embedded and Methacarn-fixed sections of human Alzheimer′s disease (AD) brain tissue.

Immunogen

Synthetic β-amyloid peptide, conjugated to KLH.

Application

Monoclonal Anti- β Amyloid Protein may be used for the localization of β -amyloid protein using various immunochemical assays such as ELISA, competitive ELISA and immunohistochemistry.
Mouse monoclonal anti-ABETA was used to treat old WT PDAPP mice with amyloid accumulation and learning deficits in an attempt to improve learning and decrease accumulation, however no response was observed.
The antibody is useful in immunohistochemistry, immunoblotting, ELISA, and competitive ELISA. Also, this antibody has been used to neutralize Aβ assemblies in brains of transgenic mice expressing a mutant form of amyloid precursor protein, and for in vivo deep tissue imaging using near-IR optical spectrum.

Biochem/physiol Actions

β-amyloid fragments are amyloidogenic and neurotoxic both in vitro and in vivo. The presence of a large number of neuritic (senile) plaques and neurofibrillary tangles in the cerebral cortex is used as a pathological marker for a disease state and presents the major criterion for the diagnosis of Alzheimer′s disease at autopsy. A monoclonal antibody reacting specifically with β-amyloid protein is valuable for studying the nature of the β-amyloid protein by enabling detection and localization of β-amyloid protein and fragments.

Physical form

Monoclonal Anti-β-Amyloid Protein is provided as ascites fluid with 15mM sodium azide as a preservative.

Storage and Stability

For continuous use, store at 2-8 °C for no more than one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

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

nwg

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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Xian-Hui Dong et al.
Experimental and therapeutic medicine, 9(4), 1319-1327 (2015-03-18)
Alzheimer's disease (AD) is a neurodegenerative brain disorder and the most common cause of dementia. New treatments for AD are required due to its increasing prevalence in aging populations. The present study evaluated the effects of the active components of
Deficits in object-in-place but not relative recency performance in the APPswe/PS1dE9 mouse model of Alzheimer?s disease: Implications for object recognition
Bonardi, C, et al.
Behavioural Brain Research, 313, 71-81 (2016)
Effects of Folic Acid on Secretases Involved in Aβ Deposition in APP/PS1 Mice
Tian, T, et al.
Nutrients, 8(9), 556-556 (2016)
Use-dependent effects of amyloidogenic fragments of β-amyloid precursor protein on synaptic plasticity in rat hippocampus in vivo
Kim, J, et al.
The Journal of Neuroscience, 21(4), 1327-1333 (2001)
Tae-Kyung Kim et al.
Experimental & molecular medicine, 44(12), 740-748 (2012-11-23)
The plant viral protease, NIa, has a strict substrate specificity for the consensus sequence of Val-Xaa-His-Gln, with a scissoring property after Gln. We recently reported that NIa efficiently cleaved the amyloid-β (Aβ) peptide, which contains the sequence Val-His-His-Gln in the

Articles

Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions.

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